Práctica+1

__Información general:__ >tr|Q9RS44|Q9RS44_DEIRA Manganese ABC transporter, permease protein, putative OS=Deinococcus radiodurans GN=DR_2283 PE=3 SV=1 > code -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By similarity). -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family. code >sp|P44660|Y359_HAEIN Probable iron transport system membrane protein HI0359 OS=Haemophilus influenzae GN=HI0359 PE=3 SV=1 >sp|Q9KD29|MNTC_BACHD Manganese transport system membrane protein mntC OS=Bacillus halodurans GN=mntC PE=3 SV=1 >tr|C1D152|C1D152_DEIDV Putative ABC transporter, permease component OS=Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) GN=Deide_07190 PE=3 SV=1 >tr|Q1J100|Q1J100_DEIGD ABC-type Mn2+ transport system, permease component OS=Deinococcus geothermalis (strain DSM 11300) GN=Dgeo_0532 PE=3 SV=1 >sp|Q8Y652|MNTC_LISMO Manganese transport system membrane protein mntC OS=Listeria monocytogenes GN=mntC PE=3 SV=1
 * Nombre del gen: DR_2283
 * AC: Q9RS44
 * Organismo: Deinococcus radiodurans
 * Artículo interesante: Genome Sequence of the Radioresistant Bacterium Deinococcus radiodurans R1. Owen White, et al.Science 286, 1571 (1999);
 * Comentarios uniprot:
 * Información en entrez protein clusters: hoja aparte.
 * Genes homólogos:

__Archivos MultiFasta:__
 * Multifasta Proteínas:


 * Multifasta CDS:

[|Deinoc. prácticas.fin.ppt]PowerPoint final de presentación de trabajo hecho hasta la fecha (30/04/10)


 * MultiFasta Proteina:**

>tr|Q9RS44|Q9RS44_DEIRA Manganese ABC transporter, permease protein, putative OS=Deinococcus radiodurans GN=DR_2283 PE=3 SV=1 MHWLTDPLQFDFFVRALLAVSLVSILCALIGAWVVLRGLSYIGDAMSHAVLPGIVSAFLL KGNLLLGAAIAAVLTALGIGWIGRRSGLKQDSAIGIVFVGMFALGIVLLSRAPTFTSDLSNF LIGNPLGVTPADLWGALAVTLGVGGLLTAIQKELLLASFDPTEARTVGLPVTRLNNLLLVL IGLVVVLTVQLVGTTLSVSLLITSSAAARLLSRSLRTMMLLAAALGILGGVSGLYASYYLD TAPGATIVLVNTAIFLLALAFRRK

>sp|P44660|Y359_HAEIN Probable iron transport system membrane protein HI0359 OS=Haemophilus influenzae GN=HI0359 PE=3 SV=1 MFDWLLEPLQFEFMQNALLTALIVSIICALLSCYLVLKGWSLMGDAISHAVLPGIVLAYL AGIPLAIGAFFSGIFCSLGVGYLKENSRIKEDTAMGIVFSGMFAIGLVMFTKIQTEEHLT HILFGNVLGVSHQELIQSAVISAIIFCLIVFKRKDFLLYCFDPSHARVAGLSPKILHYGL LILLALTIVSTMQVVGVILVVAMLIAPGITALTLTKSFDKMLWVAIASSIASSLIGVILS YHFDASTGACIILLQAAFFVIALAYSKIRIR

>sp|Q8Y652|MNTC_LISMO Manganese transport system membrane protein mntC OS=Listeria monocytogenes GN=mntC PE=3 SV=1 MLFLEGLMQYSFLQKALITSVTVGIVSGVIGSFIILRGMSLMGDAISHAVLPGVAISYMM GMNFFIGAATFGIAAALGIGFVNQKSRIKNDTAIGIVFSAFFALGIILISFAKSSTDLYH ILFGNVLAVRSSDMWMTIIIAIIVISLVALFYKEFLVSSFDPVMAEAYGLNVKFLHYFLM LLLTLVTVSALQTVGIILVVAMLITPAATAYLLTNKLSKMIVLASTFGAVSAIIGLYFSY IFNLASGAAMVLVATIIFFIAFLFAPKQGLLFSKKREVIE

code >tr|C1XUH3|C1XUH3_9DEIN ABC-type Mn2+/Zn2+ transport system, permease component OS=Meiothermus silvanus DSM 9946 GN=MesilDRAFT_19770 PE=3 SV=1 MLEALSFPFFQRALLAGVLVGAFISYYAPFVVQRKLSFLSHGLAHAAFGGVAIALFFNTE PLWVALPFTVLVALGITWVRSRTGLGEDSAIGIFLALALAFGILILSFRTSYAAEALSYL FGSLLTVTPTDLWISLAVLVLTLALLPLWGRWAYATFDRDLALADRRRVLTQDYLLSALV AVATVVAVKVVGALLVGAFLVIPAATARLWSRTFSTMTLLSVVLGITTALVGLILSYQFN VPSGASIVLLQAAIFALAFSTGRREPAG

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code >tr|Q1J100|Q1J100_DEIGD ABC-type Mn2+ transport system, permease component OS=Deinococcus geothermalis (strain DSM 11300) GN=Dgeo_0532 PE=3 SV=1 MHLLTDPLQFDFFLRALAAVVLVSILCALVGAWVVLRGLSYIGDAMSHAVLPGIVGAFLT GGNLLLGALVAAVLTALGIGAVSGRGGLKQDSAIGIVFVGMFALGVVMLSRVSTFTTDLS NFLIGNPLGVTPGDLWGALGVTLVVGALLTAVQKELLLASFDPTEARAIGLPVRWLNHLL LILIGLVVVLTVQLVGTTLSVSLLITSSAAARLLARSLKKMILLAALLGTLGGVTGLYLS YYVNTAPGATIVLVNTAIFLLALAFRRRE

>tr|C1D152|C1D152_DEIDV Putative ABC transporter, permease component OS=Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) GN=Deide_07190 PE=3 SV=1 MDWLTDPLQFDFFQRALAAVVLVSVLCALVGAWVVLRGLSYIGDAMSHAVFPGIVAAFLM KGNLLVGALIAAVLTALGIGLVSQRSGLKQDSAIGIVFVGMFALGIVMLSRAPSFTTDLS NFLIGNPLGVTPTDLWSALLVTALVGGLLTAIQKELLLASFDPTEARAIGLPVRPLESLL LILIGLVVVLTVQLVGTTLSVSLLITSSATARLLARNLKKMILTAALLGVVGGITGLYLS YFMNTAPGATIVLVNTALFLLALFFRRRE

>sp|Q9KD29|MNTC_BACHD Manganese transport system membrane protein mntC OS=Bacillus halodurans GN=mntC PE=3 SV=1 MSNLTFFFDQLLSYSYLQQALTAAILVGIICGVIGCFIILRGMALMGDAISHAVLPGVVI AYMIGASFFIGAVITGVITALAIGYVSQNSRVKEDSAIGILFTAAFALGIVLITGMRGTG VDLWHILFGNVLAVSRTDLWVTLGIGLFVLLIIILFYRPLLLSTFDPVMAQATGIPVQMI HYLLMLLLSLVTVAALQTVGIVLVVAMLITPGATAYLLTNRLPVMLCLAAMFGVISAIAG IYFSVIYDVASGASIVLVASTLFALAFFFSPKQGVLTRYWRGKRAKEMSATS code

code >tr|Q72LH4|Q72LH4_THET2 Manganese transport system membrane protein mntB OS=Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) GN=mntB PE=3 SV=1 MLEALGYPFFQRALLAGLLVSLLGGALSAFVVQRRLSFLGDGLAHAAFAGVALGLFLREE PLYLALPFTLAVALAITYVKERSGLSEDTAIGVFFALSVALGAVFLAKARGYVGDAMGYL FGSLLAVGPGDLWAVGGVVLLGLALLPLWGALAYATFDRELALADRVPVGLHDYLLSAYL ALALVVAVKVVGVLLVAAFLVIPGAAARLLGRTFAGMTLLALLFALSATLLGLYASFLLD WPSGASVVLAQALLFGLAFLKTAFSGGK

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code >sp|P31606|YCXC_CYAPA Uncharacterized membrane protein in ycf23-apcF intergenic region OS=Cyanophora paradoxa PE=3 SV=2 MLIDYLFRLPLNILFLFSHSFSSFLLPFQLHFMQRAFVIGLIAALLAGIVGSFLMLQRLT LLSDAISHSVLPGLAIAFSFGIPLIFGALLASIISVIIINWIRTESRLKEDTAIGIVFAS FFGLGILLISVIQKENKVDLNHFLFGNILGITSEDLQNTSIILAIILLFFISCYRQLKCY TFDPIMAQTIGLPINFLQSTFLILVALTIIVSMKAIGVILVLALLVTPGATGLLIGKSLE YVILTSSIIGVSCSFSGMLLSYLFNIPPGPTIVLITSLIFFILFLIINKKDSTTDSKLF

>tr|A3CTP7|A3CTP7_METMJ ABC-3 protein OS=Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) GN=Memar_0814 PE=4 SV=1 MFEILGFEFFRNALIAGVLASVACGIIGTYVVVRRMVSVSGGISHAAFGGIGLGYFLGID PLLGATGFTVATALGMGTLQLRARQQMDTIIGAVWAAGMAIGILFVYLTPGFAPDLFSYL FGNILLVPRGDILLMGVLVVIIVAVVALLYRELQAITFDPDYATVMNLPVERLSLLLLVL IALTVVMLIRVVGIILVIALLTLPAAISRLYTTRIRSMMLLAVILGIVFTVAGILLSYLL DVPSGATIILVSTLAYAGALGAERLRQGD

code >sp|Q55282|MNTB_SYNY3 Manganese transport system membrane protein mntB OS=Synechocystis sp. (strain PCC 6803) GN=mntB PE=1 SV=1 MNQLVVAFPFWHWLVEPLQYEFLIRAIWVSAFVGLVCAVLSCYITLKGWSLMGDAISHAV VPGVVLAYALNIPFAIGAFTFGFGATVAIGYVKSKTRLKEDAVIGIVFTGFFALGLVLVT KIPSNVDLFHILFGNVLGISQQDIIQTLIAGSITLIVILLRRKDLLLFCFDPNHAKAIGL RTQVMYYTLLSVLALTIVAALQTAGIILVISMLVTPGSIGYLLSDRFDHMLWYSVVSSVL SCVLGTYLSYHFDVSTGGMIVVILTTLFVIAMIGAPKYGILAQEWRKRSGPNPEDDENQT VVVDQV


 * MultiFasta CDS:**

>D. radiodurans CTACTTCCGCCGAAACGCGAGCGCCAGCAGAAAAATAGCCGTGTTCACCAGCACGATGGTCGCCCCCGGC GCGGTGTCGAGGTAATAACTGGCATACAGCCCACTGACCCCGCCGAGGATGCCCAGAGCGGCGGCGAGCA GCATCATGGTCCGCAGGCTCCGCGAGAGCAGGCGGGCGGCGGCGCTGGACGTGATCAGCAGGCTGACGCT GAGGGTGGTCCCCACGAGCTGCACCGTCAGCACCACCACCAGCCCGATCAGCACCAGCAGCAGGTTGTTC AGCCGCGTGACCGGCAGCCCCACCGTCCGCGCCTCGGTGGGGTCGAAGGAAGCGAGCAGCAGCTCCTTCT GAATCGCCGTGAGCAGCCCGCCTACCCCCAGCGTGACCGCCAGGGCGCCCCACAGGTCGGCGGGGGTCAC GCCCAGCGGGTTGCCGATCAGGAAATTGCTGAGGTCGGACGTGAAGGTGGGGGCCCGCGACAGCAGCACG ATGCCCAGCGCGAACATCCCCACGAAGACGATGCCGATGGCGCTGTCCTGTTTCAGCCCACTGCGACGTC CGATCCAGCCGATGCCCAGCGCCGTGAGCACCGCCGCAATCGCCGCGCCGAGCAGCAGGTTGCCCTTGAG GAGAAAGGCAGAGACGATGCCCGGCAGCACCGCGTGGCTCATCGCGTCCCCGATGTAACTCAGCCCGCGC AGCACCACCCAGGCGCCGATCAGCGCGCACAGGATGCTCACGAGGCTCACCGCGAGCAGCGCCCGGACAA AGAAATCGAATTGCAGCGGGTCGGTCAGCCAGTGCAT

code >H. influenzae TTATCTTATTCTAATCTTGCTATAAGCTAATGCTATAACAAAAAATGCGGCTTGCAGAAGAATAATACAA GCACCTGTTGAGGCATCAAAATGATAGCTCAATATTACGCCAATTAAGCTTGATGCAATGGAACTTGCAA TAGCAACCCATAACATTTTATCAAAAGATTTAGTAAGAGTAAGTGCGGTAATTCCTGGTGCAATTAACAT TGCCACCACCAAAATAACACCTACCACTTGCATCGTGCTTACAATGGTTAAAGCAAGTAGAATTAATAAA CCATAATGTAAAATTTTAGGAGAAAGTCCTGCAACACGGGCGTGACTTGGATCAAAACAATAAAGCAGAA AGTCTTTACGTTTAAAGACAATCAGACAAAAAATTATCGCAGAAATGACCGCACTTTGAATAAGTTCTTG ATGACTTACACCCAACACATTACCAAACAAAATATGGGTTAAATGCTCTTCTGTTTGAATTTTGGTAAAC ATAACAAGACCAATGGCAAACATTCCAGAAAATACAATGCCCATTGCGGTATCTTCTTTTATACGGCTAT TTTCTTTCAAATATCCCACACCAAGCGAACAAAAAATACCCGAGAAAAATGCACCAATGGCTAAAGGAAT TCCTGCCAAATAAGCAAGTACAATACCAGGTAATACAGCGTGAGAAATTGCATCACCCATTAATGACCAA CCTTTCAAGACTAAATAGCAAGAAAGTAACGCACAGATAATCGAAACAATCAATGCGGTCAATAAGGCAT TTTGCATAAACTCAAATTGTAGCGGTTCTAAAAGCCAATCAAACAT

>L. monocytogenes TCATTCGATAACCTCCCTTTTTTTAGAAAATAGCAAGCCTTGTTTCGGTGCGAATAAAAAGGCAATAAAG AAAATAATTGTCGCAACTAAAACCATAGCCGCACCAGATGCTAAGTTGAAAATGTAACTAAAGTAAAGTC CGATAATCGCACTCACTGCTCCAAAAGTAGAAGCAAGAACAATCATTTTGGATAATTTATTCGTAAGCAG ATAAGCTGTTGCAGCTGGCGTAATTAACATCGCCACAACTAAAATAATTCCAACCGTTTGCAAAGCGGAA ACCGTTACAAGTGTTAAAAGTAACATCAAGAAGTAATGCAAGAATTTCACATTGAGACCATATGCTTCTG CCATCACTGGATCAAACGAACTAACTAGAAACTCTTTGTAAAATAGGGCTACTAATGAAATCACGATAAT GGCAATAATAATTGTCATCCACATATCCGAACTCCGCACCGCAAGCACATTTCCAAATAAAATATGATAC AAATCCGTACTACTTTTCGCAAAGGATATTAAAATAATTCCAAGTGCAAAAAATGCACTAAAAACAATTC CAATCGCTGTATCATTTTTTATCCGACTTTTTTGATTAACAAAACCGATTCCAAGTGCCGCCGCGATGCC GAATGTAGCTGCACCAATAAAGAAGTTCATCCCCATCATATAAGAAATCGCCACTCCTGGAAGCACTGCA TGAGAAATCGCATCCCCCATAAGCGACATACCTCGTAAAATAATAAAACTACCAATAACACCTGAAACAA TACCAACCGTCACAGAAGTAATAAGGGCTTTTTGTAAAAAACTATATTGCATTAAACCTTCTAAAAACAA CAA

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code >gi|226316800:885296-886105 Deinococcus deserti VCD115, complete genome CTACTCGCGACGGCGGAAAAATAGTGCGAGCAGAAACAGGGCGGTGTTGACCAGCACGATCGTGGCGCCC GGCGCAGTATTCATGAAGTAGCTCAGGTAAAGGCCGGTGATGCCTCCAACAACGCCCAGCAGCGCAGCCG TCAGGATCATTTTCTTCAGGTTCCGGGCCAGCAGGCGCGCGGTAGCGCTTGAGGTGATCAGCAGGCTTAC GCTGAGGGTGGTGCCGACCAGTTGTACAGTCAGGACCACCACCAGTCCAATCAGAATCAGCAGCAGGCTT TCCAGGGGCCGTACCGGCAAGCCGATGGCACGCGCTTCCGTGGGATCGAAACTGGCAAGCAGCAGTTCCT TCTGGATAGCAGTCAGCAACCCGCCCACCAGCGCCGTAACGAGCAGGGCGCTCCACAGGTCTGTTGGCGT CACGCCCAGTGGATTGCCGATCAGGAAATTGCTCAGGTCGGTGGTAAAGCTCGGCGCGCGTGAGAGCATG ACTATGCCCAGCGCGAACATTCCGACAAACACGATGCCAATGGCACTGTCCTGTTTCAGCCCGCTGCGCT GACTGACCAGTCCGATCCCCAGTGCTGTAAGTACGGCGGCAATCAGAGCTCCGACCAGCAGATTTCCCTT CATCAGAAAGGCGGCCACGATTCCTGGGAACACCGCGTGACTCATGGCATCCCCGATGTAACTCAGTCCA CGCAACACCACCCATGCGCCCACCAATGCACACAGCACACTGACCAGCACCACGGCTGCCAGCGCACGCT GGAAGAAATCAAATTGCAACGGATCGGTCAGCCAGTCCAT

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code >gi|94554390:558519-559328 Deinococcus geothermalis DSM 11300, complete genome CTATTCCCGCCGCCGGAAGGCCAGCGCCAGTAGGAAGATCGCCGTGTTCACCAGCACGATGGTCGCGCCC GGCGCGGTGTTGACGTAGTAGCTGAGGTAGAGCCCCGTCACGCCGCCGAGGGTGCCCAGCAGGGCGGCGA GCAGGATCATCTTTTTCAGGCTGCGGGCCAGCAGACGCGCGGCGGCGCTGGAGGTGATCAGCAGGCTCAC GCTGAGGGTGGTCCCGACAAGCTGCACCGTCAGCACCACCACCAGGCCGATCAGGATCAGCAGCAGGTGG TTCAGCCAGCGCACCGGCAATCCGATGGCCCGCGCCTCGGTGGGGTCAAAGGACGCGAGGAGAAGCTCCT TTTGCACGGCCGTCAGCAGGGCGCCAACCACCAGTGTGACCCCAAGGGCACCCCACAGGTCACCCGGCGT GACGCCCAGCGGATTCCCGATGAGGAAGTTGCTCAGGTCGGTGGTAAAGGTGGATACGCGCGAGAGCATG ACCACGCCGAGAGCAAACATCCCCACAAAGACAATCCCGATGGCGCTGTCCTGCTTCAGCCCGCCCCGCC CGCTCACTGCGCCGATCCCCAGCGCGGTCAGGACGGCAGCCACCAGCGCTCCCAGCAGCAGATTGCCCCC CGTCAGAAACGCCCCCACAATGCCGGGCAGGACGGCGTGGCTCATCGCGTCCCCGATGTAGCTCAGTCCG CGCAGCACCACCCACGCGCCCACCAGCGCACACAGGATACTCACCAGCACGACGGCGGCAAGTGCCCGCA GAAAGAAGTCGAATTGCAGGGGATCAGTCAACAGGTGCAT

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code >gi|47118318:1473829-1474707 Bacillus halodurans C-125 DNA, complete genome ATGAGCAATCTAACCTTCTTTTTCGACCAATTGCTGAGTTACTCTTATTTGCAACAGGCGCTTACTGCTG CAATTTTAGTTGGCATCATTTGTGGAGTGATCGGTTGTTTTATTATTTTACGGGGAATGGCACTGATGGG GGATGCCATTTCTCATGCGGTATTGCCAGGTGTCGTCATTGCTTACATGATCGGTGCGAGCTTTTTTATT GGCGCCGTCATTACGGGTGTCATTACGGCACTTGCGATTGGTTATGTGTCACAAAACAGCCGAGTGAAGG AAGATTCAGCGATCGGCATTTTATTTACAGCAGCCTTCGCATTAGGGATTGTGTTAATAACAGGAATGCG CGGCACGGGAGTGGACCTTTGGCATATTTTGTTCGGAAATGTGTTAGCGGTATCGCGCACAGACCTATGG GTTACCCTGGGGATTGGTCTGTTTGTCCTGCTCATTATTATTCTCTTTTACAGACCGTTGTTGCTTAGTA CATTTGATCCCGTTATGGCACAAGCGACTGGAATTCCGGTCCAAATGATTCACTACTTGTTAATGCTGCT TTTATCTCTCGTCACGGTGGCGGCCTTGCAGACAGTTGGGATCGTTCTTGTGGTAGCGATGCTCATTACA CCAGGTGCAACTGCTTATTTATTAACGAACCGTTTGCCTGTTATGCTCTGTTTAGCGGCGATGTTCGGGG TCATTTCCGCCATTGCTGGAATCTATTTTTCGGTGATTTATGATGTGGCCTCAGGGGCTTCCATTGTTCT AGTCGCTTCTACTTTGTTTGCACTTGCCTTCTTTTTCTCACCAAAACAAGGTGTGTTGACACGCTATTGG CGAGGAAAGCGGGCGAAGGAAATGAGTGCAACCTCGTAA

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code >gi|11467282:123367-124266 Cyanophora paradoxa cyanelle, complete genome TTAAAATAATTTTGAATCAGTAGTTGAATCTTTTTTATTTATTATTAAAAAAAGAATGAAAAAAATCAAA GATGTAATTAAAACAATTGTAGGACCAGGAGGAATATTAAAAAGATAACTTAATAACATTCCAGAAAAAC TACAACTTACCCCGATAATCGAACTCGTAAGAATTACATATTCTAAACTTTTTCCTATTAATAAACCTGT AGCTCCCGGAGTAACTAATAAAGCTAAAACTAATATTACACCTATTGCTTTCATACTTACAATAATTGTT AAAGCGACTAAAATTAAAAAAGTAGATTGTAAAAAGTTAATAGGTAATCCTATAGTTTGTGCCATTATAG GGTCAAATGTATAACATTTTAATTGTCTATAACAACTTATAAAAAAAAGTAAAATAATTGCTAAAATTAT AGATGTATTTTGTAAATCTTCTGATGTAATTCCTAAAATATTACCAAATAAAAAATGATTAAGGTCGACT TTATTTTCTTTTTGAATAACACTAATTAATAAAATTCCCAATCCAAAAAACGAAGCAAAAACAATACCAA TAGCCGTATCTTCTTTTAAGCGAGACTCCGTCCTAATCCAATTTATAATAATTACACTAATAATACTTGC TAATAAAGCTCCAAAAATTAATGGAATTCCAAAACTAAATGCAATAGCTAAACCTGGTAGAACCGAGTGA CTGATAGCATCACTTAATAATGTTAAACGTTGTAACATTAAAAAAGAGCCAACAATACCAGCTAACAACG CTGCAATTAAACCAATTACAAAAGCTCGTTGCATAAAATGCAGTTGAAAAGGTAATAAAAAAGATGAGAA TGAATGTGAAAATAAAAACAAAATATTTAGGGGAAGTCTAAATAGATAATCAATTAGCAT

>gi|126177952:797746-798555 Methanoculleus marisnigri JR1, complete genome CTAGTCGCCCTGCCGGAGGCGCTCGGCCCCGAGGGCGCCCGCATACGCGAGCGTGCTCACGAGGATGATC GTCGCGCCCGAGGGGACGTCGAGGAGGTAGGAGAGCAGGATCCCCGCAACGGTGAAGACGATGCCGAGGA TGACGGCGAGGAGCATCATGCTCCGGATGCGGGTGGTGTAGAGGCGGCTGATCGCCGCCGGGAGCGTCAG GAGCGCGATCACCAGGATGATCCCCACCACCCGGATCAGCATCACCACGGTGAGCGCAATCAGCACGAGG AGGAGGAGCGAGAGCCGCTCGACCGGGAGGTTCATGACCGTCGCGTAGTCCGGGTCGAACGTGATCGCCT GGAGCTCCCGGTAGAGGAGAGCCACGACGGCGACGATGATAACGACGAGCACCCCCATCAGCAGGATGTC TCCCCTTGGGACGAGGAGGATGTTCCCGAAGAGGTAGGAGAAGAGGTCGGGGGCGAATCCCGGTGTCAGG TAGACGAAGAGGATCCCGATGGCCATCCCCGCCGCCCAGACCGCGCCGATGATGGTGTCCATCTGCTGCC GGGCACGGAGCTGGAGCGTGCCCATCCCGAGCGCCGTCGCCACGGTGAACCCGGTCGCGCCGAGGAGCGG GTCTATCCCGAGGAAGTAGCCGAGGCCGATCCCCCCGAAGGCCGCATGGGATATGCCGCCGCTGACCGAG ACCATCCGCCGCACCACGACGTAGGTGCCGATGATGCCGCAGGCCACGCTCGCGAGCACCCCGGCGATGA GGGCGTTCCTGAAGAACTCGAATCCGAGAATCTCGAACAT

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code >gi|227952205:107078-107884 Meiothermus silvanus DSM 9946 MesilDRAFT_4083028_Cont9, whole genome shotgun sequence CTACCCCGCTGGTTCGCGCCGCCCGGTGCTGAAGGCCAAGGCAAAGATCGCGGCTTGTAGGAGCACGATG CTGGCCCCGCTAGGGACATTAAACTGGTAGGACAAGATCAGACCGACCAGCGCCGTGGTAATTCCCAGCA CGACCGAGAGTAGCGTCATAGTGCTAAAAGTGCGACTCCACAACCGAGCGGTAGCCGCTGGGATCACCAA AAAAGCCCCCACCAACAACGCCCCCACCACCTTTACCGCTACCACGGTGGCTACTGCGACCAGCGCCGAG AGGAGGTAGTCTTGGGTCAGCACTCGGCGGCGGTCGGCTAGGGCTAGGTCGCGATCGAAGGTGGCATAGG CCCAGCGGCCCCACAAAGGAAGCAGGGCTAGGGTCAGCACCAGGACCGCTAGCGAGATCCAGAGGTCGGT AGGGGTGACGGTGAGCAGCGAGCCGAAGAGATACGAAAGGGCCTCGGCGGCGTAGCTGGTCCGGAAGGAG AGGATCAGGATGCCAAAGGCCAGAGCCAGGGCCAGAAAAATCCCGATGGCCGAGTCCTCGCCGAGACCCG TCCTCGAGCGCACCCAGGTGATCCCCAAAGCTACCAGCACGGTAAACGGCAGCGCCACCCATAGCGGCTC GGTATTGAAGAAAAGGGCAATCGCCACCCCCCCGAAGGCCGCGTGGGCCAATCCGTGCGAGAGGAAGGAG AGCTTGCGCTGCACCACGAAGGGGGCGTAATAGCTGATAAAAGCCCCCACCAGCACCCCGGCCAGCAGGG CGCGCTGAAAGAAAGGGAAAGAGAGGGCCTCGAGCAT

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code >gi|46197919:75666-76472 Thermus thermophilus HB27, complete genome GTGCTTGAGGCCTTGGGCTACCCCTTCTTCCAGAGGGCCCTCCTCGCCGGCCTCTTGGTGAGCCTGCTTG GAGGGGCGCTTTCCGCCTTCGTGGTGCAGAGAAGGCTTTCCTTCCTGGGGGACGGGCTCGCCCACGCCGC CTTCGCCGGGGTGGCCCTGGGGCTTTTCCTGAGGGAGGAGCCCCTCTACCTCGCCCTCCCCTTCACCCTG GCCGTGGCCCTGGCCATCACCTACGTGAAGGAGCGCTCGGGTCTTTCGGAGGACACGGCCATCGGCGTCT TCTTCGCCCTTTCCGTGGCCCTCGGGGCCGTCTTCCTCGCCAAGGCCCGGGGGTACGTGGGGGACGCCAT GGGCTACCTCTTTGGCTCCCTCCTCGCCGTGGGGCCCGGGGACCTCTGGGCCGTGGGGGGGGTGGTCCTT CTGGGCCTCGCCCTCCTTCCCCTCTGGGGCGCTTTGGCCTACGCCACCTTTGACCGGGAGCTCGCCCTCG CCGACCGGGTGCCCGTGGGGCTCCACGACTACCTCCTCTCCGCCTACCTGGCCCTCGCCCTGGTGGTGGC GGTGAAGGTGGTGGGGGTCCTCCTCGTGGCCGCCTTTTTGGTGATCCCGGGGGCGGCGGCCCGGCTTCTC GGCCGCACCTTCGCCGGCATGACCCTCCTTGCCCTCCTCTTCGCCCTCTCGGCCACCCTCCTCGGGCTTT ACGCCTCCTTCCTCCTGGACTGGCCCAGCGGGGCCAGCGTGGTCCTGGCCCAGGCCCTCCTCTTCGGCCT CGCCTTCCTTAAAACCGCGTTTTCCGGGGGGAAATAG

code

  code TTT F Phe     TCT S Ser      TAT Y Tyr      TGT C Cys TTC F Phe     TCC S Ser      TAC Y Tyr      TGC C Cys TTA L Leu     TCA S Ser      TAA * Ter      TGA * Ter TTG L Leu i   TCG S Ser      TAG * Ter      TGG W Trp
 * TABLA DE TRADUCCIÓN DE D. RADIODURANS:**

CTT L Leu     CCT P Pro      CAT H His      CGT R Arg CTC L Leu     CCC P Pro      CAC H His      CGC R Arg CTA L Leu     CCA P Pro      CAA Q Gln      CGA R Arg CTG L Leu i   CCG P Pro      CAG Q Gln      CGG R Arg

ATT I Ile i   ACT T Thr      AAT N Asn      AGT S Ser ATC I Ile i   ACC T Thr      AAC N Asn      AGC S Ser ATA I Ile i   ACA T Thr      AAA K Lys      AGA R Arg ATG M Met i   ACG T Thr      AAG K Lys      AGG R Arg

GTT V Val     GCT A Ala      GAT D Asp      GGT G Gly GTC V Val     GCC A Ala      GAC D Asp      GGC G Gly GTA V Val     GCA A Ala      GAA E Glu      GGA G Gly GTG V Val i   GCG A Ala      GAG E Glu      GGG G Gly

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Transportadores ABC modelo
Base de datos de proteínas transportadoras --> [|TCDB]

**3.A.1 The ATP-binding Cassette (ABC) Superfamily** The ABC superfamily contains both uptake and efflux transport systems, and the members of these two porter groups generally cluster loosely together with just a few exceptions ( Saurin //et al//., 1999 ). ATP hydrolysis without protein phosphorylation energizes transport. There are dozens of families within the ABC superfamily, and family generally correlates with substrate specificity. However there are exceptions. The high resolution X-ray structures of several ABC transporters, both uptake and efflux systems, have been determined, and specific details of the transport mechanisms have been proposed ( Davidson and Maloney, 2007 ; Lee //et al//., 2007 ). The porters of the ABC superfamily consist of two integral membrane domains/proteins and two cytoplasmic domains/proteins. The uptake systems (but not the efflux systems) additionally possess extracytoplasmic solute-binding receptors (one or more per system) which in Gram-negative bacteria is found in the periplasm, and in Gram-positive bacteria is present either as a lipoprotein, tethered to the external surface of the cytoplasmic membrane, or as a cell surface-associated protein, bound to the external membrane surface via electrostatic interactions. For those systems with two or more extracytoplasmic solute binding receptors, the receptors may interact in a cooperative fashion ( Biemans-Oldehinkel and Poolman, 2003 ). Both the integral membrane channel constituent(s) and the cytoplasmic ATP-hydrolyzing constituent(s) may be present as homodimers or heterodimers. Two families of ABC transporters have members in which one or two receptors are fused to either the N- or C-terminus of the translocating membrane protein. This suggests that two or even four substrate-binding sites may function in the complex. Possibly multiple receptors in proximity to the translocator enhances the transport rate. Multiple receptors may also broaden the substrate specificity of the system (van der Heide and Poolman, 2002 ). These systems with covalent receptor domains linked to the transmembrane translocators are found in the PAAT family (TC #3.A.1.3) and the QAT family (TC #3.A.1.12) (van der Heide and Poolman, 2002 ). The homodimeric LmrA drug efflux pump (TC #3.A.1.117.1) of //Lactococcus lactis// appears to function by an alternating site (half of sites) type mechanism. In many of these porters, the various domains are fused in a variety of combinations. Uptake porters generally have their constituents as distinct polypeptide chains, while efflux systems usually have them fused. ABC-type uptake systems have not been identified in eukaryotes, but ABC-type efflux systems abound in both prokaryotes and eukaryotes. **¿De verdad te estás leyendo esto Clau?** SÍ!!! The eukaryotic efflux systems often have the four domains (two cytoplasmic domains and two integral membrane domains) fused into either one or two polypeptide chains. The integral membrane porter domains each usually possesses 5 (uptake) or 6 (efflux) transmembrane spanners, but exceptions exist. For example, the MntB protein (TC #3.A.1.15.1) exhibits 9 established TMSs. The 3-dimensional structure of the //E. coli// MsbA protein (TC #3.A.1.106.1) has been solved to a resolution of 3.7 Å ( Ward //et al//., 2007 ), that of the //Staphylococcus aureus// Sav1866 protein (TC #3.A.1.106.2) has been solved to a resolution of 3.0 Å ( Dawson and Locher, 2006 ), that of the //Archaeoglobus fulgidus// ModABC complex has been solved at 3.1 Å resolution ( Hollenstein //et al//., 2007 ), that of the //E. coli// BtuCDF Vitamin B12 transporter was solved at 2.6 Å resolution ( Hvorup //et al//., 2007 ), and the maltose transporter has been solved at 2.8 Å resolution ( Oldham //et al//., 2007 ). These structures are very different, but the two transmembrane domains form a single barrel 5-6 nm in diameter and about 5 nm deep with an entral pore open either to the external or internal surface spanning much of the membrane ( Rosenberg //et al//., 2003 ). A model has been proposed allowing the channel to open up to the lipid bilayer. A half of sites model in which the two nucleotide binding domains interact in a fashion controlled by substrate binding has also been proposed ( Hou //et al//., 2003 ; Loo //et al//., 2003 ). Hollenstein et al. ( 2007 ) presented the 3.1 Å crystal structure of a putative molybdate transporter (ModB2 C2) from //Archaeoglobus fulgidus// in complex with its binding protein (ModA). Twelve transmembrane helices of the ModB subunits provide an inward-facing conformation, with a closed gate near the external membrane boundary. The ATP-hydrolyzing ModC subunits reveal a nucleotide-free, open conformation, whereas the attached binding protein aligns the substrate-binding cleft with the entrance to the presumed translocation pathway. Structural comparison of ModB2C2A with Sav1866 suggests a common alternating access and release mechanism, with binding of ATP promoting an outward-facing conformation and dissociation of the hydrolysis products promoting an inward-facing conformation. Smriti //et al.//, 2009 mapped residues proximal to the daunorubicin (DNR)-binding site in MsbA (TC#3.A.1.106.1) using site-specific, ATP-dependent quenching of DNR intrinsic fluorescence by spin labels. In the nucleotide-free MsbA intermediate, DNR-binding residues cluster at the cytoplasmic end of helices 3 and 6 at a site accessible from the membrane/water interface and extending into an aqueous chamber formed at the interface between the two transmembrane domains. **Ya aquí no has llegado seguro... Pero se puede saber que boicot es este? xDD llevo todo el finde currando y me lo estoy teniendo que leer el lunes... sí! pasa algo? xDDDDD ** Binding of a nonhydrolyzable ATP analog inverts the transporter to an outward-facing conformation. DNR may thus enter near an elbow helix parallel to the water/membrane interface, partitioning into the open chamber, and then translocating toward the periplasm upon ATP binding. The turnover rates of some transporters are inhibited by their substrates in a process termed trans-inhibition. Gerber et al. ( 2008 ) presented the crystal structure of a molybdate/tungstate ABC transporter (ModBC) from //Methanosarcina acetivorans// in a trans-inhibited state. The regulatory domains of the nucleotide-binding subunits proved to be in close contact, providing two oxyanion binding pockets at the shared interface. By specifically binding to these pockets, molybdate or tungstate prevent adenosine triphosphatase activity and lock the transporter in an inward-facing conformation, with the catalytic motifs of the nucleotide-binding domains separated. This allosteric effect prevents the transporter from switching between the inward-facing and the outward-facing states, thus interfering with the alternating access and release mechanism. The cystic fibrosis transmembrane conductance regulator (CFTR; 3.A.1.202.1) is an ATP-dependent chloride channel. Jordan //et al.//, 2008 compared CFTR protein sequences to those of ABCC4 proteins (the closest mammalian paralogs) to identify the evolutionary transition from transporter to channel activity. R352 in the sixth transmembrane helix interacts with D993 in TM9 to stabilize the open-channel state; D993 is absolutely conserved between CFTRs and ABCC4s. Thus CFTR channel activity evolved, at least in part, by converting the conformational changes associated with binding and hydrolysis of ATP, as are found in true ABC transporters, into an open permeation pathway by means of intraprotein interactions that stabilize the open state. The LolCDE complex of //Escherichia coli// (TC# 3.A.1.125.1) initiates the lipoprotein sorting to the outer membrane by catalysing their release from the inner membrane. LolC and/or LolE, membrane subunits, recognize lipoproteins anchored to the outer surface of the inner membrane, while LolD hydrolyses ATP on its inner surface. The ligand-bound LolCDE has been purified from the inner membrane in the absence of ATP ( Ito //et al//., 2006 ). Liganded LolCDE represents an intermediate of the release reaction and exhibits higher affinity for ATP than the unliganded form. ATP binding to LolD weakens the interaction between LolCDE and lipoproteins and causes their dissociation in a detergent solution, while lipoprotein release from membranes requires ATP hydrolysis. A single molecule of lipoprotein is found to bind per molecule of the LolCDE complex. The three structurally dissimilar constituents of the ABC uptake porters have generally arisen from a common ancestral porter system with minimal shuffling of constituents between/domain constituents is almost always the same. However the rates of sequence divergences differ drastically with the extracytoplasmic solute-binding receptors diverging most rapidly, the integral-membrane, channel-forming constituents diverging at an intermediate rate, and the cytoplasmic ATP-hydrolyzing constituents diverging most slowly. Thus, all ATP-hydrolyzing constituents are demonstrably homologous, but this is not true for the integral membrane constituents or the receptors. Nevertheless, clustering patterns are generally the same for all three types of proteins, and 3-dimensional structural data suggest that, in spite of their extensive sequence divergence, the extracytoplasmic solute-binding receptors are homologous to each other. Unlike most of the known ABC transporters, ABCC1 (TC #3.A.1.208.8) has an additional membrane-spanning domain (MSD) at its amino terminus with a domain arrangement of MSD0-MSD1-NBD1-MSD2-NBD2. The additional MSD0 domain consists of five putative transmembrane segments with a predicted extracellular amino terminus. It has a U-shaped folding with the bottom of the U-structure facing cytoplasm and both ends in extracellular space. This U-shaped amino terminus probably functions as a gate to regulate the drug transport activity of human ABCC1 ( Chen //et al//., 2006 ). Polar lipid trafficking is essential in eukaryotic cells as membranes of lipid assembly are often distinct from final destination membranes. A striking example is the biogenesis of the photosynthetic membranes (thylakoids) in plastids of plants. Lipid biosynthetic enzymes at the endoplasmic reticulum and the inner and outer plastid envelope membranes are involved. This compartmentalization requires extensive lipid trafficking. Mutants of //Arabidopsis// disrupt the incorporation of endoplasmic reticulum-derived lipid precursors into thylakoid lipids. Two proteins affected in two of these mutants, trigalactosyldiacylglycerol 1 (TGD1) and TGD2, encode the permease and substrate binding component, respectively, of a proposed lipid translocator at the inner chloroplast envelope membrane. A third protein, TGD3, a small ABC-type ATPase, energizer transport. As in the tgd1 and tgd2 mutants, triacylglycerols and trigalactolipids accumulate in a tgd3 mutant. The TGD3 protein shows basal ATPase activity and is localized inside the chloroplast beyond the inner chloroplast envelope membrane. Proteins orthologous to TGD1, -2, and -3 are predicted to be present in Gram-negative bacteria, and the respective genes are organized in operons suggesting a common biochemical role for the gene products. The Tgd1,2,3 system (TC#3.A.1.27.2) probably transfers ER-derived lipids to the thylakoid membrane ( Lu //et al//., 2007 ). It is one of the few known eukaryotic uptake systems. Some transporters have a conserved transmembrane protein and two nucleotide binding proteins similar to those of ABC transporters. However, unlike typical ABC transporters (E.I. Sun & M.H. Saier, unpublished results), they use small integral membrane proteins that are postulated to capture specific substrates. Our studies have shown that both of these integral membrane protein constituents of these systems are distantly related but homologous, and in this respect they resemble typical ABC porters. We postulate that these two transmembrane proteins comprise the pathway for transmembrane transport. Rodionov //et al.//, 2009 identified 21 families of these substrate capture proteins, each with a different specificity predicted by genome context analyses. Roughly half of the substrate capture proteins (335 cases) examined by Rodionov //et al.//, 2009 have a dedicated energizing module, but in 459 cases distributed among almost 100 gram-positive bacteria, different and unrelated substrate capture proteins share the same energy-coupling module. **¡Qué parrafada!** Vas a morir por esto, compañer@ muahahaha xDDDDDD Y yo haciendo un resumencito en español... y os lo habeis leido ya tó... tssss The shared use of energy-coupling modules was experimentally confirmed for folate, thiamine, and riboflavin transporters. Rodionov //et al.//, 2009 proposed the name energy-coupling factor transporters for the new class of putative ABC membrane transporters. These membrane proteins are homologues to ABC-2 exporters. When evidence is minimal for association with an ABC-type ATP-hydrolyzing subunit, these porters are placed in category 2.A (secondary carriers; e.g., 2.A.88). The uptake porters of the ABC superfamily and of the vitamin/small molecule transporters described by Rodionov //et al.//, 2009 are homologous to the porters in the VUT family (2.A.88). In fact, our studies indicated that all uptake porters of the ABC superfamily are of the ABC2 type. When evidence suggests that homologous membrane transport proteins of the ABC2 type couple transport to ATP hydrolysis using a homologue of the ABC-type ATPases, we list these proteins in the ABC superfamily. If there is no such evidence, (e.g., experimental evidence and the occurrence of the gene for the membrane transporter protein is in an operon that lacks the ATPase and auxillary subunit) then the porter is placed into family 2.A.88. Dassa and Bouige ( 2001 ) have devised a phylogenetic/functional classification system for ABC transporters that overlaps the TC system. In their system, several of the TC families are included in single families. These reveal the closer phylogenetic relationship of TC families as follows: Dassa and Bouige ( 2001 ) also provide the protein and domain organization of each of the various family-type proteins (see Table 1). The generalized transport reaction for ABC-type uptake systems is: Solute (out) + ATP → Solute (in) + ADP + Pi. The generalized transport reaction for ABC-type efflux systems is: Substrate (in) + ATP → Substrate (out) + ADP + Pi. Macromolecular structures of proteins in this family:[|3.A.1.1.1 - 1ANF] [|3.A.1.1.1 - 4MBP] [|3.A.1.1.1 - 3MBP] [|3.A.1.106.1 - 1JSQ] [|3.A.1.106.1 - 1PF4] [|3.A.1.13.1 - 1L7V] [|3.A.1.13.1 - 1N2Z]
 * **Table 1** ||
 * **D&B Family** || **TC Families** ||
 * **Uptake** ||
 * MOI || SulT, + PhoT + MolT + FeT + POPT + ThiT ||
 * OTCN || QAT + NitT + TauT ||
 * ISVH || VB12 + FeCT ||
 * **Export** ||
 * DPL || Lipid E + Glucan E + Prot1E + Prot2E + Pep1E + Pep2E + Pep3E + DrugE2 + DrugE3 + MDR + CFTR + Ste + TAP + HMT + MPE ||
 * OAD || CT1 + CT2 ||
 * EPD || EPP + PDR ||
 * DRA || DrugE1 + CPR ||
 * DRI || NatE ||
 * CLS || CPSE + LPSE + TAE ||

Transportadores ABC más o menos bien caracterizados (todos revisados en Swiss prot, el tema es que es dificil encontrar alguno que en los dominios tenga algo que no sea potencial o probable... de todas formas, yo no he encontrado nada mejor anotado de lo de Aida en Uniprot. Probable? Experimentalmente comprobado? || He encontrado un artículo sobre como infieren experimentalmente la topología de una proteína transportadora de manganeso:
 * = Nombre de la proteína ||= Accesion Number || Potencial?
 * = mntB de Bacillus subtilis ||= **O34338** || Dominio unión a ATP potencial. El resto sin anotaciones específicas, solo la global como transportador ABC ||
 * mntH de Lactobacillus plantarum || **Q8GH68** || Tiene el doble de aminoácidos que la nuestra...y los dominios aparecen como potenciales. ||
 * psaA de Streptococcus pneumoniae || **P0A4G3** || En realidad es una lipoproteína, que supuestamente tiene sitios de unión a Zn aunque la pone como transportador de manganeso. ||

[|MntB.pdf]

ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found on the same protein or on two different ones. Most ABC transporters function as a dimer and therefore are constituted of four domains, two ABC modules and two TMDs. ABC transporters are involved in the export or import of a wide variety of substrates ranging from small ions to macromolecules. The major function of ABC import systems is to provide essential nutrients to bacteria. They are found only in prokaryotes and their four constitutive domains are usually encoded by independent polypeptides (two ABC proteins and two TMD proteins). Prokaryotic importers require additional extracytoplasmic binding proteins (one or more per systems) for function. In contrast, export systems are involved in the extrusion of noxious substances, the export of extracellular toxins and the targeting of membrane components. They are found in all living organisms and in general the TMD is fused to the ABC module in a variety of combinations **(//est//** **//o es chungo//) ¿Porqué? En nuestro caso no creo que suponga ningún problema... ya que ni nuestro gen ni los otros con los que estamos comparando son de los que lo tienen fusionado... **. Some eukaryotic exporters encode the four domains on the same polypeptide chain [|PUBMED:9873074]. The ABC module (approximately two hundred amino acid residues) is known to bind and hydrolyse ATP, thereby coupling transport to ATP hydrolysis in a large number of biological processes. The cassette is duplicated in several subfamilies. Its primary sequence is highly conserved, displaying a typical phosphate-binding loop: Walker A, and a magnesium binding site: Walker B. Besides these two regions, three other conserved motifs are present in the ABC cassette: the switch region which contains a histidine loop, postulated to polarise the attaching water molecule for hydrolysis, the signature conserved motif (LSGGQ) specific to the ABC transporter, and the Q-motif (between Walker A and the signature), which interacts with the gamma phosphate through a water bond. The Walker A, Walker B, Q-loop and switch region form the nucleotide binding site [|PUBMED:11421269], [|PUBMED:1282354], [|PUBMED:9640644]. The 3D structure of a monomeric ABC module adopts a stubby L-shape with two distinct arms. ArmI (mainly beta-strand) contains Walker A and Walker B. The important residues for ATP hydrolysis and/or binding are located in the P-loop. The ATP-binding pocket is located at the extremity of armI. The perpendicular armII contains mostly the alpha helical subdomain with the signature motif. It only seems to be required for structural integrity of the ABC module. ArmII is in direct contact with the TMD. The hinge between armI and armII contains both the histidine loop and the Q-loop, making contact with the gamma phosphate of the ATP molecule. ATP hydrolysis leads to a conformational change that could facilitate ADP release. In the dimer the two ABC cassettes contact each other through hydrophobic interactions at the antiparallel beta-sheet of armI by a two-fold axis [|PUBMED:11988180], [|PUBMED:11470432], [|PUBMED:11402022], [|PUBMED:9872322], [|PUBMED:11080142], [|PUBMED:11532960]. The ATP-Binding Cassette (ABC) superfamily forms one of the largest of all protein families with a diversity of physiological functions [|PUBMED:9873074]. Several studies have shown that there is a correlation between the functional characterisation and the phylogenetic classification of the ABC cassette [|PUBMED:9873074], [|PUBMED:11421270]. More than 50 subfamilies have been described based on a phylogenetic and functional classification [|PUBMED:9873074], [|PUBMED:11421269], [|PUBMED:11421270]; (for further information see []). On the basis of sequence similarities a family of related ATP-binding proteins has been characterised [|PUBMED:2229036], [|PUBMED:3288195], [|PUBMED:3762694], [|PUBMED:3762695], [|PUBMED:1977073]. The proteins belonging to this family also contain one or two copies of the 'A' consensus sequence [|PUBMED:6329717] or the 'P-loop' [|PUBMED:2126155] (see ).
 * BUEN RESUMEN DE LOS TRANSPORTADORES ABC SACADO DE LA BASE DE DATOS PFAM (puede servir para puntualizar detalles en la intro y la anotación de la estructura):**

ABC transporters are characterized by two highly conserved NBDs that contain critical sequence motifs for ATP binding and hydrolysis, including the P loop present in many nucleotide-binding proteins and the ABC signature or C-loop motif [Leu- Ser-Gly-Gly-Gln (LSGGQ)] that is specific to ABC transporters
 * ALGUNAS CARACTERÍSTICAS DE LOS TRANSPORTADORES ABC (artículo Science)**.

Estos son algunos transportadores ABC bien caracterizados (contenidos en Swissprot) para ver los dominios que podemos esperar encontrar en nuestra proteína:
 * [|Escherichia coli (strain K12)] **[[image:E.coli_strain.jpg caption="E.coli_strain.jpg"]]
 * [|Escherichia coli (strain K12)] **[[image:E.coli_strain.jpg caption="E.coli_strain.jpg"]]
 * Interesante: P0A4G2 ([|Streptococcus pneumoniae])**
 * [|Streptococcus pneumoniae] (P42363)**[[image:E.coli_strain.jpg width="800" height="500" caption="E.coli_strain.jpg"]]
 * [|Streptococcus pneumoniae] (P42363)**[[image:E.coli_strain.jpg width="800" height="500" caption="E.coli_strain.jpg"]]
 * [|Streptococcus pneumoniae] (P42363)**[[image:E.coli_strain.jpg width="800" height="500" caption="E.coli_strain.jpg"]]