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Conserved domains on  [gi|1169391345|gb|ARC30735|]
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excinuclease ABC subunit UvrA [Bacillus sp. FDAARGOS_235]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 11478512)

excinuclease ABC subunit UvrA is a DNA-binding ATPase that recognizes DNA adducts in the nucleotide excision repair process catalyzed by the UvrABC excinuclease repair system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
3-942 0e+00

excinuclease ABC subunit UvrA;


:

Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 2079.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   3 MSKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEG 82
Cdd:PRK00349    1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  83 LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGR 162
Cdd:PRK00349   81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 163 KGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:PRK00349  161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 243 ---EEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYY 319
Cdd:PRK00349  241 dpeAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 320 PQLLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNEFGQVKENEILFEGVIPNIERRYRETSSDYVREQM 399
Cdd:PRK00349  321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 400 EKYMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDY 479
Cdd:PRK00349  401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 480 LTLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYL 559
Cdd:PRK00349  481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 560 LDIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAV 639
Cdd:PRK00349  561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 640 TGVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 719
Cdd:PRK00349  641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 720 EAKVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEF 799
Cdd:PRK00349  721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 800 FANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV 879
Cdd:PRK00349  801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 880 ESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEERSYTGKYLKEILNR 942
Cdd:PRK00349  881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
3-942 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 2079.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   3 MSKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEG 82
Cdd:PRK00349    1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  83 LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGR 162
Cdd:PRK00349   81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 163 KGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:PRK00349  161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 243 ---EEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYY 319
Cdd:PRK00349  241 dpeAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 320 PQLLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNEFGQVKENEILFEGVIPNIERRYRETSSDYVREQM 399
Cdd:PRK00349  321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 400 EKYMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDY 479
Cdd:PRK00349  401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 480 LTLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYL 559
Cdd:PRK00349  481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 560 LDIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAV 639
Cdd:PRK00349  561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 640 TGVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 719
Cdd:PRK00349  641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 720 EAKVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEF 799
Cdd:PRK00349  721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 800 FANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV 879
Cdd:PRK00349  801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 880 ESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEERSYTGKYLKEILNR 942
Cdd:PRK00349  881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
3-944 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 2000.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   3 MSKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEG 82
Cdd:COG0178     1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  83 LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGR 162
Cdd:COG0178    81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 163 KGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:COG0178   161 KGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 243 E-EELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYYPQ 321
Cdd:COG0178   241 EgEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 322 LLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEeKVYFRYVNeFGQVKENEILFEGVIPNIERRYRETSSDYVREQMEK 401
Cdd:COG0178   321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDE-KIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 402 YMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDYLT 481
Cdd:COG0178   399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLD 561
Cdd:COG0178   479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 562 IGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAVTG 641
Cdd:COG0178   559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 642 VSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEA 721
Cdd:COG0178   639 VSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPEA 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 722 KVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEFFA 801
Cdd:COG0178   719 KARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 802 NIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVES 881
Cdd:COG0178   799 NIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDK 878
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 882 GETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEERSYTGKYLKEILNRDK 944
Cdd:COG0178   879 GNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLEAAR 941
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
7-924 0e+00

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 1635.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   7 FIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEGLSPA 86
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  87 ISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGRKGAH 166
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 167 VKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGG--RVLID----V 240
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGllEVEFDddeeV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 241 MGEEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYYP 320
Cdd:TIGR00630 241 AESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 321 QLLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNEFGQVKENEILFEGVIPNIERRYRETSSDYVREQME 400
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 401 KYMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDYL 480
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 481 TLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLL 560
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 561 DIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAVT 640
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 641 GVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNE 720
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPE 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 721 AKVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEFF 800
Cdd:TIGR00630 721 AKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 801 ANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVE 880
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....
gi 1169391345 881 SGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQV 924
Cdd:TIGR00630 881 KGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEV 924
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
615-921 1.27e-170

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 497.14  E-value: 1.27e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 615 EIVGAKENNLKNAKMSFPLGTFVAVTGVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIG 694
Cdd:cd03271     2 TLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 695 RTPRSNPATYTGVFDDIRDVFaqtneakvrgyqkgrfsfnvkggrceacrgdgiikiemhflpdvyvpCEVCHGKRYNRE 774
Cdd:cd03271    82 RTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNRE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 775 TLEVKYKDKNISEVLGMTIEDGVEFFANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLY 854
Cdd:cd03271   115 TLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTLY 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 855 ILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTP 921
Cdd:cd03271   195 ILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
134-242 7.50e-52

UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 176.90  E-value: 7.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 134 QTVEQMVDRVLEYPERTKLQVLAPIVSGRKGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVV 213
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 214 KEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
484-573 3.09e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.87  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 484 RAAGTLSGGEAQRIRLATQIGSRlTGVLYiLDEPSIGLHQRDNDRLIRTLQEM-RDLGNTLIVVEHDEDTMMAADYLLDI 562
Cdd:NF000106  140 RAAAKYSGGMRRRLDLAASMIGR-PAVLY-LDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVI 217
                          90
                  ....*....|.
gi 1169391345 563 GPGAGIHGGQV 573
Cdd:NF000106  218 DRGRVIADGKV 228
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
3-942 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 2079.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   3 MSKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEG 82
Cdd:PRK00349    1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  83 LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGR 162
Cdd:PRK00349   81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 163 KGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:PRK00349  161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 243 ---EEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYY 319
Cdd:PRK00349  241 dpeAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 320 PQLLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNEFGQVKENEILFEGVIPNIERRYRETSSDYVREQM 399
Cdd:PRK00349  321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 400 EKYMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDY 479
Cdd:PRK00349  401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 480 LTLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYL 559
Cdd:PRK00349  481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 560 LDIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAV 639
Cdd:PRK00349  561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 640 TGVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 719
Cdd:PRK00349  641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 720 EAKVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEF 799
Cdd:PRK00349  721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 800 FANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV 879
Cdd:PRK00349  801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 880 ESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEERSYTGKYLKEILNR 942
Cdd:PRK00349  881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
3-944 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 2000.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   3 MSKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEG 82
Cdd:COG0178     1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  83 LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGR 162
Cdd:COG0178    81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 163 KGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:COG0178   161 KGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 243 E-EELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYYPQ 321
Cdd:COG0178   241 EgEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 322 LLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEeKVYFRYVNeFGQVKENEILFEGVIPNIERRYRETSSDYVREQMEK 401
Cdd:COG0178   321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDE-KIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 402 YMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDYLT 481
Cdd:COG0178   399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLD 561
Cdd:COG0178   479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 562 IGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAVTG 641
Cdd:COG0178   559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 642 VSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEA 721
Cdd:COG0178   639 VSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPEA 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 722 KVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEFFA 801
Cdd:COG0178   719 KARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 802 NIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVES 881
Cdd:COG0178   799 NIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDK 878
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 882 GETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEERSYTGKYLKEILNRDK 944
Cdd:COG0178   879 GNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLEAAR 941
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
7-924 0e+00

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 1635.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   7 FIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEGLSPA 86
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  87 ISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGRKGAH 166
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 167 VKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGG--RVLID----V 240
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGllEVEFDddeeV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 241 MGEEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNWDLTLNEHAIAPWEPTSSQYYP 320
Cdd:TIGR00630 241 AESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 321 QLLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNEFGQVKENEILFEGVIPNIERRYRETSSDYVREQME 400
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 401 KYMAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVELTEKQQKIAHLILREIQERVGFLVNVGLDYL 480
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 481 TLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLL 560
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 561 DIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRKVEIVGAKENNLKNAKMSFPLGTFVAVT 640
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 641 GVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNE 720
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPE 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 721 AKVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEFF 800
Cdd:TIGR00630 721 AKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 801 ANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVE 880
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....
gi 1169391345 881 SGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQV 924
Cdd:TIGR00630 881 KGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEV 924
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
3-945 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 689.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345    3 MSKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEG 82
Cdd:PRK00635     1 MPSLPVRLSGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   83 LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGR 162
Cdd:PRK00635    81 LSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAKD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  163 KGAhvkvLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVVKEGIASRLADSLESALKLGGGRVLIDvMG 242
Cdd:PRK00635   161 ILA----IRECLRQGFTKVRIDGEISPIYKFLTSGIPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSLH-FD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  243 EEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLELVIPNwDLTLNEHAIAPWEPTSSQYYPQL 322
Cdd:PRK00635   236 NQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLIQQ-NLSIEENCCPFAGNCSTYLYHTI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  323 LQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNE-FGQVKENEILFEGVIPNI--ERRYRETSSDYVREQM 399
Cdd:PRK00635   315 YQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVLPVRLFDGtLGKKTLTHKVWRGVLNEIgeKVRYSNKPSRYLPKGT 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  400 ekymAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSnvELTEKQQKIaHLILREIQERVGFLVNVGLDY 479
Cdd:PRK00635   395 ----SATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLS--QLPSKSLSI-EEVLQGLKSRLSILIDLGLPY 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  480 LTLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYL 559
Cdd:PRK00635   468 LTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRI 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  560 LDIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGDGRkVEIVGAKENNLKNAKMSFPLGTFVAV 639
Cdd:PRK00635   548 IDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKRTNSLGT-LTLSKATKHNLKDLTISLPLGRLTVV 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  640 TGVSGSGKSTMINEVLYKSLaQKLYKAKAKPGAHKEIKGLEhldKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 719
Cdd:PRK00635   627 TGVSGSGKSSLINDTLVPAV-EEFIEQGFCSNLSIQWGAIS---RLVHITRDLPGRSQRSIPLTYIKAFDDLRELFAEQP 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  720 EAKVRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPdvyVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEF 799
Cdd:PRK00635   703 RSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKF 779
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  800 FANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV 879
Cdd:PRK00635   780 FLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT 859
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345  880 ESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEErSYTGKYLKEILNRDKA 945
Cdd:PRK00635   860 HQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELIHLH-TPTAKALRPYLSSPQE 924
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
615-921 1.27e-170

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 497.14  E-value: 1.27e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 615 EIVGAKENNLKNAKMSFPLGTFVAVTGVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKEIKGLEHLDKVIDIDQSPIG 694
Cdd:cd03271     2 TLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 695 RTPRSNPATYTGVFDDIRDVFaqtneakvrgyqkgrfsfnvkggrceacrgdgiikiemhflpdvyvpCEVCHGKRYNRE 774
Cdd:cd03271    82 RTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNRE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 775 TLEVKYKDKNISEVLGMTIEDGVEFFANIPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLY 854
Cdd:cd03271   115 TLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTLY 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 855 ILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTP 921
Cdd:cd03271   195 ILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
8-936 3.91e-120

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 403.44  E-value: 3.91e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345    8 IVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQ-FLGQMDKPDVDTIEGLSPA 86
Cdd:PRK00635   941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQaLIKKTPLPSVDKVTGLSPV 1020
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   87 ISIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGTPICPNHGIEITSQTVEQMVDRVLEYPERTKLQVLAPIVSGRKgaH 166
Cdd:PRK00635  1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPIPKEED--L 1098
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  167 VKVLEDIKKQGYVRVRVDGEMLDVSEEITLdknkkhSIE---VVIDRIVVKEGIASRLADSLESALKLGGG-RVLIDVMG 242
Cdd:PRK00635  1099 FIYLQEKLKEGFLKLYANEQFYDLDEPLPT------SLEnpaIVIQHTKISEKNLSSLLSSLTLAFSLSSSiCLHIEYAG 1172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  243 EEELLFSEHHACPHCGFSIGELEPRMFSFNSPFGACPSCDGLGSKLEVDLElviPNWDLTLNEHAIAPWEPTSSQYYPQL 322
Cdd:PRK00635  1173 TSLSLTYRLGWQDSSGNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCSLL---PHKEKIAHYTPLSLFTLFFPNQDPKP 1249
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  323 LQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYfryvnefgqvkeNEILFEGVIpnierryRETSSDYVREqmekY 402
Cdd:PRK00635  1250 VYPLLKELGIPSIALFQELDTLSFESLCLGTQQHPGL------------NALLMEAML-------MESEEPLPPP----L 1306
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  403 MAEQACPKCKGGRLKPESLAVFVGDKTIADVtkysVQEVQEFFSNVELTEKQQKiAHLILREIQERVGFLVNVGLDYLTL 482
Cdd:PRK00635  1307 ISKTPCNQCQGLGVYTYAHCVRIHNTSLSDI----YQEDVTFLKKFLLTIHDDE-EPSIIQDLLNRLTFIDKVGLSYITL 1381
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  483 SRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLDI 562
Cdd:PRK00635  1382 GQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIHL 1461
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  563 GPGAGIHGGQVVSAGTpaeVMQDENSLTGKYLsgKEFIPVpLErrkgdgrkveiVGAKENNLKNAKMSFPLGTFVAVTGV 642
Cdd:PRK00635  1462 GPGSGPQGGYLLSTSA---LKQSQPDLHNTRS--SEETPT-LS-----------VSLSIHTIQNLNVSAPLHSLVAISGV 1524
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  643 SGSGKSTMINEVLYKSlAQKLYKakakpgahkeiKGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEAK 722
Cdd:PRK00635  1525 SGSGKTSLLLEGFYKQ-ACALIE-----------KGPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNFYASLTQAK 1592
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  723 VRGYQKGRFSFNVKGGRCEACRGDGIIKIEMHFLPDVYVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEFFAN 802
Cdd:PRK00635  1593 ALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFPF 1672
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  803 IPKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESG 882
Cdd:PRK00635  1673 LKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLG 1752
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1169391345  883 ETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASGTPEQVVKEERSYTGKYL 936
Cdd:PRK00635  1753 HSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYM 1806
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
8-161 7.45e-78

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 253.33  E-value: 7.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   8 IVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDTIEGLSPAI 87
Cdd:cd03270     1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345  88 SIDQKTTSRNPRSTVGTVTEIYDYLRLLFARIGtpicpnhgieiTSQTVEQMVDRVLEY--PERTklqvlAPIVSG 161
Cdd:cd03270    81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG-----------IRERLGFLVDVGLGYltLSRS-----APTLSG 140
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
340-577 9.28e-70

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 231.38  E-value: 9.28e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 340 DIPKDLFDKV--LYGSGEEKVYFryvnefgqvkeNEILFEGvipniERRYRETSSDYVREQMEKYmaeqacPKCKGGRLK 417
Cdd:cd03270    17 DIPRNKLVVItgVSGSGKSSLAF-----------DTIYAEG-----QRRYVESLSAYARQFLGQM------DKPDVDSIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 418 PESLAVFVGDKTIADVTKYSVQEVQEFFSNVELtekqqkiahLILRE-IQERVGFLVNVGLDYLTLSRAAGTLSGGEAQR 496
Cdd:cd03270    75 GLSPAIAIDQKTTSRNPRSTVGTVTEIYDYLRL---------LFARVgIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 497 IRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLDIGPGAGIHGGQVVSA 576
Cdd:cd03270   146 IRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQ 225

                  .
gi 1169391345 577 G 577
Cdd:cd03270   226 G 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-582 6.23e-55

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 206.40  E-value: 6.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   4 SKDFIVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVeslsayarqfLGQMDKPDVDTIEG- 82
Cdd:TIGR00630 610 NGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRLN----------GAKTVPGRYTSIEGl 679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  83 --LSPAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFAriGTPICpnhgieitsqtveqmvdrvleypertklqvlapivs 160
Cdd:TIGR00630 680 ehLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFA--ETPEA------------------------------------ 721
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 161 grkgahvkvlediKKQGYvrvrvdgemldvseeitldknkkhsievvidrivvkegiasrladslesalklGGGRvlidv 240
Cdd:TIGR00630 722 -------------KVRGY-----------------------------------------------------TPGR----- 730
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 241 mgeeellfsehhacphcgfsigeleprmFSFNSPFGACPSCDGLGS-KLEvdlelvipnwdltlnehaiapweptssqyy 319
Cdd:TIGR00630 731 ----------------------------FSFNVKGGRCEACQGDGViKIE------------------------------ 752
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 320 pqllqsvcnhygvdmdmsvkdipkDLFDKVLYgsgeekvyfryvnefgqvkeneilfegvIPnierryretssdyvreqm 399
Cdd:TIGR00630 753 ------------------------MHFLPDVY----------------------------VP------------------ 762
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 400 ekymaeqaCPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVEltekqqKIAhlilREIQervgFLVNVGLDY 479
Cdd:TIGR00630 763 --------CEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFFEAVP------SIS----RKLQ----TLCDVGLGY 820
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 480 LTLSRAAGTLSGGEAQRIRLATQIGSRLTG-VLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADY 558
Cdd:TIGR00630 821 IRLGQPATTLSGGEAQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADY 900
                         570       580
                  ....*....|....*....|....
gi 1169391345 559 LLDIGPGAGIHGGQVVSAGTPAEV 582
Cdd:TIGR00630 901 IIDLGPEGGDGGGTVVASGTPEEV 924
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
760-936 2.57e-53

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 201.39  E-value: 2.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 760 YVPCEVCHGKRYNRETLEVKYKDKNISEVLGMTIEDGVEFFAN--------------IPKIKRKLQTLVDVGLGYMKLGQ 825
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQltltpeekkiaeevLKEIRERLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 826 PATTLSGGEAQRVKLASELHRRSTGrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLG 905
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1169391345 906 PEGGDKGGQIVASGTPEQVVKEERSYTGKYL 936
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
614-919 8.08e-53

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 184.00  E-value: 8.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 614 VEIVGAKENNLKNAKMSFPLGTFVAVTGVSGSGKSTMINEVLYKSlAQKLY----KAKAKPGAHK----EIKGLEHLDKV 685
Cdd:cd03270     1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAE-GQRRYveslSAYARQFLGQmdkpDVDSIEGLSPA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 686 IDIDQSPIGRTPRSNPATYTGVFDDIRdvfaqtneakvrgyqkgrfsfnvkggrceacrgdgiikiemhflpdvyvpcev 765
Cdd:cd03270    80 IAIDQKTTSRNPRSTVGTVTEIYDYLR----------------------------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 766 chgkrynretlevkykdkniseVLgmtiedgvefFANIPkIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELH 845
Cdd:cd03270   107 ----------------------LL----------FARVG-IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIG 153
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 846 RRSTGrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASG 919
Cdd:cd03270   154 SGLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
134-242 7.50e-52

UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 176.90  E-value: 7.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 134 QTVEQMVDRVLEYPERTKLQVLAPIVSGRKGAHVKVLEDIKKQGYVRVRVDGEMLDVSEEITLDKNKKHSIEVVIDRIVV 213
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 214 KEGIASRLADSLESALKLGGGRVLIDVMG 242
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
408-579 1.23e-50

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 179.35  E-value: 1.23e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 408 CPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSNVEltekqqKIAHlilreiqeRVGFLVNVGLDYLTLSRAAG 487
Cdd:cd03271   103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENIP------KIAR--------KLQTLCDVGLGYIKLGQPAT 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 488 TLSGGEAQRIRLATQIGSRLTG-VLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLDIGPGA 566
Cdd:cd03271   169 TLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
                         170
                  ....*....|...
gi 1169391345 567 GIHGGQVVSAGTP 579
Cdd:cd03271   249 GDGGGQVVASGTP 261
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
614-919 2.91e-50

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 174.82  E-value: 2.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 614 VEIVGAKENNLKNAKMSFPLGTFVAVTGVSGSGKSTMINEVLYKSLAQKLYKAKAKPGAHKeikglehldkVIDIDQspi 693
Cdd:cd03238     1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNK----------LIFIDQ--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 694 grtprsnpatytgvfddirdvfaqtneakvrgyqkgrfsfnvkggrceacrgdgiikiemhflpdvyvpcevchgkrynr 773
Cdd:cd03238       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 774 etlevkykdknisevlgmtiedgveffanipkikrkLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTGrTL 853
Cdd:cd03238    68 ------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-TL 110
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 854 YILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQIVASG 919
Cdd:cd03238   111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
291-401 2.64e-49

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 169.58  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 291 DLELVIPNWDLTLNEHAIAPWEPTSSQYYPQLLQSVCNHYGVDMDMSVKDIPKDLFDKVLYGSGEEKVYFRYVNeFGQVK 370
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSR-GGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1169391345 371 ENEILFEGVIPNIERRYRETSSDYVREQMEK 401
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
408-938 1.25e-46

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 182.34  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  408 CPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFsnveLTEKQqkiahlilreIQERVGFLVNVGLDYLTLSRAAG 487
Cdd:PRK00635   743 CPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF----LDEPS----------IHEKIHALCSLGLDYLPLGRPLS 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  488 TLSGGEAQRIRLATQIGSRLTG-VLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLDIGPGA 566
Cdd:PRK00635   809 SLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEG 888
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  567 GIHGGQVVSAGTPAEVMQdENSLTGK----YLSGKEFIPVPLERRKGDG--RKVEIVGAKENNLKNAKMSFPLGTFVAVT 640
Cdd:PRK00635   889 GNLGGYLLASCSPEELIH-LHTPTAKalrpYLSSPQELPYLPDPSPKPPvpADITIKNAYQHNLKHIDLSLPRNALTAVT 967
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  641 GVSGSGKSTMINEVLYKS------------LAQKLYK-----------------AKAKPGAHK----------EI-KGLE 680
Cdd:PRK00635   968 GPSASGKHSLVFDILYAAgniayaelfppyIRQALIKktplpsvdkvtglspviAIEKTSASKnsnhsvasalEIsNGLE 1047
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  681 HLDKVIDIDQSPIGRTP--RSNP---------------ATYTGVFDDIRDVFAQTNEAKVRGYQK-----------GRF- 731
Cdd:PRK00635  1048 KLFARLGHPYSPLSGDAlrKITPqtiaeellthytkgyVTITSPIPKEEDLFIYLQEKLKEGFLKlyaneqfydldEPLp 1127
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  732 ------------------------------------------------------------------------SFNVKGGR 739
Cdd:PRK00635  1128 tslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlgwqdssgnlypnittpllSRDHEEGL 1207
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  740 CEACRGDGII----------KIEMH--------FLPDVYV---------------------------------------- 761
Cdd:PRK00635  1208 CPLCHGKGFIlkcsllphkeKIAHYtplslftlFFPNQDPkpvypllkelgipsialfqeldtlsfeslclgtqqhpgln 1287
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  762 -----------------------PCEVCHGKRYNRETLEVKYKDKNISEV----------LGMTIEDGvEFFANIPKIKR 808
Cdd:PRK00635  1288 allmeamlmeseeplppplisktPCNQCQGLGVYTYAHCVRIHNTSLSDIyqedvtflkkFLLTIHDD-EEPSIIQDLLN 1366
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  809 KLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELhrrSTGRT--LYILDEPTTGLHAHDIARLLEVLQRLVESGETVL 886
Cdd:PRK00635  1367 RLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKI---SSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI 1443
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1169391345  887 VIEHNLDVIKTADYIVDLGPEGGDKGGQIVasgTPEQVVKEERSYTGKYLKE 938
Cdd:PRK00635  1444 ATDRSGSLAEHADHLIHLGPGSGPQGGYLL---STSALKQSQPDLHNTRSSE 1492
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
470-577 5.42e-43

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 154.40  E-value: 5.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 470 GFLVNVGLDYLTLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHD 549
Cdd:cd03238    69 QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
                          90       100
                  ....*....|....*....|....*...
gi 1169391345 550 EDTMMAADYLLDIGPGAGIHGGQVVSAG 577
Cdd:cd03238   149 LDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
8-137 3.94e-23

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 100.00  E-value: 3.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345   8 IVVKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAegqrryveslSAYARQFLGQMDKPDVDTIEGL---S 84
Cdd:cd03271     1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169391345  85 PAISIDQKTTSRNPRSTVGTVTEIYDYLRLLFArigtPICpnHGIEITSQTVE 137
Cdd:cd03271    71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELFC----EVC--KGKRYNRETLE 117
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
10-72 5.81e-20

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 88.15  E-value: 5.81e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345  10 VKGARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQ---FLGQM 72
Cdd:cd03238     3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNkliFIDQL 68
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
463-943 1.77e-19

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 93.04  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERV-GFLVNVGLDYLtLSRAAGTLSGGEAQRIRLATQIGSRltGVLYILDEPSIGL---HQRDNDRLIRTLQemRD 538
Cdd:COG1123   117 AEARARVlELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMALALD--PDLLIADEPTTALdvtTQAEILDLLRELQ--RE 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 539 LGNTLIVVEHDEDtmMAADYLLDIgpgAGIHGGQVVSAGTPAEVMQDENSLtgkylsgkEFIPvPLERRKGDGRKVEIVG 618
Cdd:COG1123   192 RGTTVLLITHDLG--VVAEIADRV---VVMDDGRIVEDGPPEEILAAPQAL--------AAVP-RLGAARGRAAPAAAAA 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 619 AKENNLKNAKMSFPL------------------GTFVAVTGVSGSGKSTMinevlykslaqklykAKAkpgahkeIKGLE 680
Cdd:COG1123   258 EPLLEVRNLSKRYPVrgkggvravddvsltlrrGETLGLVGESGSGKSTL---------------ARL-------LLGLL 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 681 HLDK-VIDIDQSPIGRTPRSNPATYTG----VFddiRDVFAqtneakvrgyqkgrfSFNvkggrceacrgdgiikiemhf 755
Cdd:COG1123   316 RPTSgSILFDGKDLTKLSRRSLRELRRrvqmVF---QDPYS---------------SLN--------------------- 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 756 lpdvyvPcevchgkrynRETLevkykdknisevlGMTIEDGVEFFANIPKIKRK---LQTLVDVGLGYMKLGQPATTLSG 832
Cdd:COG1123   357 ------P----------RMTV-------------GDIIAEPLRLHGLLSRAERRervAELLERVGLPPDLADRYPHELSG 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 833 GEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKT-ADYIVDLgpeggd 910
Cdd:COG1123   408 GQRQRVAIARAL---ALEPKLLILDEPTSALDVSVQAQILNLLRDLQrELGLTYLFISHDLAVVRYiADRVAVM------ 478
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1169391345 911 KGGQIVASGTPEQVVKEERS-YTGKYLKEILNRD 943
Cdd:COG1123   479 YDGRIVEDGPTEEVFANPQHpYTRALLAAVPSLD 512
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
811-929 2.63e-17

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 82.00  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLGYMkLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH 890
Cdd:COG1122   117 EALELVGLEHL-ADRPPHELSGGQKQRVAIAGVL---AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTH 192
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1169391345 891 NLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:COG1122   193 DLDlVAELADRVIVL------DDGRIVADGTPREVFSDYE 226
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
403-596 3.10e-17

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 87.58  E-value: 3.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  403 MAEQACPKCKGGRLKPESLAVFVGDKTIADVTKYSVQEVQEFFSnveltekqqkiahlILREIQERVGFLVNVGLDYLTL 482
Cdd:PRK00635  1628 LEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFP--------------FLKKIQKPLQALIDNGLGYLPL 1693
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  483 SRAAGTLSGGEaqriRLATQIGSRL-----TGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAAD 557
Cdd:PRK00635  1694 GQNLSSLSLSE----KIAIKIAKFLylppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQAD 1769
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1169391345  558 YLLDIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYLSG 596
Cdd:PRK00635  1770 YLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
819-928 3.39e-17

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 85.97  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 819 GY-MKLGQPATTLSGGEAQRVKLASELHRrstGRTLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIKT 897
Cdd:COG4988   462 GLdTPLGEGGRGLSGGQAQRLALARALLR---DAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ 537
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1169391345 898 ADYIVDLgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:COG4988   538 ADRILVL------DDGRIVEQGTHEELLAKN 562
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
791-927 4.03e-17

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 81.65  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANI-----PKIKRKLQTLVD-VGLGYmKLGQPATTLSGGEAQRVKLASEL-HRRStgrtLYILDEPTTGL 863
Cdd:COG1131    88 LTVRENLRFFARLyglprKEARERIDELLElFGLTD-AADRKVGTLSGGMKQRLGLALALlHDPE----LLILDEPTSGL 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 864 HAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIVDLgpeggdKGGQIVASGTPEQVVKE 927
Cdd:COG1131   163 DPEARRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAII------DKGRIVADGTPDELKAR 221
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
811-929 7.15e-17

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 81.24  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLGYMKlGQPATTLSGGEAQRVKLAselhrrstgRTL------YILDEPTTGLhahDIA---RLLEVLQRLV-E 880
Cdd:COG1120   120 EALERTGLEHLA-DRPVDELSGGERQRVLIA---------RALaqepplLLLDEPTSHL---DLAhqlEVLELLRRLArE 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169391345 881 SGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:COG1120   187 RGRTVVMVLHDLNlAARYADRLVLL------KDGRIVAQGPPEEVLTPEL 230
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
816-929 2.71e-16

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 79.40  E-value: 2.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 816 VGLGYmKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVI 895
Cdd:cd03219   131 VGLAD-LADRPAGELSYGQQRRLEIARAL---ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV 206
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169391345 896 -KTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:cd03219   207 mSLADRVTVL------DQGRVIAEGTPDEVRNNPR 235
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
474-564 5.53e-16

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 76.24  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 474 NVGLDYLTLSRAAGTLSGGEAQRIRLATQIGSRLT--GVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDED 551
Cdd:cd03227    63 IVAAVSAELIFTRLQLSGGEKELSALALILALASLkpRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
                          90
                  ....*....|...
gi 1169391345 552 TMMAADYLLDIGP 564
Cdd:cd03227   143 LAELADKLIHIKK 155
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
830-907 8.13e-16

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 75.86  E-value: 8.13e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 830 LSGGEAQRVKLASELHRRST-GRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLGPE 907
Cdd:cd03227    78 LSGGEKELSALALILALASLkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
830-904 9.17e-16

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 75.36  E-value: 9.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 830 LSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTA-DYIVDL 904
Cdd:cd00267    81 LSGGQRQRVALARALLLN---PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
822-929 1.40e-15

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 77.57  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 822 KLGQPATTLSGGEAQRVKLAS---ELHRR--STGRtLYILDEPTTGLhahDIAR---LLEVLQRLVESGETVLVIEHNLD 893
Cdd:COG4138   119 KLSRPLTQLSGGEWQRVRLAAvllQVWPTinPEGQ-LLLLDEPMNSL---DVAQqaaLDRLLRELCQQGITVVMSSHDLN 194
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 894 -VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:COG4138   195 hTLRHADRVWLL------KQGKLVASGETAEVMTPEN 225
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
789-902 3.41e-15

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 75.58  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 789 LGMTIEDGVEF---FANIPK---IKRKLQTLVDVGLgYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTG 862
Cdd:cd03225    89 FGPTVEEEVAFgleNLGLPEeeiEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPD---ILLLDEPTAG 164
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169391345 863 LHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKT-ADYIV 902
Cdd:cd03225   165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVI 205
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
464-589 2.14e-14

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 73.52  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERV-GFLVNVGLDYLtLSRAAGTLSGGEAQRIRLAtqigsrltGVL------YILDEPSIGLHQRDNDRLIRTLQEM 536
Cdd:COG1122   110 EIRERVeEALELVGLEHL-ADRPPHELSGGQKQRVAIA--------GVLamepevLVLDEPTAGLDPRGRRELLELLKRL 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 537 RDLGNTLIVVEHD-EDTMMAADYLLdigpgaGIHGGQVVSAGTPAEVMQDENSL 589
Cdd:COG1122   181 NKEGKTVIIVTHDlDLVAELADRVI------VLDDGRIVADGTPREVFSDYELL 228
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
829-928 4.84e-14

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 72.81  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 829 TLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpe 907
Cdd:COG1121   139 ELSGGQQQRVLLARALAQDP---DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLL--- 212
                          90       100
                  ....*....|....*....|.
gi 1169391345 908 ggdkGGQIVASGTPEQVVKEE 928
Cdd:COG1121   213 ----NRGLVAHGPPEEVLTPE 229
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
828-929 5.40e-14

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 72.84  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 828 TTLSGGEAQRVKLASEL-----HRRSTGRTLyILDEPTTGLhahDIA---RLLEVLQRLVESGETVLVIEH--NLdVIKT 897
Cdd:COG4559   132 QTLSGGEQQRVQLARVLaqlwePVDGGPRWL-FLDEPTSAL---DLAhqhAVLRLARQLARRGGGVVAVLHdlNL-AAQY 206
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169391345 898 ADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:COG4559   207 ADRILLL------HQGRLVAQGTPEEVLTDEL 232
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
787-919 6.76e-14

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 71.80  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 787 EVLGMTIEDGVEFFANIPKIKRK--LQTLVDVGLGYMKLgQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH 864
Cdd:cd03235    89 DVVLMGLYGHKGLFRRLSKADKAkvDEALERVGLSELAD-RQIGELSGGQQQRVLLARAL---VQDPDLLLLDEPFAGVD 164
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 865 AHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpeggdkGGQIVASG 919
Cdd:cd03235   165 PKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLL-------NRTVVASG 213
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
810-919 6.97e-14

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 70.93  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 810 LQTLVDVGLGYMKlGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLhahDIA---RLLEVLQRLV-ESGETV 885
Cdd:cd03214    79 PQALELLGLAHLA-DRPFNELSGGERQRVLLARALAQEP---PILLLDEPTSHL---DIAhqiELLELLRRLArERGKTV 151
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169391345 886 LVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASG 919
Cdd:cd03214   152 VMVLHDLNlAARYADRVILL------KDGRIVAQG 180
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
455-565 7.23e-14

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 69.97  E-value: 7.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 455 QKIAHLILREIQERVGFLvnvgldyltlsraaGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQ 534
Cdd:cd00267    61 KDIAKLPLEELRRRIGYV--------------PQLSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLR 124
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169391345 535 EMRDLGNTLIVVEHD-EDTMMAADYLLDIGPG 565
Cdd:cd00267   125 ELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
790-924 1.25e-13

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 74.55  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANIPKIKRK------LQTLVDVGLGYMkLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGL 863
Cdd:COG1123    98 PVTVGDQIAEALENLGLSRAeararvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL---ALDPDLLIADEPTTAL 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 864 HAHDIARLLEVLQRLV-ESGETVLVIEHNLDVI-KTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG1123   174 DVTTQAEILDLLRELQrERGTTVLLITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEI 230
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
828-929 1.26e-13

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 71.73  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 828 TTLSGGEAQRVKLA---SELHRRSTGRTLYILDEPTTGL---HAHDIARLLEvlQRLVESGETVLVIEHNLDV-IKTADY 900
Cdd:PRK13548  133 PQLSGGEQQRVQLArvlAQLWEPDGPPRWLLLDEPTSALdlaHQHHVLRLAR--QLAHERGLAVIVVLHDLNLaARYADR 210
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 901 IVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:PRK13548  211 IVLL------HQGRLVADGTPAEVLTPET 233
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
825-929 2.20e-13

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 73.34  E-value: 2.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDV-IKTADYIVD 903
Cdd:PRK09536  135 RPVTSLSGGERQRVLLARALAQATP---VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVL 211
                          90       100
                  ....*....|....*....|....*.
gi 1169391345 904 LGpeggdkGGQIVASGTPEQVVKEER 929
Cdd:PRK09536  212 LA------DGRVRAAGPPADVLTADT 231
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
818-931 2.50e-13

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 74.10  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 818 LGY-MKLGQPATTLSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEH 890
Cdd:COG2274   599 MGYdTVVGEGGSNLSGGQRQRLAIA---------RALLrnprilILDEATSALDAETEAIILENLRRLLK-GRTVIIIAH 668
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169391345 891 NLDVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:COG2274   669 RLSTIRLADRIIVL------DKGRIVEDGTHEELLARKGLY 703
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
816-929 3.45e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 70.35  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 816 VGLGyMKLGQPATTLSGGEAQRVKLAS---ELHRRST--GRTLyILDEPTTGLhahDIAR---LLEVLQRLVESGETVLV 887
Cdd:PRK03695  114 LGLD-DKLGRSVNQLSGGEWQRVRLAAvvlQVWPDINpaGQLL-LLDEPMNSL---DVAQqaaLDRLLSELCQQGIAVVM 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 888 IEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:PRK03695  189 SSHDLNhTLRHADRVWLL------KQGKLLASGRRDEVLTPEN 225
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
825-928 5.54e-13

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 70.04  E-value: 5.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVD 903
Cdd:PRK11231  134 RRLTDLSGGQRQRAFLAMVLAQDTP---VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVV 210
                          90       100
                  ....*....|....*....|....*
gi 1169391345 904 LgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:PRK11231  211 L------ANGHVMAQGTPEEVMTPG 229
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
830-918 1.27e-12

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 66.68  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRrstGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpeg 908
Cdd:cd03216    83 LSVGERQMVEIARALAR---NARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVL---- 155
                          90
                  ....*....|
gi 1169391345 909 gdKGGQIVAS 918
Cdd:cd03216   156 --RDGRVVGT 163
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
463-586 2.00e-12

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 67.85  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGFLVN-VGLDYLtLSRAAGTLSGGEAQRIRLATQIGSRlTGVLyILDEPSIGLHQRDNDRLIRTLQEMRDLGN 541
Cdd:cd03219   118 REARERAEELLErVGLADL-ADRPAGELSYGQQRRLEIARALATD-PKLL-LLDEPAAGLNPEETEELAELIRELRERGI 194
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169391345 542 TLIVVEHDEDTMMA-ADYLLdigpgaGIHGGQVVSAGTPAEVMQDE 586
Cdd:cd03219   195 TVLLVEHDMDVVMSlADRVT------VLDQGRVIAEGTPDEVRNNP 234
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
822-924 3.18e-12

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 67.07  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 822 KLGQPATTLSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTAD- 899
Cdd:cd03224   125 RRKQLAGTLSGGEQQMLAIARALMSR---PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADr 201
                          90       100
                  ....*....|....*....|....*.
gi 1169391345 900 -YIVDlgpeggdkGGQIVASGTPEQV 924
Cdd:cd03224   202 aYVLE--------RGRVVLEGTAAEL 219
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
822-904 3.44e-12

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 70.01  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 822 KLGQPATTLSGGEAQRVKLASELHRrstGRTLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIKTADYI 901
Cdd:TIGR02857 451 PIGEGGAGLSGGQAQRLALARAFLR---DAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRI 526

                  ...
gi 1169391345 902 VDL 904
Cdd:TIGR02857 527 VVL 529
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
476-586 8.01e-12

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 69.02  E-value: 8.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 476 GLDYLTLSRAAGtLSGGEAQRIRLAtqigsRL---TGVLYILDEPSIGLHQRDNDRLIRTLQEMRDlGNTLIVVEHDEDT 552
Cdd:COG4988   462 GLDTPLGEGGRG-LSGGQAQRLALA-----RAllrDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLAL 534
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1169391345 553 MMAADYLLDigpgagIHGGQVVSAGTPAEVMQDE 586
Cdd:COG4988   535 LAQADRILV------LDDGRIVEQGTHEELLAKN 562
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
790-926 2.65e-11

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 65.42  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEF-FAN--IPK---IKRKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGL 863
Cdd:PRK13635   96 GATVQDDVAFgLENigVPReemVERVDQALRQVGMEDFLNREPHR-LSGGQKQRVAIAGVLALQPD---IIILDEATSML 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 864 HAHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPEQVVK 926
Cdd:PRK13635  172 DPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQADRVIVM------NKGEILEEGTPEEIFK 229
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
790-929 5.99e-11

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 63.72  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANIPKIKRK-LQTLVDVGLGYMKLG----QPATTLSGGEAQRVKLASEL-HRRStgrtLYILDEPTTGL 863
Cdd:COG4555    88 RLTVRENIRYFAELYGLFDEeLKKRIEELIELLGLEefldRRVGELSTGMKKKVALARALvHDPK----VLLLDEPTNGL 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 864 HAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:COG4555   164 DVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVIL------HKGKVVAQGSLDELREEIG 224
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
482-587 7.15e-11

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 63.41  E-value: 7.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGEAQRIRLAT---QIGSRLT--GVLYILDEPSIGL---HQRDNDRLIRtlqEMRDLGNTLIVVEHD-EDT 552
Cdd:PRK03695  120 LGRSVNQLSGGEWQRVRLAAvvlQVWPDINpaGQLLLLDEPMNSLdvaQQAALDRLLS---ELCQQGIAVVMSSHDlNHT 196
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 553 MMAAD--YLLdigpgagiHGGQVVSAGTPAEVMQDEN 587
Cdd:PRK03695  197 LRHADrvWLL--------KQGKLLASGRRDEVLTPEN 225
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
813-916 8.69e-11

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 62.27  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 813 LVDVGLGYMKLGQPaTTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL 892
Cdd:cd03226   111 LKDLDLYALKERHP-LSLSGGQKQRLAIAAAL---LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY 186
                          90       100
                  ....*....|....*....|....*
gi 1169391345 893 DVI-KTADYIVDLgpeggdKGGQIV 916
Cdd:cd03226   187 EFLaKVCDRVLLL------ANGAIV 205
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
790-906 9.03e-11

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 62.53  E-value: 9.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANIPKIKRKLQTLVD----VGLGYMKLGQPATTLSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHA 865
Cdd:COG4619    87 GGTVRDNLPFPFQLRERKFDRERALEllerLGLPPDILDKPVERLSGGERQRLALIRALLLQ---PDVLLLDEPTSALDP 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 866 HDIARLLEVLQRLV-ESGETVLVIEHNLDVIKT-ADYIVDLGP 906
Cdd:COG4619   164 ENTRRVEELLREYLaEEGRAVLWVSHDPEQIERvADRVLTLEA 206
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
798-931 9.20e-11

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 62.94  E-value: 9.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 798 EFFANIPKikrKLQTLVdvglgymklGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQR 877
Cdd:cd03249   120 DFIMSLPD---GYDTLV---------GERGSQLSGGQKQRIAIARALLRNPK---ILLLDEATSALDAESEKLVQEALDR 184
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 878 LVEsGETVLVIEHNLDVIKTADYIVDLGpeggdkGGQIVASGTPEQVVKEERSY 931
Cdd:cd03249   185 AMK-GRTTIVIAHRLSTIRNADLIAVLQ------NGQVVEQGTHDELMAQKGVY 231
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
823-931 1.56e-10

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 64.80  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLhahDI---ARLLEVLQRLVEsGETVLVIEHNLD 893
Cdd:COG1132   470 VGERGVNLSGGQRQRIAIA---------RALLkdppilILDEATSAL---DTeteALIQEALERLMK-GRTTIVIAHRLS 536
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169391345 894 VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:COG1132   537 TIRNADRILVL------DDGRIVEQGTHEELLARGGLY 568
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
791-926 1.86e-10

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 62.13  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFF----ANIPK--IKRK-LQTLVDVGLGYMKLGQPATtLSGGEAQRVKLAselhrrstgRTL-----YIL-D 857
Cdd:cd03261    92 LTVFENVAFPlrehTRLSEeeIREIvLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALA---------RALaldpeLLLyD 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 858 EPTTGLH---AHDIARLLEVLQRlvESGETVLVIEHNLD-VIKTADYIVDLGpeggdkGGQIVASGTPEQVVK 926
Cdd:cd03261   162 EPTAGLDpiaSGVIDDLIRSLKK--ELGLTSIMVTHDLDtAFAIADRIAVLY------DGKIVAEGTPEELRA 226
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
464-560 2.38e-10

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 61.33  E-value: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERVGFLVNVGLDYLTLSRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTL 543
Cdd:cd03225   110 EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTI 187
                          90
                  ....*....|....*...
gi 1169391345 544 IVVEHDEDTMMA-ADYLL 560
Cdd:cd03225   188 IIVTHDLDLLLElADRVI 205
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
484-586 4.09e-10

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 61.57  E-value: 4.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 484 RAAGTLSGGEAQRIRLATQIGSRLTGVLyiLDEPSIGL---HQRDndrLIRTLQEMRDLGNTLIVVEHD-EDTMMAADYL 559
Cdd:PRK11231  134 RRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlNQASRYCDHL 208
                          90       100
                  ....*....|....*....|....*..
gi 1169391345 560 ldigpgAGIHGGQVVSAGTPAEVMQDE 586
Cdd:PRK11231  209 ------VVLANGHVMAQGTPEEVMTPG 229
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
482-585 4.35e-10

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 60.53  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGEAQriRLAtqIGSRLTG--VLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMA-AD- 557
Cdd:cd03224   126 RKQLAGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADr 201
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 558 -YLLDigpgagihGGQVVSAGTPAEVMQD 585
Cdd:cd03224   202 aYVLE--------RGRVVLEGTAAELLAD 222
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
791-917 5.27e-10

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 60.44  E-value: 5.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPKIKRK---LQTLVDVGLGYmKLGQPATTLSGGEAQRVKLAselhrrstgRTLY-----IL-DE 858
Cdd:COG1136   101 LTALENVALpllLAGVSRKERReraRELLERVGLGD-RLDHRPSQLSGGQQQRVAIA---------RALVnrpklILaDE 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 859 PTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVA 917
Cdd:COG1136   171 PTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRL------RDGRIVS 224
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
475-586 6.15e-10

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 60.96  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 475 VGLDYLTlSRAAGTLSGGEAQRIRLATQIG--SRLtgvlYILDEPSIGL---HQRDNDRLIRTLQEMRDLgnTLIVVEHD 549
Cdd:PRK10575  135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAqdSRC----LLLDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHD 207
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1169391345 550 EDtmMAA---DYLLdigpgaGIHGGQVVSAGTPAEVMQDE 586
Cdd:PRK10575  208 IN--MAArycDYLV------ALRGGEMIAQGTPAELMRGE 239
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
823-927 6.23e-10

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 62.84  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIK 896
Cdd:COG4618   461 IGEGGARLSGGQRQRIGLA---------RALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA 531
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1169391345 897 TADYIVDLgpeggdKGGQIVASGTPEQVVKE 927
Cdd:COG4618   532 AVDKLLVL------RDGRVQAFGPRDEVLAR 556
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
817-928 6.25e-10

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 62.94  E-value: 6.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 817 GLGYMkLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIK 896
Cdd:PRK11174  474 GLDTP-IGDQAAGLSVGQAQRLALARALLQPCQ---LLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLA 548
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169391345 897 TADYIVDLgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:PRK11174  549 QWDQIWVM------QDGQIVQQGDYAELSQAG 574
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
461-903 7.63e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 62.52  E-value: 7.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 461 ILREIQERVGfLVNVgldyltLSRAAGTLSGGEAQRIRLATQIgSRLTGVlYILDEPSIGL--HQRDN-DRLIRTLQEmr 537
Cdd:PRK13409  192 KLDEVVERLG-LENI------LDRDISELSGGELQRVAIAAAL-LRDADF-YFFDEPTSYLdiRQRLNvARLIRELAE-- 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 538 dlGNTLIVVEHDedtMMAADYLLDIgpgagIHggqvVSAGTPaevmqdensltGKYlsgkefipvplerrkgdGrkveIV 617
Cdd:PRK13409  261 --GKYVLVVEHD---LAVLDYLADN-----VH----IAYGEP-----------GAY-----------------G----VV 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 618 gakennlknakmSFPLGTFVAvtgvsgsgkstmINEVLYKSLAqklykakakpgahkeikglehlDKVIDIDQSPIG--- 694
Cdd:PRK13409  295 ------------SKPKGVRVG------------INEYLKGYLP----------------------EENMRIRPEPIEfee 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 695 RTPRSNPATYTGV-FDDIrdvfaqtneakVRGYqkGRFSFNVKGGrcEACRGD--------GI-----IKIemhfLPDVY 760
Cdd:PRK13409  329 RPPRDESERETLVeYPDL-----------TKKL--GDFSLEVEGG--EIYEGEvigivgpnGIgkttfAKL----LAGVL 389
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 761 VPCEvchGKRYnrETLEVKYKDKNISEVLGMTIEDgveFFANIPKIKRK--LQTLVDVGLGYMKL-GQPATTLSGGEAQR 837
Cdd:PRK13409  390 KPDE---GEVD--PELKISYKPQYIKPDYDGTVED---LLRSITDDLGSsyYKSEIIKPLQLERLlDKNVKDLSGGELQR 461
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 838 VKLASELHRRStgrTLYILDEPTtglhAHdiarlLEVLQRLV----------ESGETVLVIEHNLDVIktaDYIVD 903
Cdd:PRK13409  462 VAIAACLSRDA---DLYLLDEPS----AH-----LDVEQRLAvakairriaeEREATALVVDHDIYMI---DYISD 522
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
784-928 7.71e-10

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 62.35  E-value: 7.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 784 NIseVLGMtiEDGVEFFANIPKIKRKLQTL-------VDvglgymkLGQPATTLSGGEAQRVKLASELHRRStgRTLyIL 856
Cdd:COG3845   100 NI--VLGL--EPTKGGRLDRKAARARIRELserygldVD-------PDAKVEDLSVGEQQRVEILKALYRGA--RIL-IL 165
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 857 DEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:COG3845   166 DEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVL------RRGKVVGTVDTAETSEEE 232
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
830-904 8.50e-10

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 58.77  E-value: 8.50e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 830 LSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDL 904
Cdd:cd03246    97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
790-939 8.84e-10

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 60.52  E-value: 8.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEF---FANIP--KIKRKLQT-LVDVGL-GYMKlgQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTG 862
Cdd:TIGR04520  92 GATVEDDVAFgleNLGVPreEMRKRVDEaLKLVGMeDFRD--REPHLLSGGQKQRVAIAGVLAMRP---DIIILDEATSM 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 863 LHAHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERSytgkyLKEI 939
Cdd:TIGR04520 167 LDPKGRKEVLETIRKLNkEEGITVISITHDMEEAVLADRVIVM------NKGKIVAEGTPREIFSQVEL-----LKEI 233
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
488-587 9.95e-10

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 60.17  E-value: 9.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 488 TLSGGEAQRIRLA---TQIGSRL--TGVLyILDEPSIGL---HQrdndrlIRTLQEMRDL----GNTLIVVEHDEDtmMA 555
Cdd:PRK13548  134 QLSGGEQQRVQLArvlAQLWEPDgpPRWL-LLDEPTSALdlaHQ------HHVLRLARQLaherGLAVIVVLHDLN--LA 204
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 556 ADY-----LLdigpgagiHGGQVVSAGTPAEVMQDEN 587
Cdd:PRK13548  205 ARYadrivLL--------HQGRLVADGTPAEVLTPET 233
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
813-906 1.16e-09

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 59.03  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 813 LVDVGLGYMkLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL 892
Cdd:COG4133   116 LEAVGLAGL-ADLPVRQLSAGQKRRVALARLL---LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
                          90
                  ....*....|....
gi 1169391345 893 DVIkTADYIVDLGP 906
Cdd:COG4133   192 LEL-AAARVLDLGD 204
cbiO PRK13644
energy-coupling factor transporter ATPase;
786-927 1.17e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 60.39  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 786 SEVLGMTIEDGVEFFAN---IPKI---KRKLQTLVDVGLGYMKLGQPaTTLSGGEAQRVKLASELhrrSTGRTLYILDEP 859
Cdd:PRK13644   88 TQFVGRTVEEDLAFGPEnlcLPPIeirKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGIL---TMEPECLIFDEV 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 860 TTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLgpeggDKgGQIVASGTPEQVVKE 927
Cdd:PRK13644  164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM-----DR-GKIVLEGEPENVLSD 225
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
791-924 1.20e-09

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 59.61  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF----FANIPK--IKRK-LQTLVDVGL-GYMKLgQPATtLSGGEAQRVKLAselhrrstgRTL-----YIL- 856
Cdd:COG1127    97 LTVFENVAFplreHTDLSEaeIRELvLEKLELVGLpGAADK-MPSE-LSGGMRKRVALA---------RALaldpeILLy 165
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 857 DEPTTGLH---AHDIARLLEVLQRlvESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG1127   166 DEPTAGLDpitSAVIDELIRELRD--ELGLTSVVVTHDLDsAFAIADRVAVL------ADGKIIAEGTPEEL 229
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
830-904 1.23e-09

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 58.16  E-value: 1.23e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIKTADYIVDL 904
Cdd:cd03228    97 LSGGQRQRIAIARALLRDP---PILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVL 167
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
795-902 1.89e-09

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 57.79  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 795 DGVEFFANIPKIKRKLqtlvdvglGYMkLGQPAT----------TLSGGEAQRVKLASEL-HRRStgrtLYILDEPTTGL 863
Cdd:cd03230    60 LGKDIKKEPEEVKRRI--------GYL-PEEPSLyenltvrenlKLSGGMKQRLALAQALlHDPE----LLILDEPTSGL 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1169391345 864 HAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIV 902
Cdd:cd03230   127 DPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
829-928 2.13e-09

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 59.42  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 829 TLSGGEAQRVKLASELHRRStgRTLyILDEPTTGLhahDIARLLEVL---QRLV-ESGETVLVIEHNLDVI-KTADYIVD 903
Cdd:PRK10575  147 SLSGGERQRAWIAMLVAQDS--RCL-LLDEPTSAL---DIAHQVDVLalvHRLSqERGLTVIAVLHDINMAaRYCDYLVA 220
                          90       100
                  ....*....|....*....|....*
gi 1169391345 904 LgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:PRK10575  221 L------RGGEMIAQGTPAELMRGE 239
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
792-932 2.36e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 59.86  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 792 TIEDGVEF---FANIPKIKRKLQT---LVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHA 865
Cdd:PRK13631  133 TIEKDIMFgpvALGVKKSEAKKLAkfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE---ILIFDEPTAGLDP 209
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 866 HDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpeggDKgGQIVASGTPEQVVKEERSYT 932
Cdd:PRK13631  210 KGEHEMMQLILDAKANNKTVFVITHTMEhVLEVADEVIVM-----DK-GKILKTGTPYEIFTDQHIIN 271
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
455-577 2.57e-09

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 57.45  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 455 QKIAHLILREIQERVGF----LVNVGLDYLtLSRAAGTLSGGEAQRIRLATQIGsRLTGVLyILDEPSIGL---HQRDND 527
Cdd:cd03214    61 KDLASLSPKELARKIAYvpqaLELLGLAHL-ADRPFNELSGGERQRVLLARALA-QEPPIL-LLDEPTSHLdiaHQIELL 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 528 RLIRTLqeMRDLGNTLIVVEHDED-TMMAADYLLdigpgaGIHGGQVVSAG 577
Cdd:cd03214   138 ELLRRL--ARERGKTVVMVLHDLNlAARYADRVI------LLKDGRIVAQG 180
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
794-931 2.60e-09

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 58.78  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 794 EDGVEFFANIPKIKRKLQTLVDvglGY-MKLGQPATTLSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLHAH 866
Cdd:cd03253   104 DEEVIEAAKAAQIHDKIMRFPD---GYdTIVGERGLKLSGGEKQRVAIA---------RAILknppilLLDEATSALDTH 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 867 DIARLLEVLQRLVEsGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:cd03253   172 TEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVL------KDGRIVERGTHEELLAKGGLY 229
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
463-589 3.07e-09

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 58.28  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGF-LVNVGLdyltlsRAA-----GTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLH---QRDNDRLIRTL 533
Cdd:cd03261   111 EEIREIVLEkLEAVGL------RGAedlypAELSGGMKKRVALARALA--LDPELLLYDEPTAGLDpiaSGVIDDLIRSL 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 534 QEMrdLGNTLIVVEHDEDT-MMAADYLldigpgAGIHGGQVVSAGTPAEVMQDENSL 589
Cdd:cd03261   183 KKE--LGLTSIMVTHDLDTaFAIADRI------AVLYDGKIVAEGTPEELRASDDPL 231
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
791-915 3.74e-09

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 57.88  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVE---FFANIPK--IKRKLQTLVD-VGLGYmKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH 864
Cdd:cd03255    97 LTALENVElplLLAGVPKkeRRERAEELLErVGLGD-RLNHYPSELSGGQQQRVAIARAL---ANDPKIILADEPTGNLD 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 865 AHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQI 915
Cdd:cd03255   173 SETGKEVMELLRELNkEAGTTIVVVTHDPELAEYADRIIEL------RDGKI 218
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
805-919 4.35e-09

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 57.90  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRL-VESGE 883
Cdd:cd03257   121 RKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL---ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGL 197
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 884 TVLVIEHNLDVIK-TADYIVDLgpeggdKGGQIVASG 919
Cdd:cd03257   198 TLLFITHDLGVVAkIADRVAVM------YAGKIVEEG 228
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
484-583 5.27e-09

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 59.47  E-value: 5.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 484 RAAGTLSGGEAQRIRLATQIgSRLTGVLyILDEPSIGLhqrDNDRLIRTLQEMRDL---GNTLIVVEHDEDtmMAADYLL 560
Cdd:PRK09536  135 RPVTSLSGGERQRVLLARAL-AQATPVL-LLDEPTASL---DINHQVRTLELVRRLvddGKTAVAAIHDLD--LAARYCD 207
                          90       100
                  ....*....|....*....|...
gi 1169391345 561 DIgpgAGIHGGQVVSAGTPAEVM 583
Cdd:PRK09536  208 EL---VLLADGRVRAAGPPADVL 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
475-549 7.12e-09

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 56.77  E-value: 7.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 475 VGLDYLtLSRAAGTLSGGEAQRIRLATQIGSRltGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHD 549
Cdd:cd03235   120 VGLSEL-ADRQIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHD 191
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
813-932 7.78e-09

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 57.51  E-value: 7.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 813 LVDVGLGYMKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRL-VESGETVLVIEHN 891
Cdd:COG1124   122 LEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL---ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHD 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 892 LDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQVVKEERS-YT 932
Cdd:COG1124   199 LAVVAHlCDRVAVM------QNGRIVEELTVADLLAGPKHpYT 235
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
806-929 1.08e-08

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 57.02  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVDVGLGYMKlGQPATTLSGGEAQRVKLAselhrRS--TGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGE 883
Cdd:COG1119   120 RERARELLELLGLAHLA-DRPFGTLSQGEQRRVLIA-----RAlvKDPELLILDEPTAGLDLGARELLLALLDKLAAEGA 193
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 884 TVLV-IEHNLDVIktadyivdlgPEGGD-----KGGQIVASGTPEQVVKEER 929
Cdd:COG1119   194 PTLVlVTHHVEEI----------PPGIThvlllKDGRVVAAGPKEEVLTSEN 235
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
825-933 2.55e-08

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 55.63  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTAD--YI 901
Cdd:cd03218   129 SKASSLSGGERRRVEIARAL---ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVrETLSITDraYI 205
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169391345 902 VdlgpeggdKGGQIVASGTPEQVVKEE---RSYTG 933
Cdd:cd03218   206 I--------YEGKVLAEGTPEEIAANElvrKVYLG 232
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
819-932 3.99e-08

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 54.93  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 819 GY-MKLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIKT 897
Cdd:cd03251   127 GYdTVIGERGVKLSGGQRQRIAIARALLKDP---PILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN 202
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169391345 898 ADYIVDLgpeggDKgGQIVASGTPEQVVKEERSYT 932
Cdd:cd03251   203 ADRIVVL-----ED-GKIVERGTHEELLAQGGVYA 231
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
791-926 4.67e-08

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 56.98  E-value: 4.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFA------NIPKIKRKL---QTLVDVGLG---YMKLGQPATT--LSGGEAQRVKLASELhrrSTGRTLYIL 856
Cdd:TIGR00955 114 LTVREHLMFQAhlrmprRVTKKEKRErvdEVLQALGLRkcaNTRIGVPGRVkgLSGGERKRLAFASEL---LTDPPLLFC 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 857 DEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH--NLDVIKTADYIVDLGpeggdkGGQIVASGTPEQVVK 926
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFELFDKIILMA------EGRVAYLGSPDQAVP 256
cbiO PRK13640
energy-coupling factor transporter ATPase;
789-928 4.70e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 55.58  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 789 LGMTIEDGVEF-FANIPKIKRKLQTLV-----DVGLGYMKLGQPATtLSGGEAQRVKLASELhrrSTGRTLYILDEPTTG 862
Cdd:PRK13640   98 VGATVGDDVAFgLENRAVPRPEMIKIVrdvlaDVGMLDYIDSEPAN-LSGGQKQRVAIAGIL---AVEPKIIILDESTSM 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 863 LHAHDIARLLEVLQRLVESGE-TVLVIEHNLDVIKTADYIVDLgpeggDKgGQIVASGTPEQVVKEE 928
Cdd:PRK13640  174 LDPAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVL-----DD-GKLLAQGSPVEIFSKV 234
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
825-924 4.86e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 55.40  E-value: 4.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELHRRStgRTLyILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIVD 903
Cdd:PRK13638  132 QPIQCLSHGQKKRVAIAGALVLQA--RYL-LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYV 208
                          90       100
                  ....*....|....*....|.
gi 1169391345 904 LgpeggdKGGQIVASGTPEQV 924
Cdd:PRK13638  209 L------RQGQILTHGAPGEV 223
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
826-906 5.26e-08

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 54.75  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 826 PATTLSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKT-ADYIVDL 904
Cdd:COG4778   149 PPATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDV 225

                  ..
gi 1169391345 905 GP 906
Cdd:COG4778   226 TP 227
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
824-928 5.34e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 55.38  E-value: 5.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 824 GQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGL---HAHDIARLLEVLQRlvESGETVLVIEHNLD-VIKTAD 899
Cdd:PRK10253  138 DQSVDTLSGGQRQRAWIAMVLAQETA---IMLLDEPTTWLdisHQIDLLELLSELNR--EKGYTLAAVLHDLNqACRYAS 212
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 900 YIVDLgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:PRK10253  213 HLIAL------REGKIVAQGAPKEIVTAE 235
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
791-905 5.37e-08

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 54.04  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANIPKIKRKLQTLVDVGL-GYMKLgqPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIA 869
Cdd:cd03231    88 LSVLENLRFWHADHSDEQVEEALARVGLnGFEDR--PVAQLSAGQQRRVALARLL---LSGRPLWILDEPTTALDKAGVA 162
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 870 RLLEVL-QRLVESGETVLVIEHNLDVIKTADYIVDLG 905
Cdd:cd03231   163 RFAEAMaGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
790-910 5.44e-08

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 54.72  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANI----PKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELhrRSTGRTLyILDEPTTGLHA 865
Cdd:PRK10247   94 GDTVYDNLIFPWQIrnqqPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVL-LLDEITSALDE 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169391345 866 HDIARLLEVLQRLV-ESGETVLVIEHNLDVIKTADYIVDLGPEGGD 910
Cdd:PRK10247  171 SNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINHADKVITLQPHAGE 216
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
823-904 5.61e-08

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 56.72  E-value: 5.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLhahDI---ARLLEVLQRLVESGETVLVIEHNLDVIktaD 899
Cdd:COG1245   206 LDRDISELSGGELQRVAIAAALLRDAD---FYFFDEPSSYL---DIyqrLNVARLIRELAEEGKYVLVVEHDLAIL---D 276

                  ....*
gi 1169391345 900 YIVDL 904
Cdd:COG1245   277 YLADY 281
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
768-958 6.90e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 55.00  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 768 GKRYNRETLevKYKDKNI--------SEVLGMTIEDGVEFFANIPKIKR-KLQTLVD-----VGlgyMK--LGQPATTLS 831
Cdd:PRK13632   70 GITISKENL--KEIRKKIgiifqnpdNQFIGATVEDDIAFGLENKKVPPkKMKDIIDdlakkVG---MEdyLDKEPQNLS 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 832 GGEAQRVKLASELhrrSTGRTLYILDEPTTGLHA---HDIARLLEVLQRlvESGETVLVIEHNLDVIKTADYIVDLgpeg 908
Cdd:PRK13632  145 GGQKQRVAIASVL---ALNPEIIIFDESTSMLDPkgkREIKKIMVDLRK--TRKKTLISITHDMDEAILADKVIVF---- 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 909 gdKGGQIVASGTPEQVVKEersytgkylKEILNRDK------ARMKEKIKEVELSQ 958
Cdd:PRK13632  216 --SEGKLIAQGKPKEILNN---------KEILEKAKidspfiYKLSKKLKGIDPTY 260
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
406-927 6.90e-08

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 56.35  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 406 QACPKCkGGRLKPESLAVFVGDKTI-ADVTKYSVQEVQEFFSnveLTEKQQKIAHLI--LREIQERVGFLVNVGLDYLT- 481
Cdd:TIGR03269  80 EPCPVC-GGTLEPEEVDFWNLSDKLrRRIRKRIAIMLQRTFA---LYGDDTVLDNVLeaLEEIGYEGKEAVGRAVDLIEm 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 ------LSRAAGTLSGGEAQRIRLATQIGSRltGVLYILDEPSIGLHQRDNDRLIRTLQE-MRDLGNTLIVVEHDEDTMM 554
Cdd:TIGR03269 156 vqlshrITHIARDLSGGEKQRVVLARQLAKE--PFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIE 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 555 -AADYLLdigpgaGIHGGQVVSAGTPAEVMQdensltgKYLSGKEfipvPLERRKGDGRKVEIVgaKENNLKNAKMSFPL 633
Cdd:TIGR03269 234 dLSDKAI------WLENGEIKEEGTPDEVVA-------VFMEGVS----EVEKECEVEVGEPII--KVRNVSKRYISVDR 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 634 GTFVAVTGVSGSGKSTMINEVLYKSlaqklykakakpGAHKEIkglehLDKVIdidqspIGRTPRSNPATYTGVFDDIRD 713
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTS------------GAGKTT-----LSKII------AGVLEPTSGEVNVRVGDEWVD 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 714 VfaqtneAKVRGYQKGRfsfnvkggrceACRGDGIIKIEMHFLPdvyvpcevchgkryNRETLEvkykdkNISEVLGMTI 793
Cdd:TIGR03269 352 M------TKPGPDGRGR-----------AKRYIGILHQEYDLYP--------------HRTVLD------NLTEAIGLEL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 794 EDgvEFfanipKIKRKLQTLVDVGLGYMK----LGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIA 869
Cdd:TIGR03269 395 PD--EL-----ARMKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEP---RIVILDEPTGTMDPITKV 464
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 870 RLLE-VLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKE 927
Cdd:TIGR03269 465 DVTHsILKAREEMEQTFIIVSHDMDfVLDVCDRAALM------RDGKIVKIGDPEEIVEE 518
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
791-931 7.72e-08

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 54.26  E-value: 7.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF-----FANIPKIKRK-LQTLVDVGLGYMkLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH 864
Cdd:cd03299    86 MTVYKNIAYglkkrKVDKKEIERKvLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARAL---VVNPKILLLDEPFSALD 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 865 AHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:cd03299   162 VRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWAlADKVAIM------LNGKLIQVGKPEEVFKKPKNE 224
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
475-595 8.00e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 55.03  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 475 VGLDYLTLSRAAGTLSGGEAQRIRLAtqigsrltGVL------YILDEPSIGLHQRDNDRLIRTLQEM-RDLGNTLIVVE 547
Cdd:PRK13634  132 VGLPEELLARSPFELSGGQMRRVAIA--------GVLamepevLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVT 203
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1169391345 548 HD-EDTMMAADYLLDIgpgagiHGGQVVSAGTPAEVMQDENSLTGKYLS 595
Cdd:PRK13634  204 HSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLD 246
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
791-925 1.08e-07

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 54.19  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPKIKRK---LQTLVDVGLGYMKLGQPaTTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH 864
Cdd:cd03294   117 RTVLENVAFgleVQGVPRAEREeraAEALELVGLEGWEHKYP-DELSGGMQQRVGLARAL---AVDPDILLMDEAFSALD 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 865 AHDIARLLEVLQRLV-ESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVV 925
Cdd:cd03294   193 PLIRREMQDELLRLQaELQKTIVFITHDLDeALRLGDRIAIM------KDGRLVQVGTPEEIL 249
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
791-922 1.16e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 55.89  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPKIKRKLQT---LVDVGLGYMKLGQPATtLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH 864
Cdd:PRK10535  101 LTAAQNVEVpavYAGLERKQRLLRAqelLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARAL---MNGGQVILADEPTGALD 176
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 865 AHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPE 922
Cdd:PRK10535  177 SHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI------RDGEIVRNPPAQ 228
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
487-584 1.18e-07

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 55.52  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 487 GTLSGGEAQRIRLAtqigsR-LTG--VLYILDEPSIGLhqrDND---RLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLL 560
Cdd:COG4618   466 ARLSGGQRQRIGLA-----RaLYGdpRLVVLDEPNSNL---DDEgeaALAAAIRALKARGATVVVITHRPSLLAAVDKLL 537
                          90       100
                  ....*....|....*....|....
gi 1169391345 561 DigpgagIHGGQVVSAGTPAEVMQ 584
Cdd:COG4618   538 V------LRDGRVQAFGPRDEVLA 555
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
823-931 1.33e-07

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 53.64  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRRStgRTLyILDEPTTGLHAHDIARLLEVLQRLVeSGETVLVIEHNLDVIKTADYIV 902
Cdd:cd03252   132 VGEQGAGLSGGQRQRIAIARALIHNP--RIL-IFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRII 207
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 903 DLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:cd03252   208 VM------EKGRIVEQGSHDELLAENGLY 230
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
805-919 1.40e-07

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 53.13  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKLQTLVD-VGLGYmKLGQPATTLSGGEAQRVKLASEL-HRRStgrtLYILDEPTTGLHAHDIARLLEVLQRLVESG 882
Cdd:COG2884   113 EIRRRVREVLDlVGLSD-KAKALPHELSGGEQQRVAIARALvNRPE----LLLADEPTGNLDPETSWEIMELLEEINRRG 187
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169391345 883 ETVLVIEHNLDVIKTADY-IVDLgpeggdKGGQIVASG 919
Cdd:COG2884   188 TTVLIATHDLELVDRMPKrVLEL------EDGRLVRDE 219
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
830-928 1.48e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 54.04  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVES-GETVLVIEHNLDVI-KTADYIVDLgpe 907
Cdd:PRK13652  138 LSGGEKKRVAIAGVI---AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVpEMADYIYVM--- 211
                          90       100
                  ....*....|....*....|.
gi 1169391345 908 ggDKgGQIVASGTPEQVVKEE 928
Cdd:PRK13652  212 --DK-GRIVAYGTVEEIFLQP 229
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
791-924 1.51e-07

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 53.96  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFA---NIPK--IKRKLQTLVD-VGLGYmKLGQPATTLSGGEAQRVKLASEL-HRRStgrtLYILDEPTTGL 863
Cdd:COG4152    86 MKVGEQLVYLArlkGLSKaeAKRRADEWLErLGLGD-RANKKVEELSKGNQQKVQLIAALlHDPE----LLILDEPFSGL 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 864 hahD-IAR--LLEVLQRLVESGETVLVIEHNLDVI-KTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG4152   161 ---DpVNVelLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVII------NKGRKVLSGSVDEI 216
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
791-919 1.63e-07

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 52.99  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANIPKIKRKL--QTLVDVGLGYMKlGQPATTLSGGEAQRVKLA-SELHRRStgrtLYILDEPTTGLHAHD 867
Cdd:cd03268    87 LTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIAlALLGNPD----LLILDEPTNGLDPDG 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 868 IARLLEVLQRLVESGETVLVIEHNL-DVIKTADYIVDLGpeggdkGGQIVASG 919
Cdd:cd03268   162 IKELRELILSLRDQGITVLISSHLLsEIQKVADRIGIIN------KGKLIEEG 208
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
444-607 1.66e-07

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 53.55  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 444 FFSNV----ELTEKQQKIAHLILREiqervgflvnVGLDYLtLSRAAGTLSGGEAQRIRLAtqigsR--------Ltgvl 511
Cdd:COG1119   105 FFDSIglyrEPTDEQRERARELLEL----------LGLAHL-ADRPFGTLSQGEQRRVLIA-----RalvkdpelL---- 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 512 yILDEPSIGL--HQRdnDRLIRTLQEMRDLGN-TLIVVEHdedtmmaadYLLDIGPG----AGIHGGQVVSAGTPAEVMQ 584
Cdd:COG1119   165 -ILDEPTAGLdlGAR--ELLLALLDKLAAEGApTLVLVTH---------HVEEIPPGithvLLLKDGRVVAAGPKEEVLT 232
                         170       180
                  ....*....|....*....|...
gi 1169391345 585 DENsltgkyLSGKEFIPVPLERR 607
Cdd:COG1119   233 SEN------LSEAFGLPVEVERR 249
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
774-903 1.68e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 55.18  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 774 ETLEVKYK--------DKNISEVLGMTIEDGVE---FFANIpkIKR-KLQTLVDvglgymklgQPATTLSGGEAQRVKLA 841
Cdd:COG1245   399 EDLKISYKpqyispdyDGTVEEFLRSANTDDFGssyYKTEI--IKPlGLEKLLD---------KNVKDLSGGELQRVAIA 467
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 842 SELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVES-GETVLVIEHNLDVIktaDYIVD 903
Cdd:COG1245   468 ACLSRDA---DLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLI---DYISD 524
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
471-590 1.72e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 54.09  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 471 FLVNVGLDYLTLSRAAGTLSGGEAQRIRLAtqigsrltGVL------YILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLI 544
Cdd:PRK13631  159 YLNKMGLDDSYLERSPFGLSGGQKRRVAIA--------GILaiqpeiLIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF 230
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1169391345 545 VVEHD-EDTMMAADYLLDIGPgagihgGQVVSAGTPAEVMQDENSLT 590
Cdd:PRK13631  231 VITHTmEHVLEVADEVIVMDK------GKILKTGTPYEIFTDQHIIN 271
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
830-890 1.85e-07

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 52.55  E-value: 1.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH 890
Cdd:cd03213   112 LSGGERKRVSIALEL---VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
807-924 1.88e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 53.87  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 807 KRKLQTLVD-VGLGYMKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHA---HDIARLLEVLQRlvESG 882
Cdd:PRK13634  122 KQKAREMIElVGLPEELLARSPFELSGGQMRRVAIAGVL---AMEPEVLVLDEPTAGLDPkgrKEMMEMFYKLHK--EKG 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 883 ETVLVIEHNL-DVIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:PRK13634  197 LTTVLVTHSMeDAARYADQIVVM------HKGTVFLQGTPREI 233
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
791-924 1.95e-07

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 52.95  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANIPKIKRK--LQTLVDVGL------GYMKLGQPATTLSGGEAQRVKLAselhrrstgRTLYI------L 856
Cdd:cd03260    95 GSIYDNVAYGLRLHGIKLKeeLDERVEEALrkaalwDEVKDRLHALGLSGGQQQRLCLA---------RALANepevllL 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 857 DEPTTGLHAHDIARLLEVLQRLVESgETVLVIEHNL-DVIKTADYIVDLGPeggdkgGQIVASGTPEQV 924
Cdd:cd03260   166 DEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMqQAARVADRTAFLLN------GRLVEFGPTEQI 227
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
823-934 2.06e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 52.97  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQpatTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHN----LDVIKTA 898
Cdd:PRK10895  134 MGQ---SLSGGERRRVEIARAL---AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvretLAVCERA 207
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169391345 899 dYIVdlgpeggdKGGQIVASGTPEQVVKEE---RSYTGK 934
Cdd:PRK10895  208 -YIV--------SQGHLIAHGTPTEILQDEhvkRVYLGE 237
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
828-924 2.27e-07

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 53.01  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 828 TTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLDVIKT-ADYIVDLg 905
Cdd:PRK11701  150 TTFSGGMQQRLQIARNL---VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAVARLlAHRLLVM- 225
                          90
                  ....*....|....*....
gi 1169391345 906 peggdKGGQIVASGTPEQV 924
Cdd:PRK11701  226 -----KQGRVVESGLTDQV 239
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
823-903 2.46e-07

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 52.80  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGE-TVLVIEHnlDVIkTADYI 901
Cdd:cd03237   109 LDREVPELSGGELQRVAIAACLSKDA---DIYLLDEPSAYLDVEQRLMASKVIRRFAENNEkTAFVVEH--DII-MIDYL 182

                  ..
gi 1169391345 902 VD 903
Cdd:cd03237   183 AD 184
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
487-584 2.47e-07

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 54.84  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 487 GTLSGGEAQRIRLAtqigsRltgVLY------ILDEPSIGLHQRDNDRLIRTLQEMRDlGNTLIVVEHDEDTMMAAD--Y 558
Cdd:COG2274   610 SNLSGGQRQRLAIA-----R---ALLrnprilILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADriI 680
                          90       100
                  ....*....|....*....|....*.
gi 1169391345 559 LLDigpgagihGGQVVSAGTPAEVMQ 584
Cdd:COG2274   681 VLD--------KGRIVEDGTHEELLA 698
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
445-582 2.71e-07

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 52.72  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 445 FSNVELTEKQQKIAHL-ILREIQERVGFLvnvGLDYLtLSRAAGTLSGGEAQRIRLATQIgsRLTGVLYILDEPSIGLHQ 523
Cdd:cd03299    89 YKNIAYGLKKRKVDKKeIERKVLEIAEML---GIDHL-LNRKPETLSGGEQQRVAIARAL--VVNPKILLLDEPFSALDV 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 524 RDNDRLIRTLQEMRD-LGNTLIVVEHD-EDTMMAADYLldigpgAGIHGGQVVSAGTPAEV 582
Cdd:cd03299   163 RTKEKLREELKKIRKeFGVTVLHVTHDfEEAWALADKV------AIMLNGKLIQVGKPEEV 217
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
462-562 2.74e-07

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 54.21  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 462 LREIQERVGFLVNV-----GLDYLTLSRAAGtLSGGEAQRIRLAtQIGSRLTGVLyILDEPSIGLHQRDNDRLIRTLQEM 536
Cdd:TIGR02857 428 IREALERAGLDEFVaalpqGLDTPIGEGGAG-LSGGQAQRLALA-RAFLRDAPLL-LLDEPTAHLDAETEAEVLEALRAL 504
                          90       100
                  ....*....|....*....|....*.
gi 1169391345 537 RDlGNTLIVVEHDEDTMMAADYLLDI 562
Cdd:TIGR02857 505 AQ-GRTVLLVTHRLALAALADRIVVL 529
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
805-938 2.93e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.17  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKLQTLVDVGLGYMKlgQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGET 884
Cdd:PRK13651  143 KRAAKYIELVGLDESYLQ--RSPFELSGGQKRRVALAGIL---AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT 217
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 885 VLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEErsytgKYLKE 938
Cdd:PRK13651  218 IILVTHDLDnVLEWTKRTIFF------KDGKIIKDGDTYDILSDN-----KFLIE 261
cbiO PRK13646
energy-coupling factor transporter ATPase;
775-927 3.03e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 53.24  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 775 TLEVKYKDKNISEV---LGMTI--------EDGVE---------FFANIPKIK-RKLQTLVDVGLGYMKLGQPATTLSGG 833
Cdd:PRK13646   70 TITHKTKDKYIRPVrkrIGMVFqfpesqlfEDTVEreiifgpknFKMNLDEVKnYAHRLLMDLGFSRDVMSQSPFQMSGG 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 834 EAQRVKLASELhrrSTGRTLYILDEPTTGLHA---HDIARLLEVLQrlVESGETVLVIEHNL-DVIKTADYIVDLgpegg 909
Cdd:PRK13646  150 QMRKIAIVSIL---AMNPDIIVLDEPTAGLDPqskRQVMRLLKSLQ--TDENKTIILVSHDMnEVARYADEVIVM----- 219
                         170
                  ....*....|....*...
gi 1169391345 910 dKGGQIVASGTPEQVVKE 927
Cdd:PRK13646  220 -KEGSIVSQTSPKELFKD 236
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
807-943 3.04e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 53.16  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 807 KRKLQTLVDVGL-GYMKlgQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETV 885
Cdd:PRK13639  116 KRVKEALKAVGMeGFEN--KPPHHLSGGQKKRVAIAGILAMKPE---IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITI 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 886 lviehnldVIKTADyiVDLGPEGGDK-----GGQIVASGTPEQVVKEERSYTGKYLK--------EILNRD 943
Cdd:PRK13639  191 --------IISTHD--VDLVPVYADKvyvmsDGKIIKEGTPKEVFSDIETIRKANLRlprvahliEILNKE 251
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
823-924 3.26e-07

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 53.57  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRRStgRTLyILDEPTTGLhahDIAR---LLEVLQRLVESGET-VLVIEHNLD-VIKT 897
Cdd:COG4148   127 LDRRPATLSGGERQRVAIGRALLSSP--RLL-LMDEPLAAL---DLARkaeILPYLERLRDELDIpILYVSHSLDeVARL 200
                          90       100
                  ....*....|....*....|....*..
gi 1169391345 898 ADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG4148   201 ADHVVLL------EQGRVVASGPLAEV 221
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
787-930 3.29e-07

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 52.66  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 787 EVLGMTIEDGVEffanipkikRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAH 866
Cdd:PRK10619  119 QVLGLSKQEARE---------RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPE 186
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 867 DIARLLEVLQRLVESGETVLVIEHNLDVIK-TADYIVDLgpeggdKGGQIVASGTPEQVVKEERS 930
Cdd:PRK10619  187 LVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFL------HQGKIEEEGAPEQLFGNPQS 245
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
823-926 3.60e-07

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 53.87  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRRStgRTLyILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYI 901
Cdd:COG1129   134 PDTPVGDLSVAQQQLVEIARALSRDA--RVL-ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDeVFEIADRV 210
                          90       100       110
                  ....*....|....*....|....*....|
gi 1169391345 902 VDLgpeggdKGGQIVASG-----TPEQVVK 926
Cdd:COG1129   211 TVL------RDGRLVGTGpvaelTEDELVR 234
cbiO PRK13637
energy-coupling factor transporter ATPase;
464-589 3.85e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 52.74  E-value: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERVGFLVN-VGLDYLTLS-RAAGTLSGGEAQRIRLATQIGSRLTgVLyILDEPSIGLHQRDNDRLIRTLQEMRD-LG 540
Cdd:PRK13637  118 EIENRVKRAMNiVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPK-IL-ILDEPTAGLDPKGRDEILNKIKELHKeYN 195
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169391345 541 NTLIVVEHD-EDTMMAADYLLdigpgaGIHGGQVVSAGTPAEVMQDENSL 589
Cdd:PRK13637  196 MTIILVSHSmEDVAKLADRII------VMNKGKCELQGTPREVFKEVETL 239
cbiO PRK13643
energy-coupling factor transporter ATPase;
830-927 4.24e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 52.81  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTADYIVDLgpeg 908
Cdd:PRK13643  145 LSGGQMRRVAIAGIL---AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMdDVADYADYVYLL---- 217
                          90
                  ....*....|....*....
gi 1169391345 909 gdKGGQIVASGTPEQVVKE 927
Cdd:PRK13643  218 --EKGHIISCGTPSDVFQE 234
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
830-903 4.38e-07

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 51.03  E-value: 4.38e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGE-TVLVIEHNLDVIktaDYIVD 903
Cdd:cd03222    72 LSGGELQRVAIAAALLRNA---TFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL---DYLSD 140
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
805-932 4.49e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 52.45  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKL-QTLVDVGLgYMKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGE 883
Cdd:PRK13648  118 EMHRRVsEALKQVDM-LERADYEPNALSGGQKQRVAIAGVL---ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN 193
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169391345 884 -TVLVIEHNLDVIKTADYIVDLGPeggdkgGQIVASGTPEQVVKEERSYT 932
Cdd:PRK13648  194 iTIISITHDLSEAMEADHVIVMNK------GTVYKEGTPTEIFDHAEELT 237
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
823-904 4.78e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 53.66  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRrstGRTLYILDEPTTGLhahDIA---RLLEVLQRLVEsGETVLVIEHNLDVIktaD 899
Cdd:PRK13409  206 LDRDISELSGGELQRVAIAAALLR---DADFYFFDEPTSYL---DIRqrlNVARLIRELAE-GKYVLVVEHDLAVL---D 275

                  ....*
gi 1169391345 900 YIVDL 904
Cdd:PRK13409  276 YLADN 280
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
830-920 4.89e-07

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 53.67  E-value: 4.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLAselhrrstgRTL------YILDEPTTGLHAHDIARLLEVLQRlVESGETVLVIEHNLDVIKTADYIVD 903
Cdd:COG5265   495 LSGGEKQRVAIA---------RTLlknppiLIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVDADEILV 564
                          90
                  ....*....|....*..
gi 1169391345 904 LgpeggdKGGQIVASGT 920
Cdd:COG5265   565 L------EAGRIVERGT 575
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
604-931 5.63e-07

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 53.48  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 604 LERRKGDgRKVEIV-----GAKENNLKNAKMSFPLGTFVAVTGVSGSGKSTMINevlyksLAQKLYkakakpgahkeikg 678
Cdd:PRK11176  335 IERAKGD-IEFRNVtftypGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN------LLTRFY-------------- 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 679 lehldkviDIDQSPIgrtprsnpaTYTGVfdDIRDvFAQTNeakVRGyQKGRFSFNVkggrceacrgdgiikiemHFLPD 758
Cdd:PRK11176  394 --------DIDEGEI---------LLDGH--DLRD-YTLAS---LRN-QVALVSQNV------------------HLFND 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 759 VyvpceVCHGKRYNRETlevKYKDKNISEVLGMTIedGVEFfanIPKIKRKLQTLVdvglgymklGQPATTLSGGEAQRV 838
Cdd:PRK11176  432 T-----IANNIAYARTE---QYSREQIEEAARMAY--AMDF---INKMDNGLDTVI---------GENGVLLSGGQRQRI 489
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 839 KLASELHRRSTgrtLYILDEPTTGLHA---HDIARLLEVLQRlvesGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQI 915
Cdd:PRK11176  490 AIARALLRDSP---ILILDEATSALDTeseRAIQAALDELQK----NRTSLVIAHRLSTIEKADEILVV------EDGEI 556
                         330
                  ....*....|....*.
gi 1169391345 916 VASGTPEQVVKEERSY 931
Cdd:PRK11176  557 VERGTHAELLAQNGVY 572
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
807-930 5.88e-07

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 51.68  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 807 KRKLQTLVD-VGLGYMKLGQPATtLSGGEAQRVKLASELHRRstgRTLYILDEPTTGLhahDIARLLEVLQrLV-----E 880
Cdd:COG3840   107 RAQVEQALErVGLAGLLDRLPGQ-LSGGQRQRVALARCLVRK---RPILLLDEPFSAL---DPALRQEMLD-LVdelcrE 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 881 SGETVLVIEHNL-DVIKTAD---YIVDlgpeggdkgGQIVASGTPEQVVKEERS 930
Cdd:COG3840   179 RGLTVLMVTHDPeDAARIADrvlLVAD---------GRIAADGPTAALLDGEPP 223
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
791-891 7.20e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 51.03  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANI--PKIKRKLQTLVDVGLGYMkLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDI 868
Cdd:PRK13539   88 LTVAENLEFWAAFlgGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLL---VSNRPIWILDEPTAALDAAAV 163
                          90       100
                  ....*....|....*....|...
gi 1169391345 869 ARLLEVLQRLVESGETVLVIEHN 891
Cdd:PRK13539  164 ALFAELIRAHLAQGGIVIAATHI 186
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
417-582 8.22e-07

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 51.19  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 417 KPESLAVFVGDKtiaDVTKYSVQEVQ--------------EFFSNVELTEKQQKIAHLILR-EIQERVGFLVN-VGLDYL 480
Cdd:cd03296    53 RPDSGTILFGGE---DATDVPVQERNvgfvfqhyalfrhmTVFDNVAFGLRVKPRSERPPEaEIRAKVHELLKlVQLDWL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 481 TlSRAAGTLSGGEAQRIRLATQIGSRlTGVLyILDEPSIGLHQRDNDRLIRTLQEMRD-LGNTLIVVEHD-EDTMMAADY 558
Cdd:cd03296   130 A-DRYPAQLSGGQRQRVALARALAVE-PKVL-LLDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDqEEALEVADR 206
                         170       180
                  ....*....|....*....|....
gi 1169391345 559 LLDigpgagIHGGQVVSAGTPAEV 582
Cdd:cd03296   207 VVV------MNKGRIEQVGTPDEV 224
cbiO PRK13649
energy-coupling factor transporter ATPase;
830-927 1.07e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 51.28  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTADYIVDLgpeg 908
Cdd:PRK13649  146 LSGGQMRRVAIAGILAMEPK---ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVL---- 218
                          90
                  ....*....|....*....
gi 1169391345 909 gdKGGQIVASGTPEQVVKE 927
Cdd:PRK13649  219 --EKGKLVLSGKPKDIFQD 235
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
830-903 1.09e-06

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 51.21  E-value: 1.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLhahDIARLL---EVLQRLVESGETVLVIEHNLDVIktaDYIVD 903
Cdd:cd03236   140 LSGGELQRVAIAAALARDAD---FYFFDEPSSYL---DIKQRLnaaRLIRELAEDDNYVLVVEHDLAVL---DYLSD 207
hmuV PRK13547
heme ABC transporter ATP-binding protein;
823-928 1.10e-06

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 51.37  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASEL------HRRSTGRTLYILDEPTTGL---HAHdiaRLLEVLQRLVESGET-VLVIEHNL 892
Cdd:PRK13547  139 VGRDVTTLSGGELARVQFARVLaqlwppHDAAQPPRYLLLDEPTAALdlaHQH---RLLDTVRRLARDWNLgVLAIVHDP 215
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 893 DV-IKTADYIVDLGpeggdkGGQIVASGTPEQVVKEE 928
Cdd:PRK13547  216 NLaARHADRIAMLA------DGAIVAHGAPADVLTPA 246
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
806-924 1.29e-06

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 50.64  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVDVGLGYmKLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLH---AHDIARLLEVLQRlvESG 882
Cdd:cd03256   122 KQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQP---KLILADEPVASLDpasSRQVMDLLKRINR--EEG 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 883 ETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:cd03256   196 ITVIVSLHQVDLAREyADRIVGL------KDGRIVFDGPPAEL 232
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
773-923 1.52e-06

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 50.06  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 773 RETLEVKykdKNISEVL-------GMTIEDGVEFFANIPKIKR-KLQTLVDVGLGYMKLGQ----PATTLSGGEAQRVKL 840
Cdd:cd03265    66 REPREVR---RRIGIVFqdlsvddELTGWENLYIHARLYGVPGaERRERIDELLDFVGLLEaadrLVKTYSGGMRRRLEI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 841 A-SELHRRStgrtLYILDEPTTGLHAHDIARLLEVLQRLVES-GETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVA 917
Cdd:cd03265   143 ArSLVHRPE----VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEeAEQLCDRVAII------DHGRIIA 212

                  ....*.
gi 1169391345 918 SGTPEQ 923
Cdd:cd03265   213 EGTPEE 218
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
471-565 1.55e-06

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 49.81  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 471 FLVNVGLDYLTLSRAAGTLSGGEAQRIRL--ATQIGSRltgVLyILDEPSIGLHQRDNDRLIRTLQE-MRDLGNTLIVVE 547
Cdd:COG4619   113 LLERLGLPPDILDKPVERLSGGERQRLALirALLLQPD---VL-LLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVS 188
                          90
                  ....*....|....*....
gi 1169391345 548 HDED-TMMAADYLLDIGPG 565
Cdd:COG4619   189 HDPEqIERVADRVLTLEAG 207
cbiO PRK13650
energy-coupling factor transporter ATPase;
789-924 1.92e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 50.50  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 789 LGMTIEDGVEF-FAN--IPK---IKRKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRStgrTLYILDEPTTG 862
Cdd:PRK13650   95 VGATVEDDVAFgLENkgIPHeemKERVNEALELVGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRP---KIIILDEATSM 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 863 LHAHDIARLLEVLQRLVES-GETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:PRK13650  171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVM------KNGQVESTSTPREL 227
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
414-568 1.93e-06

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 49.56  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 414 GRLKPESLAVFVGDKTIADVTK-----YSVQEV--QEFFSNV--ELT-------EKQQKIAHlILREIqervgflvnvGL 477
Cdd:cd03226    48 GLIKESSGSILLNGKPIKAKERrksigYVMQDVdyQLFTDSVreELLlglkeldAGNEQAET-VLKDL----------DL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 478 DYLTLsRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDR---LIRTLQEMrdlGNTLIVVEHDED-TM 553
Cdd:cd03226   117 YALKE-RHPLSLSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERvgeLIRELAAQ---GKAVIVITHDYEfLA 190
                         170
                  ....*....|....*
gi 1169391345 554 MAADYLLDIGPGAGI 568
Cdd:cd03226   191 KVCDRVLLLANGAIV 205
PTZ00243 PTZ00243
ABC transporter; Provisional
788-919 1.94e-06

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.09  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  788 VLGMTIEDGVEFF-----ANIPKIKRKLQTLVDVGL--GYMK--LGQPATTLSGGEAQRVKLASELHrrsTGRTLYILDE 858
Cdd:PTZ00243   732 IMNATVRGNILFFdeedaARLADAVRVSQLEADLAQlgGGLEteIGEKGVNLSGGQKARVSLARAVY---ANRDVYLLDD 808
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345  859 PTTGLHAHDIARLLE--VLQRLveSGETVLVIEHNLDVIKTADYIVDLGpeggdkGGQIVASG 919
Cdd:PTZ00243   809 PLSALDAHVGERVVEecFLGAL--AGKTRVLATHQVHVVPRADYVVALG------DGRVEFSG 863
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
790-924 2.02e-06

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 50.88  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANIPKIKRKLqtlvdvGLGYMkLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPttgLHAHDIA 869
Cdd:TIGR02142  99 GMKRARPSERRISFERVIELL------GIGHL-LGRLPGRLSGGEKQRVAIGRAL---LSSPRLLLMDEP---LAALDDP 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 870 RLLEV---LQRL-VESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:TIGR02142 166 RKYEIlpyLERLhAEFGIPILYVSHSLQeVLRLADRVVVL------EDGRVAAAGPIAEV 219
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
828-904 2.07e-06

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 49.39  E-value: 2.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 828 TTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLE-VLQRLVESGETVLVIEHNLDVIKTADYIVDL 904
Cdd:cd03250   126 INLSGGQKQRISLARAVYSDA---DIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVL 200
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
810-931 2.24e-06

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 51.36  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 810 LQTLVDVGLGY---------MKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVE 880
Cdd:PRK11160  447 IEVLQQVGLEKlleddkglnAWLGEGGRQLSGGEQRRLGIARALLHDAP---LLLLDEPTEGLDAETERQILELLAEHAQ 523
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 881 sGETVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:PRK11160  524 -NKTVLMITHRLTGLEQFDRICVM------DNGQIIEQGTHQELLAQQGRY 567
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
824-931 2.45e-06

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 51.65  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 824 GQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAhdiarllEVLQRLVES----GETVLVIEHNLDVIKTAD 899
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKP---RVLILDEATSALDA-------ECEQLLQESrsraSRTVLLIAHRLSTVERAD 681
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169391345 900 YIVDLgpeggdKGGQIVASGTPEQVVKEERSY 931
Cdd:TIGR00958 682 QILVL------KKGSVVEMGTHKQLMEDQGCY 707
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
830-902 2.59e-06

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 48.72  E-value: 2.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVE-SGETVLVIEHNLDVIKT-ADYIV 902
Cdd:cd03229   101 LSGGQQQRVALARALAMDP---DVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARlADRVV 172
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
830-924 2.71e-06

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 51.22  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLhahDI---ARLLEVLQRLV-ESGETVLVIEHNLDVI-KTADYIVDL 904
Cdd:COG4172   157 LSGGQRQRVMIAMAL---ANEPDLLIADEPTTAL---DVtvqAQILDLLKDLQrELGMALLLITHDLGVVrRFADRVAVM 230
                          90       100
                  ....*....|....*....|
gi 1169391345 905 gpeggdKGGQIVASGTPEQV 924
Cdd:COG4172   231 ------RQGEIVEQGPTAEL 244
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
807-897 2.85e-06

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 49.33  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 807 KRKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVL 886
Cdd:cd03292   115 KRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT---ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVV 190
                          90
                  ....*....|.
gi 1169391345 887 VIEHNLDVIKT 897
Cdd:cd03292   191 VATHAKELVDT 201
cbiO PRK13645
energy-coupling factor transporter ATPase;
445-590 3.38e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.01  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 445 FSNVELTEKQQKIahliLREIQERVGfLVNVGLDYLtlSRAAGTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQR 524
Cdd:PRK13645  114 FGPVNLGENKQEA----YKKVPELLK-LVQLPEDYV--KRSPFELSGGQKRRVALAGIIA--MDGNTLVLDEPTGGLDPK 184
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 525 DNDRLIRTLQEM-RDLGNTLIVVEHDEDTMM-AADYLLDIgpgagiHGGQVVSAGTPAEVMQDENSLT 590
Cdd:PRK13645  185 GEEDFINLFERLnKEYKKRIIMVTHNMDQVLrIADEVIVM------HEGKVISIGSPFEIFSNQELLT 246
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
476-587 3.49e-06

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 51.00  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 476 GLDYLTLSRAAGtLSGGEAQRIRLATQIGSrlTGVLYILDEPSIGLHQRDNDRLIRTLQEMRdLGNTLIVVEHDEDTMMA 555
Cdd:PRK11174  474 GLDTPIGDQAAG-LSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQ 549
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1169391345 556 ADYLLdigpgaGIHGGQVVSAGTPAEVMQDEN 587
Cdd:PRK11174  550 WDQIW------VMQDGQIVQQGDYAELSQAGG 575
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
830-919 3.57e-06

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 48.46  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIKTADYIVDLgpegg 909
Cdd:cd03247    99 FSGGERQRLALARILLQDAP---IVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFL----- 169
                          90
                  ....*....|
gi 1169391345 910 dKGGQIVASG 919
Cdd:cd03247   170 -ENGKIIMQG 178
cbiO PRK13642
energy-coupling factor transporter ATPase;
786-924 3.73e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 49.71  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 786 SEVLGMTIEDGVEF---FANIPK---IKRKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRSTgrtLYILDEP 859
Cdd:PRK13642   92 NQFVGATVEDDVAFgmeNQGIPReemIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPE---IIILDES 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 860 TTGLHAHDIARLLEVLQRLVESGE-TVLVIEHNLDVIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:PRK13642  168 TSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVM------KAGEIIKEAAPSEL 227
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
12-55 4.30e-06

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 47.74  E-value: 4.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1169391345  12 GARAHNLKNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQR 55
Cdd:cd03227     5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
830-933 4.52e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 49.50  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTADYIVDLgpeg 908
Cdd:PRK15056  143 LSGGQKKRVFLARAIAQQGQ---VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMV---- 215
                          90       100
                  ....*....|....*....|....*...
gi 1169391345 909 gdkGGQIVASGTPEQVVKE---ERSYTG 933
Cdd:PRK15056  216 ---KGTVLASGPTETTFTAenlELAFSG 240
cbiO PRK13645
energy-coupling factor transporter ATPase;
794-924 4.55e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 49.62  E-value: 4.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 794 EDGVEFFANIPKikrkLQTLVDVGLGYMKlgQPATTLSGGEAQRVKLASELhrRSTGRTLyILDEPTTGLHAHDIARLLE 873
Cdd:PRK13645  121 ENKQEAYKKVPE----LLKLVQLPEDYVK--RSPFELSGGQKRRVALAGII--AMDGNTL-VLDEPTGGLDPKGEEDFIN 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 874 VLQRL-VESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:PRK13645  192 LFERLnKEYKKRIIMVTHNMDqVLRIADEVIVM------HEGKVISIGSPFEI 238
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
18-44 4.69e-06

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 48.23  E-value: 4.69e-06
                          10        20
                  ....*....|....*....|....*..
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:cd03250    21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
cbiO PRK13643
energy-coupling factor transporter ATPase;
414-594 5.47e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 49.35  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 414 GRLKPESLAVFVGDKTIADVTKY-SVQEVQEFFSNVELTEKQQKIAHLILREIQ-------------ERVGF--LVNVGL 477
Cdd:PRK13643   54 GLLQPTEGKVTVGDIVVSSTSKQkEIKPVRKKVGVVFQFPESQLFEETVLKDVAfgpqnfgipkekaEKIAAekLEMVGL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 478 DYLTLSRAAGTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEH-DEDTMMAA 556
Cdd:PRK13643  134 ADEFWEKSPFELSGGQMRRVAIAGILA--MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYA 211
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1169391345 557 DYLLDigpgagIHGGQVVSAGTPAEVMQDENSLTGKYL 594
Cdd:PRK13643  212 DYVYL------LEKGHIISCGTPSDVFQEVDFLKAHEL 243
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
463-617 5.59e-06

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 49.71  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGFLVN-VGLDYLtLSRAAGTLSGGEAQRIRLAtqigsR-LT---GVLyILDEPSIGLhqrDND------RLIR 531
Cdd:COG3842   110 AEIRARVAELLElVGLEGL-ADRYPHQLSGGQQQRVALA-----RaLApepRVL-LLDEPLSAL---DAKlreemrEELR 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 532 TLQemRDLGNTLIVVEHD-EDTMMAADYLldigpgAGIHGGQVVSAGTPAEVMQ------------DENSLTGKYLSGKE 598
Cdd:COG3842   180 RLQ--RELGITFIYVTHDqEEALALADRI------AVMNDGRIEQVGTPEEIYErpatrfvadfigEANLLPGTVLGDEG 251
                         170       180
                  ....*....|....*....|....*..
gi 1169391345 599 --------FIPVPLERRKGDGRKVEIV 617
Cdd:COG3842   252 ggvrtggrTLEVPADAGLAAGGPVTVA 278
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
830-890 6.18e-06

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 48.42  E-value: 6.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH 890
Cdd:cd03234   144 ISGGERRRVSIAVQL---LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
484-564 6.31e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 49.11  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 484 RAAGTLSGGEAQRIRLATQIGSRltGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHD--------EDTMMA 555
Cdd:PRK15056  138 RQIGELSGGQKKRVFLARAIAQQ--GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNlgsvtefcDYTVMV 215

                  ....*....
gi 1169391345 556 ADYLLDIGP 564
Cdd:PRK15056  216 KGTVLASGP 224
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
463-551 6.74e-06

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 48.17  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERV-GFLVNVGLDYLTLSRAAGtLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRDLGN 541
Cdd:cd03292   111 REIRKRVpAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGT 187
                          90
                  ....*....|
gi 1169391345 542 TLIVVEHDED 551
Cdd:cd03292   188 TVVVATHAKE 197
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
790-861 7.03e-06

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 46.87  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANIPKIKRK---------LQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPT 860
Cdd:pfam00005  73 RLTVRENLRLGLLLKGLSKRekdaraeeaLEKLGLGDLADRPVGERPGTLSGGQRQRVAIARAL---LTKPKLLLLDEPT 149

                  .
gi 1169391345 861 T 861
Cdd:pfam00005 150 A 150
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
791-944 7.69e-06

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 48.45  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVeffANIPKI---------KRKLQTLVDVGLGYMKLGQ--PATtLSGGEAQRVKLASELhrrSTGRTLYILDEP 859
Cdd:cd03295    90 MTVEENI---ALVPKLlkwpkekirERADELLALVGLDPAEFADryPHE-LSGGQQQRVGVARAL---AADPPLLLMDEP 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 860 TTGLHAHDIARLLEVLQRL-VESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVkeeRSYTGKYLK 937
Cdd:cd03295   163 FGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEIL---RSPANDFVA 233

                  ....*..
gi 1169391345 938 EILNRDK 944
Cdd:cd03295   234 EFVGADR 240
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
824-909 7.70e-06

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 48.24  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 824 GQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLhahDIARLLEVLQRLVESGE--TVLVIEHNLDVIKTADYI 901
Cdd:cd03248   145 GEKGSQLSGGQKQRVAIARALIRNP---QVLILDEATSAL---DAESEQQVQQALYDWPErrTVLVIAHRLSTVERADQI 218

                  ....*...
gi 1169391345 902 VDLgpEGG 909
Cdd:cd03248   219 LVL--DGG 224
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
773-895 8.11e-06

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 48.93  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 773 RETLEVKYKDKNISevLGMTIEDGVEFFANIPKIKRKLQTLVDVGLGYmklGQPATTLSGGEAQRVKLASELHRRSTGRT 852
Cdd:pfam13304 185 LQRLVRGLKLADLN--LSDLGEGIEKSLLVDDRLRERGLILLENGGGG---ELPAFELSDGTKRLLALLAALLSALPKGG 259
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 853 LYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVI 895
Cdd:pfam13304 260 LLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
791-919 9.65e-06

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 47.75  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANIPKIKR-----KLQTLVDVgLGyMK--LGQPATTLSGGEAQRVKLASEL-HRRStgrtLYILDEPTTG 862
Cdd:cd03266    93 LTARENLEYFAGLYGLKGdeltaRLEELADR-LG-MEelLDRRVGGFSTGMRQKVAIARALvHDPP----VLLLDEPTTG 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 863 LHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASG 919
Cdd:cd03266   167 LDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVL------HRGRVVYEG 218
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
830-902 1.03e-05

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 47.04  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIV 902
Cdd:cd03215   105 LSGGNQQKVVLARWLARDPR---VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGLCDRIL 175
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
830-929 1.11e-05

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 47.68  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLAselhrrstgRTL-----YIL-DEPTTGLhahD---IARLLEVLQRLVESGETVLVIEHNL----DVik 896
Cdd:COG1126   137 LSGGQQQRVAIA---------RALamepkVMLfDEPTSAL---DpelVGEVLDVMRDLAKEGMTMVVVTHEMgfarEV-- 202
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169391345 897 tADYIV--DlgpeggdkGGQIVASGTPEQVV---KEER 929
Cdd:COG1126   203 -ADRVVfmD--------GGRIVEEGPPEEFFenpQHER 231
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
464-584 1.15e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 48.09  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERVGFLVN-VGL-DYLTlsRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRDLGN 541
Cdd:PRK13635  116 EMVERVDQALRqVGMeDFLN--REPHRLSGGQKQRVAIAGVLALQPD--IIILDEATSMLDPRGRREVLETVRQLKEQKG 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1169391345 542 -TLIVVEHDEDTMMAADYLLdigpgaGIHGGQVVSAGTPAEVMQ 584
Cdd:PRK13635  192 iTVLSITHDLDEAAQADRVI------VMNKGEILEEGTPEEIFK 229
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
414-562 1.21e-05

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 47.75  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 414 GRLKPeSLAVFVGDKTIADVTK-YSVQEVQEFFSnvELTEKQQKIAH------LILREIQERVGFLVNV-----GLDYLT 481
Cdd:cd03236    48 GKLKP-NLGKFDDPPDWDEILDeFRGSELQNYFT--KLLEGDVKVIVkpqyvdLIPKAVKGKVGELLKKkdergKLDELV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 --------LSRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDedtM 553
Cdd:cd03236   125 dqlelrhvLDRNIDQLSGGELQRVAIAAALARDAD--FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD---L 199

                  ....*....
gi 1169391345 554 MAADYLLDI 562
Cdd:cd03236   200 AVLDYLSDY 208
CP_lyasePhnL TIGR02324
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...
488-564 1.24e-05

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.


Pssm-ID: 131377 [Multi-domain]  Cd Length: 224  Bit Score: 47.39  E-value: 1.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 488 TLSGGEAQRIRLATQIGSRLTGVLyiLDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMA-ADYLLDIGP 564
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILL--LDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRVMDVTP 224
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
830-924 1.26e-05

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 48.51  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHA---HDIARLLEVLQRlvESGETVLVIEHNLDVIK-TADYIVDLg 905
Cdd:COG0444   151 LSGGMRQRVMIARAL---ALEPKLLIADEPTTALDVtiqAQILNLLKDLQR--ELGLAILFITHDLGVVAeIADRVAVM- 224
                          90
                  ....*....|....*....
gi 1169391345 906 peggdKGGQIVASGTPEQV 924
Cdd:COG0444   225 -----YAGRIVEEGPVEEL 238
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
791-905 1.26e-05

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 47.57  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVE---FFANIPKIKRKLQTLVDV-GLGYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAH 866
Cdd:PRK11614   95 MTVEENLAmggFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR---LLLLDEPSLGLAPI 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169391345 867 DIARLLEVLQRLVESGETVLVIEHNLD-VIKTAD--YIVDLG 905
Cdd:PRK11614  172 IIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrgYVLENG 213
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
792-924 1.39e-05

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 47.58  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 792 TIEDGVEF---FANIPKIKRK---LQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHA 865
Cdd:cd03258    98 TVFENVALpleIAGVPKAEIEervLELLELVGLEDKADAYPAQ-LSGGQKQRVGIARAL---ANNPKVLLCDEATSALDP 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 866 ---HDIARLLEVLQRlvESGETVLVIEHNLDVIKT-ADYIVDLGpeggdkGGQIVASGTPEQV 924
Cdd:cd03258   174 ettQSILALLRDINR--ELGLTIVLITHEMEVVKRiCDRVAVME------KGEVVEEGTVEEV 228
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
790-919 1.42e-05

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 47.19  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFANIPKI------KRKLQTLVDVGLGYMKlGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGL 863
Cdd:cd03264    86 NFTVREFLDYIAWLKGIpskevkARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPS---ILIVDEPTAGL 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 864 hahDIA---RLLEVLQRLVEsGETVLVIEHNL-DVIKTADYIVDLgpeggdKGGQIVASG 919
Cdd:cd03264   162 ---DPEeriRFRNLLSELGE-DRIVILSTHIVeDVESLCNQVAVL------NKGKLVFEG 211
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
829-924 1.82e-05

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 47.95  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 829 TLSGGEAQRVKLASELhrrSTGRTLYILDEPttgLHAHDIAR---LLEVLQRLVESGET-VLVIEHNLD-VIKTADYIVD 903
Cdd:PRK11144  128 SLSGGEKQRVAIGRAL---LTAPELLLMDEP---LASLDLPRkreLLPYLERLAREINIpILYVSHSLDeILRLADRVVV 201
                          90       100
                  ....*....|....*....|.
gi 1169391345 904 LgpeggDKgGQIVASGTPEQV 924
Cdd:PRK11144  202 L-----EQ-GKVKAFGPLEEV 216
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
489-550 1.99e-05

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 47.08  E-value: 1.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 489 LSGGEAQRIRLATQIGSRlTGVLYIlDEPSIGLHQRDNDRLIRTLQEM-RDLGNTLIVVEHDE 550
Cdd:PRK10584  147 LSGGEQQRVALARAFNGR-PDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
489-610 1.99e-05

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 47.45  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 489 LSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRD-LGNTLIVVEHD-EDTMMAADYlldigpgA 566
Cdd:PRK11831  144 LSGGMARRAALARAIA--LEPDLIMFDEPFVGQDPITMGVLVKLISELNSaLGVTCVVVSHDvPEVLSIADH-------A 214
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1169391345 567 GIHGGQ-VVSAGTPAEVMQDENSLTGKYLSGKEFIPVPLERRKGD 610
Cdd:PRK11831  215 YIVADKkIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGD 259
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
793-893 2.09e-05

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 46.52  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 793 IEDGVEFFANIPKIKRKLQTLVDVGLGYMkLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLL 872
Cdd:cd03297    96 LAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQP---ELLLLDEPFSALDRALRLQLL 171
                          90       100
                  ....*....|....*....|..
gi 1169391345 873 EVLQRLVES-GETVLVIEHNLD 893
Cdd:cd03297   172 PELKQIKKNlNIPVIFVTHDLS 193
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
482-564 2.17e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.45  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGE------AQRIRLATQIGSRLtGVLyILDEPSIGL-HQRDNDRLIRTLQEMRDLGN-TLIVVEHDEDTM 553
Cdd:cd03240   109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNLdEENIEESLAEIIEERKSQKNfQLIVITHDEELV 186
                          90
                  ....*....|.
gi 1169391345 554 MAADYLLDIGP 564
Cdd:cd03240   187 DAADHIYRVEK 197
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
489-562 2.40e-05

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.03  E-value: 2.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 489 LSGGEAQRIRLATQIGSrlTGVLYILDEPS--IGLHQRDN-DRLIRTLQEMRDlgNTLIVVEHDedtMMAADYLLDI 562
Cdd:cd03222    72 LSGGELQRVAIAAALLR--NATFYLFDEPSayLDIEQRLNaARAIRRLSEEGK--KTALVVEHD---LAVLDYLSDR 141
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
489-563 2.56e-05

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 45.45  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 489 LSGGEAQRIRLA------TQIgsrltgvlYILDEPSIGLhqrDND---RLIRTLQEMRDlGNTLIVVEHDEDTMMAAD-- 557
Cdd:cd03228    97 LSGGQRQRIAIArallrdPPI--------LILDEATSAL---DPEteaLILEALRALAK-GKTVIVIAHRLSTIRDADri 164

                  ....*.
gi 1169391345 558 YLLDIG 563
Cdd:cd03228   165 IVLDDG 170
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
806-902 2.69e-05

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 46.37  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETV 885
Cdd:cd03262   113 EERALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALAMNP---KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTM 188
                          90
                  ....*....|....*...
gi 1169391345 886 LVIEHNLDVI-KTADYIV 902
Cdd:cd03262   189 VVVTHEMGFArEVADRVI 206
cbiO PRK13641
energy-coupling factor transporter ATPase;
471-595 2.70e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 47.13  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 471 FLVNVGLDYLTLSRAAGTLSGGEAQRIRLAtqigsrltGVLYI------LDEPSIGLHQRDNDRLIRTLQEMRDLGNTLI 544
Cdd:PRK13641  128 WLKKVGLSEDLISKSPFELSGGQMRRVAIA--------GVMAYepeilcLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVI 199
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 545 VVEHDEDTMmaADYLLDIgpgAGIHGGQVVSAGTPAEVMQDENSLTGKYLS 595
Cdd:PRK13641  200 LVTHNMDDV--AEYADDV---LVLEHGKLIKHASPKEIFSDKEWLKKHYLD 245
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
488-590 3.13e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 46.67  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 488 TLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGN-TLIVVEHDEDTMMAADYLLdigpga 566
Cdd:PRK13648  142 ALSGGQKQRVAIAGVLA--LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVI------ 213
                          90       100
                  ....*....|....*....|....
gi 1169391345 567 GIHGGQVVSAGTPAEVMQDENSLT 590
Cdd:PRK13648  214 VMNKGTVYKEGTPTEIFDHAEELT 237
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
811-890 3.21e-05

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 45.81  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGL-GYMKLgqPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIE 889
Cdd:TIGR01189 110 DALAAVGLtGFEDL--PAAQLSAGQQRRLALARLW---LSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTT 184

                  .
gi 1169391345 890 H 890
Cdd:TIGR01189 185 H 185
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
791-924 3.44e-05

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 47.06  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEFFANI-----PKIKRKLQTLVD-VGLGymKLGQ--PATtLSGGEAQRVKLAselhrrstgRTLYI------L 856
Cdd:COG1118    90 MTVAENIAFGLRVrppskAEIRARVEELLElVQLE--GLADryPSQ-LSGGQRQRVALA---------RALAVepevllL 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 857 DEPTTGLHAHdIARLLE-VLQRLV-ESGETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG1118   158 DEPFGALDAK-VRKELRrWLRRLHdELGGTTVFVTHDQEeALELADRVVVM------NQGRIEQVGTPDEV 221
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
808-928 3.80e-05

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 47.13  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 808 RKLQTLVDVGLGYMKLGQPATT----LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHdiARLL--EVLQRLVES 881
Cdd:PRK13536  147 REIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARAL---INDPQLLILDEPTTGLDPH--ARHLiwERLRSLLAR 221
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1169391345 882 GETVLVIEHnldVIKTADYIVD--LGPEGGDKggqiVASGTPEQVVKEE 928
Cdd:PRK13536  222 GKTILLTTH---FMEEAERLCDrlCVLEAGRK----IAEGRPHALIDEH 263
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
808-894 3.87e-05

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 46.21  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 808 RKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASEL-HRRStgrtLYILDEPttgLHAHDIARLLEvLQRLVES----- 881
Cdd:PRK11247  113 AALQALAAVGLADRANEWPAA-LSGGQKQRVALARALiHRPG----LLLLDEP---LGALDALTRIE-MQDLIESlwqqh 183
                          90
                  ....*....|...
gi 1169391345 882 GETVLVIEHnlDV 894
Cdd:PRK11247  184 GFTVLLVTH--DV 194
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
805-896 3.95e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 47.23  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKLQTLVDVGLGYMKLGqpattlsGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGET 884
Cdd:PRK13549  126 KLLAQLKLDINPATPVGNLG-------LGQQQLVEIAKALNKQAR---LLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
                          90
                  ....*....|..
gi 1169391345 885 VLVIEHNLDVIK 896
Cdd:PRK13549  196 CIYISHKLNEVK 207
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
440-575 4.38e-05

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 47.41  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 440 EVQEFFSNVELTEKQQKIAHLILR-EIQERVGFlvnvgldyltlsrAAGTLSGGEAQRIRLATQIgsrLTGVLYIL-DEP 517
Cdd:PRK10535  108 EVPAVYAGLERKQRLLRAQELLQRlGLEDRVEY-------------QPSQLSGGQQQRVSIARAL---MNGGQVILaDEP 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 518 SIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLDigpgagIHGGQVVS 575
Cdd:PRK10535  172 TGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIE------IRDGEIVR 223
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
830-896 4.45e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 47.01  E-value: 4.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLDVIK 896
Cdd:PRK15134  157 LSGGERQRVMIAMALLTRPE---LLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVR 221
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
414-594 4.53e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 46.33  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 414 GRLKPESLAVFVGDKTIadvTKYSVQEVQEF----FSN----VELTEKQQKIA----HLILRE--IQERVGFLVN-VGLD 478
Cdd:PRK13652   52 GILKPTSGSVLIRGEPI---TKENIREVRKFvglvFQNpddqIFSPTVEQDIAfgpiNLGLDEetVAHRVSSALHmLGLE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 479 YLtLSRAAGTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRTLQEM-RDLGNTLIVVEHDEDTMMA-A 556
Cdd:PRK13652  129 EL-RDRVPHHLSGGEKKRVAIAGVIA--MEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEmA 205
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1169391345 557 DYLLdigpgaGIHGGQVVSAGTPAEVMQDENSLTGKYL 594
Cdd:PRK13652  206 DYIY------VMDKGRIVAYGTVEEIFLQPDLLARVHL 237
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
482-561 4.59e-05

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 45.86  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGEAQRIRLATQIGSrlTGVLYILDEPSIGL--HQRDN-DRLIRTLQEMRDlgNTLIVVEHDedtMMAADY 558
Cdd:cd03237   109 LDREVPELSGGELQRVAIAACLSK--DADIYLLDEPSAYLdvEQRLMaSKVIRRFAENNE--KTAFVVEHD---IIMIDY 181

                  ...
gi 1169391345 559 LLD 561
Cdd:cd03237   182 LAD 184
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
464-594 4.62e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 46.22  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERVG-FLVNVGLDYLTlSRAAGTLSGGEAQRIRLAtqigsrltGVL------YILDEPSIGLHQRDNDRLIRTLQEM 536
Cdd:PRK13639  113 EVEKRVKeALKAVGMEGFE-NKPPHHLSGGQKKRVAIA--------GILamkpeiIVLDEPTSGLDPMGASQIMKLLYDL 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 537 RDLGNTLIVVEHDEDtmMAADYLLDIgpgAGIHGGQVVSAGTPAEVMQDENSLTGKYL 594
Cdd:PRK13639  184 NKEGITIIISTHDVD--LVPVYADKV---YVMSDGKIIKEGTPKEVFSDIETIRKANL 236
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
830-947 4.67e-05

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 46.66  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLV-IEHNLD-VIKTADYIVDLgpe 907
Cdd:PRK11022  154 LSGGMSQRVMIAMAIACRP---KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVlITHDLAlVAEAAHKIIVM--- 227
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 908 ggdKGGQIVASGTPEQVVKEER-SYTGKYLKEI--LNRDKARM 947
Cdd:PRK11022  228 ---YAGQVVETGKAHDIFRAPRhPYTQALLRALpeFAQDKARL 267
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
18-45 4.90e-05

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 44.68  E-value: 4.90e-05
                          10        20
                  ....*....|....*....|....*...
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSLA 45
Cdd:cd03228    18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
cbiO PRK13637
energy-coupling factor transporter ATPase;
816-927 5.37e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 46.19  E-value: 5.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 816 VGLGYMKLGQPAT-TLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGE-TVLVIEHNL- 892
Cdd:PRK13637  130 VGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPK---ILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMe 206
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169391345 893 DVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKE 927
Cdd:PRK13637  207 DVAKLADRIIVM------NKGKCELQGTPREVFKE 235
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
463-557 5.50e-05

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 45.20  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVG-FLVNVGLDYLtLSRAAGTLSGGEAQRIRLATQIGSRlTGVLyILDEPSIGLHQRDNDRLIRTLQEM-RDLG 540
Cdd:cd03259   105 AEIRARVReLLELVGLEGL-LNRYPHELSGGQQQRVALARALARE-PSLL-LLDEPLSALDAKLREELREELKELqRELG 181
                          90
                  ....*....|....*...
gi 1169391345 541 NTLIVVEHD-EDTMMAAD 557
Cdd:cd03259   182 ITTIYVTHDqEEALALAD 199
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
823-924 5.72e-05

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 45.88  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRL-VESGETVLVIEHNLD-VIKTADY 900
Cdd:PRK09544  114 IDAPMQKLSGGETQRVLLARALLNRP---QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHlVMAKTDE 190
                          90       100
                  ....*....|....*....|....
gi 1169391345 901 IVDLgpeggdkGGQIVASGTPEQV 924
Cdd:PRK09544  191 VLCL-------NHHICCSGTPEVV 207
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
822-936 5.88e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 45.67  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 822 KLGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYI 901
Cdd:PRK14247  139 RLDAPAGKLSGGQQQRLCIARAL---AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV 215
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1169391345 902 VDLgpeggdKGGQIVASGTPEQVVKEER-SYTGKYL 936
Cdd:PRK14247  216 AFL------YKGQIVEWGPTREVFTNPRhELTEKYV 245
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
447-548 5.91e-05

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 45.18  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 447 NVELTEKQQKIAHLILREiqervgflvnVGLDYLtLSRAAGTLSGGEAQRIRLATQIgSRLTGVLyILDEPSIGLhqrdn 526
Cdd:cd03298    98 GLKLTAEDRQAIEVALAR----------VGLAGL-EKRLPGELSGGERQRVALARVL-VRDKPVL-LLDEPFAAL----- 159
                          90       100       110
                  ....*....|....*....|....*....|
gi 1169391345 527 DRLIRtlQEMRDL--------GNTLIVVEH 548
Cdd:cd03298   160 DPALR--AEMLDLvldlhaetKMTVLMVTH 187
PLN03211 PLN03211
ABC transporter G-25; Provisional
830-890 5.92e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.80  E-value: 5.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH 890
Cdd:PLN03211  207 ISGGERKRVSIAHEM---LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
447-588 6.49e-05

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 46.37  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 447 NVELTEKQQKIAHlilREIQERVGflvnvglDYLTL-------SRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSI 519
Cdd:PRK11607  111 NIAFGLKQDKLPK---AEIASRVN-------EMLGLvhmqefaKRKPHQLSGGQRQRVALARSLAKRPK--LLLLDEPMG 178
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 520 GLHQRDNDRL-IRTLQEMRDLGNTLIVVEHD-EDTMMAAdylldiGPGAGIHGGQVVSAGTPAEVMQDENS 588
Cdd:PRK11607  179 ALDKKLRDRMqLEVVDILERVGVTCVMVTHDqEEAMTMA------GRIAIMNRGKFVQIGEPEEIYEHPTT 243
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
788-902 7.10e-05

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 45.01  E-value: 7.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 788 VLGMTIEDGVEFFANIPKIKRK-------LQTLVDVgLGY---MKLGQPATTLSGGEAQRVKLASELHRRStgrTLYILD 857
Cdd:cd03290    90 LLNATVEENITFGSPFNKQRYKavtdacsLQPDIDL-LPFgdqTEIGERGINLSGGQRQRICVARALYQNT---NIVFLD 165
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1169391345 858 EPTTGLHAHDIARLLE--VLQRLVESGETVLVIEHNLDVIKTADYIV 902
Cdd:cd03290   166 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWII 212
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
811-931 7.31e-05

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 45.15  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLGYMKLGQPaTTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLV-ESGETVLVIE 889
Cdd:TIGR01184  97 EHIALVGLTEAADKRP-GQLSGGMKQRVAIARAL---SIRPKVLLLDEPFGALDALTRGNLQEELMQIWeEHRVTVLMVT 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169391345 890 HNLD-VIKTADYIVDL--GPEGgdKGGQIVASGTP-----EQVVKEERSY 931
Cdd:TIGR01184 173 HDVDeALLLSDRVVMLtnGPAA--NIGQILEVPFPrprdrLEVVEDPSYY 220
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
830-920 7.66e-05

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 46.49  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVEsGETVLVIEHNLDVIKTADYIVDLgpegg 909
Cdd:PRK13657  472 LSGGERQRLAIARALLKDP---PILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVF----- 542
                          90
                  ....*....|.
gi 1169391345 910 DKgGQIVASGT 920
Cdd:PRK13657  543 DN-GRVVESGS 552
cbiO PRK13650
energy-coupling factor transporter ATPase;
462-589 7.73e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 45.49  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 462 LREIQERVGFLVN-VGL-DYLTlsRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRD- 538
Cdd:PRK13650  114 HEEMKERVNEALElVGMqDFKE--REPARLSGGQKQRVAIAGAVAMRPK--IIILDEATSMLDPEGRLELIKTIKGIRDd 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 539 LGNTLIVVEHDEDTMMAADYLLdigpgaGIHGGQVVSAGTPAEVMQDENSL 589
Cdd:PRK13650  190 YQMTVISITHDLDEVALSDRVL------VMKNGQVESTSTPRELFSRGNDL 234
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
464-549 7.91e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 45.19  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERV-GFLVNVGLDYLTLSRAAgTLSGGEAQRIRLATQIGSRLTGVLyiLDEPSIGLHQRDNDRLIRTLQEM-RDLGN 541
Cdd:PRK11629  121 EINSRAlEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVL--ADEPTGNLDARNADSIFQLLGELnRLQGT 197

                  ....*...
gi 1169391345 542 TLIVVEHD 549
Cdd:PRK11629  198 AFLVVTHD 205
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
475-589 7.92e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 45.37  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 475 VGLDYLtLSRAAGTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRTLQEMRDLGN-TLIVVEHDEDTM 553
Cdd:PRK13632  130 VGMEDY-LDKEPQNLSGGQKQRVAIASVLA--LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA 206
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1169391345 554 MAADYLLDIGpgagihGGQVVSAGTPAEVMQDENSL 589
Cdd:PRK13632  207 ILADKVIVFS------EGKLIAQGKPKEILNNKEIL 236
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
806-956 9.08e-05

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 46.33  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVDVGLGYmKLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLV-ESGET 884
Cdd:TIGR03269 146 VGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKEP---FLFLADEPTGTLDPQTAKLVHNALEEAVkASGIS 221
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 885 VLVIEHNLDVI-KTADYIVDLgpeggdKGGQIVASGTPEQVVKeersytgKYLkeilnrDKARMKEKIKEVEL 956
Cdd:TIGR03269 222 MVLTSHWPEVIeDLSDKAIWL------ENGEIKEEGTPDEVVA-------VFM------EGVSEVEKECEVEV 275
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
486-596 9.30e-05

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 44.87  E-value: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 486 AGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMA-AD--YLLDi 562
Cdd:PRK11614  135 AGTMSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADrgYVLE- 211
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1169391345 563 gpgagihGGQVVSAGTPAEVMQDEnSLTGKYLSG 596
Cdd:PRK11614  212 -------NGHVVLEDTGDALLANE-AVRSAYLGG 237
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
821-919 9.33e-05

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 44.89  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 821 MKLGQPATTLSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHAHDIARLLEVLQRLVeSGETVLVIEHNLDVIKTADY 900
Cdd:cd03245   132 LQIGERGRGLSGGQRQAVALARALLND---PPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDR 207
                          90
                  ....*....|....*....
gi 1169391345 901 IVDLgpeggdKGGQIVASG 919
Cdd:cd03245   208 IIVM------DSGRIVADG 220
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
829-919 9.45e-05

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 44.58  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 829 TLSGGEAQRVKL-ASELHRRStgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgp 906
Cdd:cd03269   128 ELSKGNQQKVQFiAAVIHDPE----LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVLLL-- 201
                          90
                  ....*....|...
gi 1169391345 907 eggdKGGQIVASG 919
Cdd:cd03269   202 ----NKGRAVLYG 210
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
413-562 9.54e-05

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 44.79  E-value: 9.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 413 GGRLKPESLAVFVGDKTI-----ADVTKYSVQEV----QEF--------FSNVELTekqQKIAHLILREIQERV-GFLVN 474
Cdd:cd03255    51 GGLDRPTSGEVRVDGTDIsklseKELAAFRRRHIgfvfQSFnllpdltaLENVELP---LLLAGVPKKERRERAeELLER 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 475 VGLDYLtLSRAAGTLSGGEAQRIRLAtqigsR-LTG--VLYILDEPSIGLHQRDNDRLIRTLQEM-RDLGNTLIVVEHDE 550
Cdd:cd03255   128 VGLGDR-LNHYPSELSGGQQQRVAIA-----RaLANdpKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP 201
                         170
                  ....*....|..
gi 1169391345 551 DTMMAADYLLDI 562
Cdd:cd03255   202 ELAEYADRIIEL 213
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
811-932 9.57e-05

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 46.22  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLgymklgqPATTL-------SGGEAQRVKLAselhrrstgRTL------YILDEPTTGLhahDI---ARLLEV 874
Cdd:COG4172   407 EALEEVGL-------DPAARhryphefSGGQRQRIAIA---------RALilepklLVLDEPTSAL---DVsvqAQILDL 467
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 875 LQRL-VESGETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQVVKEERS-YT 932
Cdd:COG4172   468 LRDLqREHGLAYLFISHDLAVVRAlAHRVMVM------KDGKVVEQGPTEQVFDAPQHpYT 522
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
463-586 9.62e-05

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 44.98  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGF-LVNVGLDYLTlSRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRD-LG 540
Cdd:PRK11300  128 SEALDRAATwLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPE--ILMLDEPAAGLNPKETKELDELIAELRNeHN 204
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1169391345 541 NTLIVVEHDEDTMMA-ADYLLDIGPGAGIhggqvvSAGTPAEVMQDE 586
Cdd:PRK11300  205 VTVLLIEHDMKLVMGiSDRIYVVNQGTPL------ANGTPEEIRNNP 245
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
830-928 9.98e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 45.11  E-value: 9.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTADYIVDLgpeg 908
Cdd:PRK13647  139 LSYGQKKRVAIAGVLAMDPD---VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVL---- 211
                          90       100
                  ....*....|....*....|
gi 1169391345 909 gdKGGQIVASGTPEQVVKEE 928
Cdd:PRK13647  212 --KEGRVLAEGDKSLLTDED 229
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
14-207 1.02e-04

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 46.34  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  14 RAHNlkNIDVTIPRNQLVVVTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDkpdvDTIEGLSPAI-SIDQK 92
Cdd:cd14875    64 KAFN--AIFVQGLGNQSVVISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKID----ENLKWSNPVMeSFGNA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  93 TTSRNPRStvgtvTEIYDYLRLLFArigtpicPNHGIEITSQTVEQMVDR---VLEYPERTKLQVLAPIVSGRKGAHVKV 169
Cdd:cd14875   138 RTVRNDNS-----SRFGKYIKLYFD-------PTSGVMVGGQTVTYLLEKsriIMQSPGERNYHIFYEMLAGLSPEEKKE 205
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1169391345 170 LEDIKK-QGY---------VRVRVDGEMLDVSEEItldKNKKHSIEVV 207
Cdd:cd14875   206 LGGLKTaQDYkclnggntfVRRGVDGKTLDDAHEF---QNVRHALSMI 250
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
445-581 1.12e-04

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 44.67  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 445 FSNVELtekQQKIAHLILREIQERVGFLvnvgLDYLTLSRAA----GTLSGGEAQRIRLATQIGSRlTGVLYiLDEPSIG 520
Cdd:cd03265    91 WENLYI---HARLYGVPGAERRERIDEL----LDFVGLLEAAdrlvKTYSGGMRRRLEIARSLVHR-PEVLF-LDEPTIG 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 521 LHQRDNDRLIRTLQEM-RDLGNTLIVVEHDedtMMAADYLLDigPGAGIHGGQVVSAGTPAE 581
Cdd:cd03265   162 LDPQTRAHVWEYIEKLkEEFGMTILLTTHY---MEEAEQLCD--RVAIIDHGRIIAEGTPEE 218
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
16-44 1.20e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 43.39  E-value: 1.20e-04
                          10        20
                  ....*....|....*....|....*....
gi 1169391345  16 HNLKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:cd00267    13 TALDNVSLTLKAGEIVALVGPNGSGKSTL 41
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
791-909 1.48e-04

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 44.00  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPKIKRK---LQTLVDVGLG-----YmklgqPATtLSGGEAQRVKLAselhrrstgRTLYI---- 855
Cdd:cd03293    88 LTVLDNVALgleLQGVPKAEAReraEELLELVGLSgfenaY-----PHQ-LSGGMRQRVALA---------RALAVdpdv 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 856 --LDEPTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLD-VIKTADYIVDLGPEGG 909
Cdd:cd03293   153 llLDEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDeAVFLADRVVVLSARPG 210
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
800-937 1.62e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 45.79  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  800 FANIPKIKRKLQTLVDVGLG-YMKlgqpatTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDiARLLE--VLQ 876
Cdd:PTZ00265  1334 FAAIDEFIESLPNKYDTNVGpYGK------SLSGGQKQRIAIARALLREP---KILLLDEATSSLDSNS-EKLIEktIVD 1403
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169391345  877 RLVESGETVLVIEHNLDVIKTADYIVDLgpEGGDKGGQIV-ASGTPEQVVKEERSYTGKYLK 937
Cdd:PTZ00265  1404 IKDKADKTIITIAHRIASIKRSDKIVVF--NNPDRTGSFVqAHGTHEELLSVQDGVYKKYVK 1463
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
488-566 1.73e-04

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 43.96  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 488 TLSGGEAQRIRLAtqigsRltGV-----LYILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMA-ADYLLD 561
Cdd:COG4778   152 TFSGGEQQRVNIA-----R--GFiadppLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVD 224

                  ....*
gi 1169391345 562 IGPGA 566
Cdd:COG4778   225 VTPFS 229
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
830-931 1.78e-04

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 43.67  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHN---LDVIKtADYIVDLgp 906
Cdd:cd03217   105 FSGGEKKRNEILQLLLLEPD---LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK-PDRVHVL-- 178
                          90       100
                  ....*....|....*....|....*.
gi 1169391345 907 eggdKGGQIVASGTPEQVVK-EERSY 931
Cdd:cd03217   179 ----YDGRIVKSGDKELALEiEKKGY 200
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
489-573 1.96e-04

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 42.97  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 489 LSGGEAQRIRLAtqigsRltgVLY------ILDEPSIGLHQrDNDRLI-RTLQEMRDLGNTLIVVEHDEDTMMAADYLLD 561
Cdd:cd03246    97 LSGGQRQRLGLA-----R---ALYgnprilVLDEPNSHLDV-EGERALnQAIAALKAAGATRIVIAHRPETLASADRILV 167
                          90
                  ....*....|..
gi 1169391345 562 igpgagIHGGQV 573
Cdd:cd03246   168 ------LEDGRV 173
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
414-582 1.99e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 44.23  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 414 GRLKPESLAVFVGDKTIaDVTKYSVQEVQEFFSNVELTEKQQkiahLILREIQERVGF-LVNVGL----------DYLTL 482
Cdd:PRK13638   49 GLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPEQQ----IFYTDIDSDIAFsLRNLGVpeaeitrrvdEALTL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 483 SRAAG-------TLSGGEAQRIRLAtqiGSRLTGVLYIL-DEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMM 554
Cdd:PRK13638  124 VDAQHfrhqpiqCLSHGQKKRVAIA---GALVLQARYLLlDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIY 200
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1169391345 555 A---ADYLLdigpgagiHGGQVVSAGTPAEV 582
Cdd:PRK13638  201 EisdAVYVL--------RQGQILTHGAPGEV 223
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
437-584 2.00e-04

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 44.08  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 437 SVQEVQEFFSnveltekqqKIAHLILREIQERVGFLV-NVGLDyLTLSRAAGTLSGGEAQRIRLATQIGSRLTgvLYILD 515
Cdd:COG4555    90 TVRENIRYFA---------ELYGLFDEELKKRIEELIeLLGLE-EFLDRRVGELSTGMKKKVALARALVHDPK--VLLLD 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 516 EPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMA-ADYLLdIgpgagIHGGQVVSAGTPAEVMQ 584
Cdd:COG4555   158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVV-I-----LHKGKVVAQGSLDELRE 221
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
807-896 2.04e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 44.04  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 807 KRKLQTLVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRL-VESGETV 885
Cdd:PRK11629  124 SRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNP---RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAF 199
                          90
                  ....*....|.
gi 1169391345 886 LVIEHNLDVIK 896
Cdd:PRK11629  200 LVVTHDLQLAK 210
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
18-45 2.25e-04

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 43.61  E-value: 2.25e-04
                          10        20
                  ....*....|....*....|....*...
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSLA 45
Cdd:cd03225    17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
811-919 2.29e-04

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 43.64  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLGYMKLG----QPATTLSGGEAQRVKLASELHRRstgRTLYILDEPTTGLHA---HDIARLLEVLQRlvESGE 883
Cdd:cd03298   106 RQAIEVALARVGLAglekRLPGELSGGERQRVALARVLVRD---KPVLLLDEPFAALDPalrAEMLDLVLDLHA--ETKM 180
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 884 TVLVIEHNL-DVIKTADYIVDLgpeggdKGGQIVASG 919
Cdd:cd03298   181 TVLMVTHQPeDAKRLAQRVVFL------DNGRIAAQG 211
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
445-597 2.34e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 43.75  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 445 FSNVELTEKQQKIAHlILREIQERVGFLVNVGLDYLT----LSRAAGTLSGGEAQRIRLATQIGSRLTGVLyiLDEPSIG 520
Cdd:PRK14247  100 FENVALGLKLNRLVK-SKKELQERVRWALEKAQLWDEvkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLL--ADEPTAN 176
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 521 LHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLldigpgAGIHGGQVVSAGTPAEVMQD-ENSLTGKYLSGK 597
Cdd:PRK14247  177 LDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV------AFLYKGQIVEWGPTREVFTNpRHELTEKYVTGR 248
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
797-904 2.35e-04

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 43.85  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 797 VEFFANIPKiKRKLQTLVDVGLGYMKlGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQ 876
Cdd:PRK09984  122 FSWFTREQK-QRALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQA---KVILADEPIASLDPESARIVMDTLR 196
                          90       100       110
                  ....*....|....*....|....*....|
gi 1169391345 877 RLVES-GETVLVIEHNLD-VIKTADYIVDL 904
Cdd:PRK09984  197 DINQNdGITVVVTLHQVDyALRYCERIVAL 226
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
825-916 2.42e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 44.66  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLD-VIKTAD--YI 901
Cdd:PRK15439  399 QAARTLSGGNQQKVLIAKCLEASPQ---LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEeIEQMADrvLV 475
                          90
                  ....*....|....*
gi 1169391345 902 VDLGPEGGDKGGQIV 916
Cdd:PRK15439  476 MHQGEISGALTGAAI 490
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
829-909 2.57e-04

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 42.53  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 829 TLSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLhahDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYIV 902
Cdd:cd03223    91 VLSGGEQQRLAFA---------RLLLhkpkfvFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVL 158

                  ....*..
gi 1169391345 903 DLGPEGG 909
Cdd:cd03223   159 DLDGEGG 165
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
792-924 2.83e-04

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 44.30  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 792 TIEDGVEF---FANIPK--IKRKLQTLVD-VGLG-----YmklgqPATtLSGGEAQRVKLAselhrrstgRTL----YIL 856
Cdd:COG1135    98 TVAENVALpleIAGVPKaeIRKRVAELLElVGLSdkadaY-----PSQ-LSGGQKQRVGIA---------RALannpKVL 162
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 857 --DEPTTGLHAHDIARLLEVLQRLVES-GETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG1135   163 lcDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRiCDRVAVL------ENGRIVEQGPVLDV 228
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
416-583 2.83e-04

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 43.44  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 416 LKPESLAVFVGDKTIA--DVTK------YSVQEVQEF-----FSNVELTEKQQKIAHlilREIQERVGFLVN-VGLDYLT 481
Cdd:cd03295    51 IEPTSGEIFIDGEDIReqDPVElrrkigYVIQQIGLFphmtvEENIALVPKLLKWPK---EKIRERADELLAlVGLDPAE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LS-RAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLhqrdnDRLIR-TLQE-----MRDLGNTLIVVEHD-EDTM 553
Cdd:cd03295   128 FAdRYPHELSGGQQQRVGVARALAADPP--LLLMDEPFGAL-----DPITRdQLQEefkrlQQELGKTIVFVTHDiDEAF 200
                         170       180       190
                  ....*....|....*....|....*....|
gi 1169391345 554 MAADYLldigpgAGIHGGQVVSAGTPAEVM 583
Cdd:cd03295   201 RLADRI------AIMKNGEIVQVGTPDEIL 224
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
458-925 3.05e-04

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 44.43  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 458 AHLILREIQervgflvnvgLDYLTLSRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMR 537
Cdd:TIGR02633 121 AKNLLRELQ----------LDADNVTRPVGDYGGGQQQLVEIAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRDLK 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 538 DLGNTLIVVEHDEDTMMAADYLLDIgpgagIHGGQVVsAGTPAEVMQDENSLTgkYLSGKEFIPV-PLERRK-GD----G 611
Cdd:TIGR02633 189 AHGVACVYISHKLNEVKAVCDTICV-----IRDGQHV-ATKDMSTMSEDDIIT--MMVGREITSLyPHEPHEiGDvileA 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 612 RKV---EIVGAKENNLKNAKMSFPLGTFVAVTGVSGSGKSTMInevlykslaQKLYKAKakPGAHkeikglehlDKVIDI 688
Cdd:TIGR02633 261 RNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELV---------QALFGAY--PGKF---------EGNVFI 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 689 DQSPIgrtprsnpatytgvfdDIRDVfAQTNEAKVRGYQKGRfsfnvkggrceacRGDGIIkiemhflPDVYVpcevchG 768
Cdd:TIGR02633 321 NGKPV----------------DIRNP-AQAIRAGIAMVPEDR-------------KRHGIV-------PILGV------G 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 769 KRYNRETLEvKYKDKnisevlgMTIEDGVEFFANIPKIKR-KLQTlvdvglgyMKLGQPATTLSGGEAQRVKLASELhrr 847
Cdd:TIGR02633 358 KNITLSVLK-SFCFK-------MRIDAAAELQIIGSAIQRlKVKT--------ASPFLPIGRLSGGNQQKAVLAKML--- 418
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 848 STGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTADYIVDLGpEGGDKGGQIVASGTPEQVV 925
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIG-EGKLKGDFVNHALTQEQVL 496
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
805-929 3.36e-04

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 43.44  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKLQTLVDVGLGYMKlGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH---AHDIARLLEVLQRlvES 881
Cdd:PRK11300  130 ALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCM---VTQPEILMLDEPAAGLNpkeTKELDELIAELRN--EH 203
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1169391345 882 GETVLVIEHNLD-VIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:PRK11300  204 NVTVLLIEHDMKlVMGISDRIYVV------NQGTPLANGTPEEIRNNPD 246
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
475-551 3.52e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 43.54  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 475 VGLDYLTLSRAAGTLSGGEAQRIRLAtqigsrltGVL------YILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEH 548
Cdd:PRK13651  152 VGLDESYLQRSPFELSGGQKRRVALA--------GILamepdfLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223

                  ...
gi 1169391345 549 DED 551
Cdd:PRK13651  224 DLD 226
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
456-582 3.53e-04

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 43.91  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 456 KIAHLILREIQERVGFLVN-VGLDYLtLSRAAGTLSGGEAQRIRLATQIgsrltgV----LYILDEPsigL-----HQRD 525
Cdd:COG3839   101 KLRKVPKAEIDRRVREAAElLGLEDL-LDRKPKQLSGGQRQRVALGRAL------VrepkVFLLDEP---LsnldaKLRV 170
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 526 NDRL-IRTLQemRDLGNTLIVVEHD-EDTMMAADYLldigpgAGIHGGQVVSAGTPAEV 582
Cdd:COG3839   171 EMRAeIKRLH--RRLGTTTIYVTHDqVEAMTLADRI------AVMNDGRIQQVGTPEEL 221
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
790-921 3.57e-04

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 42.88  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 790 GMTIEDGVEFFA---NIPKIKRKLQtlVDVGLGYMKLGQ----PATTLSGGeaQRVKLaselhrrST------GRTLYIL 856
Cdd:cd03263    89 ELTVREHLRFYArlkGLPKSEIKEE--VELLLRVLGLTDkankRARTLSGG--MKRKL-------SLaialigGPSVLLL 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 857 DEPTTGLhahD-IAR--LLEVLQRLVeSGETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTP 921
Cdd:cd03263   158 DEPTSGL---DpASRraIWDLILEVR-KGRSIILTTHSMDEAEAlCDRIAIM------SDGKLRCIGSP 216
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
806-896 3.71e-04

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 44.05  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETV 885
Cdd:TIGR02633 118 YLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR---LLILDEPSSSLTEKETEILLDIIRDLKAHGVAC 194
                          90
                  ....*....|.
gi 1169391345 886 LVIEHNLDVIK 896
Cdd:TIGR02633 195 VYISHKLNEVK 205
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
813-890 3.71e-04

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 43.16  E-value: 3.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 813 LVDVGLGYMKLGQPATtLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH 890
Cdd:PRK09493  121 LAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKP---KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
825-928 3.79e-04

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 44.25  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLhahDIARLLEVLQRLVE---SGETVLVIEHNLD-VIKTADY 900
Cdd:COG3845   398 TPARSLSGGNQQKVILARELSRDP---KLLIAAQPTRGL---DVGAIEFIHQRLLElrdAGAAVLLISEDLDeILALSDR 471
                          90       100
                  ....*....|....*....|....*...
gi 1169391345 901 IVDLgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:COG3845   472 IAVM------YEGRIVGEVPAAEATREE 493
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
791-893 3.86e-04

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 43.15  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPKIKRK---LQTLVDVGLG-----YmklgqPATtLSGGEAQRVKLAselhrrstgRTLYI---- 855
Cdd:COG1116    95 LTVLDNVALgleLRGVPKAERReraRELLELVGLAgfedaY-----PHQ-LSGGMRQRVAIA---------RALANdpev 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169391345 856 --LDEPTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLD 893
Cdd:COG1116   160 llMDEPFGALDALTRERLQDELLRLWqETGKTVLFVTHDVD 200
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
830-927 4.05e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 43.54  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLhahDIARLLEVLQRLVE----SGETVLVIEHNLDVIKTADYIVDLg 905
Cdd:PRK13633  145 LSGGQKQRVAIAGILAMRP---ECIIFDEPTAML---DPSGRREVVNTIKElnkkYGITIILITHYMEEAVEADRIIVM- 217
                          90       100
                  ....*....|....*....|..
gi 1169391345 906 peggdKGGQIVASGTPEQVVKE 927
Cdd:PRK13633  218 -----DSGKVVMEGTPKEIFKE 234
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
795-899 4.06e-04

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 43.09  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 795 DGVEFFANIPKI-----KRKLQTLVDVglgyMKLG----QPATTLSGGEAQRVKL-ASELHRRStgrtLYILDEPTTGLH 864
Cdd:cd03267   114 DSFYLLAAIYDLpparfKKRLDELSEL----LDLEelldTPVRQLSLGQRMRAEIaAALLHEPE----ILFLDEPTIGLD 185
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169391345 865 AHDIARLLEVLQRLV-ESGETVLVIEHNL-DVIKTAD 899
Cdd:cd03267   186 VVAQENIRNFLKEYNrERGTTVLLTSHYMkDIEALAR 222
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
453-597 4.07e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 43.11  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 453 KQQKIAHLILREIQERVGFLVNVgldYLTLSRAAGTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRT 532
Cdd:PRK14246  121 KEKREIKKIVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARALA--LKPKVLLMDEPTSMIDIVNSQAIEKL 195
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 533 LQEMRDLGNTLIVVEHDEDTMMAADYLldigpgAGIHGGQVVSAGTPAEVMQD-ENSLTGKYLSGK 597
Cdd:PRK14246  196 ITELKNEIAIVIVSHNPQQVARVADYV------AFLYNGELVEWGSSNEIFTSpKNELTEKYVIGR 255
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
830-908 4.12e-04

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 41.67  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLhahDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIVDLGPEG 908
Cdd:cd03221    71 LSGGEKMRLALAKLL---LENPNLLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLdQVATKIIELEDGK 144
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
463-577 4.36e-04

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 42.67  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGFLVN-VGLDYLtLSRAAGTLSGGEAQRIRLATQIGSRLTGVLyiLDEPSIGLHQRDNDRLIRTLQEM-RDLG 540
Cdd:cd03297   106 REDRISVDELLDlLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLL--LDEPFSALDRALRLQLLPELKQIkKNLN 182
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169391345 541 NTLIVVEHD--EDTMMAADYLLdigpgagIHGGQVVSAG 577
Cdd:cd03297   183 IPVIFVTHDlsEAEYLADRIVV-------MEDGRLQYIG 214
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
464-596 4.74e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 43.03  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQER-VGFLVNVGLDYLTLSRAAGTLSGGEAQRIRLATQIGSRLTGVLYilDEPSIGLHQRDNDRLIRTLQEMRDLGNT 542
Cdd:PRK10619  127 EARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQQLAEEGKT 204
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 543 LIVVEHD-EDTMMAADYLLdigpgaGIHGGQVVSAGTPAEVMQDENS-LTGKYLSG 596
Cdd:PRK10619  205 MVVVTHEmGFARHVSSHVI------FLHQGKIEEEGAPEQLFGNPQSpRLQQFLKG 254
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
805-936 5.00e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 43.11  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 805 KIKRKLQTLVD-----VGLG---YMKLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGL---HAHDIARLLE 873
Cdd:PRK14246  121 KEKREIKKIVEeclrkVGLWkevYDRLNSPASQLSGGQQQRLTIARALALKP---KVLLMDEPTSMIdivNSQAIEKLIT 197
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169391345 874 VLQRLVesgeTVLVIEHN-LDVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERS-YTGKYL 936
Cdd:PRK14246  198 ELKNEI----AIVIVSHNpQQVARVADYVAFL------YNGELVEWGSSNEIFTSPKNeLTEKYV 252
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
476-550 5.41e-04

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 43.50  E-value: 5.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 476 GLDYLTLSRAAgTLSGGEAQRIRLATQIgsrLTGV-LYILDEPSIGLHQRDNDRLIRTLQEMRDlGNTLIVVEHDE 550
Cdd:TIGR02868 460 GLDTVLGEGGA-RLSGGERQRLALARAL---LADApILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
823-888 5.52e-04

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 43.47  E-value: 5.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELHrrsTGRTLYILDEPTTGLhahDI-AR--LLEVLQRLVESGETVLVI 888
Cdd:COG1129   388 PEQPVGNLSGGNQQKVVLAKWLA---TDPKVLILDEPTRGI---DVgAKaeIYRLIRELAAEGKAVIVI 450
cbiO PRK13649
energy-coupling factor transporter ATPase;
475-594 5.61e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 42.81  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 475 VGLDYLTLSRAAGTLSGGEAQRIRLATqIGSRLTGVLyILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEH-DEDTM 553
Cdd:PRK13649  132 VGISESLFEKNPFELSGGQMRRVAIAG-ILAMEPKIL-VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVA 209
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1169391345 554 MAAD--YLLDigpgagihGGQVVSAGTPAEVMQDENSLTGKYL 594
Cdd:PRK13649  210 NYADfvYVLE--------KGKLVLSGKPKDIFQDVDFLEEKQL 244
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
830-916 5.88e-04

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 41.85  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEH--NLDVIKTADYIVDLgpe 907
Cdd:cd03232   109 LSVEQRKRLTIGVEL---AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHqpSASIFEKFDRLLLL--- 182

                  ....*....
gi 1169391345 908 ggDKGGQIV 916
Cdd:cd03232   183 --KRGGKTV 189
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
820-935 6.01e-04

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 43.55  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 820 YMKLGQPATTLSGGEAQRVKLASELhrRSTGRTLyILDEPTTGLHA---HDIARLLevlqRLVESGETVLVIEHNLDVIK 896
Cdd:PRK10790  467 YTPLGEQGNNLSVGQKQLLALARVL--VQTPQIL-ILDEATANIDSgteQAIQQAL----AAVREHTTLVVIAHRLSTIV 539
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169391345 897 TADYIVDLgpeggdKGGQIVASGTPEQVVKEERSYTGKY 935
Cdd:PRK10790  540 EADTILVL------HRGQAVEQGTHQQLLAAQGRYWQMY 572
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
472-549 6.65e-04

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 42.11  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 472 LVNVGLDYLTLSRAAGTLSGGEAQRIRLAtqigsR---LTGVLYILDEPSIGLHQRDNDRLIRTLQEMRD-LGNTLIVVE 547
Cdd:cd03257   129 LVGVGLPEEVLNRYPHELSGGQRQRVAIA-----RalaLNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFIT 203

                  ..
gi 1169391345 548 HD 549
Cdd:cd03257   204 HD 205
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
18-52 6.69e-04

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 42.35  E-value: 6.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSLaFDTIYAE 52
Cdd:COG2884    18 LSDVSLEIEKGEFVFLTGPSGAGKSTL-LKLLYGE 51
cbiO PRK13646
energy-coupling factor transporter ATPase;
414-590 6.72e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 42.84  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 414 GRLKPESLAVFVGDKTIADVTK--------------YSVQEVQEFFSNVEL-TEKQQKIAHLILREIQERV-GFLVNVGL 477
Cdd:PRK13646   55 ALLKPTTGTVTVDDITITHKTKdkyirpvrkrigmvFQFPESQLFEDTVEReIIFGPKNFKMNLDEVKNYAhRLLMDLGF 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 478 DYLTLSRAAGTLSGGEAQRIRLATQIGsrLTGVLYILDEPSIGLHQRDNDRLIRTLQEMR-DLGNTLIVVEHDEDTMmaA 556
Cdd:PRK13646  135 SRDVMSQSPFQMSGGQMRKIAIVSILA--MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEV--A 210
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1169391345 557 DYLLDIgpgAGIHGGQVVSAGTPAEVMQDENSLT 590
Cdd:PRK13646  211 RYADEV---IVMKEGSIVSQTSPKELFKDKKKLA 241
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
489-557 7.29e-04

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 41.40  E-value: 7.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 489 LSGGEAQRIRLATQIGSRlTGVLyILDEPSIGLHQRDNDRLIRTLQEMRD-LGNTLIVVEHD-EDTMMAAD 557
Cdd:cd03229   101 LSGGQQQRVALARALAMD-PDVL-LLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLAD 169
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
18-45 7.36e-04

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 41.09  E-value: 7.36e-04
                          10        20
                  ....*....|....*....|....*...
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSLA 45
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
811-904 7.83e-04

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 43.13  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRlvESGeTVLVIEH 890
Cdd:COG0488   134 EILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEP---DLLLLDEPTNHLDLESIEWLEEFLKN--YPG-TVLVVSH 207
                          90
                  ....*....|....*..
gi 1169391345 891 N---LDviKTADYIVDL 904
Cdd:COG0488   208 DryfLD--RVATRILEL 222
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
825-902 1.04e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 42.59  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 825 QPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTADYIV 902
Cdd:PRK11288  392 QLIMNLSGGNQQKAILGRWL---SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIV 467
cbiO PRK13641
energy-coupling factor transporter ATPase;
810-938 1.11e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 42.12  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 810 LQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIE 889
Cdd:PRK13641  126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE---ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169391345 890 HNL-DVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEERSYTGKYLKE 938
Cdd:PRK13641  203 HNMdDVAEYADDVLVL------EHGKLIKHASPKEIFSDKEWLKKHYLDE 246
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
830-920 1.12e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 41.54  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIVDLgpeg 908
Cdd:PRK11124  142 LSGGQQQRVAIARALMMEP---QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYM---- 214
                          90
                  ....*....|..
gi 1169391345 909 gdKGGQIVASGT 920
Cdd:PRK11124  215 --ENGHIVEQGD 224
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
791-927 1.17e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 42.38  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---------FANIPKIKRKLQTLVD-VGLGYMKLGQPATtLSGGEAQRVKLASELhrrSTGRTLYILDEPT 860
Cdd:PRK10851   89 MTVFDNIAFgltvlprreRPNAAAIKAKVTQLLEmVQLAHLADRYPAQ-LSGGQKQRVALARAL---AVEPQILLLDEPF 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 861 TGLHAHDIARLLEVLQRLVESGE--TVLVIEHNLDVIKTADYIVDLGPeggdkgGQIVASGTPEQVVKE 927
Cdd:PRK10851  165 GALDAQVRKELRRWLRQLHEELKftSVFVTHDQEEAMEVADRVVVMSQ------GNIEQAGTPDQVWRE 227
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
417-582 1.18e-03

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 41.45  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 417 KPESLAVFVGDKTIADVTKYSVQEVQEF-----------FSNVE--LTEKQQKIAhlilrEIQERVG-FLVNVGLDYLtL 482
Cdd:cd03300    51 TPTSGEILLDGKDITNLPPHKRPVNTVFqnyalfphltvFENIAfgLRLKKLPKA-----EIKERVAeALDLVQLEGY-A 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 483 SRAAGTLSGGEAQRIRLATQIGSRlTGVLyILDEP--SIGLHQRDNDRL-IRTLQemRDLGNTLIVVEHD-EDTMMAADY 558
Cdd:cd03300   125 NRKPSQLSGGQQQRVAIARALVNE-PKVL-LLDEPlgALDLKLRKDMQLeLKRLQ--KELGITFVFVTHDqEEALTMSDR 200
                         170       180
                  ....*....|....*....|....
gi 1169391345 559 LldigpgAGIHGGQVVSAGTPAEV 582
Cdd:cd03300   201 I------AVMNKGKIQQIGTPEEI 218
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
791-924 1.37e-03

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 42.01  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPK--IKRKLQTLVD-VGLGYMkLGQPATTLSGGEAQRVKLAselhrrstgRTLYI------LDE 858
Cdd:COG3842    92 LTVAENVAFglrMRGVPKaeIRARVAELLElVGLEGL-ADRYPHQLSGGQQQRVALA---------RALAPeprvllLDE 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 859 PTTGLHAHDIARLLEVLQRLV-ESGETVLVIEHNLD---VIktADYIVDLgpeggdKGGQIVASGTPEQV 924
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQrELGITFIYVTHDQEealAL--ADRIAVM------NDGRIEQVGTPEEI 223
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
18-45 1.41e-03

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 42.51  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*...
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSLA 45
Cdd:COG2274   491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
18-44 1.48e-03

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 41.18  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|....*..
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:COG1136    24 LRGVSLSIEAGEFVAIVGPSGSGKSTL 50
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
813-922 1.57e-03

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 41.27  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 813 LVDVGLG-----YmklgqPATtLSGGEAQRVKLAselhrR--STGRTLYILDEPTTGLHAHD---IARLLEVLQRlvESG 882
Cdd:COG4181   131 LERVGLGhrldhY-----PAQ-LSGGEQQRVALA-----RafATEPAILFADEPTGNLDAATgeqIIDLLFELNR--ERG 197
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1169391345 883 ETVLVIEHNLDVIKTADYIVDLGpeggdkGGQIVASGTPE 922
Cdd:COG4181   198 TTLVLVTHDPALAARCDRVLRLR------AGRLVEDTAAT 231
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
488-586 1.72e-03

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 41.51  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 488 TLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGL---HQRDndrLIRTLQEM-RDLGNTLIVVEHD-EDTMMAADYLLdi 562
Cdd:PRK10253  143 TLSGGQRQRAWIAMVLAQETA--IMLLDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDlNQACRYASHLI-- 215
                          90       100
                  ....*....|....*....|....
gi 1169391345 563 gpgaGIHGGQVVSAGTPAEVMQDE 586
Cdd:PRK10253  216 ----ALREGKIVAQGAPKEIVTAE 235
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
810-906 1.77e-03

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 41.22  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 810 LQTLVDVGLGYMK--LGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVES-GETVL 886
Cdd:PRK10418  119 TAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAP---FIIADEPTTDLDVVAQARILDLLESIVQKrALGML 195
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 887 VIEHNLDVI-KTAD--------YIVDLGP 906
Cdd:PRK10418  196 LVTHDMGVVaRLADdvavmshgRIVEQGD 224
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
822-931 1.92e-03

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 42.24  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  822 KLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLE--VLQRLVESGETVLVIEHNLDVIKTAD 899
Cdd:TIGR00957  753 EIGEKGVNLSGGQKQRVSLARAVYSNA---DIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVD 829
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1169391345  900 YIVDLGpeggdkGGQIVASGTPEQVVKEERSY 931
Cdd:TIGR00957  830 VIIVMS------GGKISEMGSYQELLQRDGAF 855
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
458-589 1.99e-03

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 40.93  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 458 AHLILREIQErvgflvnvGLDYLTLSRAAGtLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLhQRDNDRLIrtLQEMR 537
Cdd:cd03252   117 AHDFISELPE--------GYDTIVGEQGAG-LSGGQRQRIAIARALIHNPR--ILIFDEATSAL-DYESEHAI--MRNMH 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169391345 538 DL--GNTLIVVEHDEDTMMAADYLLdigpgaGIHGGQVVSAGTPAEVMqDENSL 589
Cdd:cd03252   183 DIcaGRTVIIIAHRLSTVKNADRII------VMEKGRIVEQGSHDELL-AENGL 229
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
793-893 2.00e-03

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 41.22  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 793 IEDGVEF---FANIPKIKRK---LQTLVDVGL-GYMKlgQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHA 865
Cdd:PRK11248   87 VQDNVAFglqLAGVEKMQRLeiaHQMLKKVGLeGAEK--RYIWQLSGGQRQRVGIARAL---AANPQLLLLDEPFGALDA 161
                          90       100
                  ....*....|....*....|....*....
gi 1169391345 866 HDIARLLEVLQRL-VESGETVLVIEHNLD 893
Cdd:PRK11248  162 FTREQMQTLLLKLwQETGKQVLLITHDIE 190
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-576 2.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 368 QVKENEILFEGVIPNIE--RRYRETSSDYvREQMEKYmaEQACPKCKGGRLKPESLAvfvgdktiADVTKYSVQEVQEFF 445
Cdd:PRK03918  681 ELEELEKRREEIKKTLEklKEELEEREKA-KKELEKL--EKALERVEELREKVKKYK--------ALLKERALSKVGEIA 749
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 446 SNV--ELTEkqQKIAHLILREIQERVgflvNVGLDYLTLSRAAGTLSGGEaqriRLATQIGSRLTGVLY--------ILD 515
Cdd:PRK03918  750 SEIfeELTE--GKYSGVRVKAEENKV----KLFVVYQGKERPLTFLSGGE----RIALGLAFRLALSLYlagnipllILD 819
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169391345 516 EPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMAADYLLDIGPGAGIHGGQVVSA 576
Cdd:PRK03918  820 EPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVIRVSLEGGVSKVEVVSL 880
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
830-925 2.49e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 41.33  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVE-SGETVLVIEHNLDVI-KTADYIVDLgpe 907
Cdd:PRK15093  159 LTEGECQKVMIAIALANQPR---LLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLsQWADKINVL--- 232
                          90
                  ....*....|....*...
gi 1169391345 908 ggdKGGQIVASGTPEQVV 925
Cdd:PRK15093  233 ---YCGQTVETAPSKELV 247
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
806-914 2.57e-03

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 40.63  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVD-VGLgYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLH---AHDIARLLEVLQRLves 881
Cdd:PRK10908  114 IRRRVSAALDkVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPA---VLLADEPTGNLDdalSEGILRLFEEFNRV--- 186
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1169391345 882 GETVLVIEHNLDVIKTADYIVDLGPEGGDKGGQ 914
Cdd:PRK10908  187 GVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
791-919 2.75e-03

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 40.20  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 791 MTIEDGVEF---FANIPK---IKRKLQTLVDVGLGYMkLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLH 864
Cdd:cd03259    87 LTVAENIAFglkLRGVPKaeiRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREP---SLLLLDEPLSALD 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345 865 AHDIARLLEVLQRLVES-GETVLVIEHNL-DVIKTADYIVDLgpeggdKGGQIVASG 919
Cdd:cd03259   163 AKLREELREELKELQRElGITTIYVTHDQeEALALADRIAVM------NEGRIVQVG 213
hmuV PRK13547
heme ABC transporter ATP-binding protein;
482-586 2.79e-03

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 40.58  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 482 LSRAAGTLSGGEAQRIRLA-----------TQIGSRltgvLYILDEPSIGLHQRDNDRLIRTLQEM-RD--LGNTLIVve 547
Cdd:PRK13547  139 VGRDVTTLSGGELARVQFArvlaqlwpphdAAQPPR----YLLLDEPTAALDLAHQHRLLDTVRRLaRDwnLGVLAIV-- 212
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169391345 548 HDEDtmMAADYLLDIgpgAGIHGGQVVSAGTPAEVMQDE 586
Cdd:PRK13547  213 HDPN--LAARHADRI---AMLADGAIVAHGAPADVLTPA 246
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
826-890 2.83e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 41.47  E-value: 2.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169391345 826 PATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLhahDIaRLLEVLQRLVESGE-TVLVIEH 890
Cdd:PRK11147  437 PVKALSGGERNRLLLARLFLKPSN---LLILDEPTNDL---DV-ETLELLEELLDSYQgTVLLVSH 495
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
830-920 3.00e-03

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 40.38  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVI-KTADYIV 902
Cdd:COG4161   142 LSGGQQQRVAIA---------RALMmepqvlLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVV 212
                          90
                  ....*....|....*...
gi 1169391345 903 DLgpeggdKGGQIVASGT 920
Cdd:COG4161   213 YM------EKGRIIEQGD 224
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
484-573 3.09e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.87  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 484 RAAGTLSGGEAQRIRLATQIGSRlTGVLYiLDEPSIGLHQRDNDRLIRTLQEM-RDLGNTLIVVEHDEDTMMAADYLLDI 562
Cdd:NF000106  140 RAAAKYSGGMRRRLDLAASMIGR-PAVLY-LDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVI 217
                          90
                  ....*....|.
gi 1169391345 563 GPGAGIHGGQV 573
Cdd:NF000106  218 DRGRVIADGKV 228
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
18-44 3.26e-03

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 40.11  E-value: 3.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:COG4181    28 LKGISLEVEAGESVAIVGASGSGKSTL 54
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
513-559 3.74e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1169391345 513 ILDEPSIGLHQRDNDRLIRTLQEMRDLG-NTLIVVEHDEDTMMAADYL 559
Cdd:PRK02224  816 ILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHDDELVGAADDL 863
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
825-955 3.77e-03

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 41.07  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 825 QPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLveSGeTVLVIEHN---LDVIktADYI 901
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKP---DMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHDryfLDNV--AGWI 228
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 902 VDLgpeggDKGGQIVASGT----PEQvvKEERsytgkyLKEILNRDKARMKEKIKEVE 955
Cdd:TIGR03719 229 LEL-----DRGRGIPWEGNysswLEQ--KQKR------LEQEEKEESARQKTLKRELE 273
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
463-551 3.80e-03

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 40.04  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGF-LVNVGLdyltLSRAA---GTLSGGEAQRIRLAtqigsRltGVLY-----ILDEPSIGLHQRDNDRLIRTL 533
Cdd:COG2884   112 KEIRRRVREvLDLVGL----SDKAKalpHELSGGEQQRVAIA-----R--ALVNrpellLADEPTGNLDPETSWEIMELL 180
                          90
                  ....*....|....*...
gi 1169391345 534 QEMRDLGNTLIVVEHDED 551
Cdd:COG2884   181 EEINRRGTTVLIATHDLE 198
cbiO PRK13642
energy-coupling factor transporter ATPase;
477-582 4.44e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 40.08  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 477 LDYLTlsRAAGTLSGGEAQRIRLATQIGSRLTgvLYILDEPSIGLHQRDNDRLIRTLQEMRDLGN-TLIVVEHDEDTMMA 555
Cdd:PRK13642  131 LDFKT--REPARLSGGQKQRVAVAGIIALRPE--IIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS 206
                          90       100
                  ....*....|....*....|....*..
gi 1169391345 556 ADYLLdigpgaGIHGGQVVSAGTPAEV 582
Cdd:PRK13642  207 SDRIL------VMKAGEIIKEAAPSEL 227
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
18-44 4.49e-03

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 39.86  E-value: 4.49e-03
                          10        20
                  ....*....|....*....|....*..
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:cd03256    17 LKDVSLSINPGEFVALIGPSGAGKSTL 43
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
464-594 4.52e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 40.22  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 464 EIQERV-GFLVNVGLDYLTlSRAAGTLSGGEAQRIRLAtqigsrltGVL------YILDEPSIGLHQRDNDRLIRTLQEM 536
Cdd:PRK13636  117 EVRKRVdNALKRTGIEHLK-DKPTHCLSFGQKKRVAIA--------GVLvmepkvLVLDEPTAGLDPMGVSEIMKLLVEM 187
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169391345 537 -RDLGNTLIVVEHDEDTMMaadylLDIGPGAGIHGGQVVSAGTPAEVMQDENSLTGKYL 594
Cdd:PRK13636  188 qKELGLTIIIATHDIDIVP-----LYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNL 241
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
489-563 4.74e-03

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 39.22  E-value: 4.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169391345 489 LSGGEAQRIRLAtQIGSRLTGVLyILDEPSIGLHQRDNDRLIRTL-QEMRDlgNTLIVVEHDEDTMMAAD--YLLDIG 563
Cdd:cd03247    99 FSGGERQRLALA-RILLQDAPIV-LLDEPTVGLDPITERQLLSLIfEVLKD--KTLIWITHHLTGIEHMDkiLFLENG 172
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
476-561 5.74e-03

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 40.54  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 476 GLDYLtLSRAAGTLSGGEAQRIRLATQIgSRlTGVLYILDEPSIGL--HQRDN-DRLIRTLQEMRdlGNTLIVVEHDedt 552
Cdd:COG1245   444 GLEKL-LDKNVKDLSGGELQRVAIAACL-SR-DADLYLLDEPSAHLdvEQRLAvAKAIRRFAENR--GKTAMVVDHD--- 515

                  ....*....
gi 1169391345 553 MMAADYLLD 561
Cdd:COG1245   516 IYLIDYISD 524
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
476-584 5.81e-03

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 40.53  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 476 GLDYLtLSRAAGTLSGGEAQRIRLA------TQIgsrltgvlYILDEPSIGLhqrD--NDRLIRtlQEMRDL--GNTLIV 545
Cdd:COG1132   465 GYDTV-VGERGVNLSGGQRQRIAIArallkdPPI--------LILDEATSAL---DteTEALIQ--EALERLmkGRTTIV 530
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169391345 546 VEHDEDTMMAAD--YLLDigpgagihGGQVVSAGTPAEVMQ 584
Cdd:COG1132   531 IAHRLSTIRNADriLVLD--------DGRIVEQGTHEELLA 563
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
488-586 5.87e-03

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 39.49  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 488 TLSGGEAQRIRLATQIGSRLTGVLyiLDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDedtmmaADYLLDIGPGAG 567
Cdd:PRK10895  137 SLSGGERRRVEIARALAANPKFIL--LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN------VRETLAVCERAY 208
                          90       100
                  ....*....|....*....|
gi 1169391345 568 I-HGGQVVSAGTPAEVMQDE 586
Cdd:PRK10895  209 IvSQGHLIAHGTPTEILQDE 228
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
830-924 5.99e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 40.22  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 830 LSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHA---HDIARLLEVLQRLVESGetVLVIEHNLDVI-KTADYIVDLg 905
Cdd:PRK10261  169 LSGGMRQRVMIAMALSCRPA---VLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVaEIADRVLVM- 242
                          90
                  ....*....|....*....
gi 1169391345 906 peggdKGGQIVASGTPEQV 924
Cdd:PRK10261  243 -----YQGEAVETGSVEQI 256
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
806-941 6.17e-03

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 39.35  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 806 IKRKLQTLVDVGLGYMKLGQPaTTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGETV 885
Cdd:PRK11264  122 TARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPE---VILFDEPTSALDPELVGEVLNTIRQLAQEKRTM 197
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169391345 886 LVIEHNL----DVIKTADYIvdlgpeggdKGGQIVASGTPEQVV---KEERsyTGKYLKEILN 941
Cdd:PRK11264  198 VIVTHEMsfarDVADRAIFM---------DQGRIVEQGPAKALFadpQQPR--TRQFLEKFLL 249
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
18-44 6.20e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 39.17  E-value: 6.20e-03
                          10        20
                  ....*....|....*....|....*..
gi 1169391345  18 LKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:COG2401    46 LRDLNLEIEPGEIVLIVGASGSGKSTL 72
PLN03232 PLN03232
ABC transporter C family member; Provisional
822-958 6.41e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 40.73  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345  822 KLGQPATTLSGGEAQRVKLASELHRRStgrTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNLDVIKTADYI 901
Cdd:PLN03232   733 EIGERGVNISGGQKQRVSMARAVYSNS---DIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRI 809
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169391345  902 VDLGPeggdkgGQIVASGTPEQVVKEERSYtgKYLKEILNRDKARMKEKIKEVELSQ 958
Cdd:PLN03232   810 ILVSE------GMIKEEGTFAELSKSGSLF--KKLMENAGKMDATQEVNTNDENILK 858
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
804-928 6.46e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.03  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 804 PKIKRKLQTLVDVGLGYMKLGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVESGE 883
Cdd:PRK15439  115 QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR---ILILDEPTASLTPAETERLFSRIRELLAQGV 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169391345 884 TVLVIEHNL-DVIKTADYIVDLgpeggdKGGQIVASGTPEQVVKEE 928
Cdd:PRK15439  192 GIVFISHKLpEIRQLADRISVM------RDGTIALSGKTADLSTDD 231
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
624-655 6.51e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 38.99  E-value: 6.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169391345 624 LKNAKMSFPLGTFVAVTGVSGSGKSTMINEVL 655
Cdd:cd03250    21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALL 52
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
489-557 6.53e-03

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 38.56  E-value: 6.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169391345 489 LSGGEAQRIRLATQI--GSRLTgvlyILDEPSIGLHQRDNDRLIRTLQEMRDLGNTLIVVEHDEDTMMA-AD 557
Cdd:cd03216    83 LSVGERQMVEIARALarNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiAD 150
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
811-922 6.62e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 40.18  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 811 QTLVDVGLGYM--KLGQPA---TTLSGGEAQRVKLAselhrrstgRTLY------ILDEPTTGLHAHDIARLLEVL-QRL 878
Cdd:COG4178   462 EALEAVGLGHLaeRLDEEAdwdQVLSLGEQQRLAFA---------RLLLhkpdwlFLDEATSALDEENEAALYQLLrEEL 532
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1169391345 879 VESgeTVLVIEHNLDVIKTADYIVDLGPEGgdkGGQIVASGTPE 922
Cdd:COG4178   533 PGT--TVISVGHRSTLAAFHDRVLELTGDG---SWQLLPAEAPA 571
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
16-44 6.66e-03

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 39.05  E-value: 6.66e-03
                          10        20
                  ....*....|....*....|....*....
gi 1169391345  16 HNLKNIDVTIPRNQLVVVTGLSGSGKSSL 44
Cdd:cd03262    14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTL 42
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
854-935 6.87e-03

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 39.29  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 854 YILDEpttGLHAHDIA---RLLEVLQRLVESGETVLVIEHNLDVIKT-ADYIVDLgpeggdKGGQIVASGTPEQVVKEER 929
Cdd:COG1134   168 LLVDE---VLAVGDAAfqkKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWL------EKGRLVMDGDPEEVIAAYE 238

                  ....*.
gi 1169391345 930 SYTGKY 935
Cdd:COG1134   239 ALLAGR 244
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
823-902 6.95e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 40.15  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 823 LGQPATTLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLHAHDIARLLEVLQRLVESGETVLVIEHNL-DVIKTADYI 901
Cdd:PRK09700  403 VNQNITELSGGNQQKVLISKWL---CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRI 479

                  .
gi 1169391345 902 V 902
Cdd:PRK09700  480 A 480
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
456-555 8.18e-03

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 38.78  E-value: 8.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 456 KIAHLILREIQERVGFLVNV-GLDYLtLSRAAGTLSGGEAQRIRLATQIgsrltgV----LYILDEP--SIGLHQRDNDR 528
Cdd:cd03301    98 KLRKVPKDEIDERVREVAELlQIEHL-LDRKPKQLSGGQRQRVALGRAI------VrepkVFLMDEPlsNLDAKLRVQMR 170
                          90       100
                  ....*....|....*....|....*...
gi 1169391345 529 L-IRTLQemRDLGNTLIVVEHDEDTMMA 555
Cdd:cd03301   171 AeLKRLQ--QRLGTTTIYVTHDQVEAMT 196
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
807-895 8.68e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 39.06  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 807 KRKLQTLVDVGLGYMKlGQPATTLSGGEAQRVKLASELHRRSTgrtLYILDEPTTGLHAHDIARLLEVLQRLVES-GETV 885
Cdd:PRK13636  120 KRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPK---VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTI 195
                          90
                  ....*....|
gi 1169391345 886 LVIEHNLDVI 895
Cdd:PRK13636  196 IIATHDIDIV 205
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
801-896 8.86e-03

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 39.40  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 801 ANIPK--IKRKLQTLVD-VGLGYMKLGQPATtLSGGEAQRVKLASELhrrSTGRTLYILDEPTTGLH---AHDIARLLEV 874
Cdd:PRK11153  110 AGTPKaeIKARVTELLElVGLSDKADRYPAQ-LSGGQKQRVAIARAL---ASNPKVLLCDEATSALDpatTRSILELLKD 185
                          90       100
                  ....*....|....*....|..
gi 1169391345 875 LQRlvESGETVLVIEHNLDVIK 896
Cdd:PRK11153  186 INR--ELGLTIVLITHEMDVVK 205
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
463-582 9.61e-03

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 39.36  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169391345 463 REIQERVGFLVN-VGLDYLTlSRAAGTLSGGEAQRI---R-LATQigsrlTGVLyILDEPSIGL--HQRDNDR--LIRTL 533
Cdd:COG1118   108 AEIRARVEELLElVQLEGLA-DRYPSQLSGGQRQRValaRaLAVE-----PEVL-LLDEPFGALdaKVRKELRrwLRRLH 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169391345 534 QEmrdLGNTLIVVEHD-EDTMMAADYLLdIgpgagIHGGQVVSAGTPAEV 582
Cdd:COG1118   181 DE---LGGTTVFVTHDqEEALELADRVV-V-----MNQGRIEQVGTPDEV 221
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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