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Conserved domains on  [gi|489956980|ref|WP_003860287|]
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MULTISPECIES: excinuclease ABC subunit UvrA [Enterobacter]

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;
1-940 0e+00

excinuclease ABC subunit UvrA;


:

Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 2019.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   1 MDKIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDDA 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDKR-NFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 320 MLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYMNDRGDTSVRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 400 FISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 560 IGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 640 GVSGSGKSTLINDTLFPIAQTALNGATLaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 720 EARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQLR 879
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 880 DQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPLL 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-940 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 2019.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   1 MDKIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDDA 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDKR-NFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 320 MLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYMNDRGDTSVRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 400 FISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 560 IGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 640 GVSGSGKSTLINDTLFPIAQTALNGATLaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 720 EARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQLR 879
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 880 DQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPLL 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-940 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1900.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   1 MDKIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:COG0178   83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDda 240
Cdd:COG0178  163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD-- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDKR-NFYYFQ 319
Cdd:COG0178  241 EGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPsSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 320 MLKSLAEHYKFDVEAPWASLSANVHKVILFGSGkENIEFKYMNdRGDTSVRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSD-EKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 400 FISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVID 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 560 IGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVEIPLGVLTCVT 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 640 GVSGSGKSTLINDTLFPIAQTALNGATlAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:COG0178  638 GVSGSGKSTLVNDILYPALARKLNGAK-EKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTP 716
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 720 EARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:COG0178  717 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 796
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQLR 879
Cdd:COG0178  797 FENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLV 876
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 880 DQGNTIVVIEHNLDVIKTADWIVDLgpeggsgggEILVSGTPETVAECEASHTARFLKPLL 940
Cdd:COG0178  877 DKGNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-925 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: 1707.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980    3 KIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   83 ISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEH 162
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  163 TKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDD--- 239
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDeev 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  240 AKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDK-RNFYYF 318
Cdd:TIGR00630 241 AESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKsTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  319 QMLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYMNDRGDTSVRRHPFEGVLHNMERRYKETESSAVREELA 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  399 KFISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  479 TLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVI 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  559 DIGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANPeKVLKLTGARGNNLKDVTLTLPVGLFTCI 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNG-KFLTLKGARENNLKNITVSIPLGLFTCI 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  639 TGVSGSGKSTLINDTLFPIAQTALNGATLaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGV 718
Cdd:TIGR00630 640 TGVSGSGKSTLINDTLYPALANRLNGAKT-VPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  719 PEARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEARE 798
Cdd:TIGR00630 719 PEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  799 FFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQL 878
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*..
gi 489956980  879 RDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVA 925
Cdd:TIGR00630 879 VDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
613-921 1.12e-154

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: 455.54  E-value: 1.12e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQTALNGAtLAEPAPYRDIQGLEHFDKVIDIDQSP 692
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLK-KEQPGNHDRIEGLEHIDKVIVIDQSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 693 IGRTPRSNPATYTGVFTPVRELFagvpearsrgytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpCDQCKGKRYN 772
Cdd:cd03271   80 IGRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYN 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 773 RETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQT 852
Cdd:cd03271  113 RETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKT 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 853 LYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTP 921
Cdd:cd03271  193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
290-399 7.46e-48

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 165.34  E-value: 7.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  290 DPDRVIQNPELSLAGGAIRGWDK-RNFYYFQMLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYmNDRGDTS 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKkRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYY-SRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 489956980  369 VRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
GguA NF040905
sugar ABC transporter ATP-binding protein;
807-901 1.76e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.80  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLqtLMDVGLTyirlgQSATTLSG----GEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQG 882
Cdd:NF040905 120 AREL--LAKVGLD-----ESPDTLVTdigvGKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKAQG 189
                         90       100
                 ....*....|....*....|
gi 489956980 883 NTIVVIEHNL-DVIKTADWI 901
Cdd:NF040905 190 ITSIIISHKLnEIRRVADSI 209
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-940 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 2019.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   1 MDKIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDDA 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDKR-NFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 320 MLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYMNDRGDTSVRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 400 FISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 560 IGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 640 GVSGSGKSTLINDTLFPIAQTALNGATLaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 720 EARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQLR 879
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 880 DQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPLL 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-940 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1900.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   1 MDKIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:COG0178   83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDda 240
Cdd:COG0178  163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD-- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDKR-NFYYFQ 319
Cdd:COG0178  241 EGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPsSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 320 MLKSLAEHYKFDVEAPWASLSANVHKVILFGSGkENIEFKYMNdRGDTSVRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSD-EKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 400 FISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVID 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 560 IGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVEIPLGVLTCVT 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 640 GVSGSGKSTLINDTLFPIAQTALNGATlAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:COG0178  638 GVSGSGKSTLVNDILYPALARKLNGAK-EKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTP 716
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 720 EARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:COG0178  717 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 796
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQLR 879
Cdd:COG0178  797 FENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLV 876
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 880 DQGNTIVVIEHNLDVIKTADWIVDLgpeggsgggEILVSGTPETVAECEASHTARFLKPLL 940
Cdd:COG0178  877 DKGNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-925 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: 1707.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980    3 KIEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   83 ISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEH 162
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  163 TKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVVSDMDD--- 239
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDeev 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  240 AKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDK-RNFYYF 318
Cdd:TIGR00630 241 AESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKsTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  319 QMLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYMNDRGDTSVRRHPFEGVLHNMERRYKETESSAVREELA 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  399 KFISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGLNYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  479 TLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVI 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  559 DIGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANPeKVLKLTGARGNNLKDVTLTLPVGLFTCI 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNG-KFLTLKGARENNLKNITVSIPLGLFTCI 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  639 TGVSGSGKSTLINDTLFPIAQTALNGATLaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGV 718
Cdd:TIGR00630 640 TGVSGSGKSTLINDTLYPALANRLNGAKT-VPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  719 PEARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEARE 798
Cdd:TIGR00630 719 PEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  799 FFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHQL 878
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*..
gi 489956980  879 RDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVA 925
Cdd:TIGR00630 879 VDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1-940 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 660.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980    1 MDKIEVR--GARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEG 78
Cdd:PRK00635    1 MPSLPVRlsGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   79 LSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKEr 158
Cdd:PRK00635   81 LSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAK- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  159 kgeHTKTLENLASQGYIRARIDGEVCD----LSDPpkleLQKKHTIEVVIDRFKVREDLATRLAESFETALELSGGTAVV 234
Cdd:PRK00635  160 ---DILAIRECLRQGFTKVRIDGEISPiykfLTSG----IPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  235 SdmddAKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNpELS-------LAGGAi 307
Cdd:PRK00635  233 H----FDNQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLIQQ-NLSieenccpFAGNC- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  308 rgwdkRNFYYFQMLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYMNDR-GDTSVRRHPFEGVLHNMERRYK 386
Cdd:PRK00635  307 -----STYLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVLPVRLFDGTlGKKTLTHKVWRGVLNEIGEKVR 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  387 ETESSAvrEELAKFISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAkiaEKVLKEIGDR 466
Cdd:PRK00635  382 YSNKPS--RYLPKGTSATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKSLSI---EEVLQGLKSR 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEH 546
Cdd:PRK00635  457 LSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  547 DEDAIRAADHVIDIGPGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRvaANPEKVLKLTGARGNNLKDV 626
Cdd:PRK00635  537 DEQMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKR--TNSLGTLTLSKATKHNLKDL 614
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  627 TLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQTALNGatlaEPAPYRDIQGLEhFDKVIDIDQSPIGRTPRSNPATYTG 706
Cdd:PRK00635  615 TISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQ----GFCSNLSIQWGA-ISRLVHITRDLPGRSQRSIPLTYIK 689
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  707 VFTPVRELFAGVPEARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPdiyVPCDQCKGKRYNRETLEIKYKGKTIH 786
Cdd:PRK00635  690 AFDDLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIA 766
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  787 EVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFA 866
Cdd:PRK00635  767 DILEMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTH 846
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980  867 DIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEaSHTARFLKPLL 940
Cdd:PRK00635  847 DIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELIHLH-TPTAKALRPYL 919
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
613-921 1.12e-154

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: 455.54  E-value: 1.12e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQTALNGAtLAEPAPYRDIQGLEHFDKVIDIDQSP 692
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLK-KEQPGNHDRIEGLEHIDKVIVIDQSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 693 IGRTPRSNPATYTGVFTPVRELFagvpearsrgytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpCDQCKGKRYN 772
Cdd:cd03271   80 IGRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYN 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 773 RETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQT 852
Cdd:cd03271  113 RETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKT 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 853 LYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTP 921
Cdd:cd03271  193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-939 2.98e-105

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 359.91  E-value: 2.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980    4 IEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQflSLMEK---PDVDHIEGLS 80
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQ--ALIKKtplPSVDKVTGLS 1018
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLYARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERkg 160
Cdd:PRK00635 1019 PVIAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPIPKEE-- 1096
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKhtiEVVIDRFKVREDLATRLAESFETALELSGgTAVVSDMDDA 240
Cdd:PRK00635 1097 DLFIYLQEKLKEGFLKLYANEQFYDLDEPLPTSLENP---AIVIQHTKISEKNLSSLLSSLTLAFSLSS-SICLHIEYAG 1172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  241 KAEELLFSANFACPIcGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFD----PDRVIQNPELSLAggairgwdkRNFY 316
Cdd:PRK00635 1173 TSLSLTYRLGWQDSS-GNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCSllphKEKIAHYTPLSLF---------TLFF 1242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  317 ---YFQMLKSLAEHYKFDVEAPWASLSANVHKVILFGS----GKENIEFKYMNdrgdtsvrRHPFEGVLHNMerrykete 389
Cdd:PRK00635 1243 pnqDPKPVYPLLKELGIPSIALFQELDTLSFESLCLGTqqhpGLNALLMEAML--------MESEEPLPPPL-------- 1306
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  390 ssavreelakfISNRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLKlSGQrakiAEKVLKEIGDRLKF 469
Cdd:PRK00635 1307 -----------ISKTPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTIH-DDE----EPSIIQDLLNRLTF 1370
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  470 LVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDED 549
Cdd:PRK00635 1371 IDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGS 1450
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  550 AIRAADHVIDIGPGAGVHGGQVVAEGTLKDimavpesLTGQYMSGKRKIEVPKQRVAANPekvlkltgargNNLKDVTLT 629
Cdd:PRK00635 1451 LAEHADHLIHLGPGSGPQGGYLLSTSALKQ-------SQPDLHNTRSSEETPTLSVSLSI-----------HTIQNLNVS 1512
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  630 LPVGLFTCITGVSGSGKSTLINDTLFPIAQTALNgatlaepapyrdiQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFT 709
Cdd:PRK00635 1513 APLHSLVAISGVSGSGKTSLLLEGFYKQACALIE-------------KGPSVFSEIIFLDSHPQISSQRSDISTYFDIAP 1579
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  710 PVRELFAGVPEARSRGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVL 789
Cdd:PRK00635 1580 SLRNFYASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLL 1659
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  790 DMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQ 869
Cdd:PRK00635 1660 QTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKS 1739
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  870 QLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPL 939
Cdd:PRK00635 1740 ALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCNL 1809
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-116 8.85e-75

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: 244.86  E-value: 8.85e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   4 IEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAI 83
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489956980  84 SIEQKSTSHNPRSTVGTITEIHDYLRLLYARVG 116
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
463-575 1.67e-68

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: 227.53  E-value: 1.67e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 463 IGDRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVI 542
Cdd:cd03270  114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489956980 543 VVEHDEDAIRAADHVIDIGPGAGVHGGQVVAEG 575
Cdd:cd03270  194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
290-399 7.46e-48

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 165.34  E-value: 7.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  290 DPDRVIQNPELSLAGGAIRGWDK-RNFYYFQMLKSLAEHYKFDVEAPWASLSANVHKVILFGSGKENIEFKYmNDRGDTS 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKkRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYY-SRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 489956980  369 VRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
617-904 1.29e-47

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: 169.36  E-value: 1.29e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 617 GARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQTALNgATLAepaPYRDiQGLEHFDK-----------V 685
Cdd:cd03270    5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYV-ESLS---AYAR-QFLGQMDKpdvdsieglspA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 686 IDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVPearsrgytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpcdq 765
Cdd:cd03270   80 IAIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG---------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 766 ckgkrynretleikykgktihevldmtieeareffdavpaLARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELS 845
Cdd:cd03270  114 ----------------------------------------IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIG 153
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 846 KRGTGqTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03270  154 SGLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
130-238 1.70e-47

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 164.58  E-value: 1.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  130 QTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVIDRFKV 209
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 489956980  210 REDLATRLAESFETALELSGGTAVVSDMD 238
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
406-576 6.31e-46

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: 165.87  E-value: 6.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 406 CATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNLklsgqrAKIAEKvlkeigdrLKFLVNVGLNYLTLSRSAE 485
Cdd:cd03271  103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENI------PKIARK--------LQTLCDVGLGYIKLGQPAT 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLASQIGAGLVG-VMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIGPGA 564
Cdd:cd03271  169 TLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
                        170
                 ....*....|..
gi 489956980 565 GVHGGQVVAEGT 576
Cdd:cd03271  249 GDGGGQVVASGT 260
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
465-575 4.42e-45

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: 160.18  E-value: 4.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 465 DRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVV 544
Cdd:cd03238   66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489956980 545 EHDEDAIRAADHVIDIGPGAGVHGGQVVAEG 575
Cdd:cd03238  146 EHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
760-936 2.35e-43

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: 170.58  E-value: 2.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  760 YVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREFFD-----------AVPALAR---KLQTLMDVGLTYIRLGQ 825
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNqltltpeekkiAEEVLKEireRLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  826 SATTLSGGEAQRVKLARELSKRGTGqTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLG 905
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         170       180       190
                  ....*....|....*....|....*....|.
gi 489956980  906 PEGGSGGGEILVSGTPETVAECEASHTARFL 936
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
784-919 3.13e-41

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: 149.40  E-value: 3.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 784 TIHEVLDMTIEEAREFFDAVPALA-RKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGqTLYILDEPTTG 862
Cdd:cd03238   41 GLYASGKARLISFLPKFSRNKLIFiDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-TLFILDEPSTG 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489956980 863 LHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSG 919
Cdd:cd03238  120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
406-716 2.07e-32

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 136.88  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  406 CATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFNNlklsgqRAKIAEKVlkeigdrlKFLVNVGLNYLTLSRSAE 485
Cdd:PRK00635  743 CPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLD------EPSIHEKI--------HALCSLGLDYLPLGRPLS 808
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  486 TLSGGEAQRIRLASQIGAGLVG-VMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIGPGA 564
Cdd:PRK00635  809 SLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEG 888
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  565 GVHGGQVVAEGTLKDIMAV--PESLTGQ-YMSGKRKI-EVPKQRVAANPEKVLKLTGARGNNLKDVTLTLPVGLFTCITG 640
Cdd:PRK00635  889 GNLGGYLLASCSPEELIHLhtPTAKALRpYLSSPQELpYLPDPSPKPPVPADITIKNAYQHNLKHIDLSLPRNALTAVTG 968
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  641 VSGSGKSTLINDTLFPIAQTAlngatLAEPAPYRDIQGL------------EHFDKVIDIDQSPIGRTPRSNPATYTGVF 708
Cdd:PRK00635  969 PSASGKHSLVFDILYAAGNIA-----YAELFPPYIRQALikktplpsvdkvTGLSPVIAIEKTSASKNSNHSVASALEIS 1043

                  ....*...
gi 489956980  709 TPVRELFA 716
Cdd:PRK00635 1044 NGLEKLFA 1051
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
461-902 9.31e-21

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: 96.90  E-value: 9.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 461 KEIGDR-LKFLVNVGLNYLtLSRSAETLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGL---HQRDNERLLGTLVhlRN 536
Cdd:COG1123  117 AEARARvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL-ALDPDLL-IADEPTTALdvtTQAEILDLLRELQ--RE 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 537 LGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVPKQRVAANPekVLKL 615
Cdd:COG1123  192 RGTTVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEP--LLEV 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 616 TG------ARGNN----LKDVTLTLPVGLFTCITGVSGSGKSTLindtlfpiAQTALngatlaepapyrdiqGLEHFDK- 684
Cdd:COG1123  264 RNlskrypVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTL--------ARLLL---------------GLLRPTSg 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 685 VIDIDQSPIGRTPRSNpatytgvftpVRELFAGV------PEArsrgytpgrfSFNVRggrceacqgdgvikvemhflpd 758
Cdd:COG1123  321 SILFDGKDLTKLSRRS----------LRELRRRVqmvfqdPYS----------SLNPR---------------------- 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 759 iyvpcdqckgkrynretleikykgKTIHEvldmTIEEAREFFDAVPA--LARKLQTLMD-VGLTYIRLGQSATTLSGGEA 835
Cdd:COG1123  359 ------------------------MTVGD----IIAEPLRLHGLLSRaeRRERVAELLErVGLPPDLADRYPHELSGGQR 410
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 836 QRVKLARELSkrgTGQTLYILDEPTTGLhfaD--IQ-QLLDVLHQLRDQGN-TIVVIEHNLDVIKT-ADWIV 902
Cdd:COG1123  411 QRVAIARALA---LEPKLLILDEPTSAL---DvsVQaQILNLLRDLQRELGlTYLFISHDLAVVRYiADRVA 476
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
4-65 1.19e-17

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: 81.60  E-value: 1.19e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980   4 IEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFL 65
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL 62
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
4-112 1.50e-17

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: 83.43  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   4 IEVRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAegqrryveslSAYARQFLSLMEKPDVDHIEGL---S 80
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489956980  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLY 112
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELF 102
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
830-904 7.38e-17

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: 78.83  E-value: 7.38e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 830 LSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTA-DWIVDL 904
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
623-902 1.65e-16

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: 79.11  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqtalngatlaepapyRDIQGLehfdkvididqspigrtprsNPA 702
Cdd:cd03235   15 LEDVSFEVKPGEFLAIVGPNGAGKSTLL-----------------------KAILGL--------------------LKP 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 703 TyTGVFTpvrelFAGVPEARSR---GYTPGRFSFNVrggrceacqgDGVIKVE----MHFLPDIyvpcdqCKGKRYNRET 775
Cdd:cd03235   52 T-SGSIR-----VFGKPLEKERkriGYVPQRRSIDR----------DFPISVRdvvlMGLYGHK------GLFRRLSKAD 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 776 LEIkykgktIHEVLDMtieeareffdavpalarklqtlmdVGLTYIRLgQSATTLSGGEAQRVKLARELSKRGTgqtLYI 855
Cdd:cd03235  110 KAK------VDEALER------------------------VGLSELAD-RQIGELSGGQQQRVLLARALVQDPD---LLL 155
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489956980 856 LDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:cd03235  156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
807-902 9.75e-16

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: 77.12  E-value: 9.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQTLMDVGLtYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIV 886
Cdd:cd03225  113 ERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLA---MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTII 188
                         90
                 ....*....|....*..
gi 489956980 887 VIEHNLDVIKT-ADWIV 902
Cdd:cd03225  189 IVTHDLDLLLElADRVI 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
623-929 1.04e-15

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 77.82  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqtALNGatLAEPApyrdiQG-LEHFDKVIDIDQSPIG------R 695
Cdd:COG1121   22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLK---------AILG--LLPPT-----SGtVRLFGKPPRRARRRIGyvpqraE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 696 TPRSNPATytgvftpVRELfagvpearsrgytpgrfsfnVRGGRceacqgdgviKVEMHFLpdiyvpcdqckgKRYNRET 775
Cdd:COG1121   86 VDWDFPIT-------VRDV--------------------VLMGR----------YGRRGLF------------RRPSRAD 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 776 LEIkykgktIHEVLDMT-IEEareffdavpaLARKlqtlmdvgltyiRLGQsattLSGGEAQRVKLARELSKRGtgqTLY 854
Cdd:COG1121  117 REA------VDEALERVgLED----------LADR------------PIGE----LSGGQQQRVLLARALAQDP---DLL 161
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 855 ILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD-VIKTADWIVDLgpeggsgGGEILVSGTPETVAECEA 929
Cdd:COG1121  162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLL-------NRGLVAHGPPEEVLTPEN 230
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
623-904 1.64e-15

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: 80.57  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdTL--FpiaQTALNGATLAEPAPYRDIQGLEHFDKVIDIDQSPigrtprsn 700
Cdd:COG4988  353 LDGLSLTIPPGERVALVGPSGAGKSTLLN-LLlgF---LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNP-------- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 701 patytgvftpvrELFAG-VPEarsrgytpgrfsfNVRGGRCEAcqgdgvikvemhflpdiyvpcdqckgkrynreTLEik 779
Cdd:COG4988  421 ------------YLFAGtIRE-------------NLRLGRPDA--------------------------------SDE-- 441
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 780 ykgkTIHEVLDMTieEAREFfdaVPALARKLQTlmdvgltyiRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEP 859
Cdd:COG4988  442 ----ELEAALEAA--GLDEF---VAALPDGLDT---------PLGEGGRGLSGGQAQRLALARALLRDA---PLLLLDEP 500
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489956980 860 TTGLhfaDI---QQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:COG4988  501 TAHL---DAeteAEILQALRRLA-KGRTVILITHRLALLAQADRILVL 544
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
445-587 6.48e-15

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: 75.06  E-value: 6.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 445 NLKLSgqRAKIAEKVLKeigdrlkFLVNVGLNYLtLSRSAETLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLH 520
Cdd:COG1122  103 NLGLP--REEIRERVEE-------ALELVGLEHL-ADRPPHELSGGQKQRVAIAGVL------AMepevLVLDEPTAGLD 166
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 521 QRDNERLLGTLVHLRNLGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGQVVAEGTLKDIMAVPESL 587
Cdd:COG1122  167 PRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREVFSDYELL 228
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
487-562 1.15e-14

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: 72.39  E-value: 1.15e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 487 LSGGEAQRIRLASQIG--AGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIGP 562
Cdd:cd03227   78 LSGGEKELSALALILAlaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
615-924 9.39e-14

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: 72.00  E-value: 9.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 615 LTGARGNN--LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqtALNGatLAEPApyrdiQGlehfdkVIDIDQSP 692
Cdd:COG1120    7 LSVGYGGRpvLDDVSLSLPPGEVTALLGPNGSGKSTLLR---------ALAG--LLKPS-----SG------EVLLDGRD 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 693 IGRTPRsnpatytgvftpvRELfagvpeARSRGY----TPGRFSFNVRggrcEAcqgdgvikVEM----Hflpdiyvpcd 764
Cdd:COG1120   65 LASLSR-------------REL------ARRIAYvpqePPAPFGLTVR----EL--------VALgrypH---------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 765 QCKGKRYNRETLEIkykgktIHEVLDMTieeareffdavpalarklqtlmdvGLTYIRlGQSATTLSGGEAQRVKLAREL 844
Cdd:COG1120  104 LGLFGRPSAEDREA------VEEALERT------------------------GLEHLA-DRPVDELSGGERQRVLIARAL 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 845 skrgTGQT-LYILDEPTTGLhfaDI---QQLLDVLHQL-RDQGNTIVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVS 918
Cdd:COG1120  153 ----AQEPpLLLLDEPTSHL---DLahqLEVLELLRRLaRERGRTVVMVLHDLNlAARYADRLVLL------KDGRIVAQ 219

                 ....*.
gi 489956980 919 GTPETV 924
Cdd:COG1120  220 GPPEEV 225
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
816-904 9.45e-14

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: 70.08  E-value: 9.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 816 VGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQ-TLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDV 894
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILALASLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|
gi 489956980 895 IKTADWIVDL 904
Cdd:cd03227  144 AELADKLIHI 153
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
811-902 1.21e-13

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: 71.21  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 811 QTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEH 890
Cdd:COG1122  117 EALELVGLEHLA-DRPPHELSGGQKQRVAIAGVLA---MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTH 192
                         90
                 ....*....|...
gi 489956980 891 NLD-VIKTADWIV 902
Cdd:COG1122  193 DLDlVAELADRVI 205
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
790-902 2.12e-13

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 70.86  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 790 DMTIEEAREFF------DAVPALARKLQTLMDVGLTyIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGL 863
Cdd:COG1131   87 DLTVRENLRFFarlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHD---PELLILDEPTSGL 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489956980 864 hfaD---IQQLLDVLHQLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG1131  163 ---DpeaRRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVA 202
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
805-893 5.45e-13

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: 68.23  E-value: 5.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKL----QTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELskrgTGQT-LYILDEPTTGLHFADIQQLLDVLHQL- 878
Cdd:cd03214   70 ELARKIayvpQALELLGLAHLA-DRPFNELSGGERQRVLLARAL----AQEPpILLLDEPTSHLDIAHQIELLELLRRLa 144
                         90
                 ....*....|....*
gi 489956980 879 RDQGNTIVVIEHNLD 893
Cdd:cd03214  145 RERGKTVVMVLHDLN 159
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
487-563 8.09e-13

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: 66.88  E-value: 8.09e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 487 LSGGEAQRIRLASQIgAGLVGVmYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHD-EDAIRAADHVIDIGPG 563
Cdd:cd00267   81 LSGGQRQRVALARAL-LLNPDL-LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
830-902 1.06e-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: 1.06e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:cd03216   83 LSVGERQMVEIARALA---RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
799-925 2.36e-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: 67.46  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 799 FFDAVPALARKLQTLMD-VGLTYiRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQ 877
Cdd:cd03219  113 ARREEREARERAEELLErVGLAD-LADRPAGELSYGQQRRLEIARALA---TDPKLLLLDEPAAGLNPEETEELAELIRE 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489956980 878 LRDQGNTIVVIEHNLDVI-KTADWIVDLgpeggsGGGEILVSGTPETVA 925
Cdd:cd03219  189 LRERGITVLLVEHDMDVVmSLADRVTVL------DQGRVIAEGTPDEVR 231
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
400-563 3.38e-12

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 66.76  E-value: 3.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 400 FISNRSCATCEGTRLRREARHVFVEntalPTISDMSIGHAMDF---FNNLKLSGQRAKiaekvlkeigdrlKFLVNVGLN 476
Cdd:COG4619   58 YLDGKPLSAMPPPEWRRQVAYVPQE----PALWGGTVRDNLPFpfqLRERKFDRERAL-------------ELLERLGLP 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 477 YLTLSRSAETLSGGEAQRIRLAS------QIgaglvgvmYVLDEPSIGLHQrDNERLLGTLVH--LRNLGNTVIVVEHDE 548
Cdd:COG4619  121 PDILDKPVERLSGGERQRLALIRalllqpDV--------LLLDEPTSALDP-ENTRRVEELLReyLAEEGRAVLWVSHDP 191
                        170
                 ....*....|....*.
gi 489956980 549 DAI-RAADHVIDIGPG 563
Cdd:COG4619  192 EQIeRVADRVLTLEAG 207
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
445-558 5.37e-12

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: 65.95  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 445 NLKLSG-QRAKIAEKVLKEigdrlkflvnVGLNYLtLSRSAETLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGL 519
Cdd:cd03225  103 NLGLPEeEIEERVEEALEL----------VGLEGL-RDRSPFTLSGGQKQRVAIAGVL------AMdpdiLLLDEPTAGL 165
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489956980 520 HQRDNERLLGTLVHLRNLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:cd03225  166 DPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVI 205
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
623-896 1.66e-11

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 64.45  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqtALNGatLAEPApyrdiQGLEHFDKViDIDQSPigrtprsnpa 702
Cdd:COG4619   16 LSPVSLTLEAGECVAITGPSGSGKSTLLR---------ALAD--LDPPT-----SGEIYLDGK-PLSAMP---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 703 tytgvftpvrelfagVPEARSR-GY---TPGRFSFNVRggrceacqgdgvikvemHFLPDIYvpcdQCKGKRYNRETLEi 778
Cdd:COG4619   69 ---------------PPEWRRQvAYvpqEPALWGGTVR-----------------DNLPFPF----QLRERKFDRERAL- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 779 kykgktihevldmtieeareffdavPALARklqtlmdVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDE 858
Cdd:COG4619  112 -------------------------ELLER-------LGLPPDILDKPVERLSGGERQRLALIRALL---LQPDVLLLDE 156
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489956980 859 PTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIK 896
Cdd:COG4619  157 PTSALDPENTRRVEELLREYLAEEGrAVLWVSHDPEQIE 195
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
473-589 2.50e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 65.43  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 473 VGLNYLTLSRSAETLSGGEAQRIRLAsqigaglvGV------MYVLDEPSIGLHQRDNERLLGTLVHLRNLGN-TVIVVE 545
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRVAIA--------GVlamepeVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVT 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489956980 546 HD-EDAIRAADHVIDIgpgagvHGGQVVAEGTLKDIMAVPESLTG 589
Cdd:PRK13634 204 HSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEA 242
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
822-893 2.56e-11

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: 64.38  E-value: 2.56e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD 893
Cdd:cd03224  125 RRKQLAGTLSGGEQQMLAIARALMSR---PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNAR 193
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
801-892 4.46e-11

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 64.09  E-value: 4.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 801 DAVPALARKLQtLMDvgltyiRLGQSATTLSGGEAQRVKLAREL-----SKRGTGQtLYILDEPTTGLhfaDIQQ---LL 872
Cdd:COG4138  105 QLLAQLAEALG-LED------KLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEGQ-LLLLDEPMNSL---DVAQqaaLD 173
                         90       100
                 ....*....|....*....|
gi 489956980 873 DVLHQLRDQGNTIVVIEHNL 892
Cdd:COG4138  174 RLLRELCQQGITVVMSSHDL 193
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
830-904 6.68e-11

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: 61.85  E-value: 6.68e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
830-904 8.20e-11

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: 61.63  E-value: 8.20e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDI---QQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03228   97 LSGGQRQRIAIARALLRDP---PILILDEATSAL---DPeteALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVL 167
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
452-895 1.07e-10

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 65.05  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 452 RAKIAEKVlKEIGDRLKFLVNvglnyltLSRSAETLSGGEAQR---IRLASQiGAGLVgvmyVLDEPSIGLHQRDNERLL 528
Cdd:COG3845  115 RKAARARI-RELSERYGLDVD-------PDAKVEDLSVGEQQRveiLKALYR-GARIL----ILDEPTAVLTPQEADELF 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 529 GTLVHLRNLGNTVIVVEH--DEdAIRAADHVIdigpgagV-HGGQVVAEGTLKDimAVPESLTgQYMSGkRKIEVPKQRV 605
Cdd:COG3845  182 EILRRLAAEGKSIIFITHklRE-VMAIADRVT-------VlRRGKVVGTVDTAE--TSEEELA-ELMVG-REVLLRVEKA 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 606 AANP-EKVLKL-----TGARGNN-LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqtALNGatLAEPAPYRdiqg 678
Cdd:COG3845  250 PAEPgEVVLEVenlsvRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAE---------ALAG--LRPPASGS---- 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 679 lehfdkvIDIDQSPIGR-TPRSnpatytgvftpVREL-FAGVPEARsrgytpgrfsfnvrggrceacQGDGVikvemhfl 756
Cdd:COG3845  315 -------IRLDGEDITGlSPRE-----------RRRLgVAYIPEDR---------------------LGRGL-------- 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 757 pdiyvpcdqckgkrynretleikykgktiheVLDMTIEE------------AREFF---DAVPALARKLQTLMDVgltyi 821
Cdd:COG3845  348 -------------------------------VPDMSVAEnlilgryrrppfSRGGFldrKAIRAFAEELIEEFDV----- 391
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956980 822 R---LGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI 895
Cdd:COG3845  392 RtpgPDTPARSLSGGNQQKVILARELSRDP---KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEI 465
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
830-902 1.12e-10

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: 61.26  E-value: 1.12e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaDI---QQLLDVLHQLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:cd03230   96 LSGGMKQRLALAQALLHD---PELLILDEPTSGL---DPesrREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
824-892 1.14e-10

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 63.21  E-value: 1.14e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956980 824 GQSATTLSGGEAQRVKLAREL-----SKRGTGQTLyILDEPTTGLhfaDI---QQLLDVLHQLRDQGNTIVVIEHNL 892
Cdd:COG4559  128 GRSYQTLSGGEQQRVQLARVLaqlwePVDGGPRWL-FLDEPTSAL---DLahqHAVLRLARQLARRGGGVVAVLHDL 200
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
623-902 1.25e-10

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: 62.57  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqtalngatlaepapyRDIQGLEHFDK-VIDIDqspiGRTPRSNP 701
Cdd:COG4555   17 LKDVSFTAKDGEITGLLGPNGAGKTTLL-----------------------RMLAGLLKPDSgSILID----GEDVRKEP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 702 atytgvftpvrelfagvPEARSR-GYTPGRFSFnvrggrceacqgdgvikvemhflpdiyvpcdqckgkrYNRETLE--I 778
Cdd:COG4555   70 -----------------REARRQiGVLPDERGL-------------------------------------YDRLTVRenI 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 779 KYKGkTIHevlDMTIEEAREFFDAvpaLARKLQtLMDVgltyirLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDE 858
Cdd:COG4555   96 RYFA-ELY---GLFDEELKKRIEE---LIELLG-LEEF------LDRRVGELSTGMKKKVALARALVHD---PKVLLLDE 158
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489956980 859 PTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG4555  159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVV 203
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
791-896 1.34e-10

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: 62.14  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEA-----REFFDAVPALARK---LQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG 862
Cdd:cd03257   99 MTIGEQiaeplRIHGKLSKKEARKeavLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA---LNPKLLIADEPTSA 175
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489956980 863 LHfADIQ-QLLDVLHQLRDQ-GNTIVVIEHNLDVIK 896
Cdd:cd03257  176 LD-VSVQaQILDLLKKLQEElGLTLLFITHDLGVVA 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
623-902 1.47e-10

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: 64.92  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqtALNGATlaePAPYRdIQGLEHFDKViDIDQSPIGrtprsnpa 702
Cdd:COG1123   22 VDGVSLTIAPGETVALVGESGSGKSTLAL---------ALMGLL---PHGGR-ISGEVLLDGR-DLLELSEA-------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 703 tytgvftpvrelfagvpearsrgytpgrfsfnVRGGRceacqgdgvikVEMHFlpdiyvpcdQCKGKRYNRETLeikykG 782
Cdd:COG1123   80 --------------------------------LRGRR-----------IGMVF---------QDPMTQLNPVTV-----G 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 783 KTIHEVL---DMTIEEAREffdavpalaRKLQTLMDVGLTyIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEP 859
Cdd:COG1123  103 DQIAEALenlGLSRAEARA---------RVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDPD---LLIADEP 169
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489956980 860 TTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG1123  170 TTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVaEIADRVV 214
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
805-904 1.57e-10

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 61.98  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGN 883
Cdd:COG1136  123 ERAREL--LERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNRP---KLILADEPTGNLDSKTGEEVLELLRELnRELGT 196
                         90       100
                 ....*....|....*....|.
gi 489956980 884 TIVVIEHNLDVIKTADWIVDL 904
Cdd:COG1136  197 TIVMVTHDPELAARADRVIRL 217
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
619-904 2.92e-10

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: 63.84  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  619 RGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQT----ALNGATLAE--PAPYRDiqglehfdKVIDIDQSP 692
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTegsiAVNGVPLADadADSWRD--------QIAWVPQHP 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  693 igrtprsnpatytgvftpvrelfagvpearsrGYTPGRFSFNVRGGRCEAcqgdgvikvemhflpdiyvpcdqckgkryn 772
Cdd:TIGR02857 406 --------------------------------FLFAGTIAENIRLARPDA------------------------------ 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  773 retleikyKGKTIHEVLdmtieEAREFFDAVPALARKLQTlmdvgltyiRLGQSATTLSGGEAQRVKLARELSKrgtGQT 852
Cdd:TIGR02857 424 --------SDAEIREAL-----ERAGLDEFVAALPQGLDT---------PIGEGGAGLSGGQAQRLALARAFLR---DAP 478
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489956980  853 LYILDEPTTGLHFADIQQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIVVL 529
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
822-904 3.97e-10

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 63.63  E-value: 3.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLrDQGNTIVVIEHNLDVIKTADWI 901
Cdd:COG4987  464 WLGEGGRRLSGGERRRLALARALLRD---APILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRI 539

                 ...
gi 489956980 902 VDL 904
Cdd:COG4987  540 LVL 542
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
784-892 5.05e-10

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 60.94  E-value: 5.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 784 TIHEVLDMTIEEAREFFDAVPALARklQTLMDVGLTYIRlGQSATTLSGGEAQRVKLAR---ELSKRGTGQTLYILDEPT 860
Cdd:PRK13548  92 TVEEVVAMGRAPHGLSRAEDDALVA--AALAQVDLAHLA-GRDYPQLSGGEQQRVQLARvlaQLWEPDGPPRWLLLDEPT 168
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489956980 861 TGLhfaDI---QQLLDVLHQL-RDQGNTIVVIEHNL 892
Cdd:PRK13548 169 SAL---DLahqHHVLRLARQLaHERGLAVIVVLHDL 201
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
473-575 5.33e-10

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: 59.37  E-value: 5.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 473 VGLNYLtLSRSAETLSGGEAQRIRLAsqigAGLVGV--MYVLDEPSIGL---HQRdneRLLGTLVHL-RNLGNTVIVVEH 546
Cdd:cd03214   85 LGLAHL-ADRPFNELSGGERQRVLLA----RALAQEppILLLDEPTSHLdiaHQI---ELLELLRRLaRERGKTVVMVLH 156
                         90       100       110
                 ....*....|....*....|....*....|
gi 489956980 547 DED-AIRAADHVIDIgpgagvHGGQVVAEG 575
Cdd:cd03214  157 DLNlAARYADRVILL------KDGRIVAQG 180
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
487-582 5.93e-10

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: 62.85  E-value: 5.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLHQRDNERLLGTLVHLRNlGNTVIVVEHDEDAIRAADHVIDi 560
Cdd:COG4988  474 LSGGQAQRLALArallrdAPL--------LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILV- 543
                         90       100
                 ....*....|....*....|..
gi 489956980 561 gpgagVHGGQVVAEGTLKDIMA 582
Cdd:COG4988  544 -----LDDGRIVEQGTHEELLA 560
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
770-899 7.79e-10

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 60.28  E-value: 7.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 770 RYNRETLEIKYKGKTIHEvlDMTIEEARE---FFDAVPALARKLQTLMDV-GLTYIRLGQSATTLSGGEAQRVKLARELS 845
Cdd:PRK11614  76 KIMREAVAIVPEGRRVFS--RMTVEENLAmggFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 846 KRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD-VIKTAD 899
Cdd:PRK11614 154 SQ---PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLAD 205
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
482-585 9.58e-10

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: 59.76  E-value: 9.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 482 RSAETLSGGEAQRIrlasQIGAGLVG--VMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVI 558
Cdd:cd03219  139 RPAGELSYGQQRRL----EIARALATdpKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVT 214
                         90       100
                 ....*....|....*....|....*...
gi 489956980 559 digpgagV-HGGQVVAEGTLKDIMAVPE 585
Cdd:cd03219  215 -------VlDQGRVIAEGTPDEVRNNPR 235
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
805-904 1.00e-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: 59.43  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGN 883
Cdd:cd03255  117 RRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIARALANDP---KIILADEPTGNLDSETGKEVMELLRELnKEAGT 192
                         90       100
                 ....*....|....*....|.
gi 489956980 884 TIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03255  193 TIVVVTHDPELAEYADRIIEL 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
829-904 1.01e-09

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: 59.19  E-value: 1.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 829 TLSGGEAQRVKLARE-LSKRgtgqTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI-KTADWIVDL 904
Cdd:cd03226  126 SLSGGQKQRLAIAAAlLSGK----DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLL 199
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
623-904 1.77e-09

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: 61.77  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqtalngatLaepapyrdIQGLEHFDK-VIDIDQSPIGRTPRSNP 701
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLLK---------------L--------LLGLYEPTSgRILIDGIDLRQIDPASL 547
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 702 ATYTGVFTPVRELFAG-VPEarsrgytpgrfsfNVRGGRceacqgdgvikvemhflPDIyvpcdqckgkrynreTLEiky 780
Cdd:COG2274  548 RRQIGVVLQDVFLFSGtIRE-------------NITLGD-----------------PDA---------------TDE--- 579
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 781 kgkTIHEVLDMTieEAREFfdaVPALARKLQTLmdvgltyirLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPT 860
Cdd:COG2274  580 ---EIIEAARLA--GLHDF---IEALPMGYDTV---------VGEGGSNLSGGQRQRLAIARALLRN---PRILILDEAT 639
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489956980 861 TGLHFADIQQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:COG2274  640 SALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVL 682
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
826-904 2.07e-09

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: 58.98  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 826 SATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKT-ADWIVDL 904
Cdd:COG4778  149 PPATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDV 225
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
830-902 2.64e-09

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: 57.44  E-value: 2.64e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELskrGTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:cd03215  105 LSGGNQQKVVLARWL---ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGLCDRIL 175
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
482-581 2.76e-09

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 58.87  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 482 RSAETLSGGEAQRIRLASQIGAGLVGVMyvLDEPSIGL---HQRDnerLLGTLVHLRNLGNTVIVVEHD-EDAIRAADHV 557
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlNQASRYCDHL 208
                         90       100
                 ....*....|....*....|....
gi 489956980 558 IDIgpgagvHGGQVVAEGTLKDIM 581
Cdd:PRK11231 209 VVL------ANGHVMAQGTPEEVM 226
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
801-892 2.91e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 58.79  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 801 DAVPALARKLQtLMDvgltyiRLGQSATTLSGGEAQRVKLA-------RELSKRGtgqTLYILDEPTTGLhfaDIQQ--L 871
Cdd:PRK03695 105 SALNEVAEALG-LDD------KLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAG---QLLLLDEPMNSL---DVAQqaA 171
                         90       100
                 ....*....|....*....|..
gi 489956980 872 LD-VLHQLRDQGNTIVVIEHNL 892
Cdd:PRK03695 172 LDrLLSELCQQGIAVVMSSHDL 193
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
791-893 3.40e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 59.33  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREffdavpaLARKLQTLmdVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK13651 136 VSKEEAKK-------RAAKYIEL--VGLDESYLQRSPFELSGGQKRRVALAGILAME---PDFLVFDEPTAGLDPQGVKE 203
                         90       100
                 ....*....|....*....|...
gi 489956980 871 LLDVLHQLRDQGNTIVVIEHNLD 893
Cdd:PRK13651 204 ILEIFDNLNKQGKTIILVTHDLD 226
cbiO PRK13645
energy-coupling factor transporter ATPase;
457-602 3.51e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 59.25  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 457 EKVLKEIGDRLKfLVNVGLNYLtlSRSAETLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLVHL-R 535
Cdd:PRK13645 124 QEAYKKVPELLK-LVQLPEDYV--KRSPFELSGGQKRRVALAGIIA--MDGNTLVLDEPTGGLDPKGEEDFINLFERLnK 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 536 NLGNTVIVVEHDEDAI-RAADHVIDIgpgagvHGGQVVAEGTLKDIMAVPESLTgqymsgKRKIEVPK 602
Cdd:PRK13645 199 EYKKRIIMVTHNMDQVlRIADEVIVM------HEGKVISIGSPFEIFSNQELLT------KIEIDPPK 254
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
805-902 4.36e-09

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 60.03  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMD-VGLTyIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGN 883
Cdd:COG1129  116 AMRRRARELLArLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDAR---VLILDEPTASLTEREVERLFRIIRRLKAQGV 191
                         90       100
                 ....*....|....*....|
gi 489956980 884 TIVVIEHNLD-VIKTADWIV 902
Cdd:COG1129  192 AIIYISHRLDeVFEIADRVT 211
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
830-902 6.34e-09

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: 56.43  E-value: 6.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQ-GNTIVVIEHNLDVIKT-ADWIV 902
Cdd:cd03229  101 LSGGQQQRVALARALAMD---PDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVV 172
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
439-604 8.21e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 57.25  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 439 AMDFFNNLKLS---GQRAKIAEKVLKEIGDRLKflvnvglnyLT--LSRSAETLSGGEAQRIRLAS---QI--GAGLVGV 508
Cdd:PRK03695  83 AMPVFQYLTLHqpdKTRTEAVASALNEVAEALG---------LDdkLGRSVNQLSGGEWQRVRLAAvvlQVwpDINPAGQ 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 509 MYVLDEPSIGLhqrD--NERLLGTLVH-LRNLGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGQVVAEGTLKDIMAvP 584
Cdd:PRK03695 154 LLLLDEPMNSL---DvaQQAALDRLLSeLCQQGIAVVMSSHDlNHTLRHADRVWLL------KQGKLLASGRRDEVLT-P 223
                        170       180
                 ....*....|....*....|
gi 489956980 585 ESLTGQYMSGKRKIEVPKQR 604
Cdd:PRK03695 224 ENLAQVFGVNFRRLDVEGHP 243
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
822-901 9.72e-09

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: 58.99  E-value: 9.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARelskrgtgqTLY------ILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI 895
Cdd:COG4618  460 RIGEGGARLSGGQRQRIGLAR---------ALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL 530

                 ....*.
gi 489956980 896 KTADWI 901
Cdd:COG4618  531 AAVDKL 536
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
806-904 9.77e-09

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 58.97  E-value: 9.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 806 LARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTI 885
Cdd:PRK10535 122 LLRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALM---NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTV 197
                         90
                 ....*....|....*....
gi 489956980 886 VVIEHNLDVIKTADWIVDL 904
Cdd:PRK10535 198 IIVTHDPQVAAQAERVIEI 216
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
813-895 1.04e-08

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: 57.12  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 813 LMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaD--IQ-QLLDVLHQLRDQ-GNTIVVI 888
Cdd:COG1124  122 LEQVGLPPSFLDRYPHQLSGGQRQRVAIARALI---LEPELLLLDEPTSAL---DvsVQaEILNLLKDLREErGLTYLFV 195

                 ....*..
gi 489956980 889 EHNLDVI 895
Cdd:COG1124  196 SHDLAVV 202
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
440-586 1.17e-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: 56.58  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 440 MDFFNNL-----KLSGQRAKIAEKVlKEIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIRLASqigaGLV--GVMYVL 512
Cdd:cd03299   86 MTVYKNIayglkKRKVDKKEIERKV-LEIAEML------GIDHL-LNRKPETLSGGEQQRVAIAR----ALVvnPKILLL 153
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 513 DEPSIGLHQRDNERLLGTLVHLR-NLGNTVIVVEHD-EDAIRAADHVidigpgAGVHGGQVVAEGTLKDIMAVPES 586
Cdd:cd03299  154 DEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDfEEAWALADKV------AIMLNGKLIQVGKPEEVFKKPKN 223
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
780-904 1.74e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.28  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 780 YKGKTIhEVLDMTIEeaREFFDAVpalARKLqtlmdvGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEP 859
Cdd:PRK13409 176 FKGKVR-ELLKKVDE--RGKLDEV---VERL------GLENI-LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEP 239
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489956980 860 TTGLhfaDIQQLLDVLHQLRD--QGNTIVVIEHNLDVIktaDWIVDL 904
Cdd:PRK13409 240 TSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVL---DYLADN 280
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
787-893 1.78e-08

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.52  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 787 EVLDMTIEEAREffdavpalaRKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFA 866
Cdd:PRK10619 119 QVLGLSKQEARE---------RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME---PEVLLFDEPTSALDPE 186
                         90       100
                 ....*....|....*....|....*..
gi 489956980 867 DIQQLLDVLHQLRDQGNTIVVIEHNLD 893
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMG 213
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
782-902 1.93e-08

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: 56.99  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 782 GKTIHEVL----DMTIEEAREffdavpalaRKLQTLMDVGLTY--IRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYI 855
Cdd:COG0444  106 GDQIAEPLrihgGLSKAEARE---------RAIELLERVGLPDpeRRLDRYPHELSGGMRQRVMIARALA---LEPKLLI 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489956980 856 LDEPTTGLHfADIQ-QLLDVLHQLRDQ-GNTIVVIEHNLDVIK-TADWIV 902
Cdd:COG0444  174 ADEPTTALD-VTIQaQILNLLKDLQRElGLAILFITHDLGVVAeIADRVA 222
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
806-896 2.09e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 58.02  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 806 LARKLQTLMDVgltYIRLGQsattLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTI 885
Cdd:PRK13549 127 LLAQLKLDINP---ATPVGN----LGLGQQQLVEIAKALNKQAR---LLILDEPTASLTESETAVLLDIIRDLKAHGIAC 196
                         90
                 ....*....|.
gi 489956980 886 VVIEHNLDVIK 896
Cdd:PRK13549 197 IYISHKLNEVK 207
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
480-582 3.93e-08

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: 54.75  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQriRLAsqIGAGLVG--VMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDED-AIRAADH 556
Cdd:cd03224  126 RKQLAGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARfALEIADR 201
                         90       100
                 ....*....|....*....|....*...
gi 489956980 557 --VIDigpgagvhGGQVVAEGTLKDIMA 582
Cdd:cd03224  202 ayVLE--------RGRVVLEGTAAELLA 221
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
481-576 3.97e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 55.55  E-value: 3.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 481 SRSAETLSGGEAQRIRLA---SQI--GAGLVGVMYvLDEPSIGL---HQRDNERLLGTLVHLRNLGntVIVVEHDED-AI 551
Cdd:PRK13548 129 GRDYPQLSGGEQQRVQLArvlAQLwePDGPPRWLL-LDEPTSALdlaHQHHVLRLARQLAHERGLA--VIVVLHDLNlAA 205
                         90       100
                 ....*....|....*....|....*
gi 489956980 552 RAADHVIDIgpgagvHGGQVVAEGT 576
Cdd:PRK13548 206 RYADRIVLL------HQGRLVADGT 224
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
790-890 4.29e-08

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: 54.41  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 790 DMTIEEAREF---FDAVPALARKLQTLMD-VGLTYiRLGQSATTLSGGEAQRVKLAR-ELSKRgtgqTLYILDEPTTGLH 864
Cdd:COG4133   89 ELTVRENLRFwaaLYGLRADREAIDEALEaVGLAG-LADLPVRQLSAGQKRRVALARlLLSPA----PLWLLDEPFTALD 163
                         90       100
                 ....*....|....*....|....*.
gi 489956980 865 FADIQQLLDVLHQLRDQGNTIVVIEH 890
Cdd:COG4133  164 AAGVALLAELIAAHLARGGAVLLTTH 189
cbiO PRK13641
energy-coupling factor transporter ATPase;
413-624 4.77e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 55.61  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 413 RLRREARHVF-------VENTALptiSDMSIGHamdffNNLKLSGQRAKIAEkvlkeigdrLKFLVNVGLNYLTLSRSAE 485
Cdd:PRK13641  82 KLRKKVSLVFqfpeaqlFENTVL---KDVEFGP-----KNFGFSEDEAKEKA---------LKWLKKVGLSEDLISKSPF 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLAsqigaglvGVM------YVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAI-RAADHVI 558
Cdd:PRK13641 145 ELSGGQMRRVAIA--------GVMayepeiLCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVL 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 559 digpgaGVHGGQVVAEGTLKDIMAVPESLTGQYMSG------KRKIEVPKQRVAANPEKVLKLTGARGNNLK 624
Cdd:PRK13641 217 ------VLEHGKLIKHASPKEIFSDKEWLKKHYLDEpatsrfASKLEKGGFKFSEMPLTIDELVDGIKNNLK 282
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
790-892 5.09e-08

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: 56.60  E-value: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  790 DMTIEEAREFFDAVpALARKLQTLMDvGLTyIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQ 869
Cdd:TIGR02868 435 DATDEELWAALERV-GLADWLRALPD-GLD-TVLGEGGARLSGGERQRLALARALL---ADAPILLLDEPTEHLDAETAD 508
                          90       100
                  ....*....|....*....|...
gi 489956980  870 QLLDVLHQLrDQGNTIVVIEHNL 892
Cdd:TIGR02868 509 ELLEDLLAA-LSGRTVVLITHHL 530
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
805-932 6.12e-08

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 56.19  E-value: 6.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMD-VGLTyIRLGQSATTLSGGEAQRVKLARELSkRGTgQTLyILDEPTTGLHFADIQQLLDVLHQLRDQGN 883
Cdd:COG3845  117 AARARIRELSErYGLD-VDPDAKVEDLSVGEQQRVEILKALY-RGA-RIL-ILDEPTAVLTPQEADELFEILRRLAAEGK 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489956980 884 TIVVIEHNLDVIKT-ADWIVdlgpeggsgggeILVSGtpETVAECEASHT 932
Cdd:COG3845  193 SIIFITHKLREVMAiADRVT------------VLRRG--KVVGTVDTAET 228
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
830-890 6.37e-08

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: 53.71  E-value: 6.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEH 890
Cdd:cd03213  112 LSGGERKRVSIALELVSN---PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
805-902 7.11e-08

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 54.38  E-value: 7.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARklqtlmdVGLTYI--RL-GQsattLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RD 880
Cdd:COG3840  113 ALER-------VGLAGLldRLpGQ----LSGGQRQRVALARCLVRK---RPILLLDEPFSALDPALRQEMLDLVDELcRE 178
                         90       100
                 ....*....|....*....|...
gi 489956980 881 QGNTIVVIEHNL-DVIKTADWIV 902
Cdd:COG3840  179 RGLTVLMVTHDPeDAARIADRVL 201
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
791-890 7.72e-08

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 54.33  E-value: 7.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREffdavpaLARKLqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK09493 108 ASKEEAEK-------QAREL--LAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVK---PKLMLFDEPTSALDPELRHE 174
                         90       100
                 ....*....|....*....|
gi 489956980 871 LLDVLHQLRDQGNTIVVIEH 890
Cdd:PRK09493 175 VLKVMQDLAEEGMTMVIVTH 194
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
822-902 8.01e-08

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: 54.08  E-value: 8.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaD------IQQLLDVLHqlrdQGNTIVVIEHNLDVI 895
Cdd:cd03249  132 LVGERGSQLSGGQKQRIAIARALLRN---PKILLLDEATSAL---DaeseklVQEALDRAM----KGRTTIVIAHRLSTI 201

                 ....*..
gi 489956980 896 KTADWIV 902
Cdd:cd03249  202 RNADLIA 208
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
787-896 9.17e-08

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 53.90  E-value: 9.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 787 EVLDMTIEEAREffdAVPALarklqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFA 866
Cdd:COG2884  105 RVTGKSRKEIRR---RVREV------LDLVGLSD-KAKALPHELSGGEQQRVAIARALVNR---PELLLADEPTGNLDPE 171
                         90       100       110
                 ....*....|....*....|....*....|
gi 489956980 867 DIQQLLDVLHQLRDQGNTIVVIEHNLDVIK 896
Cdd:COG2884  172 TSWEIMELLEEINRRGTTVLIATHDLELVD 201
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
805-895 1.08e-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: 53.94  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLqtLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGN- 883
Cdd:COG1119  121 ERAREL--LELLGLAHLA-DRPFGTLSQGEQRRVLIARALVKDPE---LLILDEPTAGLDLGARELLLALLDKLAAEGAp 194
                         90
                 ....*....|..
gi 489956980 884 TIVVIEHNLDVI 895
Cdd:COG1119  195 TLVLVTHHVEEI 206
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
486-558 1.08e-07

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: 53.31  E-value: 1.08e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 486 TLSGGEAQRIRLAsQIgagLVG--VMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:cd03235  132 ELSGGQQQRVLLA-RA---LVQdpDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVL 203
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
487-597 1.26e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 55.50  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIGPGAGV 566
Cdd:PRK10535 145 LSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489956980 567 H--GGQVVAEGTLKDIMAVPE-SLTGQYMSGKRK 597
Cdd:PRK10535 223 RnpPAQEKVNVAGGTEPVVNTaSGWRQFVSGFRE 256
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
473-581 1.44e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 54.02  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 473 VGLNYLTlSRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGL---HQRDNERLLGTLVHLRNLgnTVIVVEHDED 549
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQD--SRCLLLDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDIN 209
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489956980 550 -AIRAADHVIdigpgaGVHGGQVVAEGTLKDIM 581
Cdd:PRK10575 210 mAARYCDYLV------ALRGGEMIAQGTPAELM 236
GguA NF040905
sugar ABC transporter ATP-binding protein;
807-901 1.76e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.80  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLqtLMDVGLTyirlgQSATTLSG----GEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQG 882
Cdd:NF040905 120 AREL--LAKVGLD-----ESPDTLVTdigvGKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKAQG 189
                         90       100
                 ....*....|....*....|
gi 489956980 883 NTIVVIEHNL-DVIKTADWI 901
Cdd:NF040905 190 ITSIIISHKLnEIRRVADSI 209
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
830-896 1.83e-07

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: 52.97  E-value: 1.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQ-GNTIVVIEHNLDVIK 896
Cdd:cd03258  141 LSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVK 205
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
782-861 1.86e-07

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: 51.49  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  782 GKTIHEVLDMTIEEAREFFDAVPALARKLQTLMD-VGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPT 860
Cdd:pfam00005  73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGlGDLADRPVGERPGTLSGGQRQRVAIARALLTK---PKLLLLDEPT 149

                  .
gi 489956980  861 T 861
Cdd:pfam00005 150 A 150
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
830-923 2.19e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 53.35  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNL-DVIKTADWIVdlgpeg 908
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQ---VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTV------ 213
                         90
                 ....*....|....*
gi 489956980 909 gSGGGEILVSGTPET 923
Cdd:PRK15056 214 -MVKGTVLASGPTET 227
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
830-924 2.53e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 53.10  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIKTADWIVDLgpeg 908
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQ---PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVM---- 213
                         90
                 ....*....|....*.
gi 489956980 909 gsGGGEILVSGTPETV 924
Cdd:PRK13635 214 --NKGEILEEGTPEEI 227
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
787-902 2.53e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 54.47  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 787 EVLDMTIEEAR--EFFDAVPAlarklqtlmdvGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLH 864
Cdd:PRK11174 453 EQLQQALENAWvsEFLPLLPQ-----------GLDTP-IGDQAAGLSVGQAQRLALARALLQPC---QLLLLDEPTASLD 517
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489956980 865 FADIQQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWIV 902
Cdd:PRK11174 518 AHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIW 554
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
486-582 2.88e-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: 54.37  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLASqigAglvgvMY------VLDEPSIGLhqrDNE---RLLGTLVHLRNLGNTVIVVEHDEDAIRAADH 556
Cdd:COG4618  467 RLSGGQRQRIGLAR---A-----LYgdprlvVLDEPNSNL---DDEgeaALAAAIRALKARGATVVVITHRPSLLAAVDK 535
                         90       100
                 ....*....|....*....|....*.
gi 489956980 557 VIDIgpgagvHGGQVVAEGTLKDIMA 582
Cdd:COG4618  536 LLVL------RDGRVQAFGPRDEVLA 555
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
445-566 3.17e-07

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: 51.87  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 445 NLKLSGQRAKIAEKVLKEIGdrlkflvnvgLNYLTLsRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLhQRDN 524
Cdd:cd03226   96 GLKELDAGNEQAETVLKDLD----------LYALKE-RHPLSLSGGQKQRLAIAAALLSG--KDLLIFDEPTSGL-DYKN 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489956980 525 ERLLGTLV-HLRNLGNTVIVVEHDED-AIRAADHVIDIGPGAGV 566
Cdd:cd03226  162 MERVGELIrELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
791-893 3.27e-07

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: 51.98  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREFFDAVPALAR--------KLQTLMDVGLTYIRLGQSattLSGGEAQRVKLARELSKRgtgQTLYILDEPTTG 862
Cdd:cd03266   93 LTARENLEYFAGLYGLKGdeltarleELADRLGMEELLDRRVGG---FSTGMRQKVAIARALVHD---PPVLLLDEPTTG 166
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489956980 863 LHFADIQQLLDVLHQLRDQGNTIVVIEHNLD 893
Cdd:cd03266  167 LDVMATRALREFIRQLRALGKCILFSTHIMQ 197
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
828-924 4.18e-07

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 52.32  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 828 TTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD-VIKTADWIVDLgp 906
Cdd:PRK11231 137 TDLSGGQRQRAFLAMVLAQ---DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVL-- 211
                         90
                 ....*....|....*...
gi 489956980 907 eggsGGGEILVSGTPETV 924
Cdd:PRK11231 212 ----ANGHVMAQGTPEEV 225
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
822-902 4.20e-07

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: 51.95  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGL--HFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTAD 899
Cdd:cd03290  133 EIGERGINLSGGQRQRICVARALYQN---TNIVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHAD 209

                 ...
gi 489956980 900 WIV 902
Cdd:cd03290  210 WII 212
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
816-904 4.56e-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: 53.63  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 816 VGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDIQQLL---DVLHQLRDQGNTIVVIEHNL 892
Cdd:COG1245  200 LGLENI-LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEPSSYL---DIYQRLnvaRLIRELAEEGKYVLVVEHDL 272
                         90
                 ....*....|..
gi 489956980 893 DVIktaDWIVDL 904
Cdd:COG1245  273 AIL---DYLADY 281
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
790-929 4.91e-07

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: 51.77  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 790 DMTIEE-----AREFFDAVPALARKLQTLM-DVGLTYIRLgQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG- 862
Cdd:cd03218   89 KLTVEEnilavLEIRGLSKKEREEKLEELLeEFHITHLRK-SKASSLSGGERRRVEIARALA---TNPKFLLLDEPFAGv 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956980 863 --LHFADIQQLldvLHQLRDQGNTIVVIEHN----LDVIKTADWIVDlgpeggsggGEILVSGTPETVAECEA 929
Cdd:cd03218  165 dpIAVQDIQKI---IKILKDRGIGVLITDHNvretLSITDRAYIIYE---------GKVLAEGTPEEIAANEL 225
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
825-924 4.94e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 53.31  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 825 QSATTLSGGEAQRVKLARELSKrgtgQT-LYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDV-IKTADWIV 902
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQ----ATpVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELV 210
                         90       100
                 ....*....|....*....|..
gi 489956980 903 DLgpeggsGGGEILVSGTPETV 924
Cdd:PRK09536 211 LL------ADGRVRAAGPPADV 226
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
511-888 5.27e-07

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 53.48  E-value: 5.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 511 VLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVI---DigpgagvhgGQVVAEGTLKDImaVPES 586
Cdd:COG1129  163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTvlrD---------GRLVGTGPVAEL--TEDE 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 587 LTgQYMSGkRKIE--VPKQRVAANPEkVLKLTG-ARGNNLKDVTLTLP----VGlftcITGVSGSGKSTLINdTLFpiaq 659
Cdd:COG1129  232 LV-RLMVG-RELEdlFPKRAAAPGEV-VLEVEGlSVGGVVRDVSFSVRageiLG----IAGLVGAGRTELAR-ALF---- 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 660 talngatlaepapyrdiqGLEHFDK-VIDIDQSPI-GRTPRSnpAtytgvftpVRELFAGVPEARsrgytpgrfsfnvrg 737
Cdd:COG1129  300 ------------------GADPADSgEIRLDGKPVrIRSPRD--A--------IRAGIAYVPEDR--------------- 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 738 grceacQGDGVikvemhflpdiyvpcdqckgkrynretleikykgktiheVLDMTIEE------------------AREF 799
Cdd:COG1129  337 ------KGEGL---------------------------------------VLDLSIREnitlasldrlsrgglldrRRER 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 800 fdavpALARKLQTLMDvgltyIR---LGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaDI---QQLLD 873
Cdd:COG1129  372 -----ALAEEYIKRLR-----IKtpsPEQPVGNLSGGNQQKVVLAKWLA---TDPKVLILDEPTRGI---DVgakAEIYR 435
                        410
                 ....*....|....*
gi 489956980 874 VLHQLRDQGNTIVVI 888
Cdd:COG1129  436 LIRELAAEGKAVIVI 450
cbiO PRK13644
energy-coupling factor transporter ATPase;
777-924 5.37e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 52.30  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 777 EIKYKGKTIHEVLDMTIEEAreffdAVPALarKLQTLMDVGLTYIRLGQ----SATTLSGGEAQRVKLARELSKRgtgQT 852
Cdd:PRK13644  87 ETQFVGRTVEEDLAFGPENL-----CLPPI--EIRKRVDRALAEIGLEKyrhrSPKTLSGGQGQCVALAGILTME---PE 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 853 LYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM------DRGKIVLEGEPENV 222
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
807-921 5.64e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.55  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQT--LMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNT 884
Cdd:PRK13631 152 AKKLAKfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQ---PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT 228
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489956980 885 IVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVSGTP 921
Cdd:PRK13631 229 VFVITHTMEhVLEVADEVIVM------DKGKILKTGTP 260
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
790-936 6.29e-07

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: 51.52  E-value: 6.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 790 DMTIEE--A---REFFDAVPALARKL--QTLMDVGLtyirlGQSATT----LSGGEAQRVKLARelskrgtgqTL----- 853
Cdd:COG1127   96 SLTVFEnvAfplREHTDLSEAEIRELvlEKLELVGL-----PGAADKmpseLSGGMRKRVALAR---------ALaldpe 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 854 YIL-DEPTTGLhfaD------IQQLldvLHQLRDQ-GNTIVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:COG1127  162 ILLyDEPTAGL---DpitsavIDEL---IRELRDElGLTSVVVTHDLDsAFAIADRVAVL------ADGKIIAEGTPEEL 229
                        170
                 ....*....|..
gi 489956980 925 AECEASHTARFL 936
Cdd:COG1127  230 LASDDPWVRQFL 241
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
822-902 6.53e-07

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 53.24  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHF---ADIQQLLDVLHqlrdQGNTIVVIEHNLDVIKTA 898
Cdd:COG1132  469 VVGERGVNLSGGQRQRIAIARALLKDP---PILILDEATSALDTeteALIQEALERLM----KGRTTIVIAHRLSTIRNA 541

                 ....
gi 489956980 899 DWIV 902
Cdd:COG1132  542 DRIL 545
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
791-924 8.13e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 51.94  E-value: 8.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREffdavpaLARKLQTLmdVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK13634 116 VSEEDAKQ-------KAREMIEL--VGLPEELLARSPFELSGGQMRRVAIAGVLAME---PEVLVLDEPTAGLDPKGRKE 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 871 LLDVLHQLRDQGN-TIVVIEHNL-DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13634 184 MMEMFYKLHKEKGlTTVLVTHSMeDAARYADQIVVM------HKGTVFLQGTPREI 233
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
781-895 9.29e-07

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: 9.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 781 KGKTIhEVLDMTIEeaREFFDavpalarklqTLMDV-GLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEP 859
Cdd:cd03236  104 KGKVG-ELLKKKDE--RGKLD----------ELVDQlELRHV-LDRNIDQLSGGELQRVAIAAALARDA---DFYFFDEP 166
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489956980 860 TTGLhfaDIQQLLD---VLHQLRDQGNTIVVIEHNLDVI 895
Cdd:cd03236  167 SSYL---DIKQRLNaarLIRELAEDDNYVLVVEHDLAVL 202
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
480-587 9.80e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 51.55  E-value: 9.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLAsqigaGLVGV---MYVLDEPSIGLHQRDNERLLGTLVHLRNLGN-TVIVVEHDEDAIRAAD 555
Cdd:PRK13635 134 LNREPHRLSGGQKQRVAIA-----GVLALqpdIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQAD 208
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489956980 556 HVIDIgpgagvHGGQVVAEGTLKDIMAVPESL 587
Cdd:PRK13635 209 RVIVM------NKGEILEEGTPEEIFKSGHML 234
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
805-904 9.85e-07

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: 50.55  E-value: 9.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMDVGLTYIrlGQSATTLSGGEAQRVKLAREL-SKRGtgqtLYILDEPTTGL--HFAdiQQLLD--VLHQLR 879
Cdd:cd03250  105 ALEPDLEILPDGDLTEI--GEKGINLSGGQKQRISLARAVySDAD----IYLLDDPLSAVdaHVG--RHIFEncILGLLL 176
                         90       100
                 ....*....|....*....|....*
gi 489956980 880 DqGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03250  177 N-NKTRILVTHQLQLLPHADQIVVL 200
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
467-565 1.07e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 50.48  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGLHQrDNERLLGTLVH--LRNLGNTVIVV 544
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALDE-SNKHNVNEIIHryVREQNIAVLWV 194
                         90       100
                 ....*....|....*....|.
gi 489956980 545 EHDEDAIRAADHVIDIGPGAG 565
Cdd:PRK10247 195 THDKDEINHADKVITLQPHAG 215
cbiO PRK13637
energy-coupling factor transporter ATPase;
462-580 1.22e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 51.20  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 462 EIGDRLKFLVN-VGLNYLTLS-RSAETLSGGEAQRIRLAsqigaGLVGVM---YVLDEPSIGLHQRDNERLLGTLVHL-R 535
Cdd:PRK13637 118 EIENRVKRAMNiVGLDYEDYKdKSPFELSGGQKRRVAIA-----GVVAMEpkiLILDEPTAGLDPKGRDEILNKIKELhK 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489956980 536 NLGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGQVVAEGTLKDI 580
Cdd:PRK13637 193 EYNMTIILVSHSmEDVAKLADRIIVM------NKGKCELQGTPREV 232
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
830-897 1.34e-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: 50.10  E-value: 1.34e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKT 897
Cdd:cd03292  137 LSGGEQQRVAIARAIVNS---PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
804-896 1.35e-06

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: 52.13  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  804 PALARKLQTLM-DVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQG 882
Cdd:TIGR02633 115 NAMYLRAKNLLrELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR---LLILDEPSSSLTEKETEILLDIIRDLKAHG 191
                          90
                  ....*....|....
gi 489956980  883 NTIVVIEHNLDVIK 896
Cdd:TIGR02633 192 VACVYISHKLNEVK 205
cbiO PRK13649
energy-coupling factor transporter ATPase;
805-924 1.44e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 50.90  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARklQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNT 884
Cdd:PRK13649 123 ALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAME---PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489956980 885 IVVIEHNL-DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13649 198 IVLVTHLMdDVANYADFVYVL------EKGKLVLSGKPKDI 232
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
814-902 1.66e-06

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 51.94  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 814 MDVGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFAD---IQQLLDVLHQLRdqgnTIVVIEH 890
Cdd:PRK11176 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQKNR----TSLVIAH 537
                         90
                 ....*....|..
gi 489956980 891 NLDVIKTADWIV 902
Cdd:PRK11176 538 RLSTIEKADEIL 549
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
480-575 1.72e-06

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: 49.83  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASqigaGLV---GVMyVLDEPSIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHD-EDAIRAA 554
Cdd:cd03259  124 LNRYPHELSGGQQQRVALAR----ALArepSLL-LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDqEEALALA 198
                         90       100
                 ....*....|....*....|.
gi 489956980 555 DHVidigpgAGVHGGQVVAEG 575
Cdd:cd03259  199 DRI------AVMNEGRIVQVG 213
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
414-595 1.79e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 50.30  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 414 LRREARHVFVENTALPTIS---DMSIGHAMD-FFNNLKLSGQRAKIA-EK--VLKEIGDRLkflvnvglnyltlSRSAET 486
Cdd:PRK14247  80 LRRRVQMVFQIPNPIPNLSifeNVALGLKLNrLVKSKKELQERVRWAlEKaqLWDEVKDRL-------------DAPAGK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVidigpgAGV 566
Cdd:PRK14247 147 LSGGQQQRLCIARAL--AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV------AFL 218
                        170       180       190
                 ....*....|....*....|....*....|
gi 489956980 567 HGGQVVAEGTLKDIMAVPE-SLTGQYMSGK 595
Cdd:PRK14247 219 YKGQIVEWGPTREVFTNPRhELTEKYVTGR 248
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
823-904 1.83e-06

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: 50.18  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 823 LGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDqGNTIVVIEHNLDVIKTADWIV 902
Cdd:cd03252  132 VGEQGAGLSGGQRQRIAIARALI---HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRII 207

                 ..
gi 489956980 903 DL 904
Cdd:cd03252  208 VM 209
cbiO PRK13645
energy-coupling factor transporter ATPase;
794-902 1.85e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.78  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 794 EEAREFFDAVPALARKLQTLMDvgltYIRlgQSATTLSGGEAQRVKLARELSKrgTGQTLyILDEPTTGLHFADIQQLLD 873
Cdd:PRK13645 121 ENKQEAYKKVPELLKLVQLPED----YVK--RSPFELSGGQKRRVALAGIIAM--DGNTL-VLDEPTGGLDPKGEEDFIN 191
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489956980 874 VLHQL-RDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:PRK13645 192 LFERLnKEYKKRIIMVTHNMDqVLRIADEVI 222
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
830-902 2.00e-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: 48.85  E-value: 2.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLD-VLHQLRDQgnTIVVIEHNLDVIKTADWIV 902
Cdd:cd03247   99 FSGGERQRLALARILLQDA---PIVLLDEPTVGLDPITERQLLSlIFEVLKDK--TLIWITHHLTGIEHMDKIL 167
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
805-893 2.19e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 50.37  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTlmdVGLTYIRlGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGN 883
Cdd:PRK10253 123 AVTKAMQA---TGITHLA-DQSVDTLSGGQRQRAWIAMVLAQE---TAIMLLDEPTTWLDISHQIDLLELLSELnREKGY 195
                         90
                 ....*....|
gi 489956980 884 TIVVIEHNLD 893
Cdd:PRK10253 196 TLAAVLHDLN 205
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
822-892 2.24e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 50.16  E-value: 2.24e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQgNTIVVIEHNL 892
Cdd:PRK14239 141 RLHDSALGLSGGQQQRVCIARVLA---TSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSM 207
cbiO PRK13640
energy-coupling factor transporter ATPase;
811-924 2.51e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.18  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 811 QTLMDVGLT-YIRlgQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVI 888
Cdd:PRK13640 126 DVLADVGMLdYID--SEPANLSGGQKQRVAIAGILA---VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISI 200
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489956980 889 EHNLDVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13640 201 THDIDEANMADQVLVL------DDGKLLAQGSPVEI 230
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
487-560 2.53e-06

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: 51.13  E-value: 2.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980  487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLVHLRNlGNTVIVVEHDEDAIRAADHVIDI 560
Cdd:TIGR02857 459 LSGGQAQRLALARAFlrDAPLL----LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
804-904 2.58e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 49.71  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 804 PALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELskrgtgQTL---YILDEPTTGLHFADIQQLLDVLHQL-R 879
Cdd:PRK10247 112 PDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL------QFMpkvLLLDEITSALDESNKHNVNEIIHRYvR 185
                         90       100
                 ....*....|....*....|....*
gi 489956980 880 DQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:PRK10247 186 EQNIAVLWVTHDKDEINHADKVITL 210
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
805-890 2.69e-06

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: 49.45  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNT 884
Cdd:cd03262  112 AEERALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMN---PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMT 187

                 ....*.
gi 489956980 885 IVVIEH 890
Cdd:cd03262  188 MVVVTH 193
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
811-932 3.39e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 49.75  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 811 QTLMDVGLtYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIE 889
Cdd:PRK13648 125 EALKQVDM-LERADYEPNALSGGQKQRVAIAGVLA---LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISIT 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489956980 890 HNLDVIKTADWIVDLgpeggsGGGEILVSGTPETVAECEASHT 932
Cdd:PRK13648 201 HDLSEAMEADHVIVM------NKGTVYKEGTPTEIFDHAEELT 237
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
771-895 3.63e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 50.77  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 771 YNRETLEIKYKGKT----------------IHEVLD----MTIEE----AREFFDAVPALA-RKLQTLMDVGLTyiRLG- 824
Cdd:PRK10762  54 YTRDAGSILYLGKEvtfngpkssqeagigiIHQELNlipqLTIAEniflGREFVNRFGRIDwKKMYAEADKLLA--RLNl 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 825 -----QSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI 895
Cdd:PRK10762 132 rfssdKLVGELSIGEQQMVEIAKVLS---FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
791-890 3.65e-06

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: 48.64  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREFFDAVPALARKLQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQ 870
Cdd:cd03231   88 LSVLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLL---SGRPLWILDEPTTALDKAGVAR 163
                         90       100
                 ....*....|....*....|
gi 489956980 871 LLDVLHQLRDQGNTIVVIEH 890
Cdd:cd03231  164 FAEAMAGHCARGGMVVLTTH 183
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
830-904 3.82e-06

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: 47.44  E-value: 3.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDvlhQLRDQGNTIVVIEHNLDVI-KTADWIVDL 904
Cdd:cd03221   71 LSGGEKMRLALAKLLLENP---NLLLLDEPTNHLDLESIEALEE---ALKEYPGTVILVSHDRYFLdQVATKIIEL 140
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
830-924 3.97e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 49.69  E-value: 3.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKT-ADWIVDLgpeg 908
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMK---PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVM---- 210
                         90
                 ....*....|....*.
gi 489956980 909 gsGGGEILVSGTPETV 924
Cdd:PRK13639 211 --SDGKIIKEGTPKEV 224
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
623-890 4.09e-06

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: 48.97  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqtalngATLAepapyrdiqGLEhfdkvididqspigrTPRSNPA 702
Cdd:COG4181   28 LKGISLEVEAGESVAIVGASGSGKSTLL--------------GLLA---------GLD---------------RPTSGTV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 703 TYTGvftpvRELFAGVPEARSRgytpgrfsfnVRGGRCeacqgdGVIKVEMHFLPdiyvpcdqckgkrynreTLeikykg 782
Cdd:COG4181   70 RLAG-----QDLFALDEDARAR----------LRARHV------GFVFQSFQLLP-----------------TL------ 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 783 kTIHEVLDMTIEEAREffdaVPALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG 862
Cdd:COG4181  106 -TALENVMLPLELAGR----RDARARARALLERVGLGH-RLDHYPAQLSGGEQQRVALARAFA---TEPAILFADEPTGN 176
                        250       260
                 ....*....|....*....|....*....
gi 489956980 863 LHFADIQQLLDVLHQL-RDQGNTIVVIEH 890
Cdd:COG4181  177 LDAATGEQIIDLLFELnRERGTTLVLVTH 205
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
623-888 4.11e-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: 48.81  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfPIAQTALNGATLaepapyrdiqglehfdkvididqspigrtprsnpa 702
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLD----AISGRVEGGGTT----------------------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 703 tyTGvftpvRELFAGVPeaRSRGYTPGRFSFnVRggrceacQGDgvikvemHFLPDIYVpcdqckgkrynRETLeikykg 782
Cdd:cd03234   64 --SG-----QILFNGQP--RKPDQFQKCVAY-VR-------QDD-------ILLPGLTV-----------RETL------ 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 783 kTIHEVLDMTieeaREFFDAVPALARKLQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG 862
Cdd:cd03234  103 -TYTAILRLP----RKSSDAIRKKRVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLL---WDPKVLILDEPTSG 173
                        250       260
                 ....*....|....*....|....*...
gi 489956980 863 LhfaDIQQLLDVLHQLRD--QGNTIVVI 888
Cdd:cd03234  174 L---DSFTALNLVSTLSQlaRRNRIVIL 198
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
783-896 4.42e-06

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 50.47  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 783 KTIHEVLDMTIEEAREffdavPALARKLQTLMDVGLTYI--RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPT 860
Cdd:PRK15134 113 KQLYEVLSLHRGMRRE-----AARGEILNCLDRVGIRQAakRLTDYPHQLSGGERQRVMIAMALLTR---PELLIADEPT 184
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489956980 861 TGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIK 896
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVR 221
cbiO PRK13646
energy-coupling factor transporter ATPase;
791-902 4.63e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 49.39  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREffdavpalaRKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK13646 116 MNLDEVKN---------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA---MNPDIIVLDEPTAGLDPQSKRQ 183
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489956980 871 LLDVLHQLR-DQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:PRK13646 184 VMRLLKSLQtDENKTIILVSHDMnEVARYADEVI 217
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
487-571 5.08e-06

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: 47.60  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASqigaglvgVMY------VLDEPSIGLHQrDNERLLGTLV-HLRNLGNTVIVVEHDEDAIRAADHVID 559
Cdd:cd03246   97 LSGGQRQRLGLAR--------ALYgnprilVLDEPNSHLDV-EGERALNQAIaALKAAGATRIVIAHRPETLASADRILV 167
                         90
                 ....*....|..
gi 489956980 560 IgpgagvHGGQV 571
Cdd:cd03246  168 L------EDGRV 173
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
824-904 5.56e-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: 48.62  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 824 GQSATTLSGGEAQRVKLARELSKrgTGQTLyILDEPTTGLHfADIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVD 903
Cdd:cd03248  145 GEKGSQLSGGQKQRVAIARALIR--NPQVL-ILDEATSALD-AESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILV 220

                 .
gi 489956980 904 L 904
Cdd:cd03248  221 L 221
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
487-591 5.65e-06

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: 48.65  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASQIGAGLVGVMYvlDEPSIGLhqrD--NERLLGTLVHL--RNLGNTVIVVEHDEDAIRA-ADHVidig 561
Cdd:cd03261  137 LSGGMKKRVALARALALDPELLLY--DEPTAGL---DpiASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRI---- 207
                         90       100       110
                 ....*....|....*....|....*....|
gi 489956980 562 pgAGVHGGQVVAEGTLKDIMAVPESLTGQY 591
Cdd:cd03261  208 --AVLYDGKIVAEGTPEELRASDDPLVRQF 235
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
801-925 5.90e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 48.96  E-value: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 801 DAVPALAR-KLQTLMDvgltyirlgQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLR 879
Cdd:PRK09544 100 DILPALKRvQAGHLID---------APMQKLSGGETQRVLLARALLNR---PQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489956980 880 DQGN-TIVVIEHNLD-VIKTADWIVDLgpeggsgGGEILVSGTPETVA 925
Cdd:PRK09544 168 RELDcAVLMVSHDLHlVMAKTDEVLCL-------NHHICCSGTPEVVS 208
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
808-893 5.95e-06

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 48.86  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 808 RKLQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIV 886
Cdd:PRK09984 132 RALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQA---KVILADEPIASLDPESARIVMDTLRDInQNDGITVV 207

                 ....*..
gi 489956980 887 VIEHNLD 893
Cdd:PRK09984 208 VTLHQVD 214
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
788-902 6.17e-06

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 48.47  E-value: 6.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 788 VLDMTIEEAREffdavpaLARKLqtlmdvgLTYIRLGQSATT----LSGGEAQRVKLARELSKRgtGQTLyILDEPTTGL 863
Cdd:PRK11124 110 VLGLSKDQALA-------RAEKL-------LERLRLKPYADRfplhLSGGQQQRVAIARALMME--PQVL-LFDEPTAAL 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489956980 864 HFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVV 212
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
430-587 6.46e-06

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: 49.90  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 430 TISDmSIGHAMDFFNNLKLSGQRAKIAEkVLKEigdrlkflvnVGLNYLTLSRSAETLSGGEAQRIRLASQIGAG--LVg 507
Cdd:COG1123  360 TVGD-IIAEPLRLHGLLSRAERRERVAE-LLER----------VGLPPDLADRYPHELSGGQRQRVAIARALALEpkLL- 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 508 vmyVLDEPSIGL---HQRdneRLLGTLVHL-RNLGNTVIVVEHDEDAIRA-ADHVIdigpgagV-HGGQVVAEGTLKDIM 581
Cdd:COG1123  427 ---ILDEPTSALdvsVQA---QILNLLRDLqRELGLTYLFISHDLAVVRYiADRVA-------VmYDGRIVEDGPTEEVF 493

                 ....*.
gi 489956980 582 AVPESL 587
Cdd:COG1123  494 ANPQHP 499
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
828-894 8.38e-06

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 48.38  E-value: 8.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 828 TTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLDV 894
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLV---THPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAV 214
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
793-904 8.48e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 48.50  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 793 IEEAREFFDAVPALARKLQTLMDVgltYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLL 872
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARALALK---PKVLLMDEPTSMIDIVNSQAIE 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489956980 873 DVLHQLRDQgNTIVVIEHN-LDVIKTADWIVDL 904
Cdd:PRK14246 194 KLITELKNE-IAIVIVSHNpQQVARVADYVAFL 225
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
822-904 8.97e-06

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: 48.00  E-value: 8.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWI 901
Cdd:cd03253  130 IVGERGLKLSGGEKQRVAIARAILK---NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKI 205

                 ...
gi 489956980 902 VDL 904
Cdd:cd03253  206 IVL 208
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
809-903 9.33e-06

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: 48.17  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 809 KLQTLMDvgltyirlgQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHQLR----DQGNT 884
Cdd:cd03237  104 QIEQILD---------REVPELSGGELQRVAIAACLSKDA---DIYLLDEPSAYL---DVEQRLMASKVIRrfaeNNEKT 168
                         90
                 ....*....|....*....
gi 489956980 885 IVVIEHnlDVIkTADWIVD 903
Cdd:cd03237  169 AFVVEH--DII-MIDYLAD 184
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
829-893 1.03e-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: 47.66  E-value: 1.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 829 TLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLD 893
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHD---PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
808-904 1.03e-05

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: 47.95  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 808 RKLQTLMDVGLT---YIRlgqsATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGN 883
Cdd:cd03256  124 RALAALERVGLLdkaYQR----ADQLSGGQQQRVAIARALMQQ---PKLILADEPVASLDPASSRQVMDLLKRInREEGI 196
                         90       100
                 ....*....|....*....|..
gi 489956980 884 TIVVIEHNLDVIKT-ADWIVDL 904
Cdd:cd03256  197 TVIVSLHQVDLAREyADRIVGL 218
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
791-902 1.04e-05

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: 47.60  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREFFDAVPALARKL--QTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADI 868
Cdd:cd03268   87 LTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGN---PDLLILDEPTNGLDPDGI 162
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489956980 869 QQLLDVLHQLRDQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:cd03268  163 KELRELILSLRDQGITVLISSHLLsEIQKVADRIG 197
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
486-582 1.12e-05

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: 49.45  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrDNE---RLLGTLVHLRNlGNTVIVVEHDEDAIRAADH 556
Cdd:COG2274  611 NLSGGQRQRLAIArallrnPRI--------LILDEATSAL---DAEteaIILENLRRLLK-GRTVIIIAHRLSTIRLADR 678
                         90       100
                 ....*....|....*....|....*.
gi 489956980 557 VIDIgpgagvHGGQVVAEGTLKDIMA 582
Cdd:COG2274  679 IIVL------DKGRIVEDGTHEELLA 698
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
487-558 1.14e-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: 46.61  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrDNE---RLLGTLVHLRNlGNTVIVVEHDEDAIRAADHV 557
Cdd:cd03228   97 LSGGQRQRIAIArallrdPPI--------LILDEATSAL---DPEteaLILEALRALAK-GKTVIVIAHRLSTIRDADRI 164

                 .
gi 489956980 558 I 558
Cdd:cd03228  165 I 165
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
775-903 1.23e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.04  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 775 TLEIKYKGKTIHEVLDMTIEEareFFDAVPA----------LARKLQ--TLMDvgltyirlgQSATTLSGGEAQRVKLAR 842
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVED---LLRSITDdlgssyykseIIKPLQleRLLD---------KNVKDLSGGELQRVAIAA 466
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 843 ELSKRGtgqTLYILDEPTTGLhfaDIQQLLDVL----HQLRDQGNTIVVIEHNLDVIktaDWIVD 903
Cdd:PRK13409 467 CLSRDA---DLYLLDEPSAHL---DVEQRLAVAkairRIAEEREATALVVDHDIYMI---DYISD 522
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
794-895 1.37e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 48.18  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 794 EEAREFFDAV--PAlARKlqtlmdvgltyiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQL 871
Cdd:PRK09473 137 EESVRMLDAVkmPE-ARK------------RMKMYPHEFSGGMRQRVMIAMALLCR---PKLLIADEPTTALDVTVQAQI 200
                         90       100
                 ....*....|....*....|....*
gi 489956980 872 LDVLHQLRDQGNT-IVVIEHNLDVI 895
Cdd:PRK09473 201 MTLLNELKREFNTaIIMITHDLGVV 225
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
829-896 1.38e-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: 47.10  E-value: 1.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 829 TLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLDVIK 896
Cdd:cd03298  128 ELSGGERQRVALARVLVRD---KPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAK 193
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
417-585 1.40e-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: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 417 EARHVFvENTALPtisdmsighamdffnnLKLSGQ-RAKIAEKVLkeigDRLKFlvnVGLNYLTLSRSAEtLSGGEAQRI 495
Cdd:cd03258   95 SSRTVF-ENVALP----------------LEIAGVpKAEIEERVL----ELLEL---VGLEDKADAYPAQ-LSGGQKQRV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 496 RLASqigaGLVGVMYVL--DEPSIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHDEDAIRA-ADHVidigpgAGVHGGQV 571
Cdd:cd03258  150 GIAR----ALANNPKVLlcDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRiCDRV------AVMEKGEV 219
                        170
                 ....*....|....
gi 489956980 572 VAEGTLKDIMAVPE 585
Cdd:cd03258  220 VEEGTVEEVFANPQ 233
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
482-581 1.42e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 47.67  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 482 RSAETLSGGEAQRIRLAsQIGAGLVGVMyVLDEPSIGL---HQRDNERLLGTLVhlRNLGNTVIVVEHD-EDAIRAADHV 557
Cdd:PRK10253 139 QSVDTLSGGQRQRAWIA-MVLAQETAIM-LLDEPTTWLdisHQIDLLELLSELN--REKGYTLAAVLHDlNQACRYASHL 214
                         90       100
                 ....*....|....*....|....
gi 489956980 558 IdigpgaGVHGGQVVAEGTLKDIM 581
Cdd:PRK10253 215 I------ALREGKIVAQGAPKEIV 232
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
468-549 1.49e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 48.16  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 468 KFLVNVGLNYLTLSRSAETLSGGEAQRIRLAsqigaGLVGV---MYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVV 544
Cdd:PRK13651 147 KYIELVGLDESYLQRSPFELSGGQKRRVALA-----GILAMepdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILV 221

                 ....*
gi 489956980 545 EHDED 549
Cdd:PRK13651 222 THDLD 226
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
788-926 1.62e-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: 48.65  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  788 VLDMTIEEAREF-FDAVPALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHfa 866
Cdd:TIGR03269 127 VLDNVLEALEEIgYEGKEAVGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKE---PFLFLADEPTGTLD-- 200
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980  867 diQQLLDVLHQLRDQGntivVIEHNLDVIKTADW---IVDLGPEGG-SGGGEILVSGTPETVAE 926
Cdd:TIGR03269 201 --PQTAKLVHNALEEA----VKASGISMVLTSHWpevIEDLSDKAIwLENGEIKEEGTPDEVVA 258
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
825-940 1.73e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 47.69  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 825 QSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI-KTADWIVD 903
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQAR---YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYV 208
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489956980 904 LgpeggsGGGEILVSGTP-ETVAECEASHTARFLKPLL 940
Cdd:PRK13638 209 L------RQGQILTHGAPgEVFACTEAMEQAGLTQPWL 240
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
810-892 1.85e-05

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 48.28  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 810 LQTLMDVGLTYIR---------LGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHQLRd 880
Cdd:PRK11160 447 IEVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARALLHDA---PLLLLDEPTEGLDAETERQILELLAEHA- 522
                         90
                 ....*....|..
gi 489956980 881 QGNTIVVIEHNL 892
Cdd:PRK11160 523 QNKTVLMITHRL 534
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
410-595 1.86e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 47.35  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 410 EGTRLRREARHVFVENTALPTISDM-SIGHAMDFfNNLKLSGQRAKIAEKVLKEIGDRLKFlvnvglnYLTLSRSAETLS 488
Cdd:PRK14246  84 DAIKLRKEVGMVFQQPNPFPHLSIYdNIAYPLKS-HGIKEKREIKKIVEECLRKVGLWKEV-------YDRLNSPASQLS 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 489 GGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVidigpgAGVHG 568
Cdd:PRK14246 156 GGQQQRLTIARALA--LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYV------AFLYN 227
                        170       180
                 ....*....|....*....|....*...
gi 489956980 569 GQVVAEGTLKDIMAVPES-LTGQYMSGK 595
Cdd:PRK14246 228 GELVEWGSSNEIFTSPKNeLTEKYVIGR 255
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
806-904 1.88e-05

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 48.56  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 806 LARKLQTLMDvGLtYIRLGQSATTLSGGEAQRVKLARELSKrgTGQTLyILDEPTTGLHFADIQQLLDVLHQLRDQgNTI 885
Cdd:PRK10790 455 LAELARSLPD-GL-YTPLGEQGNNLSVGQKQLLALARVLVQ--TPQIL-ILDEATANIDSGTEQAIQQALAAVREH-TTL 528
                         90
                 ....*....|....*....
gi 489956980 886 VVIEHNLDVIKTADWIVDL 904
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVL 547
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
446-584 1.99e-05

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: 46.91  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 446 LKLSG-QRAKIAEKVlkeigDRLKFLVNVGLNYLtLSRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDN 524
Cdd:cd03295  100 PKLLKwPKEKIRERA-----DELLALVGLDPAEF-ADRYPHELSGGQQQRVGVARALAAD--PPLLLMDEPFGALDPITR 171
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 525 ERLLGTLVHL-RNLGNTVIVVEHD-EDAIRAADHVidigpgAGVHGGQVVAEGTLKDIMAVP 584
Cdd:cd03295  172 DQLQEEFKRLqQELGKTIVFVTHDiDEAFRLADRI------AIMKNGEIVQVGTPDEILRSP 227
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
829-902 2.09e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 47.98  E-value: 2.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 829 TLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:PRK11288 396 NLSGGNQQKAILGRWLS---EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIV 467
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
788-896 2.47e-05

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 46.93  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 788 VLDMTIEEAREffdavpaLARKLqtlmdvgLTYIRLGQSATT----LSGGEAQRVKLARELSKRgtGQTLyILDEPTTGL 863
Cdd:COG4161  110 VLGLSKEQARE-------KAMKL-------LARLRLTDKADRfplhLSGGQQQRVAIARALMME--PQVL-LFDEPTAAL 172
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489956980 864 HFADIQQLLDVLHQLRDQGNTIVVIEHNLDVIK 896
Cdd:COG4161  173 DPEITAQVVEIIRELSQTGITQVIVTHEVEFAR 205
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
480-562 2.63e-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: 46.06  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGE------AQRIRLASQIGAGLvGVMyVLDEPSIGLhqrDNERLLGTLV-----HLRNLGNTVIVVEHDE 548
Cdd:cd03240  109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNL---DEENIEESLAeiieeRKSQKNFQLIVITHDE 183
                         90
                 ....*....|....
gi 489956980 549 DAIRAADHVIDIGP 562
Cdd:cd03240  184 ELVDAADHIYRVEK 197
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
830-896 2.78e-05

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 47.38  E-value: 2.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQ-GNTIVVIEHNLDVIK 896
Cdd:COG1135  141 LSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVR 205
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
822-902 2.81e-05

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: 46.46  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLhfaD------IQQLLDVLHQLRdqgnTIVVIEHNLDVI 895
Cdd:cd03251  131 VIGERGVKLSGGQRQRIAIARALLK---DPPILILDEATSAL---DteserlVQAALERLMKNR----TTFVIAHRLSTI 200

                 ....*..
gi 489956980 896 KTADWIV 902
Cdd:cd03251  201 ENADRIV 207
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
14-40 2.84e-05

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: 45.92  E-value: 2.84e-05
                         10        20
                 ....*....|....*....|....*..
gi 489956980  14 LKNINLIIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
824-902 3.18e-05

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 47.79  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  824 GQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHfADIQQLldvLHQLRDQGN-TIVVIEHNLDVIKTADWIV 902
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRK---PRVLILDEATSALD-AECEQL---LQESRSRASrTVLLIAHRLSTVERADQIL 684
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
774-903 3.70e-05

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: 47.47  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 774 ETLEIKYKGKTIHEVLDMTIEE-----AREFFDAVPA---LARKLQ--TLMDvgltyirlgQSATTLSGGEAQRVKLARE 843
Cdd:COG1245  399 EDLKISYKPQYISPDYDGTVEEflrsaNTDDFGSSYYkteIIKPLGleKLLD---------KNVKDLSGGELQRVAIAAC 469
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 844 LSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHQLR----DQGNTIVVIEHNLDVIktaDWIVD 903
Cdd:COG1245  470 LSRDA---DLYLLDEPSAHL---DVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLI---DYISD 524
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
791-924 3.92e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 46.04  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREFFDAVPALARKLQTLMDVGLTYIR--LGQSattLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADI 868
Cdd:PRK10895 100 MAVLQIRDDLSAEQREDRANELMEEFHIEHLRdsMGQS---LSGGERRRVEIARALA---ANPKFILLDEPFAGVDPISV 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 869 QQLLDVLHQLRDQGNTIVVIEHN----LDVIKTAdWIVDlgpeggsgGGEILVSGTPETV 924
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNvretLAVCERA-YIVS--------QGHLIAHGTPTEI 224
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
823-893 3.98e-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: 45.75  E-value: 3.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 823 LGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLD 893
Cdd:cd03297  125 LNRYPAQLSGGEKQRVALARALAAQ---PELLLLDEPFSALDRALRLQLLPELKQIKKNLNiPVIFVTHDLS 193
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
774-923 4.33e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.72  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  774 ETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLmdvgltyirLGQSATTLSGGEAQRVKLARELSKrgtGQTL 853
Cdd:PTZ00265  533 ELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETL---------VGSNASKLSGGQKQRISIARAIIR---NPKI 600
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980  854 YILDEPTTGLHFADIQQLLDVLHQLRDQGNTI-VVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPET 923
Cdd:PTZ00265  601 LILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPT 671
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
811-890 4.49e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 47.35  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  811 QTLMDVGL-----TYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTI 885
Cdd:TIGR00955 143 EVLQALGLrkcanTRIGVPGRVKGLSGGERKRLAFASELL---TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTI 219

                  ....*
gi 489956980  886 VVIEH 890
Cdd:TIGR00955 220 ICTIH 224
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
470-902 4.87e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 47.09  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 470 LVNVGLNyLTLSRSAETLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDED 549
Cdd:PRK09700 130 LLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM--LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 550 AIRA-ADHVIDIGPGAGVHGGqVVAEGTLKDI--MAVPESLTGQYMSGKRKIEVPKQRVAAnpeKVLKLTGARGNNLKDV 626
Cdd:PRK09700 207 EIRRiCDRYTVMKDGSSVCSG-MVSDVSNDDIvrLMVGRELQNRFNAMKENVSNLAHETVF---EVRNVTSRDRKKVRDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 627 TLTLPVGLFTCITGVSGSGKSTLINdTLF---PIA--QTALNGATLaepapyrdiqglehfdkvididqspigrTPRSNp 701
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMN-CLFgvdKRAggEIRLNGKDI----------------------------SPRSP- 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 702 atytgvFTPVRELFAGVPEA-RSRGYTPGrFSfnvrggrceacqgdgvIKVEMHFLPDIYVPcdqckgkrynretleiKY 780
Cdd:PRK09700 333 ------LDAVKKGMAYITESrRDNGFFPN-FS----------------IAQNMAISRSLKDG----------------GY 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 781 KGK--TIHEVLDM-TIEEAREFfdavpaLARKLQTlmdvgltyirLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILD 857
Cdd:PRK09700 374 KGAmgLFHEVDEQrTAENQREL------LALKCHS----------VNQNITELSGGNQQKVLISKWLC---CCPEVIIFD 434
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 489956980 858 EPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIA 480
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-568 5.39e-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: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrDNE-RLLGTLVHLR---NLGNTVIVVEHD---EDA 550
Cdd:cd03237  109 LDREVPELSGGELQRVAIAACLSkdADI----YLLDEPSAYL---DVEqRLMASKVIRRfaeNNEKTAFVVEHDiimIDY 181
                         90
                 ....*....|....*...
gi 489956980 551 IraADHVIDIGPGAGVHG 568
Cdd:cd03237  182 L--ADRLIVFEGEPSVNG 197
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
805-896 6.05e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 45.58  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGN 883
Cdd:PRK11629 122 INSRALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNN---PRLVLADEPTGNLDARNADSIFQLLGELnRLQGT 197
                         90
                 ....*....|...
gi 489956980 884 TIVVIEHNLDVIK 896
Cdd:PRK11629 198 AFLVVTHDLQLAK 210
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
830-896 6.06e-05

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 46.33  E-value: 6.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSKRGTgqtlyIL--DEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLDVIK 896
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPK-----VLlcDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVK 205
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
830-922 6.48e-05

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: 45.57  E-value: 6.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaD------IQQLLDVLHQLrdQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:cd03261  137 LSGGMKKRVALARALA---LDPELLLYDEPTAGL---DpiasgvIDDLIRSLKKE--LGLTSIMVTHDLDtAFAIADRIA 208
                         90       100
                 ....*....|....*....|
gi 489956980 903 DLgpeggsGGGEILVSGTPE 922
Cdd:cd03261  209 VL------YDGKIVAEGTPE 222
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
796-888 6.56e-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: 45.26  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 796 AREFFDAVPAL---------ARKLQTLMDVGLtYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfa 866
Cdd:cd03264   89 VREFLDYIAWLkgipskevkARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD---PSILIVDEPTAGL--- 161
                         90       100
                 ....*....|....*....|..
gi 489956980 867 DIQQLLDVLHQLRDQGNTIVVI 888
Cdd:cd03264  162 DPEERIRFRNLLSELGEDRIVI 183
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
412-560 6.71e-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: 45.17  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 412 TRLRReaRHV-FV-------------ENTALPtisdmsighamdffnnLKLSGQRAKIAEKVLKEIGDRlkflvnVGLNY 477
Cdd:cd03255   77 AAFRR--RHIgFVfqsfnllpdltalENVELP----------------LLLAGVPKKERRERAEELLER------VGLGD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 478 LtLSRSAETLSGGEAQRIRLASqigAGLVGVMYVL-DEPSIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHDEDAIRAAD 555
Cdd:cd03255  133 R-LNHYPSELSGGQQQRVAIAR---ALANDPKIILaDEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYAD 208

                 ....*
gi 489956980 556 HVIDI 560
Cdd:cd03255  209 RIIEL 213
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
623-902 6.97e-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: 45.37  E-value: 6.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqtalngatlaepapyRDIQGLEHFDK-VIDIDQSPIGRTPRSnp 701
Cdd:COG1126   17 LKGISLDVEKGEVVVIIGPSGSGKSTLL-----------------------RCINLLEEPDSgTITVDGEDLTDSKKD-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 702 atytgvftpvrelfagVPEARSRgytpgrfsfnvrggrceacqgdgvikVEMHFlpdiyvpcdQckgkRYNretLeikYK 781
Cdd:COG1126   72 ----------------INKLRRK--------------------------VGMVF---------Q----QFN---L---FP 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 782 GKTIHE--------VLDMTIEEAREffdavpaLARKLqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELS---Krgtg 850
Cdd:COG1126   91 HLTVLEnvtlapikVKKMSKAEAEE-------RAMEL--LERVGLAD-KADAYPAQLSGGQQQRVAIARALAmepK---- 156
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 851 qtlYIL-DEPTTGLhfaD---IQQLLDVLHQLRDQGNTIVVIEHNL----DViktADWIV 902
Cdd:COG1126  157 ---VMLfDEPTSAL---DpelVGEVLDVMRDLAKEGMTMVVVTHEMgfarEV---ADRVV 207
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
454-601 7.27e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 45.75  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 454 KIAEKVLKEIGDRLKFLVNVgLNYLtlSRSAETLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLVH 533
Cdd:PRK13632 113 KVPPKKMKDIIDDLAKKVGM-EDYL--DKEPQNLSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDPKGKREIKKIMVD 187
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 534 LRNLGN-TVIVVEHDEDAIRAADHVIDIGpgagvhGGQVVAEGTLKDIMAVPESLTgqymsgKRKIEVP 601
Cdd:PRK13632 188 LRKTRKkTLISITHDMDEAILADKVIVFS------EGKLIAQGKPKEILNNKEILE------KAKIDSP 244
hmuV PRK13547
heme ABC transporter ATP-binding protein;
823-924 7.38e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 45.59  E-value: 7.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 823 LGQSATTLSGGEAQRVKLARELSK------RGTGQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLDV- 894
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLAQlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLa 218
                         90       100       110
                 ....*....|....*....|....*....|
gi 489956980 895 IKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13547 219 ARHADRIAML------ADGAIVAHGAPADV 242
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
782-902 7.68e-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: 7.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 782 GKTIHEVL----DMTIEEAReffdavpalARKLQTLMDVGLT--YIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYI 855
Cdd:COG4172  112 GKQIAEVLrlhrGLSGAAAR---------ARALELLERVGIPdpERRLDAYPHQLSGGQRQRVMIAMALA---NEPDLLI 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489956980 856 LDEPTTGLhfaD--IQ-QLLDVLHQL-RDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG4172  180 ADEPTTAL---DvtVQaQILDLLKDLqRELGMALLLITHDLGVVrRFADRVA 228
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
806-901 7.94e-05

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: 45.33  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 806 LARKLQTLMDVGLT-----YIRlgqsatTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQL-R 879
Cdd:cd03294  138 EERAAEALELVGLEgwehkYPD------ELSGGMQQRVGLARALA---VDPDILLMDEAFSALDPLIRREMQDELLRLqA 208
                         90       100
                 ....*....|....*....|...
gi 489956980 880 DQGNTIVVIEHNLD-VIKTADWI 901
Cdd:cd03294  209 ELQKTIVFITHDLDeALRLGDRI 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
822-892 8.02e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 45.41  E-value: 8.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNL 892
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVK---PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
3-594 8.28e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 46.75  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980    3 KIEVRgARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQrryveslsayarqflSLMEKPDvdhiEGLSPA 82
Cdd:PRK00635 1496 TLSVS-LSIHTIQNLNVSAPLHSLVAISGVSGSGKTSLLLEGFYKQAC---------------ALIEKGP----SVFSEI 1555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980   83 ISIEQKSTSHNPRSTVGTITEIHDYLRLLYARvgeprcpdhdvplaaqtvsqmvdnvLSQpegkrlmllapiikerkgeh 162
Cdd:PRK00635 1556 IFLDSHPQISSQRSDISTYFDIAPSLRNFYAS-------------------------LTQ-------------------- 1590
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  163 tktlenlasqgyiraridgevcdlsdppklelqkkhtievvidrfkvredlatrlaesfetalelsggtavvsdmddAKA 242
Cdd:PRK00635 1591 -----------------------------------------------------------------------------AKA 1593
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  243 eeLLFSAnfacpicgySMreleprlFSFNNPAGACPTCDGLGVQqyfdpdrviqnpelslaggairgWDKRNFYyfqmlk 322
Cdd:PRK00635 1594 --LNISA---------SM-------FSTNTKQGQCSDCWGLGYQ-----------------------WIDRAFY------ 1626
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  323 slaehykfdveapwaslsanvhkvilfgsgkeniefkymndrgdtsvrrhpfegvlhNMERryketessavreelakfis 402
Cdd:PRK00635 1627 ---------------------------------------------------------ALEK------------------- 1630
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  403 nRSCATCEGTRLRREARHVFVENTALPTISDMSIGHAMDFFnnlklsgqrakiaeKVLKEIGDRLKFLVNVGLNYLTLSR 482
Cdd:PRK00635 1631 -RPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETF--------------PFLKKIQKPLQALIDNGLGYLPLGQ 1695
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  483 SAETLSGGEAQRIRLASQIG-AGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIG 561
Cdd:PRK00635 1696 NLSSLSLSEKIAIKIAKFLYlPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMG 1775
                         570       580       590
                  ....*....|....*....|....*....|...
gi 489956980  562 PGAGVHGGQVVAEGTLKDIMAVPESLTGQYMSG 594
Cdd:PRK00635 1776 PGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
830-893 8.77e-05

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 44.96  E-value: 8.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLD 893
Cdd:PRK10771 130 LSGGQRQRVALARCLVRE---QPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLE 191
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
454-547 9.40e-05

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: 46.32  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 454 KIAEK-VLKEIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIrlasQIGAGLV--GVMYVLDEPSIGL--HQRDN-ERL 527
Cdd:COG1245  186 KVDERgKLDELAEKL------GLENI-LDRDISELSGGELQRV----AIAAALLrdADFYFFDEPSSYLdiYQRLNvARL 254
                         90       100
                 ....*....|....*....|
gi 489956980 528 LGTLVhlrNLGNTVIVVEHD 547
Cdd:COG1245  255 IRELA---EEGKYVLVVEHD 271
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
486-581 9.53e-05

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: 45.08  E-value: 9.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIrlasQIGAGLVG--VMYVLDEPSIGL--HQRdnERLLGTLVHLRNLGNTVI--VVEHDEDAIRAADHVID 559
Cdd:COG1119  142 TLSQGEQRRV----LIARALVKdpELLILDEPTAGLdlGAR--ELLLALLDKLAAEGAPTLvlVTHHVEEIPPGITHVLL 215
                         90       100
                 ....*....|....*....|..
gi 489956980 560 IgpgagvHGGQVVAEGTLKDIM 581
Cdd:COG1119  216 L------KDGRVVAAGPKEEVL 231
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
822-891 9.81e-05

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 44.77  E-value: 9.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHN 891
Cdd:PRK10584 139 RLDHLPAQLSGGEQQRVALARAFNGR---PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
823-902 1.00e-04

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: 45.48  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 823 LGQSATTLSGGEAQRVKLAREL--SKRgtgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGNT-IVVIEHNLD-VIKTA 898
Cdd:COG4148  127 LDRRPATLSGGERQRVAIGRALlsSPR-----LLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDeVARLA 201

                 ....
gi 489956980 899 DWIV 902
Cdd:COG4148  202 DHVV 205
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
788-892 1.05e-04

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 45.13  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 788 VLDMTIE-------EAREffdAVPALARKLqtLMDVGLT-----YIRlgqsatTLSGGEAQRVKLARELSKRgtgQTLYI 855
Cdd:PRK11264 102 VLENIIEgpvivkgEPKE---EATARAREL--LAKVGLAgketsYPR------RLSGGQQQRVAIARALAMR---PEVIL 167
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489956980 856 LDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNL 892
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
830-895 1.09e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 45.78  E-value: 1.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI 895
Cdd:PRK10938 136 LSTGETRKTLLCQALM---SEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEI 198
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
487-589 1.11e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 45.07  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASqIGAGLVGVMyVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVIDIGpgag 565
Cdd:PRK13639 138 LSGGQKKRVAIAG-ILAMKPEII-VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMS---- 211
                         90       100
                 ....*....|....*....|....
gi 489956980 566 vhGGQVVAEGTLKDIMAVPESLTG 589
Cdd:PRK13639 212 --DGKIIKEGTPKEVFSDIETIRK 233
PLN03211 PLN03211
ABC transporter G-25; Provisional
816-890 1.16e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.03  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 816 VGLTYIRlgqsatTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEH 890
Cdd:PLN03211 199 IGNSFIR------GISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
825-892 1.25e-04

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: 44.48  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 825 QSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQgNTIVVIEHNL 892
Cdd:cd03260  137 LHALGLSGGQQQRLCLARALANE---PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNM 200
cbiO PRK13637
energy-coupling factor transporter ATPase;
816-924 1.29e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 45.04  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 816 VGLTYIRL-GQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQ-GNTIVVIEHNL- 892
Cdd:PRK13637 130 VGLDYEDYkDKSPFELSGGQKRRVAIAGVVAME---PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMe 206
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489956980 893 DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13637 207 DVAKLADRIIVM------NKGKCELQGTPREV 232
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
825-899 1.36e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 45.43  E-value: 1.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 825 QSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLHQlrdQGNTIVVIEHNLD-VIKTAD 899
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEAS---PQLLIVDEPTRGVDVsarNDIYQLIRSIAA---QNVAVLFISSDLEeIEQMAD 471
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
805-924 1.37e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 44.60  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 805 ALARKLQTLMDVGLTYIrLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLH---FADIQQLLDvlhQLRDQ 881
Cdd:PRK11300 130 ALDRAATWLERVGLLEH-ANRQAGNLAYGQQRRLEIARCMV---TQPEILMLDEPAAGLNpkeTKELDELIA---ELRNE 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489956980 882 -GNTIVVIEHNLD-VIKTADWIVDLGPEGGsgggeiLVSGTPETV 924
Cdd:PRK11300 203 hNVTVLLIEHDMKlVMGISDRIYVVNQGTP------LANGTPEEI 241
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
829-904 1.40e-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: 43.30  E-value: 1.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 829 TLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaDIQQLLDVLHQLRDQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03223   91 VLSGGEQQRLAFARLLLHK---PKFVFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL 160
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
830-902 1.64e-04

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: 45.58  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaDIQQLLDVLHQLRD--QGNTIVVIEHNLDVIKTADWIV 902
Cdd:COG5265  495 LSGGEKQRVAIARTLLKN---PPILIFDEATSAL---DSRTERAIQAALREvaRGRTTLVIAHRLSTIVDADEIL 563
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
613-902 1.66e-04

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: 45.10  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLIND----TLFPIAQTALNGATLAEPApyrdiqglehfdkvidi 688
Cdd:TIGR02142   3 ARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLiaglTRPDEGEIVLNGRTLFDSR----------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  689 dqspigrtprsnpatyTGVFTPvrelfagvPEARSRGYTpgrfsFNvrggrceacqgdgvikvEMHFLPDIYVpcdqckg 768
Cdd:TIGR02142  66 ----------------KGIFLP--------PEKRRIGYV-----FQ-----------------EARLFPHLSV------- 92
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  769 krynRETLEIKYKgktihevlDMTIEEAREFFDAVPALarklqtlmdVGLTYIrLGQSATTLSGGEAQRVKLARELSkrg 848
Cdd:TIGR02142  93 ----RGNLRYGMK--------RARPSERRISFERVIEL---------LGIGHL-LGRLPGRLSGGEKQRVAIGRALL--- 147
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980  849 TGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNT-IVVIEHNLD-VIKTADWIV 902
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQeVLRLADRVV 203
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
462-547 1.74e-04

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: 45.16  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 462 EIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrD-NERLLGTLV---HLR 535
Cdd:COG1245  438 EIIKPL------GLEKL-LDKNVKDLSGGELQRVAIAACLSrdADL----YLLDEPSAHL---DvEQRLAVAKAirrFAE 503
                         90
                 ....*....|..
gi 489956980 536 NLGNTVIVVEHD 547
Cdd:COG1245  504 NRGKTAMVVDHD 515
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
783-902 1.79e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 45.34  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 783 KTIHEVL-----DMTIEEAREFFDAVPAL---ARKLQTLMDVgltyirLGQSATTLSGGEAQRVKLARELSKRGtgqTLY 854
Cdd:PRK13657 423 RSIEDNIrvgrpDATDEEMRAAAERAQAHdfiERKPDGYDTV------VGERGRQLSGGERQRLAIARALLKDP---PIL 493
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489956980 855 ILDEPTTGLHFADIQQLLDVLHQLRdQGNTIVVIEHNLDVIKTADWIV 902
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRIL 540
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
415-575 2.02e-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: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 415 RREARHVFVENTALPTIS-DMSIGHAMDffNNLKLSGQRAKIAEKVLKEigdrlkflvnVGLNYLtLSRSAETLSGGEAQ 493
Cdd:cd03298   69 DRPVSMLFQENNLFAHLTvEQNVGLGLS--PGLKLTAEDRQAIEVALAR----------VGLAGL-EKRLPGELSGGERQ 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 494 RIRLASQigagLV---GVMyVLDEP--SIGLHQRDNERLLGTLVHlRNLGNTVIVVEHD-EDAIRAADHVIDIgpgagvH 567
Cdd:cd03298  136 RVALARV----LVrdkPVL-LLDEPfaALDPALRAEMLDLVLDLH-AETKMTVLMVTHQpEDAKRLAQRVVFL------D 203

                 ....*...
gi 489956980 568 GGQVVAEG 575
Cdd:cd03298  204 NGRIAAQG 211
hmuV PRK13547
heme ABC transporter ATP-binding protein;
480-601 2.22e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 44.05  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 480 LSRSAETLSGGEAQRIRLA---SQI---GAGLVGVMY-VLDEPSIGLHQRDNERLLGTLVHLR---NLGNTVIVveHDED 549
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFArvlAQLwppHDAAQPPRYlLLDEPTAALDLAHQHRLLDTVRRLArdwNLGVLAIV--HDPN 216
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489956980 550 -AIRAADHVidigpgAGVHGGQVVAEGTLKDIMAvPESLTGQYMSGKRKIEVP 601
Cdd:PRK13547 217 lAARHADRI------AMLADGAIVAHGAPADVLT-PAHIARCYGFAVRLVDAG 262
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
623-902 2.39e-04

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 43.75  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtLfpiaqtalngatlaepapyrdIQGL-EHFDKVIDIDQSPIGRTPRSNp 701
Cdd:cd03254   19 LKDINFSIKPGETVAIVGPTGAGKTTLIN--L---------------------LMRFyDPQKGQILIDGIDIRDISRKS- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 702 atytgvftpVRELFAGVPEarSRGYTPGRFSFNVRGGRCEAcqgdgvikvemhflpdiyvpcdqckgkryNRETLEIKYK 781
Cdd:cd03254   75 ---------LRSMIGVVLQ--DTFLFSGTIMENIRLGRPNA-----------------------------TDEEVIEAAK 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 782 GKTIHEVLdMTIEEareffdavpalarklqtlmdvGLTYIrLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTT 861
Cdd:cd03254  115 EAGAHDFI-MKLPN---------------------GYDTV-LGENGGNLSQGERQLLAIARAMLRD---PKILILDEATS 168
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489956980 862 GLHF---ADIQQLLDVLHqlrdQGNTIVVIEHNLDVIKTADWIV 902
Cdd:cd03254  169 NIDTeteKLIQEALEKLM----KGRTSIIIAHRLSTIKNADKIL 208
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
623-651 2.46e-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: 43.61  E-value: 2.46e-04
                         10        20
                 ....*....|....*....|....*....
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIN 651
Cdd:cd03293   20 LEDISLSVEEGEFVALVGPSGCGKSTLLR 48
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
822-892 2.52e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 44.00  E-value: 2.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQgNTIVVIEHNL 892
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQ---PEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNM 210
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
417-899 2.55e-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: 44.82  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  417 EARHVFVENTALPTISDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEigdrLKFLVNVGLNYLTLSRSAETLSGGEAQRIR 496
Cdd:TIGR02633  76 ERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRA----KNLLRELQLDADNVTRPVGDYGGGQQQLVE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  497 LASQIGAGLVgvMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVIDIGPGAgvHGGQVVAEG 575
Cdd:TIGR02633 152 IAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ--HVATKDMST 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  576 -TLKDI--MAVPESLTGQYMSGKRKI--EVPKQR--VAANPekvlklTGARGNNLKDVTLTLPVGLFTCITGVSGSGKST 648
Cdd:TIGR02633 228 mSEDDIitMMVGREITSLYPHEPHEIgdVILEARnlTCWDV------INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTE 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  649 LIndtlfpiaqTALNGATLAEpapyrdiqglehFDKVIDIDQSPIG-RTPRSnpatytgvftPVRELFAGVPEARSRgyt 727
Cdd:TIGR02633 302 LV---------QALFGAYPGK------------FEGNVFINGKPVDiRNPAQ----------AIRAGIAMVPEDRKR--- 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  728 pgrfsfnvrggrceacqgDGVIkvemhflPDIYVpcdqckGKRYNRETLEiKYKGKtihevldMTIEEAREffdavpala 807
Cdd:TIGR02633 348 ------------------HGIV-------PILGV------GKNITLSVLK-SFCFK-------MRIDAAAE--------- 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  808 rklQTLMDVGLTYIRLGQSA-----TTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQG 882
Cdd:TIGR02633 380 ---LQIIGSAIQRLKVKTASpflpiGRLSGGNQQKAVLAKMLL---TNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG 453
                         490
                  ....*....|....*...
gi 489956980  883 NTIVVIEHNL-DVIKTAD 899
Cdd:TIGR02633 454 VAIIVVSSELaEVLGLSD 471
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
807-894 2.62e-04

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 43.90  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLHQlrDQGN 883
Cdd:PRK11247 112 DAALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHR---PGLLLLDEPLGALDAltrIEMQDLIESLWQ--QHGF 185
                         90
                 ....*....|.
gi 489956980 884 TIVVIEHnlDV 894
Cdd:PRK11247 186 TVLLVTH--DV 194
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
783-892 2.66e-04

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 43.91  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 783 KTIHEVLDmtiEEAREFFDAVPA--LARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPT 860
Cdd:PRK10419 106 KTVREIIR---EPLRHLLSLDKAerLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALA---VEPKLLILDEAV 179
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489956980 861 TGLHFADIQQLLDVLHQLRDQGNT-IVVIEHNL 892
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDL 212
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
487-575 2.69e-04

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: 42.69  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLV-HLRNlgNTVIVVEHDEDAIRAADHVIDIgpg 563
Cdd:cd03247   99 FSGGERQRLALARILlqDAPIV----LLDEPTVGLDPITERQLLSLIFeVLKD--KTLIWITHHLTGIEHMDKILFL--- 169
                         90
                 ....*....|..
gi 489956980 564 agvHGGQVVAEG 575
Cdd:cd03247  170 ---ENGKIIMQG 178
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
807-893 2.75e-04

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: 43.28  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQTLMDVGLTyIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLHqlRDQGN 883
Cdd:cd03259  109 ARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALARE---PSLLLLDEPLSALDAklrEELREELKELQ--RELGI 182
                         90
                 ....*....|
gi 489956980 884 TIVVIEHNLD 893
Cdd:cd03259  183 TTIYVTHDQE 192
cbiO PRK13641
energy-coupling factor transporter ATPase;
794-899 2.98e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 43.66  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 794 EEAREffdavpalaRKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLD 873
Cdd:PRK13641 119 DEAKE---------KALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYE---PEILCLDEPAAGLDPEGRKEMMQ 186
                         90       100
                 ....*....|....*....|....*..
gi 489956980 874 VLHQLRDQGNTIVVIEHNL-DVIKTAD 899
Cdd:PRK13641 187 LFKDYQKAGHTVILVTHNMdDVAEYAD 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
487-558 2.99e-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: 42.56  E-value: 2.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 487 LSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLHQRDNERLLGTLVHLR-NLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:cd03229  101 LSGGQQQRVALARAL------AMdpdvLLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDlDEAARLADRVV 172
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
487-558 3.20e-04

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: 42.42  E-value: 3.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVI 558
Cdd:cd03216   83 LSVGERQMVEIARALarNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVT 153
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
830-895 3.35e-04

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: 42.56  E-value: 3.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHQLR----DQGNTIVVIEHNLDVI 895
Cdd:cd03222   72 LSGGELQRVAIAAALLRNA---TFYLFDEPSAYL---DIEQRLNAARAIRrlseEGKKTALVVEHDLAVL 135
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
487-601 3.46e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 43.60  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASQIGAGLVGVMYvlDEPSIGlhqrDNERLLGTLVHL-----RNLGNTVIVVEHD-EDAIRAADHVIDI 560
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMF--DEPFVG----QDPITMGVLVKLiselnSALGVTCVVVSHDvPEVLSIADHAYIV 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489956980 561 GpgagvhGGQVVAEGTLKDIMAVPESLTGQYMSGKRKIEVP 601
Cdd:PRK11831 218 A------DKKIVAHGSAQALQANPDPRVRQFLDGIADGPVP 252
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
487-587 3.61e-04

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 43.98  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRI---R-LASQIGAGLvgvmyvLDEPSIGL--HQRDN-ERLLGTLvhLRNLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:COG1118  134 LSGGQRQRValaRaLAVEPEVLL------LDEPFGALdaKVRKElRRWLRRL--HDELGGTTVFVTHDqEEALELADRVV 205
                         90       100       110
                 ....*....|....*....|....*....|
gi 489956980 559 digpgagV-HGGQVVAEGTLKDIMAVPESL 587
Cdd:COG1118  206 -------VmNQGRIEQVGTPDEVYDRPATP 228
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
14-41 3.74e-04

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: 42.37  E-value: 3.74e-04
                         10        20
                 ....*....|....*....|....*...
gi 489956980  14 LKNINLIIPRDKLIVVTGLSGSGKSSLA 41
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
481-594 3.75e-04

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 42.94  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 481 SRSAETLSGGEAQRIrlasQIGAGLVGV--MYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDED-AIRAADHv 557
Cdd:PRK11614 132 IQRAGTMSGGEQQML----AIGRALMSQprLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADR- 206
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489956980 558 idigpGAGVHGGQVVAEGTLKDIMAvPESLTGQYMSG 594
Cdd:PRK11614 207 -----GYVLENGHVVLEDTGDALLA-NEAVRSAYLGG 237
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
777-896 3.76e-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: 42.51  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 777 EIKYKGKTIhevLDMTIEE-ARE-FFDA------VPALarklqTLMDVgLTYIRLGqsattLSGGEAQRVKLARELSKRg 848
Cdd:cd03217   58 EILFKGEDI---TDLPPEErARLgIFLAfqyppeIPGV-----KNADF-LRYVNEG-----FSGGEKKRNEILQLLLLE- 122
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489956980 849 tgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHN---LDVIK 896
Cdd:cd03217  123 --PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK 171
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
830-902 4.04e-04

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: 43.19  E-value: 4.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQL-RDQGNTIVVIEHNLDVIKTADWIV 902
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMR---PDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVLADRVI 207
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
793-904 4.73e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 43.90  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 793 IEEAREFFDAVPALARKLQTLMDV-----------------GLTYIRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYI 855
Cdd:COG0488   99 LEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilsglGFPEEDLDRPVSELSGGWRRRVALARALLSEP---DLLL 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489956980 856 LDEPTTGLHFADIQQLLDVLHQLRdqgNTIVVIEHN---LDviKTADWIVDL 904
Cdd:COG0488  176 LDEPTNHLDLESIEWLEEFLKNYP---GTVLVVSHDryfLD--RVATRILEL 222
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
804-901 4.77e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.89  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 804 PALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHQLRDQGN 883
Cdd:PRK15439 115 QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR---ILILDEPTASLTPAETERLFSRIRELLAQGV 191
                         90
                 ....*....|....*....
gi 489956980 884 TIVVIEHNL-DVIKTADWI 901
Cdd:PRK15439 192 GIVFISHKLpEIRQLADRI 210
cbiO PRK13643
energy-coupling factor transporter ATPase;
807-924 4.97e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.18  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQTlmdVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIV 886
Cdd:PRK13643 125 AEKLEM---VGLADEFWEKSPFELSGGQMRRVAIAGILAME---PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVV 198
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489956980 887 VIEHNL-DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13643 199 LVTHLMdDVADYADYVYLL------EKGHIISCGTPSDV 231
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
807-890 5.41e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 43.28  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQTLMDVGLTYIRLGQSATT----LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQG 882
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARALI---NDPQLLILDEPTTGLDPHARHLIWERLRSLLARG 222

                 ....*...
gi 489956980 883 NTIVVIEH 890
Cdd:PRK13536 223 KTILLTTH 230
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
811-904 5.55e-04

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 43.64  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 811 QTLMDVGLTYI--RLGQSA---TTLSGGEAQRVKLARELskrgtgqtLY-----ILDEPTTGLhfaDIQQLLDVLHQLRD 880
Cdd:COG4178  462 EALEAVGLGHLaeRLDEEAdwdQVLSLGEQQRLAFARLL--------LHkpdwlFLDEATSAL---DEENEAALYQLLRE 530
                         90       100
                 ....*....|....*....|....*.
gi 489956980 881 Q--GNTIVVIEHNLDVIKTADWIVDL 904
Cdd:COG4178  531 ElpGTTVISVGHRSTLAAFHDRVLEL 556
cbiO PRK13640
energy-coupling factor transporter ATPase;
454-587 5.68e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 42.86  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 454 KIAEKVLKEIGdrlkflvnvGLNYLtlSRSAETLSGGEAQRIRLasqigAGLVGV---MYVLDEPSIGLHQRDNERLLGT 530
Cdd:PRK13640 122 KIVRDVLADVG---------MLDYI--DSEPANLSGGQKQRVAI-----AGILAVepkIIILDESTSMLDPAGKEQILKL 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 531 LVHLRNLGN-TVIVVEHDEDAIRAADHVIDIgpgagvHGGQVVAEGTLKDIMAVPESL 587
Cdd:PRK13640 186 IRKLKKKNNlTVISITHDIDEANMADQVLVL------DDGKLLAQGSPVEIFSKVEML 237
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
462-547 5.76e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 43.64  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 462 EIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrD-NERLLGTLV---HLR 535
Cdd:PRK13409 436 EIIKPL------QLERL-LDKNVKDLSGGELQRVAIAACLSrdADL----YLLDEPSAHL---DvEQRLAVAKAirrIAE 501
                         90
                 ....*....|..
gi 489956980 536 NLGNTVIVVEHD 547
Cdd:PRK13409 502 EREATALVVDHD 513
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
830-893 6.30e-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: 42.07  E-value: 6.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 830 LSGGEAQRVKLARELSKRgtGQTLyILDEPttglhFA--------DIQQLLdvLHQLRDQGNTIVVIEHNLD 893
Cdd:cd03293  132 LSGGMRQRVALARALAVD--PDVL-LLDEP-----FSaldaltreQLQEEL--LDIWRETGKTVLLVTHDID 193
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
830-891 7.12e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 42.90  E-value: 7.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGL--HFADIQQlLDVLHQLRDQGNTIVVIEHN 891
Cdd:PRK11607 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALdkKLRDRMQ-LEVVDILERVGVTCVMVTHD 209
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
795-904 7.43e-04

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: 43.39  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  795 EAREFFDAVPA--LARKLQTLMDVgltyIRL---GQSATTLSGGEAQRVKLAREL-SKrgtgQTLYILDEPTTGLhfaDI 868
Cdd:TIGR03719 126 ELQEIIDAADAwdLDSQLEIAMDA----LRCppwDADVTKLSGGERRRVALCRLLlSK----PDMLLLDEPTNHL---DA 194
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 489956980  869 QQLLDVLHQLRDQGNTIVVIEHN---LDVIktADWIVDL 904
Cdd:TIGR03719 195 ESVAWLERHLQEYPGTVVAVTHDryfLDNV--AGWILEL 231
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
467-597 7.94e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 42.26  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEH 546
Cdd:PRK10619 133 VKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL--AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489956980 547 D-EDAIRAADHVIDIgpgagvHGGQVVAEGTLKDIMAVPES-LTGQYMSGKRK 597
Cdd:PRK10619 211 EmGFARHVSSHVIFL------HQGKIEEEGAPEQLFGNPQSpRLQQFLKGSLK 257
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
458-547 7.98e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 43.26  E-value: 7.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 458 KVLKEIGDRLKfLVNVglnyltLSRSAETLSGGEAQRIRLAsqigAGLV--GVMYVLDEPSIGLHQRdnERLLGTLVhLR 535
Cdd:PRK13409 191 GKLDEVVERLG-LENI------LDRDISELSGGELQRVAIA----AALLrdADFYFFDEPTSYLDIR--QRLNVARL-IR 256
                         90
                 ....*....|....
gi 489956980 536 NL--GNTVIVVEHD 547
Cdd:PRK13409 257 ELaeGKYVLVVEHD 270
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-41 8.41e-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: 41.68  E-value: 8.41e-04
                         10        20
                 ....*....|....*....|....*...
gi 489956980  14 LKNINLIIPRDKLIVVTGLSGSGKSSLA 41
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
791-924 8.42e-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: 41.90  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTIEEAREffdAVPAL---------ARKLQTLMDVGLTYIRLGQS-ATTLSGGEAQRVKLARELSkrgTGQTLYILDEPT 860
Cdd:cd03295   90 MTVEENIA---LVPKLlkwpkekirERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALA---ADPPLLLMDEPF 163
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956980 861 TGL----------HFADIQQLLdvlhqlrdqGNTIVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:cd03295  164 GALdpitrdqlqeEFKRLQQEL---------GKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEI 223
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
830-895 9.84e-04

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 42.59  E-value: 9.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 830 LSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHNLDVI 895
Cdd:PRK11288 141 LSIGQRQMVEIAKALAR---NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEI 203
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-547 1.02e-03

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: 41.97  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 480 LSRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPS--IGLHQRDN-ERLLGTLVhlrNLGNTVIVVEHD 547
Cdd:cd03236  133 LDRNIDQLSGGELQRVAIAAALARD--ADFYFFDEPSsyLDIKQRLNaARLIRELA---EDDNYVLVVEHD 198
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
791-896 1.02e-03

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 42.39  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 791 MTI-----EEAREFFdavPALAR-----KLQTLMD-VGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEP 859
Cdd:PRK15079 115 MTIgeiiaEPLRTYH---PKLSRqevkdRVKAMMLkVGLLPNLINRYPHEFSGGQCQRIGIARALILE---PKLIICDEP 188
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489956980 860 TTGLHFAdIQ-QLLDVLHQL-RDQGNTIVVIEHNLDVIK 896
Cdd:PRK15079 189 VSALDVS-IQaQVVNLLQQLqREMGLSLIFIAHDLAVVK 226
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
830-895 1.04e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 42.92  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLHQLRDQGntIVVIEHNLDVI 895
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVV 232
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
486-564 1.23e-03

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: 41.27  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLAsqigAGLVG---VMyVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVIDIG 561
Cdd:COG4778  152 TFSGGEQQRVNIA----RGFIAdppLL-LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226

                 ...
gi 489956980 562 PGA 564
Cdd:COG4778  227 PFS 229
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
829-902 1.25e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 42.17  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 829 TLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNT-IVVIEHNLD-VIKTADWIV 902
Cdd:PRK11144 128 SLSGGEKQRVAIGRALL---TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDeILRLADRVV 200
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
487-575 1.39e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 41.64  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDED-AIRAADHVIDIgpgag 565
Cdd:PRK13647 139 LSYGQKKRVAIAGVLA--MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVL----- 211
                         90
                 ....*....|
gi 489956980 566 vHGGQVVAEG 575
Cdd:PRK13647 212 -KEGRVLAEG 220
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
424-584 1.48e-03

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 42.14  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 424 ENTAL--PTISDMSIGHAMdffnnlklsgQRAKIAEKVlkeigDRLKflvnVGLNYLTLSRSAeTLSGGEAQRIRLASQI 501
Cdd:PRK11174 441 DNVLLgnPDASDEQLQQAL----------ENAWVSEFL-----PLLP----QGLDTPIGDQAA-GLSVGQAQRLALARAL 500
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 502 GAGlvGVMYVLDEPSIGLHQRDNERLLGTLVHLRNlGNTVIVVEHDEDAIRAADH--VIDigpgagvhGGQVVAEGTLKD 579
Cdd:PRK11174 501 LQP--CQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQWDQiwVMQ--------DGQIVQQGDYAE 569

                 ....*
gi 489956980 580 IMAVP 584
Cdd:PRK11174 570 LSQAG 574
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
830-902 1.50e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 41.51  E-value: 1.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIKTADWIV 902
Cdd:PRK13632 143 LSGGQKQRVAIASVLA---LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVI 213
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
485-587 1.52e-03

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 41.53  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 485 ETLSGGEAQRIRLAsqiGAGLVGVMYVL-DEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIgpg 563
Cdd:PRK13638 135 QCLSHGQKKRVAIA---GALVLQARYLLlDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYV--- 208
                         90       100
                 ....*....|....*....|....
gi 489956980 564 agVHGGQVVAEGTLKDIMAVPESL 587
Cdd:PRK13638 209 --LRQGQILTHGAPGEVFACTEAM 230
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
829-895 1.62e-03

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 41.63  E-value: 1.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956980 829 TLSGGEAQRVKLArelskrgtgQT------LYILDEPTTGLhfaD---IQQLLDVLHQLRDQGNTIVVIEHNLDVI 895
Cdd:COG4152  129 ELSKGNQQKVQLI---------AAllhdpeLLILDEPFSGL---DpvnVELLKDVIRELAAKGTTVIFSSHQMELV 192
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
823-902 1.80e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 42.32  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  823 LGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIKTADWI 901
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLRE---PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDKI 1428

                  .
gi 489956980  902 V 902
Cdd:PTZ00265 1429 V 1429
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
830-898 1.99e-03

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 41.27  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIKTA 898
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACR---PKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEA 220
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
14-41 2.13e-03

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: 39.55  E-value: 2.13e-03
                          10        20
                  ....*....|....*....|....*...
gi 489956980   14 LKNINLIIPRDKLIVVTGLSGSGKSSLA 41
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
14-41 2.38e-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: 41.74  E-value: 2.38e-03
                         10        20
                 ....*....|....*....|....*...
gi 489956980  14 LKNINLIIPRDKLIVVTGLSGSGKSSLA 41
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
cbiO PRK13642
energy-coupling factor transporter ATPase;
830-902 2.49e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 40.85  E-value: 2.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TIVVIEHNLDVIKTADWIV 902
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALR---PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRIL 211
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
6-51 2.88e-03

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: 39.27  E-value: 2.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489956980   6 VRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQR 51
Cdd:cd03227    3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
790-893 2.89e-03

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: 40.53  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  790 DMTIEEAREFFDavpalarklQTLMDVGLTYI---RLGQsattLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFA 866
Cdd:TIGR01184  85 DLSKSERRAIVE---------EHIALVGLTEAadkRPGQ----LSGGMKQRVAIARALSIR---PKVLLLDEPFGALDAL 148
                          90       100
                  ....*....|....*....|....*...
gi 489956980  867 DIQQLLDVLHQL-RDQGNTIVVIEHNLD 893
Cdd:TIGR01184 149 TRGNLQEELMQIwEEHRVTVLMVTHDVD 176
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
6-40 3.06e-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: 40.24  E-value: 3.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489956980   6 VRGARTHNLKNINLIIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd03256    9 TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTL 43
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
790-890 3.24e-03

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: 39.65  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  790 DMTIEEAREFFDAVPALARK--LQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFAD 867
Cdd:TIGR01189  87 ELSALENLHFWAAIHGGAQRtiEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWL---SRRPLWILDEPTTALDKAG 162
                          90       100
                  ....*....|....*....|...
gi 489956980  868 IQQLLDVLHQLRDQGNTIVVIEH 890
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
822-892 3.43e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 40.46  E-value: 3.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 822 RLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQgNTIVVIEHNL 892
Cdd:PRK14271 156 RLSDSPFRLSGGQQQLLCLARTLA---VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNL 222
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
828-897 3.57e-03

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: 40.01  E-value: 3.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 828 TTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVV-IEHNLDVIKT 897
Cdd:cd03299  128 ETLSGGEQQRVAIARALV---VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWA 195
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
484-548 3.64e-03

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: 40.81  E-value: 3.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956980  484 AETLSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLVHLRNlGNTVIVVEHDE 548
Cdd:TIGR02868 469 GARLSGGERQRLALARALlaDAPIL----LLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
487-574 3.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEaqRI------RLA-SQIGAGLVGVMyVLDEPSIGLHQRDNERLLGTLV-HLRNLGNtVIVVEHDEDAIRAADHVI 558
Cdd:PRK03918 789 LSGGE--RIalglafRLAlSLYLAGNIPLL-ILDEPTPFLDEERRRKLVDIMErYLRKIPQ-VIIVSHDEELKDAADYVI 864
                         90
                 ....*....|....*.
gi 489956980 559 DIGPGAGVHGGQVVAE 574
Cdd:PRK03918 865 RVSLEGGVSKVEVVSL 880
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
487-563 4.04e-03

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: 38.58  E-value: 4.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956980 487 LSGGEAQRIRLASqigAGLVGV-MYVLDEPSIGLhqrDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVIDIGPG 563
Cdd:cd03221   71 LSGGEKMRLALAK---LLLENPnLLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
830-893 4.08e-03

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 40.07  E-value: 4.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPttglhFA--DIQ---QLLDVLHQL-RDQGNTIVVIEHNLD 893
Cdd:COG1116  139 LSGGMRQRVAIARALA---NDPEVLLMDEP-----FGalDALtreRLQDELLRLwQETGKTVLFVTHDVD 200
PLN03232 PLN03232
ABC transporter C family member; Provisional
795-902 4.58e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 41.11  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  795 EAREFFDAVPALArkLQTLMDV--GLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLL 872
Cdd:PLN03232  706 ESERYWRAIDVTA--LQHDLDLlpGRDLTEIGERGVNISGGQKQRVSMARAVY---SNSDIYIFDDPLSALDAHVAHQVF 780
                          90       100       110
                  ....*....|....*....|....*....|
gi 489956980  873 DVLHQLRDQGNTIVVIEHNLDVIKTADWIV 902
Cdd:PLN03232  781 DSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
414-563 4.61e-03

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: 39.70  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 414 LRREARHVFVENTALPTisdmsighaMDFFNNLKLSgqrAKIAEKVLKEIGDRLKFLVN-VGLNYLTLSRSAEtLSGGEA 492
Cdd:cd03292   76 LRRKIGVVFQDFRLLPD---------RNVYENVAFA---LEVTGVPPREIRKRVPAALElVGLSHKHRALPAE-LSGGEQ 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 493 QRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADH-VIDIGPG 563
Cdd:cd03292  143 QRVAIARAIVNS--PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERG 212
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
482-588 4.64e-03

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 40.60  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 482 RSAETLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGLhqrDNERLLGTLVHLRNL---GNTVIVVEHDED-AIRAADHV 557
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARAL-AQATPVL-LLDEPTASL---DINHQVRTLELVRRLvddGKTAVAAIHDLDlAARYCDEL 209
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489956980 558 IdigpgagvhggqVVAEGTLKDIMAVPESLT 588
Cdd:PRK09536 210 V------------LLADGRVRAAGPPADVLT 228
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
485-588 4.79e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 40.12  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 485 ETLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLVHLRNLGN-TVIVVEHDEDAIRAADHVIDIgpg 563
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLA--LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVM--- 215
                         90       100
                 ....*....|....*....|....*
gi 489956980 564 agvHGGQVVAEGTLKDIMAVPESLT 588
Cdd:PRK13648 216 ---NKGTVYKEGTPTEIFDHAEELT 237
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
440-587 5.01e-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: 39.53  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 440 MDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLVNVGlNYLtlSRSAETLSGGEAQRIRLASQIgaglvgVM----YVLDEP 515
Cdd:cd03300   87 LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYA--NRKPSQLSGGQQQRVAIARAL------VNepkvLLLDEP 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 516 SIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHD-EDAIRAADHVidigpgAGVHGGQVVAEGTLKDIMAVPESL 587
Cdd:cd03300  158 LGALDLKLRKDMQLELKRLqKELGITFVFVTHDqEEALTMSDRI------AVMNKGKIQQIGTPEEIYEEPANR 225
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
434-575 5.24e-03

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: 39.41  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 434 MSIGH----AMDFFNNLKLSGQRAKIAEKVLKEIGDRLKFLvnvglnyltlSRSAETLSGGEAQRIRLASQIGAG--LVg 507
Cdd:cd03257   99 MTIGEqiaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEVL----------NRYPHELSGGQRQRVAIARALALNpkLL- 167
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980 508 vmyVLDEPSIGLHQRDNERLLGTLVHLRN-LGNTVIVVEHDEDAIRA-ADHVIdigpgagV-HGGQVVAEG 575
Cdd:cd03257  168 ---IADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKiADRVA-------VmYAGKIVEEG 228
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
830-901 6.23e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 39.79  E-value: 6.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956980 830 LSGGEAQRVKLARELSKRGtgQTLyILDEPTTGLHFADIQQLLDVLHQLRDQ-GNTIVVIEHNLDVI-KTADWI 901
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEP--QVL-VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVpEMADYI 208
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
623-691 6.41e-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: 6.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQTALNGA-TLAEPAPYRDIQGLEHFDKVIDIDQS 691
Cdd:COG2401   46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCvDVPDNQFGREASLIDAIGRKGDFKDA 115
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
623-651 6.75e-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: 39.04  E-value: 6.75e-03
                         10        20
                 ....*....|....*....|....*....
gi 489956980 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIN 651
Cdd:cd03259   16 LDDLSLTVEPGEFLALLGPSGCGKTTLLR 44
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
486-657 6.77e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.10  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLASQIG--AGLVgvmyVLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRAADHVIDIgpg 563
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSynAKIV----IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITI--- 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 564 agVHGGQVVAEGTLKDI-------MAVPESLTGQYmsgKRKIEVPKQRVAanpeKVLKLTGARGNNLKDVTLTLPVGLFT 636
Cdd:PRK10982 207 --LRDGQWIATQPLAGLtmdkiiaMMVGRSLTQRF---PDKENKPGEVIL----EVRNLTSLRQPSIRDVSFDLHKGEIL 277
                        170       180
                 ....*....|....*....|.
gi 489956980 637 CITGVSGSgKSTLINDTLFPI 657
Cdd:PRK10982 278 GIAGLVGA-KRTDIVETLFGI 297
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
487-560 6.83e-03

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: 38.71  E-value: 6.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956980 487 LSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLhqrDNERLLGTLVHLRNL----GNTVIVVEHDedaIRAADHVIDI 560
Cdd:cd03222   72 LSGGELQRVAIAAALLRN--ATFYLFDEPSAYL---DIEQRLNAARAIRRLseegKKTALVVEHD---LAVLDYLSDR 141
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
486-576 7.04e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 40.15  E-value: 7.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 486 TLSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrD--NERLLgtLVHLRNL--GNTVIVVEHDEDAIRAAD 555
Cdd:COG1132  476 NLSGGQRQRIAIArallkdPPI--------LILDEATSAL---DteTEALI--QEALERLmkGRTTIVIAHRLSTIRNAD 542
                         90       100
                 ....*....|....*....|..
gi 489956980 556 HVIdigpgagV-HGGQVVAEGT 576
Cdd:COG1132  543 RIL-------VlDDGRIVEQGT 557
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
807-896 7.22e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.07  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 807 ARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGN-TI 885
Cdd:PRK15134 403 QQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILK---PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAY 479
                         90
                 ....*....|.
gi 489956980 886 VVIEHNLDVIK 896
Cdd:PRK15134 480 LFISHDLHVVR 490
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
487-580 7.59e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 39.30  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 487 LSGGEAQRIRLasqigAGLVGVM---YVLDEPSIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHDEDAIRAADHVIDIgp 562
Cdd:PRK13633 145 LSGGQKQRVAI-----AGILAMRpecIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVM-- 217
                         90
                 ....*....|....*...
gi 489956980 563 gagvHGGQVVAEGTLKDI 580
Cdd:PRK13633 218 ----DSGKVVMEGTPKEI 231
CP_lyasePhnL TIGR02324
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...
486-562 7.96e-03

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: 38.91  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  486 TLSGGEAQRIRLASqigaGLVgVMY---VLDEPSIGLHQRDNERLLGTLVHLRNLGNTVIVVEHDEDAIRA-ADHVIDIG 561
Cdd:TIGR02324 149 TFSGGEQQRVNIAR----GFI-ADYpilLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRVMDVT 223

                  .
gi 489956980  562 P 562
Cdd:TIGR02324 224 P 224
PTZ00243 PTZ00243
ABC transporter; Provisional
14-40 7.99e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.15  E-value: 7.99e-03
                          10        20
                  ....*....|....*....|....*..
gi 489956980   14 LKNINLIIPRDKLIVVTGLSGSGKSSL 40
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTL 702
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
830-897 8.17e-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: 39.92  E-value: 8.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956980  830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaDIQQLLDVLHQLRDQGNTIVVIEHN---LDVIKT 897
Cdd:TIGR03719 444 LSGGERNRVHLAKTLK---SGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHDrwfLDRIAT 508
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
434-558 8.42e-03

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 39.63  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 434 MSIGHAMDFfnNLKLSG-QRAKIAEKVlKEIGDRLKflvnvgLNYLtLSRSAETLSGGeaQRIRLAsqIGAGLVG--VMY 510
Cdd:PRK11000  90 LSVAENMSF--GLKLAGaKKEEINQRV-NQVAEVLQ------LAHL-LDRKPKALSGG--QRQRVA--IGRTLVAepSVF 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489956980 511 VLDEPSIGLHQ--RDNERLLGTLVHLRnLGNTVIVVEHDE-DAIRAADHVI 558
Cdd:PRK11000 156 LLDEPLSNLDAalRVQMRIEISRLHKR-LGRTMIYVTHDQvEAMTLADKIV 205
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
830-891 8.64e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 38.70  E-value: 8.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956980 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHQLRDQGNTIVVIEHN 891
Cdd:PRK13539 128 LSAGQKRRVALARLLV---SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
484-649 8.75e-03

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: 39.79  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  484 AETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNErllgtLVH------LRNLGNTVIVVEHDEDAI-RAADH 556
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKE--PFLFLADEPTGTLDPQTAK-----LVHnaleeaVKASGISMVLTSHWPEVIeDLSDK 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980  557 VIDIgpgagvHGGQVVAEGTlkdimavPESLTGQYMSGKRkiEVPKQRVAANPEKVLKLTGA--------RG--NNLKDV 626
Cdd:TIGR03269 239 AIWL------ENGEIKEEGT-------PDEVVAVFMEGVS--EVEKECEVEVGEPIIKVRNVskryisvdRGvvKAVDNV 303
                         170       180
                  ....*....|....*....|...
gi 489956980  627 TLTLPVGLFTCITGVSGSGKSTL 649
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTL 326
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-40 8.78e-03

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: 39.02  E-value: 8.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489956980   4 IEVRGART-----HNLKNINLIIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd03261    1 IELRGLTKsfggrTVLKGVDLDVRRGEILAIIGPSGSGKSTL 42
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
423-547 9.31e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 38.64  E-value: 9.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 423 VENTALPTIsdmsIGHAmdffnnlklsgQRAKIAEKVLKeigdrlkFLVNVGLNYLTLSRSAEtLSGGEAQRIRLASqig 502
Cdd:PRK11629 105 LENVAMPLL----IGKK-----------KPAEINSRALE-------MLAAVGLEHRANHRPSE-LSGGERQRVAIAR--- 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489956980 503 aGLVG--VMYVLDEPSIGLHQRDNE---RLLGTLVhlRNLGNTVIVVEHD 547
Cdd:PRK11629 159 -ALVNnpRLVLADEPTGNLDARNADsifQLLGELN--RLQGTAFLVVTHD 205
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
487-548 9.43e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 38.61  E-value: 9.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956980 487 LSGGEAQRIRLASQIgAGLVGVMYVlDEPSIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHDE 548
Cdd:PRK10584 147 LSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
407-576 9.51e-03

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: 38.50  E-value: 9.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 407 ATCEGTRLRREARHVFventalptiSDMSIGHAMDFFNNLKLSGQRAKIAEKVLKEIGDRLkflvnvgLNYLTL----SR 482
Cdd:cd03265   64 VVREPREVRRRIGIVF---------QDLSVDDELTGWENLYIHARLYGVPGAERRERIDEL-------LDFVGLleaaDR 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956980 483 SAETLSGGEAQRIrlasQIGAGLVGV--MYVLDEPSIGLHQRDNERLLGTLVHL-RNLGNTVIVVEHD-EDAIRAADHVi 558
Cdd:cd03265  128 LVKTYSGGMRRRL----EIARSLVHRpeVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYmEEAEQLCDRV- 202
                        170
                 ....*....|....*...
gi 489956980 559 digpgAGVHGGQVVAEGT 576
Cdd:cd03265  203 -----AIIDHGRIIAEGT 215
 
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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