NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16131884|ref|NP_418482|]
View 

UvrABC excision nuclease subunit A [Escherichia coli str. K-12 substr. MG1655]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 2026.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    1 MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDP 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRR-NFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  320 MLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  400 FISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  560 IGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  640 GVSGSGKSTLINDTLFPIAQRQLNGATIaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  720 ESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLR 879
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  880 DQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPML 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: 2026.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    1 MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDP 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRR-NFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  320 MLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  400 FISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  560 IGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  640 GVSGSGKSTLINDTLFPIAQRQLNGATIaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  720 ESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLR 879
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  880 DQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPML 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: 1912.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   1 MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:COG0178   3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:COG0178  83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDP 240
Cdd:COG0178 163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDEG 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 241 kaEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRR-NFYYFQ 319
Cdd:COG0178 243 --EELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPsSSYYFQ 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 320 MLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGkENIEFKYMNdRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:COG0178 321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSD-EKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 400 FISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLT 479
Cdd:COG0178 399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVID 559
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 560 IGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:COG0178 559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVEIPLGVLTCVT 637
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 640 GVSGSGKSTLINDTLFPIAQRQLNGATiAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:COG0178 638 GVSGSGKSTLVNDILYPALARKLNGAK-EKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTP 716
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 720 ESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:COG0178 717 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 796
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLR 879
Cdd:COG0178 797 FENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLV 876
                       890       900       910       920       930       940
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884 880 DQGNTIVVIEHNLDVIKTADWIVDLgpeggsgggEILVSGTPETVAECEASHTARFLKPML 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: 1723.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884     3 KIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    83 ISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEH 162
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   163 TKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDPK- 241
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEv 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   242 --AEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWD-RRNFYYF 318
Cdd:TIGR00630 241 aeSKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKkSTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   319 QMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELA 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   399 KFISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   479 TLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVI 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   559 DIGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANPeKVLKLTGARGNNLKDVTLTLPVGLFTCI 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNG-KFLTLKGARENNLKNITVSIPLGLFTCI 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   639 TGVSGSGKSTLINDTLFPIAQRQLNGATiAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGV 718
Cdd:TIGR00630 640 TGVSGSGKSTLINDTLYPALANRLNGAK-TVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   719 PESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEARE 798
Cdd:TIGR00630 719 PEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   799 FFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKL 878
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*..
gi 16131884   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 1.46e-155

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: 457.85  E-value: 1.46e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGATIAePAPYRDIQGLEHFDKVIDIDQSP 692
Cdd:cd03271   1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQ-PGNHDRIEGLEHIDKVIVIDQSP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 693 IGRTPRSNPATYTGVFTPVRELFagvpesrargytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpCDQCKGKRYN 772
Cdd:cd03271  80 IGRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYN 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 773 RETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQT 852
Cdd:cd03271 113 RETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKT 192
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884 853 LYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTP 921
Cdd:cd03271 193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
290-399 6.63e-48

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 165.72  E-value: 6.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   290 DPDRVIQNPELSLAGGAIRGWD-RRNFYYFQMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYmNDRGDTS 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGkKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYY-SRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 16131884   369 IRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
GguA NF040905
sugar ABC transporter ATP-binding protein;
807-901 2.76e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.03  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLqtLMDVGLTyirlgQSATTLSG----GEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQG 882
Cdd:NF040905 120 AREL--LAKVGLD-----ESPDTLVTdigvGKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKAQG 189
                         90       100
                 ....*....|....*....|
gi 16131884  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: 2026.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    1 MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDP 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  241 KAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRR-NFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  320 MLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  400 FISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  560 IGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  640 GVSGSGKSTLINDTLFPIAQRQLNGATIaEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  720 ESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLR 879
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  880 DQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPML 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: 1912.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   1 MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:COG0178   3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKG 160
Cdd:COG0178  83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDP 240
Cdd:COG0178 163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDEG 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 241 kaEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRR-NFYYFQ 319
Cdd:COG0178 243 --EELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPsSSYYFQ 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 320 MLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGkENIEFKYMNdRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:COG0178 321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSD-EKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 400 FISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLT 479
Cdd:COG0178 399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 480 LSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVID 559
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 560 IGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANpEKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:COG0178 559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVEIPLGVLTCVT 637
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 640 GVSGSGKSTLINDTLFPIAQRQLNGATiAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVP 719
Cdd:COG0178 638 GVSGSGKSTLVNDILYPALARKLNGAK-EKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTP 716
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 720 ESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREF 799
Cdd:COG0178 717 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 796
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 800 FDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLR 879
Cdd:COG0178 797 FENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLV 876
                       890       900       910       920       930       940
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884 880 DQGNTIVVIEHNLDVIKTADWIVDLgpeggsgggEILVSGTPETVAECEASHTARFLKPML 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: 1723.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884     3 KIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    83 ISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEH 162
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   163 TKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDPK- 241
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEv 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   242 --AEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWD-RRNFYYF 318
Cdd:TIGR00630 241 aeSKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKkSTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   319 QMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELA 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   399 KFISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   479 TLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVI 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   559 DIGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANPeKVLKLTGARGNNLKDVTLTLPVGLFTCI 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNG-KFLTLKGARENNLKNITVSIPLGLFTCI 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   639 TGVSGSGKSTLINDTLFPIAQRQLNGATiAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGV 718
Cdd:TIGR00630 640 TGVSGSGKSTLINDTLYPALANRLNGAK-TVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   719 PESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEARE 798
Cdd:TIGR00630 719 PEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   799 FFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKL 878
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*..
gi 16131884   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: 666.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884     1 MDKIEVR--GARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEG 78
Cdd:PRK00635    1 MPSLPVRlsGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    79 LSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKEr 158
Cdd:PRK00635   81 LSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAK- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   159 kgeHTKTLENLASQGYIRARIDGEVCD----LSDPpkleLQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVV 234
Cdd:PRK00635  160 ---DILAIRECLRQGFTKVRIDGEISPiykfLTSG----IPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   235 ADmddpKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNpELS-------LAGGAi 307
Cdd:PRK00635  233 HF----DNQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLIQQ-NLSieenccpFAGNC- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   308 rgwdrRNFYYFQMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDR-GDTSIRRHPFEGVLHNMERRYK 386
Cdd:PRK00635  307 -----STYLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVLPVRLFDGTlGKKTLTHKVWRGVLNEIGEKVR 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   387 ETESSAvrEELAKFISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKlagQRAKIAEKILKEIGDR 466
Cdd:PRK00635  382 YSNKPS--RYLPKGTSATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLP---SKSLSIEEVLQGLKSR 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEH 546
Cdd:PRK00635  457 LSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   547 DEDAIRAADHVIDIGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRvpANPEKVLKLTGARGNNLKDV 626
Cdd:PRK00635  537 DEQMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKR--TNSLGTLTLSKATKHNLKDL 614
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   627 TLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGatiaEPAPYRDIQGLEhFDKVIDIDQSPIGRTPRSNPATYTG 706
Cdd:PRK00635  615 TISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQ----GFCSNLSIQWGA-ISRLVHITRDLPGRSQRSIPLTYIK 689
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   707 VFTPVRELFAGVPESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPdiyVPCDQCKGKRYNRETLEIKYKGKTIH 786
Cdd:PRK00635  690 AFDDLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIA 766
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   787 EVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFA 866
Cdd:PRK00635  767 DILEMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTH 846
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884   867 DIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEaSHTARFLKPML 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 1.46e-155

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: 457.85  E-value: 1.46e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGATIAePAPYRDIQGLEHFDKVIDIDQSP 692
Cdd:cd03271   1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQ-PGNHDRIEGLEHIDKVIVIDQSP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 693 IGRTPRSNPATYTGVFTPVRELFagvpesrargytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpCDQCKGKRYN 772
Cdd:cd03271  80 IGRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYN 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 773 RETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQT 852
Cdd:cd03271 113 RETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKT 192
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884 853 LYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTP 921
Cdd:cd03271 193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-930 1.07e-103

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 355.29  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884     4 IEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQflSLMEK---PDVDHIEGLS 80
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQ--ALIKKtplPSVDKVTGLS 1018
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884    81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERkg 160
Cdd:PRK00635 1019 PVIAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPIPKEE-- 1096
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   161 EHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKhtiEVVVDRFKVRDDLTQRLAESFETALELSGgTAVVADMDDP 240
Cdd:PRK00635 1097 DLFIYLQEKLKEGFLKLYANEQFYDLDEPLPTSLENP---AIVIQHTKISEKNLSSLLSSLTLAFSLSS-SICLHIEYAG 1172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   241 KAEELLFSANFACPIcGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFD----PDRVIQNPELSLAGGAIRGWDRRNFY 316
Cdd:PRK00635 1173 TSLSLTYRLGWQDSS-GNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCSllphKEKIAHYTPLSLFTLFFPNQDPKPVY 1251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   317 yfQMLKSLadhyKFDVEAPWGSLSANVHKVVLYGS----GKENIEFKYMNdrgdtsirRHPFEGVLHNMerryketessa 392
Cdd:PRK00635 1252 --PLLKEL----GIPSIALFQELDTLSFESLCLGTqqhpGLNALLMEAML--------MESEEPLPPPL----------- 1306
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   393 vreelakfISNRPCASCEGTRLRREARHVYVENTPLPAI--SDMsighamEFFNNLKLAGQRAKiAEKILKEIGDRLKFL 470
Cdd:PRK00635 1307 --------ISKTPCNQCQGLGVYTYAHCVRIHNTSLSDIyqEDV------TFLKKFLLTIHDDE-EPSIIQDLLNRLTFI 1371
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   471 VNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDA 550
Cdd:PRK00635 1372 DKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSL 1451
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   551 IRAADHVIDIGPGAGVHGGEVVAEGPLeaimavpesltgqymsgkrKIEVPKKRVPANPEKVLKLT-GARGNNLKDVTLT 629
Cdd:PRK00635 1452 AEHADHLIHLGPGSGPQGGYLLSTSAL-------------------KQSQPDLHNTRSSEETPTLSvSLSIHTIQNLNVS 1512
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   630 LPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNgatiaepapyrdiQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFT 709
Cdd:PRK00635 1513 APLHSLVAISGVSGSGKTSLLLEGFYKQACALIE-------------KGPSVFSEIIFLDSHPQISSQRSDISTYFDIAP 1579
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   710 PVRELFAGVPESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVL 789
Cdd:PRK00635 1580 SLRNFYASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLL 1659
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   790 DMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQ 869
Cdd:PRK00635 1660 QTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKS 1739
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884   870 QLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEAS 930
Cdd:PRK00635 1740 ALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDS 1800
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-116 6.25e-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: 245.25  E-value: 6.25e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   4 IEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAI 83
Cdd:cd03270   1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131884  84 SIEQKSTSHNPRSTVGTITEIHDYLRLLFARVG 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 1.88e-69

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: 230.22  E-value: 1.88e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 463 IGDRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVI 542
Cdd:cd03270 114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131884 543 VVEHDEDAIRAADHVIDIGPGAGVHGGEVVAEG 575
Cdd:cd03270 194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
617-904 4.21e-50

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: 176.29  E-value: 4.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 617 GARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLngatIAEPAPYRDiQGLEHFDK-----------V 685
Cdd:cd03270   5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRY----VESLSAYAR-QFLGQMDKpdvdsieglspA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 686 IDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVPesrargytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpcdq 765
Cdd:cd03270  80 IAIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG---------------------------------------------- 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 766 ckgkrynretleikykgktihevldmtieeareffdavpaLARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELS 845
Cdd:cd03270 114 ----------------------------------------IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIG 153
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884 846 KRGTGqTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03270 154 SGLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
290-399 6.63e-48

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 165.72  E-value: 6.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   290 DPDRVIQNPELSLAGGAIRGWD-RRNFYYFQMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYmNDRGDTS 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGkKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYY-SRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 16131884   369 IRRHPFEGVLHNMERRYKETESSAVREELAK 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
130-238 1.08e-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: 164.96  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   130 QTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKV 209
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 16131884   210 RDDLTQRLAESFETALELSGGTAVVADMD 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 1.53e-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: 167.41  E-value: 1.53e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 406 CASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLklagqrAKIAEKilkeigdrLKFLVNVGLNYLTLSRSAE 485
Cdd:cd03271 103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENI------PKIARK--------LQTLCDVGLGYIKLGQPAT 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 486 TLSGGEAQRIRLASQIGAGLVG-VMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIGPGA 564
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
                       170
                ....*....|..
gi 16131884 565 GVHGGEVVAEGP 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 3.56e-46

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: 163.26  E-value: 3.56e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 465 DRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVV 544
Cdd:cd03238  66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                        90       100       110
                ....*....|....*....|....*....|.
gi 16131884 545 EHDEDAIRAADHVIDIGPGAGVHGGEVVAEG 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 2.04e-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: 170.96  E-value: 2.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   760 YVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREFFD-----------AVPALAR---KLQTLMDVGLTYIRLGQ 825
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNqltltpeekkiAEEVLKEireRLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   826 SATTLSGGEAQRVKLARELSKRGTGqTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLG 905
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         170       180       190
                  ....*....|....*....|....*....|.
gi 16131884   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 ...
613-919 4.54e-42

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: 151.71  E-value: 4.54e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGATiaePAPYRDiqglehfdKVIDIDQsp 692
Cdd:cd03238   1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFL---PKFSRN--------KLIFIDQ-- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 693 igrtprsnpatytgvftpvrelfagvpesrargytpgrfsfnvrggrceacqgdgvikvemhflpdiyvpcdqckgkryn 772
Cdd:cd03238     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 773 retleikykgktihevldmtieeareffdavpalarkLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGqT 852
Cdd:cd03238  68 -------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-T 109
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884 853 LYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSG 919
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
405-721 1.18e-35

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 147.28  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   405 PCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNlklagqRAKIAEKIlkeigdrlKFLVNVGLNYLTLSRSA 484
Cdd:PRK00635  742 PCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLD------EPSIHEKI--------HALCSLGLDYLPLGRPL 807
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   485 ETLSGGEAQRIRLASQIGAGLVG-VMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIGPG 563
Cdd:PRK00635  808 SSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPE 887
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   564 AGVHGGEVVAE-GPLEAI-MAVPESLTGQ-YMSGKRKIEVPKKRVPANP-EKVLKLTGARGNNLKDVTLTLPVGLFTCIT 639
Cdd:PRK00635  888 GGNLGGYLLAScSPEELIhLHTPTAKALRpYLSSPQELPYLPDPSPKPPvPADITIKNAYQHNLKHIDLSLPRNALTAVT 967
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   640 GVSGSGKSTLINDT-----------LFPIAQRQlngATIAE-PAPYRD-IQGLEhfdKVIDIDQSPIGRTPRSNPATYTG 706
Cdd:PRK00635  968 GPSASGKHSLVFDIlyaagniayaeLFPPYIRQ---ALIKKtPLPSVDkVTGLS---PVIAIEKTSASKNSNHSVASALE 1041
                         330
                  ....*....|....*..
gi 16131884   707 VFTPVRELFA--GVPES 721
Cdd:PRK00635 1042 ISNGLEKLFArlGHPYS 1058
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
461-902 5.18e-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: 97.67  E-value: 5.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 461 KEIGDR-LKFLVNVGLNYLtLSRSAETLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGL---HQRDNERLLGTLIhlRD 536
Cdd:COG1123 117 AEARARvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL-ALDPDLL-IADEPTTALdvtTQAEILDLLRELQ--RE 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 537 LGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPkkRVPANPEKVLKL 615
Cdd:COG1123 192 RGTTVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAA--PAAAAAEPLLEV 263
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 616 TG------ARGNN----LKDVTLTLPVGLFTCITGVSGSGKSTLindtlfpiaqrqlnGATIAepapyrdiqGLEHFDK- 684
Cdd:COG1123 264 RNlskrypVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTL--------------ARLLL---------GLLRPTSg 320
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 685 VIDIDQSPIGRTPRSNpatytgvftpVRELFAGV------PESrargytpgrfSFNVRggrceacqgdgvikvemhflpd 758
Cdd:COG1123 321 SILFDGKDLTKLSRRS----------LRELRRRVqmvfqdPYS----------SLNPR---------------------- 358
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 759 iyvpcdqckgkrynretleikykgKTIHEvldmTIEEAREFFDAVPA--LARKLQTLMD-VGLTYIRLGQSATTLSGGEA 835
Cdd:COG1123 359 ------------------------MTVGD----IIAEPLRLHGLLSRaeRRERVAELLErVGLPPDLADRYPHELSGGQR 410
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884 836 QRVKLARELSkrgTGQTLYILDEPTTGLhfaD--IQ-QLLDVLHKLRDQGN-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 8.09e-18

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: 81.99  E-value: 8.09e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884   4 IEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFL 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 8.15e-18

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: 84.20  E-value: 8.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   4 IEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAegqrryveslSAYARQFLSLMEKPDVDHIEGL---S 80
Cdd:cd03271   1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                        90       100       110
                ....*....|....*....|....*....|..
gi 16131884  81 PAISIEQKSTSHNPRSTVGTITEIHDYLRLLF 112
Cdd:cd03271  71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELF 102
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
830-904 6.70e-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: 6.70e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884 830 LSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTA-DWIVDL 904
Cdd:cd00267  81 LSGGQRQRVALARALLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
807-902 5.61e-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: 77.51  E-value: 5.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 807 ARKLQTLMDVGLtYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIV 886
Cdd:cd03225 113 ERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLA---MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTII 188
                        90
                ....*....|....*..
gi 16131884 887 VIEHNLDVIKT-ADWIV 902
Cdd:cd03225 189 IVTHDLDLLLElADRVI 205
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
623-902 6.32e-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: 77.57  E-value: 6.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqrqlngatiaepapyRDIQGLehfdkvididqspigrtprsNPA 702
Cdd:cd03235  15 LEDVSFEVKPGEFLAIVGPNGAGKSTLL-----------------------KAILGL--------------------LKP 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 703 TyTGVFTpvrelFAGVPESRAR---GYTPGRFSFNVrggrceacqgDGVIKVE----MHFLPDIyvpcdqCKGKRYNRET 775
Cdd:cd03235  52 T-SGSIR-----VFGKPLEKERkriGYVPQRRSIDR----------DFPISVRdvvlMGLYGHK------GLFRRLSKAD 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 776 LEIkykgktIHEVLDMtieeareffdavpalarklqtlmdVGLTYI---RLGQsattLSGGEAQRVKLARELSKRGTgqt 852
Cdd:cd03235 110 KAK------VDEALER------------------------VGLSELadrQIGE----LSGGQQQRVLLARALVQDPD--- 152
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 16131884 853 LYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
623-929 1.11e-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: 1.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqrqlngatiaepapyrdiqglehfdKVIdidqspigrtprsnpa 702
Cdd:COG1121  22 LEDVSLTIPPGEFVAIVGPNGAGKSTLL---------------------------------KAI---------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 703 tyTGVFTPVR---ELFaGVPESRAR---GYTPGRFSFN----------VRGGRceacqgdgviKVEMHFLpdiyvpcdqc 766
Cdd:COG1121  53 --LGLLPPTSgtvRLF-GKPPRRARrriGYVPQRAEVDwdfpitvrdvVLMGR----------YGRRGLF---------- 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 767 kgKRYNRETLEIkykgktIHEVLDMT-IEEareffdavpaLARKlqtlmdvgltyiRLGQsattLSGGEAQRVKLARELS 845
Cdd:COG1121 110 --RRPSRADREA------VDEALERVgLED----------LADR------------PIGE----LSGGQQQRVLLARALA 155
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 846 KRGtgqTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD-VIKTADWIVDLgpeggsgGGEILVSGTPETV 924
Cdd:COG1121 156 QDP---DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLL-------NRGLVAHGPPEEV 225

                ....*
gi 16131884 925 AECEA 929
Cdd:COG1121 226 LTPEN 230
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
623-904 3.04e-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: 79.80  E-value: 3.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdTL--FPIAQR---QLNG---ATIAEPAPYRDIqglehfdkvididqSPIG 694
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLN-LLlgFLPPYSgsiLINGvdlSDLDPASWRRQI--------------AWVP 417
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 695 RTPRsnpatytgvftpvreLFAG-VPEsrargytpgrfsfNVRGGRCEAcqgdgvikvemhflpdiyvpcdqckgkrynr 773
Cdd:COG4988 418 QNPY---------------LFAGtIRE-------------NLRLGRPDA------------------------------- 438
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 774 eTLEikykgkTIHEVLDMTieEAREFfdaVPALARKLQTlmdvgltyiRLGQSATTLSGGEAQRVKLARELSKRGtgqTL 853
Cdd:COG4988 439 -SDE------ELEAALEAA--GLDEF---VAALPDGLDT---------PLGEGGRGLSGGQAQRLALARALLRDA---PL 494
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131884 854 YILDEPTTGLhfaDI---QQLLDVLHKLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:COG4988 495 LLLDEPTAHL---DAeteAEILQALRRLA-KGRTVILITHRLALLAQADRILVL 544
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
487-562 3.10e-15

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: 74.32  E-value: 3.10e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 487 LSGGEAQRIRLASQIG--AGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIGP 562
Cdd:cd03227  78 LSGGEKELSALALILAlaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
816-904 2.65e-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: 71.62  E-value: 2.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 816 VGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQ-TLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDV 894
Cdd:cd03227  64 VAAVSAELIFTRLQLSGGEKELSALALILALASLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                        90
                ....*....|
gi 16131884 895 IKTADWIVDL 904
Cdd:cd03227 144 AELADKLIHI 153
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
404-594 7.01e-14

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 76.41  E-value: 7.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   404 RPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFnnlklagqrakiaeKILKEIGDRLKFLVNVGLNYLTLSRS 483
Cdd:PRK00635 1631 RPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETF--------------PFLKKIQKPLQALIDNGLGYLPLGQN 1696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   484 AETLSGGEAQRIRLASQIG-AGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIGP 562
Cdd:PRK00635 1697 LSSLSLSEKIAIKIAKFLYlPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGP 1776
                         170       180       190
                  ....*....|....*....|....*....|..
gi 16131884   563 GAGVHGGEVVAEGPLEAIMAVPESLTGQYMSG 594
Cdd:PRK00635 1777 GSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
445-587 8.88e-14

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 71.59  E-value: 8.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 445 NLKLAG-QRAKIAEKILKEigdrlkflvnVGLNYLtLSRSAETLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGL 519
Cdd:COG1122 103 NLGLPReEIRERVEEALEL----------VGLEHL-ADRPPHELSGGQKQRVAIAGVL------AMepevLVLDEPTAGL 165
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884 520 HQRDNERLLGTLIHLRDLGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGEVVAEGPLEAIMAVPESL 587
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREVFSDYELL 228
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
811-902 1.17e-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: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 811 QTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEH 890
Cdd:COG1122 117 EALELVGLEHLA-DRPPHELSGGQKQRVAIAGVLA---MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTH 192
                        90
                ....*....|...
gi 16131884 891 NLD-VIKTADWIV 902
Cdd:COG1122 193 DLDlVAELADRVI 205
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
790-902 3.30e-13

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 70.09  E-value: 3.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 790 DMTIEEAREFF------DAVPALARKLQTLMDVGLTyIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGL 863
Cdd:COG1131  87 DLTVRENLRFFarlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHD---PELLILDEPTSGL 162
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 16131884 864 hfaD---IQQLLDVLHKLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG1131 163 ---DpeaRRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVA 202
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
487-563 5.51e-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: 67.66  E-value: 5.51e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 487 LSGGEAQRIRLASQIgAGLVGVmYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHD-EDAIRAADHVIDIGPG 563
Cdd:cd00267  81 LSGGQRQRVALARAL-LLNPDL-LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
805-893 5.83e-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: 5.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKL----QTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELskrgTGQT-LYILDEPTTGLHFADIQQLLDVLHKL- 878
Cdd:cd03214  70 ELARKIayvpQALELLGLAHLA-DRPFNELSGGERQRVLLARAL----AQEPpILLLDEPTSHLDIAHQIELLELLRRLa 144
                        90
                ....*....|....*
gi 16131884 879 RDQGNTIVVIEHNLD 893
Cdd:cd03214 145 RERGKTVVMVLHDLN 159
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
830-902 1.04e-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: 67.07  E-value: 1.04e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD-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 1.73e-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: 68.23  E-value: 1.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 799 FFDAVPALARKLQTLMD-VGLTYiRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHK 877
Cdd:cd03219 113 ARREEREARERAEELLErVGLAD-LADRPAGELSYGQQRRLEIARALA---TDPKLLLLDEPAAGLNPEETEELAELIRE 188
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16131884 878 LRDQGNTIVVIEHNLDVI-KTADWIVDLgpeggsGGGEILVSGTPETVA 925
Cdd:cd03219 189 LRERGITVLLVEHDMDVVmSLADRVTVL------DQGRVIAEGTPDEVR 231
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
457-558 1.90e-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: 67.49  E-value: 1.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 457 EKILKEIGDRLKFlvnVGLNYLtLSRSAETLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLHQRDNERLLGTLI 532
Cdd:cd03225 109 EEIEERVEEALEL---VGLEGL-RDRSPFTLSGGQKQRVAIAGVL------AMdpdiLLLDEPTAGLDPAGRRELLELLK 178
                        90       100
                ....*....|....*....|....*..
gi 16131884 533 HLRDLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:cd03225 179 KLKAEGKTIIIVTHDlDLLLELADRVI 205
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
615-924 1.91e-12

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: 68.15  E-value: 1.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 615 LTGARGNN--LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqRQLNGatIAEPApyrdiQGlehfdkVIDIDQSP 692
Cdd:COG1120   7 LSVGYGGRpvLDDVSLSLPPGEVTALLGPNGSGKSTLL---------RALAG--LLKPS-----SG------EVLLDGRD 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 693 IGRTPRsnpatytgvftpvRELfagvpeSRARGY----TPGRFSFNVRggrcEAcqgdgvikVEM----Hflpdiyvpcd 764
Cdd:COG1120  65 LASLSR-------------REL------ARRIAYvpqePPAPFGLTVR----EL--------VALgrypH---------- 103
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 765 QCKGKRYNRETLEIkykgktIHEVLDMTieeareffdavpalarklqtlmdvGLTYIRlGQSATTLSGGEAQRVKLAREL 844
Cdd:COG1120 104 LGLFGRPSAEDREA------VEEALERT------------------------GLEHLA-DRPVDELSGGERQRVLIARAL 152
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 845 skrgTGQT-LYILDEPTTGLhfaDI---QQLLDVLHKL-RDQGNTIVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVS 918
Cdd:COG1120 153 ----AQEPpLLLLDEPTSHL---DLahqLEVLELLRRLaRERGRTVVMVLHDLNlAARYADRLVLL------KDGRIVAQ 219

                ....*.
gi 16131884 919 GTPETV 924
Cdd:COG1120 220 GPPEEV 225
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
400-563 6.20e-12

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 65.99  E-value: 6.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 400 FISNRPCASCEGTRLRREARHVYVEntplPAISDMSIGHAMEF---FNNLKLAGQRAKiaekilkeigdrlKFLVNVGLN 476
Cdd:COG4619  58 YLDGKPLSAMPPPEWRRQVAYVPQE----PALWGGTVRDNLPFpfqLRERKFDRERAL-------------ELLERLGLP 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 477 YLTLSRSAETLSGGEAQRIRLAS------QIgaglvgvmYVLDEPSIGLHQrDNERLLGTLIH--LRDLGNTVIVVEHDE 548
Cdd:COG4619 121 PDILDKPVERLSGGERQRLALIRalllqpDV--------LLLDEPTSALDP-ENTRRVEELLReyLAEEGRAVLWVSHDP 191
                       170
                ....*....|....*.
gi 16131884 549 DAI-RAADHVIDIGPG 563
Cdd:COG4619 192 EQIeRVADRVLTLEAG 207
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
822-893 2.33e-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: 2.33e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD 893
Cdd:cd03224 125 RRKQLAGTLSGGEQQMLAIARALMSR---PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNAR 193
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
452-895 4.15e-11

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 66.59  E-value: 4.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 452 RAKIAEKIlKEIGDRLKFLVNvglnyltLSRSAETLSGGEAQR---IRLASQiGAGLVgvmyVLDEPSIGLHQRDNERLL 528
Cdd:COG3845 115 RKAARARI-RELSERYGLDVD-------PDAKVEDLSVGEQQRveiLKALYR-GARIL----ILDEPTAVLTPQEADELF 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 529 GTLIHLRDLGNTVIVVEH--DEdAIRAADHVIdigpgagV-HGGEVVAEGPLEAimAVPESLTgQYMSGkRKIEVPKKRV 605
Cdd:COG3845 182 EILRRLAAEGKSIIFITHklRE-VMAIADRVT-------VlRRGKVVGTVDTAE--TSEEELA-ELMVG-REVLLRVEKA 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 606 PANP-EKVLKL-----TGARGNN-LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqrqlngATIAepapyrdiqG 678
Cdd:COG3845 250 PAEPgEVVLEVenlsvRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELA--------------EALA---------G 306
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 679 LEHFDK-VIDIDQSPIGR-TPRSnpatytgvftpVREL-FAGVPESRargytpgrfsfnvrggrceacQGDGVikvemhf 755
Cdd:COG3845 307 LRPPASgSIRLDGEDITGlSPRE-----------RRRLgVAYIPEDR---------------------LGRGL------- 347
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 756 lpdiyvpcdqckgkrynretleikykgktiheVLDMTIEE------------AREFF---DAVPALARKLQTLMDVglty 820
Cdd:COG3845 348 --------------------------------VPDMSVAEnlilgryrrppfSRGGFldrKAIRAFAEELIEEFDV---- 391
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 821 iR---LGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:COG3845 392 -RtpgPDTPARSLSGGNQQKVILARELSRDP---KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEI 465
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
830-904 4.16e-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: 62.40  E-value: 4.16e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDI---QQLLDVLHKLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03228  97 LSGGQRQRIAIARALLRDP---PILILDEATSAL---DPeteALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVL 167
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
801-892 5.74e-11

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 63.71  E-value: 5.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 801 DAVPALARKLQtLMDvgltyiRLGQSATTLSGGEAQRVKLAREL-----SKRGTGQtLYILDEPTTGLhfaDIQQ---LL 872
Cdd:COG4138 105 QLLAQLAEALG-LED------KLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEGQ-LLLLDEPMNSL---DVAQqaaLD 173
                        90       100
                ....*....|....*....|
gi 16131884 873 DVLHKLRDQGNTIVVIEHNL 892
Cdd:COG4138 174 RLLRELCQQGITVVMSSHDL 193
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
623-896 6.53e-11

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 62.91  E-value: 6.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTL---INDtLFPIA--QRQLNGATIAE-PAP-YRDiqglehfdKVIDIDQSPIgr 695
Cdd:COG4619  16 LSPVSLTLEAGECVAITGPSGSGKSTLlraLAD-LDPPTsgEIYLDGKPLSAmPPPeWRR--------QVAYVPQEPA-- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 696 tprsnpatytgvftpvreLFAGvpesrargytpgrfsfNVRggrceacqgdgvikvemHFLPDIYvpcdQCKGKRYNRET 775
Cdd:COG4619  85 ------------------LWGG----------------TVR-----------------DNLPFPF----QLRERKFDRER 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 776 LEikykgktihevldmtieeareffdavPALARklqtlmdVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYI 855
Cdd:COG4619 110 AL--------------------------ELLER-------LGLPPDILDKPVERLSGGERQRLALIRALL---LQPDVLL 153
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 16131884 856 LDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIK 896
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGrAVLWVSHDPEQIE 195
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
791-896 7.77e-11

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: 62.91  E-value: 7.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 791 MTIEEA-----REFFDAVPALARK---LQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG 862
Cdd:cd03257  99 MTIGEQiaeplRIHGKLSKKEARKeavLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA---LNPKLLIADEPTSA 175
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131884 863 LHfADIQ-QLLDVLHKLRDQ-GNTIVVIEHNLDVIK 896
Cdd:cd03257 176 LD-VSVQaQILDLLKKLQEElGLTLLFITHDLGVVA 210
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
830-902 8.87e-11

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: 61.64  E-value: 8.87e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaDI---QQLLDVLHKLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:cd03230  96 LSGGMKQRLALAQALLHD---PELLILDEPTSGL---DPesrREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
592-904 1.62e-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: 64.62  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   592 MSGKRKIEVPKKRVPANPEKVLKLTGA------RGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTL-FPIAQR---Q 661
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPASSLEFSGVsvaypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLgFVDPTEgsiA 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   662 LNGATIAE--PAPYRDiqglehfdKVIDIDQSPigrtprsnpatytgvftpvrelfagvpesrarGYTPGRFSFNVRGGR 739
Cdd:TIGR02857 381 VNGVPLADadADSWRD--------QIAWVPQHP--------------------------------FLFAGTIAENIRLAR 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   740 CEAcqgdgvikvemhflpdiyvpcdqckgkrynretleikyKGKTIHEVLdmtieEAREFFDAVPALARKLQTlmdvglt 819
Cdd:TIGR02857 421 PDA--------------------------------------SDAEIREAL-----ERAGLDEFVAALPQGLDT------- 450
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   820 yiRLGQSATTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHKLRdQGNTIVVIEHNLDVIKTAD 899
Cdd:TIGR02857 451 --PIGEGGAGLSGGQAQRLALARAFLR---DAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALAD 524

                  ....*
gi 16131884   900 WIVDL 904
Cdd:TIGR02857 525 RIVVL 529
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
805-904 1.77e-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: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGN 883
Cdd:COG1136 123 ERAREL--LERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNRP---KLILADEPTGNLDSKTGEEVLELLRELnRELGT 196
                        90       100
                ....*....|....*....|.
gi 16131884 884 TIVVIEHNLDVIKTADWIVDL 904
Cdd:COG1136 197 TIVMVTHDPELAARADRVIRL 217
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
830-904 2.14e-10

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 60.31  E-value: 2.14e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03246  97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
824-892 2.82e-10

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 62.06  E-value: 2.82e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884 824 GQSATTLSGGEAQRVKLAREL-----SKRGTGQTLyILDEPTTGLhfaDI---QQLLDVLHKLRDQGNTIVVIEHNL 892
Cdd:COG4559 128 GRSYQTLSGGEQQRVQLARVLaqlwePVDGGPRWL-FLDEPTSAL---DLahqHAVLRLARQLARRGGGVVAVLHDL 200
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
793-902 3.20e-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: 63.77  E-value: 3.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 793 IEEAREFFDAVPALARK--LQTLMDVGLTyIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQ 870
Cdd:COG1123 105 IAEALENLGLSRAEARArvLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDPD---LLIADEPTTALDVTTQAE 180
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131884 871 LLDVLHKL-RDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG1123 181 ILDLLRELqRERGTTVLLITHDLGVVaEIADRVV 214
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
473-575 4.37e-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: 59.76  E-value: 4.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 473 VGLNYLtLSRSAETLSGGEAQRIRLAsqigAGLVGV--MYVLDEPSIGL---HQRdneRLLGTLIHL-RDLGNTVIVVEH 546
Cdd:cd03214  85 LGLAHL-ADRPFNELSGGERQRVLLA----RALAQEppILLLDEPTSHLdiaHQI---ELLELLRRLaRERGKTVVMVLH 156
                        90       100       110
                ....*....|....*....|....*....|
gi 16131884 547 DED-AIRAADHVIDIgpgagvHGGEVVAEG 575
Cdd:cd03214 157 DLNlAARYADRVILL------KDGRIVAQG 180
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
482-585 4.67e-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: 60.91  E-value: 4.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 482 RSAETLSGGEAQRIrlasQIGAGLVG--VMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVI 558
Cdd:cd03219 139 RPAGELSYGQQRRL----EIARALATdpKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVT 214
                        90       100
                ....*....|....*....|....*...
gi 16131884 559 digpgagV-HGGEVVAEGPLEAIMAVPE 585
Cdd:cd03219 215 -------VlDQGRVIAEGTPDEVRNNPR 235
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
822-904 5.18e-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: 63.25  E-value: 5.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLrDQGNTIVVIEHNLDVIKTADWI 901
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRD---APILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRI 539

                ...
gi 16131884 902 VDL 904
Cdd:COG4987 540 LVL 542
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
623-902 6.65e-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: 60.64  E-value: 6.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqrqlngaTIAepapyrdiqGLEHFDK-VIDIDqspiGRTPRSNP 701
Cdd:COG4555  17 LKDVSFTAKDGEITGLLGPNGAGKTTLLR--------------MLA---------GLLKPDSgSILID----GEDVRKEP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 702 ATYtgvftpVRELfagvpesrarGYTPGRFSFnvrggrceacqgdgvikvemhflpdiyvpcdqckgkrYNRETLE--IK 779
Cdd:COG4555  70 REA------RRQI----------GVLPDERGL-------------------------------------YDRLTVRenIR 96
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 780 YKGkTIHevlDMTIEEAREFFDAvpaLARKLQtLMDVgltyirLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEP 859
Cdd:COG4555  97 YFA-ELY---GLFDEELKKRIEE---LIELLG-LEEF------LDRRVGELSTGMKKKVALARALVHD---PKVLLLDEP 159
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 16131884 860 TTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVV 203
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
829-904 7.32e-10

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: 59.58  E-value: 7.32e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 829 TLSGGEAQRVKLARE-LSKRgtgqTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI-KTADWIVDL 904
Cdd:cd03226 126 SLSGGQKQRLAIAAAlLSGK----DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLL 199
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
805-904 7.93e-10

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: 59.81  E-value: 7.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGN 883
Cdd:cd03255 117 RRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIARALANDP---KIILADEPTGNLDSETGKEVMELLRELnKEAGT 192
                        90       100
                ....*....|....*....|.
gi 16131884 884 TIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03255 193 TIVVVTHDPELAEYADRIIEL 213
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
791-893 1.21e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 60.49  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  791 MTIEEAREffdavpaLARKLQTLmdVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK13651 136 VSKEEAKK-------RAAKYIEL--VGLDESYLQRSPFELSGGQKRRVALAGILAME---PDFLVFDEPTAGLDPQGVKE 203
                         90       100
                 ....*....|....*....|...
gi 16131884  871 LLDVLHKLRDQGNTIVVIEHNLD 893
Cdd:PRK13651 204 ILEIFDNLNKQGKTIILVTHDLD 226
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
623-904 2.08e-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: 61.39  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqrqLngatiaepapyrdIQGLEHFDK-VIDIDQSPIGRTPRSNP 701
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLK----------L-------------LLGLYEPTSgRILIDGIDLRQIDPASL 547
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 702 ATYTGVFTPVRELFAG-VPEsrargytpgrfsfNVRGGRceacqgdgvikvemhflPDIyvpcdqckgkrynreTLEiky 780
Cdd:COG2274 548 RRQIGVVLQDVFLFSGtIRE-------------NITLGD-----------------PDA---------------TDE--- 579
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 781 kgkTIHEVLDMTieEAREFfdaVPALARKLQTLmdvgltyirLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPT 860
Cdd:COG2274 580 ---EIIEAARLA--GLHDF---IEALPMGYDTV---------VGEGGSNLSGGQRQRLAIARALLRN---PRILILDEAT 639
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 16131884 861 TGLHFADIQQLLDVLHKLRdQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:COG2274 640 SALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVL 682
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
473-589 2.59e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 59.26  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  473 VGLNYLTLSRSAETLSGGEAQRIRLAsqigaglvGV------MYVLDEPSIGLHQRDNERLLGTLIHL-RDLGNTVIVVE 545
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRVAIA--------GVlamepeVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVT 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16131884  546 HD-EDAIRAADHVIDIgpgagvHGGEVVAEGPLEAIMAVPESLTG 589
Cdd:PRK13634 204 HSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEA 242
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
784-892 3.14e-09

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 58.63  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  784 TIHEVLDMTIEEAREFFDAVPALARklQTLMDVGLTYIRlGQSATTLSGGEAQRVKLAR---ELSKRGTGQTLYILDEPT 860
Cdd:PRK13548  92 TVEEVVAMGRAPHGLSRAEDDALVA--AALAQVDLAHLA-GRDYPQLSGGEQQRVQLARvlaQLWEPDGPPRWLLLDEPT 168
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16131884  861 TGLhfaDIQQLLDVLHKLRD----QGNTIVVIEHNL 892
Cdd:PRK13548 169 SAL---DLAHQHHVLRLARQlaheRGLAVIVVLHDL 201
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
770-899 3.29e-09

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 58.35  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  770 RYNRETLEIKYKGKTIHEvlDMTIEEARE---FFDAVPALARKLQTLMDV-GLTYIRLGQSATTLSGGEAQRVKLARELS 845
Cdd:PRK11614  76 KIMREAVAIVPEGRRVFS--RMTVEENLAmggFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16131884  846 KRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD-VIKTAD 899
Cdd:PRK11614 154 SQ---PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLAD 205
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
801-892 3.41e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 58.41  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  801 DAVPALARKLQtLMDvgltyiRLGQSATTLSGGEAQRVKLA-------RELSKRGtgqTLYILDEPTTGLhfaDIQQ--L 871
Cdd:PRK03695 105 SALNEVAEALG-LDD------KLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAG---QLLLLDEPMNSL---DVAQqaA 171
                         90       100
                 ....*....|....*....|..
gi 16131884  872 LD-VLHKLRDQGNTIVVIEHNL 892
Cdd:PRK03695 172 LDrLLSELCQQGIAVVMSSHDL 193
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
480-582 3.78e-09

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: 57.83  E-value: 3.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 480 LSRSAETLSGGEAQriRLAsqIGAGLVG--VMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDED-AIRAADH 556
Cdd:cd03224 126 RKQLAGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARfALEIADR 201
                        90       100
                ....*....|....*....|....*...
gi 16131884 557 --VIDigpgagvhGGEVVAEGPLEAIMA 582
Cdd:cd03224 202 ayVLE--------RGRVVLEGTAAELLA 221
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
830-902 3.83e-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: 57.06  E-value: 3.83e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884 830 LSGGEAQRVKLARELskrGTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:cd03215 105 LSGGNQQKVVLARWL---ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGLCDRIL 175
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
826-904 4.09e-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: 57.83  E-value: 4.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 826 SATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKT-ADWIVDL 904
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDV 225
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
487-582 4.12e-09

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: 60.16  E-value: 4.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 487 LSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLHQRDNERLLGTLIHLRDlGNTVIVVEHDEDAIRAADHVIDi 560
Cdd:COG4988 474 LSGGQAQRLALArallrdAPL--------LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILV- 543
                        90       100
                ....*....|....*....|..
gi 16131884 561 gpgagVHGGEVVAEGPLEAIMA 582
Cdd:COG4988 544 -----LDDGRIVEQGTHEELLA 560
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
805-902 4.28e-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: 4.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLQTLMD-VGLTyIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGN 883
Cdd:COG1129 116 AMRRRARELLArLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDAR---VLILDEPTASLTEREVERLFRIIRRLKAQGV 191
                        90       100
                ....*....|....*....|
gi 16131884 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 9.37e-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: 55.66  E-value: 9.37e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQ-GNTIVVIEHNLDVIKT-ADWIV 902
Cdd:cd03229 101 LSGGQQQRVALARALAMD---PDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVV 172
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
813-895 9.85e-09

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 57.12  E-value: 9.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 813 LMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaD--IQ-QLLDVLHKLRDQ-GNTIVVI 888
Cdd:COG1124 122 LEQVGLPPSFLDRYPHQLSGGQRQRVAIARALI---LEPELLLLDEPTSAL---DvsVQaEILNLLKDLREErGLTYLFV 195

                ....*..
gi 16131884 889 EHNLDVI 895
Cdd:COG1124 196 SHDLAVV 202
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
780-904 1.12e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.05  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  780 YKGKTIhEVLDMTIEeaREFFDAVpalARKLqtlmdvGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEP 859
Cdd:PRK13409 176 FKGKVR-ELLKKVDE--RGKLDEV---VERL------GLENI-LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEP 239
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 16131884  860 TTGLhfaDIQQLLDVLHKLRD--QGNTIVVIEHNLDVIktaDWIVDL 904
Cdd:PRK13409 240 TSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVL---DYLADN 280
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
486-558 1.18e-08

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 56.39  E-value: 1.18e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884 486 TLSGGEAQRIRLAsQIgagLVG--VMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:cd03235 132 ELSGGQQQRVLLA-RA---LVQdpDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVL 203
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
782-902 1.65e-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: 57.37  E-value: 1.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 782 GKTIHEVL----DMTIEEAREffdavpalaRKLQTLMDVGLTY--IRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYI 855
Cdd:COG0444 106 GDQIAEPLrihgGLSKAEARE---------RAIELLERVGLPDpeRRLDRYPHELSGGMRQRVMIARALA---LEPKLLI 173
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 16131884 856 LDEPTTGLHfADIQ-QLLDVLHKLRDQ-GNTIVVIEHNLDVIK-TADWIV 902
Cdd:COG0444 174 ADEPTTALD-VTIQaQILNLLKDLQRElGLAILFITHDLGVVAeIADRVA 222
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
822-902 2.02e-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: 56.01  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaD------IQQLLDVLHKlrdqGNTIVVIEHNLDVI 895
Cdd:cd03249 132 LVGERGSQLSGGQKQRIAIARALLRN---PKILLLDEATSAL---DaeseklVQEALDRAMK----GRTTIVIAHRLSTI 201

                ....*..
gi 16131884 896 KTADWIV 902
Cdd:cd03249 202 RNADLIA 208
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
787-893 2.24e-08

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.13  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  787 EVLDMTIEEAREffdavpalaRKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFA 866
Cdd:PRK10619 119 QVLGLSKQEARE---------RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME---PEVLLFDEPTSALDPE 186
                         90       100
                 ....*....|....*....|....*..
gi 16131884  867 DIQQLLDVLHKLRDQGNTIVVIEHNLD 893
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMG 213
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
822-901 2.64e-08

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: 57.45  E-value: 2.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARelskrgtgqTLY------ILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLAR---------ALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL 530

                ....*.
gi 16131884 896 KTADWI 901
Cdd:COG4618 531 AAVDKL 536
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
487-597 2.88e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 57.81  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  487 LSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIgpgagv 566
Cdd:PRK10535 145 LSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI------ 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 16131884  567 HGGEVVAEGPLE---AIMAVPESLT------GQYMSGKRK 597
Cdd:PRK10535 217 RDGEIVRNPPAQekvNVAGGTEPVVntasgwRQFVSGFRE 256
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
806-896 4.09e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 56.86  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  806 LARKLQTLMDVgltYIRLGQsattLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTI 885
Cdd:PRK13549 127 LLAQLKLDINP---ATPVGN----LGLGQQQLVEIAKALNKQAR---LLILDEPTASLTESETAVLLDIIRDLKAHGIAC 196
                         90
                 ....*....|.
gi 16131884  886 VVIEHNLDVIK 896
Cdd:PRK13549 197 IYISHKLNEVK 207
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
830-890 4.41e-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: 54.09  E-value: 4.41e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEH 890
Cdd:cd03213 112 LSGGERKRVSIALELVSN---PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
445-566 4.96e-08

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: 54.19  E-value: 4.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 445 NLKLAGQRAKIAEKILKEIGdrlkflvnvgLNYLTLsRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLhQRDN 524
Cdd:cd03226  96 GLKELDAGNEQAETVLKDLD----------LYALKE-RHPLSLSGGQKQRLAIAAALLSG--KDLLIFDEPTSGL-DYKN 161
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16131884 525 ERLLGTLI-HLRDLGNTVIVVEHDED-AIRAADHVIDIGPGAGV 566
Cdd:cd03226 162 MERVGELIrELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
790-892 5.36e-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: 5.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   790 DMTIEEAREFFDAVpALARKLQTLMDvGLTyIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQ 869
Cdd:TIGR02868 435 DATDEELWAALERV-GLADWLRALPD-GLD-TVLGEGGARLSGGERQRLALARALL---ADAPILLLDEPTEHLDAETAD 508
                          90       100
                  ....*....|....*....|...
gi 16131884   870 QLLDVLHKLrDQGNTIVVIEHNL 892
Cdd:TIGR02868 509 ELLEDLLAA-LSGRTVVLITHHL 530
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
806-904 5.56e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 56.66  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  806 LARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTI 885
Cdd:PRK10535 122 LLRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALM---NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTV 197
                         90
                 ....*....|....*....
gi 16131884  886 VVIEHNLDVIKTADWIVDL 904
Cdd:PRK10535 198 IIVTHDPQVAAQAERVIEI 216
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
467-570 5.90e-08

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 54.33  E-value: 5.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGLHQrDNERLLGTLIH--LRDLGNTVIVV 544
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALDE-SNKHNVNEIIHryVREQNIAVLWV 194
                         90       100
                 ....*....|....*....|....*.
gi 16131884  545 EHDEDAIRAADHVIDIGPgagvHGGE 570
Cdd:PRK10247 195 THDKDEINHADKVITLQP----HAGE 216
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
805-932 7.15e-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: 7.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLQTLMD-VGLTyIRLGQSATTLSGGEAQRVKLARELSkRGTgQTLyILDEPTTGLHFADIQQLLDVLHKLRDQGN 883
Cdd:COG3845 117 AARARIRELSErYGLD-VDPDAKVEDLSVGEQQRVEILKALY-RGA-RIL-ILDEPTAVLTPQEADELFEILRRLAAEGK 192
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 16131884 884 TIVVIEHNLDVIKT-ADWIVdlgpeggsgggeILVSGtpETVAECEASHT 932
Cdd:COG3845 193 SIIFITHKLREVMAiADRVT------------VLRRG--KVVGTVDTAET 228
cbiO PRK13645
energy-coupling factor transporter ATPase;
457-602 7.44e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 55.01  E-value: 7.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  457 EKILKEIGDRLKfLVNVGLNYLtlSRSAETLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLIHL-R 535
Cdd:PRK13645 124 QEAYKKVPELLK-LVQLPEDYV--KRSPFELSGGQKRRVALAGIIA--MDGNTLVLDEPTGGLDPKGEEDFINLFERLnK 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884  536 DLGNTVIVVEHDEDAI-RAADHVIDIgpgagvHGGEVVAEGPLEAIMAVPESLTgqymsgKRKIEVPK 602
Cdd:PRK13645 199 EYKKRIIMVTHNMDQVlRIADEVIVM------HEGKVISIGSPFEIFSNQELLT------KIEIDPPK 254
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
473-581 7.53e-08

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 54.79  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  473 VGLNYLTlSRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGL---HQRDNERLLGTLIHLRDLgnTVIVVEHDED 549
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQD--SRCLLLDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDIN 209
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16131884  550 -AIRAADHVIdigpgaGVHGGEVVAEGPLEAIM 581
Cdd:PRK10575 210 mAARYCDYLV------ALRGGEMIAQGTPAELM 236
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
482-581 8.05e-08

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 54.63  E-value: 8.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  482 RSAETLSGGEAQRIRLASQIGAGLVGVMyvLDEPSIGL---HQRDnerLLGTLIHLRDLGNTVIVVEHD-EDAIRAADHV 557
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlNQASRYCDHL 208
                         90       100
                 ....*....|....*....|....
gi 16131884  558 IDIgpgagvHGGEVVAEGPLEAIM 581
Cdd:PRK11231 209 VVL------ANGHVMAQGTPEEVM 226
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
511-888 8.45e-08

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 55.79  E-value: 8.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 511 VLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVI---DigpgagvhgGEVVAEGPLEAImaVPES 586
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTvlrD---------GRLVGTGPVAEL--TEDE 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 587 LTgQYMSGKRKIEVPKKRVPANPEKVLKLTG-ARGNNLKDVTLTLP----VGlftcITGVSGSGKSTLINdTLFpiaqrq 661
Cdd:COG1129 232 LV-RLMVGRELEDLFPKRAAAPGEVVLEVEGlSVGGVVRDVSFSVRageiLG----IAGLVGAGRTELAR-ALF------ 299
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 662 lngatiaepapyrdiqGLEHFDK-VIDIDQSPI-GRTPRSnpAtytgvftpVRELFAGVPESRargytpgrfsfnvrggr 739
Cdd:COG1129 300 ----------------GADPADSgEIRLDGKPVrIRSPRD--A--------IRAGIAYVPEDR----------------- 336
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 740 ceacQGDGVikvemhflpdiyvpcdqckgkrynretleikykgktiheVLDMTIEE------------------AREFfd 801
Cdd:COG1129 337 ----KGEGL---------------------------------------VLDLSIREnitlasldrlsrgglldrRRER-- 371
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 802 avpALARKLQTLMDvgltyIR---LGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaDI---QQLLDVL 875
Cdd:COG1129 372 ---ALAEEYIKRLR-----IKtpsPEQPVGNLSGGNQQKVVLAKWLA---TDPKVLILDEPTRGI---DVgakAEIYRLI 437
                       410
                ....*....|...
gi 16131884 876 HKLRDQGNTIVVI 888
Cdd:COG1129 438 RELAAEGKAVIVI 450
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
805-895 9.34e-08

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 54.32  E-value: 9.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLqtLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGN- 883
Cdd:COG1119 121 ERAREL--LELLGLAHLA-DRPFGTLSQGEQRRVLIARALVKDPE---LLILDEPTAGLDLGARELLLALLDKLAAEGAp 194
                        90
                ....*....|..
gi 16131884 884 TIVVIEHNLDVI 895
Cdd:COG1119 195 TLVLVTHHVEEI 206
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
790-890 1.01e-07

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: 53.25  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 790 DMTIEEAREF---FDAVPALARKLQTLMD-VGLTYiRLGQSATTLSGGEAQRVKLAR-ELSKRgtgqTLYILDEPTTGLH 864
Cdd:COG4133  89 ELTVRENLRFwaaLYGLRADREAIDEALEaVGLAG-LADLPVRQLSAGQKRRVALARlLLSPA----PLWLLDEPFTALD 163
                        90       100
                ....*....|....*....|....*.
gi 16131884 865 FADIQQLLDVLHKLRDQGNTIVVIEH 890
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTTH 189
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
830-896 1.09e-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: 53.74  E-value: 1.09e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQ-GNTIVVIEHNLDVIK 896
Cdd:cd03258 141 LSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVK 205
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
787-896 1.18e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 53.52  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 787 EVLDMTIEEAREffdAVPALarklqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFA 866
Cdd:COG2884 105 RVTGKSRKEIRR---RVREV------LDLVGLSD-KAKALPHELSGGEQQRVAIARALVNR---PELLLADEPTGNLDPE 171
                        90       100       110
                ....*....|....*....|....*....|
gi 16131884 867 DIQQLLDVLHKLRDQGNTIVVIEHNLDVIK 896
Cdd:COG2884 172 TSWEIMELLEEINRRGTTVLIATHDLELVD 201
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
791-890 1.56e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 53.56  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  791 MTIEEAREffdavpaLARKLqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK09493 108 ASKEEAEK-------QAREL--LAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVK---PKLMLFDEPTSALDPELRHE 174
                         90       100
                 ....*....|....*....|
gi 16131884  871 LLDVLHKLRDQGNTIVVIEH 890
Cdd:PRK09493 175 VLKVMQDLAEEGMTMVIVTH 194
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
486-582 1.66e-07

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 55.14  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 486 TLSGGEAQRIRLASqigAglvgvMY------VLDEPSIGLhqrDNE---RLLGTLIHLRDLGNTVIVVEHDEDAIRAADH 556
Cdd:COG4618 467 RLSGGQRQRIGLAR---A-----LYgdprlvVLDEPNSNL---DDEgeaALAAAIRALKARGATVVVITHRPSLLAAVDK 535
                        90       100
                ....*....|....*....|....*.
gi 16131884 557 VIDIgpgagvHGGEVVAEGPLEAIMA 582
Cdd:COG4618 536 LLVL------RDGRVQAFGPRDEVLA 555
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
782-861 1.81e-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: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   782 GKTIHEVLDMTIEEAREFFDAVPALARKLQTLMD-VGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPT 860
Cdd:pfam00005  73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGlGDLADRPVGERPGTLSGGQRQRVAIARALLTK---PKLLLLDEPT 149

                  .
gi 16131884   861 T 861
Cdd:pfam00005 150 A 150
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
440-586 1.82e-07

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 53.11  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 440 MEFFNNL-----KLAGQRAKIAEKIlKEIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIRLASqigaGLV--GVMYVL 512
Cdd:cd03299  86 MTVYKNIayglkKRKVDKKEIERKV-LEIAEML------GIDHL-LNRKPETLSGGEQQRVAIAR----ALVvnPKILLL 153
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884 513 DEPSIGLHQRDNERLLGTLIHLRD-LGNTVIVVEHD-EDAIRAADHVidigpgAGVHGGEVVAEGPLEAIMAVPES 586
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKeFGVTVLHVTHDfEEAWALADKV------AIMLNGKLIQVGKPEEVFKKPKN 223
cbiO PRK13644
energy-coupling factor transporter ATPase;
777-924 2.09e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 53.45  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  777 EIKYKGKTIHEVLDMTIEEAreffdAVPALarKLQTLMDVGLTYIRLGQ----SATTLSGGEAQRVKLARELSKRgtgQT 852
Cdd:PRK13644  87 ETQFVGRTVEEDLAFGPENL-----CLPPI--EIRKRVDRALAEIGLEKyrhrSPKTLSGGQGQCVALAGILTME---PE 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884  853 LYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM------DRGKIVLEGEPENV 222
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
805-902 2.50e-07

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 52.45  E-value: 2.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARklqtlmdVGLTYI--RL-GQsattLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RD 880
Cdd:COG3840 113 ALER-------VGLAGLldRLpGQ----LSGGQRQRVALARCLVRK---RPILLLDEPFSALDPALRQEMLDLVDELcRE 178
                        90       100
                ....*....|....*....|...
gi 16131884 881 QGNTIVVIEHNL-DVIKTADWIV 902
Cdd:COG3840 179 RGLTVLMVTHDPeDAARIADRVL 201
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
814-902 2.56e-07

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 54.64  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  814 MDVGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFAD---IQQLLDVLHKLRdqgnTIVVIEH 890
Cdd:PRK11176 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQKNR----TSLVIAH 537
                         90
                 ....*....|..
gi 16131884  891 NLDVIKTADWIV 902
Cdd:PRK11176 538 RLSTIEKADEIL 549
GguA NF040905
sugar ABC transporter ATP-binding protein;
807-901 2.76e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.03  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLqtLMDVGLTyirlgQSATTLSG----GEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQG 882
Cdd:NF040905 120 AREL--LAKVGLD-----ESPDTLVTdigvGKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKAQG 189
                         90       100
                 ....*....|....*....|
gi 16131884  883 NTIVVIEHNL-DVIKTADWI 901
Cdd:NF040905 190 ITSIIISHKLnEIRRVADSI 209
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
830-923 2.80e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 52.96  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  830 LSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNL-DVIKTADWIVdlgpeg 908
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQ---VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTV------ 213
                         90
                 ....*....|....*
gi 16131884  909 gSGGGEILVSGTPET 923
Cdd:PRK15056 214 -MVKGTVLASGPTET 227
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
816-904 3.58e-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: 54.02  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 816 VGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDIQQLLDV---LHKLRDQGNTIVVIEHNL 892
Cdd:COG1245 200 LGLENI-LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEPSSYL---DIYQRLNVarlIRELAEEGKYVLVVEHDL 272
                        90
                ....*....|..
gi 16131884 893 DVIktaDWIVDL 904
Cdd:COG1245 273 AIL---DYLADY 281
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
787-902 3.76e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 54.08  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  787 EVLDMTIEEAR--EFFDAVPAlarklqtlmdvGLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLH 864
Cdd:PRK11174 453 EQLQQALENAWvsEFLPLLPQ-----------GLDTP-IGDQAAGLSVGQAQRLALARALLQPC---QLLLLDEPTASLD 517
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131884  865 FADIQQLLDVLHKLRdQGNTIVVIEHNLDVIKTADWIV 902
Cdd:PRK11174 518 AHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIW 554
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
805-904 3.90e-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: 51.70  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLQTLMDVGLTYIrlGQSATTLSGGEAQRVKLAREL-SKRGtgqtLYILDEPTTGL--HFAdiQQLLD--VLHKLR 879
Cdd:cd03250 105 ALEPDLEILPDGDLTEI--GEKGINLSGGQKQRISLARAVySDAD----IYLLDDPLSAVdaHVG--RHIFEncILGLLL 176
                        90       100
                ....*....|....*....|....*
gi 16131884 880 DqGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03250 177 N-NKTRILVTHQLQLLPHADQIVVL 200
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
822-902 4.28e-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: 4.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGL--HFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTAD 899
Cdd:cd03290 133 EIGERGINLSGGQRQRICVARALYQN---TNIVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHAD 209

                ...
gi 16131884 900 WIV 902
Cdd:cd03290 210 WII 212
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
825-924 4.37e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 53.31  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  825 QSATTLSGGEAQRVKLARELSKrgtgQT-LYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDV-IKTADWIV 902
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQ----ATpVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELV 210
                         90       100
                 ....*....|....*....|..
gi 16131884  903 DLgpeggsGGGEILVSGTPETV 924
Cdd:PRK09536 211 LL------ADGRVRAAGPPADV 226
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
822-902 4.44e-07

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 53.63  E-value: 4.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHF---ADIQQLLDVLHKlrdqGNTIVVIEHNLDVIKTA 898
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDP---PILILDEATSALDTeteALIQEALERLMK----GRTTIVIAHRLSTIRNA 541

                ....
gi 16131884 899 DWIV 902
Cdd:COG1132 542 DRIL 545
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
434-587 4.88e-07

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: 53.37  E-value: 4.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 434 MSIGHAMEF---FNNLKLAGQRAKIAEKILKEigdrlkflvnVGLNYLTLSRSAETLSGGEAQRIRLASQIGAG--LVgv 508
Cdd:COG1123 359 MTVGDIIAEplrLHGLLSRAERRERVAELLER----------VGLPPDLADRYPHELSGGQRQRVAIARALALEpkLL-- 426
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 509 myVLDEPSIGL---HQRdneRLLGTLIHLRD-LGNTVIVVEHDEDAIRA-ADHVIdigpgagV-HGGEVVAEGPLEAIMA 582
Cdd:COG1123 427 --ILDEPTSALdvsVQA---QILNLLRDLQReLGLTYLFISHDLAVVRYiADRVA-------VmYDGRIVEDGPTEEVFA 494

                ....*
gi 16131884 583 VPESL 587
Cdd:COG1123 495 NPQHP 499
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
830-924 5.31e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 52.32  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIKTADWIVDLgpeg 908
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQ---PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVM---- 213
                         90
                 ....*....|....*.
gi 16131884  909 gsGGGEILVSGTPETV 924
Cdd:PRK13635 214 --NKGEILEEGTPEEI 227
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
790-936 5.68e-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: 5.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 790 DMTIEE--A---REFFDAVPALARKL--QTLMDVGLtyirlGQSATT----LSGGEAQRVKLARelskrgtgqTL----- 853
Cdd:COG1127  96 SLTVFEnvAfplREHTDLSEAEIRELvlEKLELVGL-----PGAADKmpseLSGGMRKRVALAR---------ALaldpe 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 854 YIL-DEPTTGLhfaD------IQQLldvLHKLRDQ-GNTIVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:COG1127 162 ILLyDEPTAGL---DpitsavIDEL---IRELRDElGLTSVVVTHDLDsAFAIADRVAVL------ADGKIIAEGTPEEL 229
                       170
                ....*....|..
gi 16131884 925 AECEASHTARFL 936
Cdd:COG1127 230 LASDDPWVRQFL 241
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
807-921 6.62e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.16  E-value: 6.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLQT--LMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNT 884
Cdd:PRK13631 152 AKKLAKfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQ---PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT 228
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131884  885 IVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVSGTP 921
Cdd:PRK13631 229 VFVITHTMEhVLEVADEVIVM------DKGKILKTGTP 260
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
481-588 7.00e-07

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 51.70  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  481 SRSAETLSGGEAQRIRLA---SQI--GAGLVGVMYvLDEPSIGL---HQRDNERLLGTLIHLRdlGNTVIVVEHDED-AI 551
Cdd:PRK13548 129 GRDYPQLSGGEQQRVQLArvlAQLwePDGPPRWLL-LDEPTSALdlaHQHHVLRLARQLAHER--GLAVIVVLHDLNlAA 205
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131884  552 RAADHVIDIgpgagvHGGEVVAEGPLEAIMAvPESLT 588
Cdd:PRK13548 206 RYADRIVLL------HQGRLVADGTPAEVLT-PETLR 235
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
623-888 7.80e-07

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: 51.12  E-value: 7.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfPIAQRQLNGATIaepapyrdiqglehfdkvididqspigrtprsnpa 702
Cdd:cd03234  23 LNDVSLHVESGQVMAILGSSGSGKTTLLD----AISGRVEGGGTT----------------------------------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 703 tyTGvftpvRELFAGVPESRARgyTPGRFSFnVRggrceacQGDgvikvemHFLPDIYVpcdqckgkrynRETLeikykg 782
Cdd:cd03234  64 --SG-----QILFNGQPRKPDQ--FQKCVAY-VR-------QDD-------ILLPGLTV-----------RETL------ 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 783 kTIHEVLDMTieeaREFFDAVPALARKLQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG 862
Cdd:cd03234 103 -TYTAILRLP----RKSSDAIRKKRVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLL---WDPKVLILDEPTSG 173
                       250       260
                ....*....|....*....|....*...
gi 16131884 863 LhfaDIQQLLDVLHKLRD--QGNTIVVI 888
Cdd:cd03234 174 L---DSFTALNLVSTLSQlaRRNRIVIL 198
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
823-904 8.70e-07

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 50.95  E-value: 8.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 823 LGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDqGNTIVVIEHNLDVIKTADWIV 902
Cdd:cd03252 132 VGEQGAGLSGGQRQRIAIARALI---HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRII 207

                ..
gi 16131884 903 DL 904
Cdd:cd03252 208 VM 209
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
439-600 8.92e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 51.09  E-value: 8.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  439 AMEFFNNLKL---AGQRAKIAEKILKEIGDRLKflvnvglnyLT--LSRSAETLSGGEAQRIRLAS---QI--GAGLVGV 508
Cdd:PRK03695  83 AMPVFQYLTLhqpDKTRTEAVASALNEVAEALG---------LDdkLGRSVNQLSGGEWQRVRLAAvvlQVwpDINPAGQ 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  509 MYVLDEPSIGLhqrD--NERLLGTLIH-LRDLGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGEVVAEGPLEAIMAvP 584
Cdd:PRK03695 154 LLLLDEPMNSL---DvaQQAALDRLLSeLCQQGIAVVMSSHDlNHTLRHADRVWLL------KQGKLLASGRRDEVLT-P 223
                        170
                 ....*....|....*.
gi 16131884  585 ESLTGQYMSGKRKIEV 600
Cdd:PRK03695 224 ENLAQVFGVNFRRLDV 239
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
790-929 9.02e-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: 51.00  E-value: 9.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 790 DMTIEE-----AREFFDAVPALARKLQTLM-DVGLTYIRLgQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTG- 862
Cdd:cd03218  89 KLTVEEnilavLEIRGLSKKEREEKLEELLeEFHITHLRK-SKASSLSGGERRRVEIARALA---TNPKFLLLDEPFAGv 164
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131884 863 --LHFADIQQLldvLHKLRDQGNTIVVIEHN----LDVIKTADWIVDlgpeggsggGEILVSGTPETVAECEA 929
Cdd:cd03218 165 dpIAVQDIQKI---IKILKDRGIGVLITDHNvretLSITDRAYIIYE---------GKVLAEGTPEEIAANEL 225
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
830-897 9.40e-07

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: 50.48  E-value: 9.40e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKT 897
Cdd:cd03292 137 LSGGEQQRVAIARAIVNS---PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
828-924 9.95e-07

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 51.17  E-value: 9.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  828 TTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD-VIKTADWIVDLgp 906
Cdd:PRK11231 137 TDLSGGQRQRAFLAMVLAQ---DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVL-- 211
                         90
                 ....*....|....*...
gi 16131884  907 eggsGGGEILVSGTPETV 924
Cdd:PRK11231 212 ----ANGHVMAQGTPEEV 225
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
791-924 1.04e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 51.56  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  791 MTIEEAREffdavpaLARKLQTLmdVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK13634 116 VSEEDAKQ-------KAREMIEL--VGLPEELLARSPFELSGGQMRRVAIAGVLAME---PEVLVLDEPTAGLDPKGRKE 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884  871 LLDVLHKLRDQGN-TIVVIEHNL-DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13634 184 MMEMFYKLHKEKGlTTVLVTHSMeDAARYADQIVVM------HKGTVFLQGTPREI 233
cbiO PRK13649
energy-coupling factor transporter ATPase;
805-924 1.07e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 51.28  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  805 ALARklQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNT 884
Cdd:PRK13649 123 ALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAME---PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 16131884  885 IVVIEHNL-DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13649 198 IVLVTHLMdDVANYADFVYVL------EKGKLVLSGKPKDI 232
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
791-893 1.20e-06

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 50.44  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 791 MTIEEAREFFDAVPALAR--------KLQTLMDVGLTYIRLGQSattLSGGEAQRVKLARELSKRgtgQTLYILDEPTTG 862
Cdd:cd03266  93 LTARENLEYFAGLYGLKGdeltarleELADRLGMEELLDRRVGG---FSTGMRQKVAIARALVHD---PPVLLLDEPTTG 166
                        90       100       110
                ....*....|....*....|....*....|.
gi 16131884 863 LHFADIQQLLDVLHKLRDQGNTIVVIEHNLD 893
Cdd:cd03266 167 LDVMATRALREFIRQLRALGKCILFSTHIMQ 197
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
781-895 1.24e-06

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 50.83  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 781 KGKTIhEVLDMTIEeaREFFDavpalarklqTLMDV-GLTYIrLGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEP 859
Cdd:cd03236 104 KGKVG-ELLKKKDE--RGKLD----------ELVDQlELRHV-LDRNIDQLSGGELQRVAIAAALARDA---DFYFFDEP 166
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131884 860 TTGLhfaDIQQLLD---VLHKLRDQGNTIVVIEHNLDVI 895
Cdd:cd03236 167 SSYL---DIKQRLNaarLIRELAEDDNYVLVVEHDLAVL 202
cbiO PRK13645
energy-coupling factor transporter ATPase;
794-902 1.28e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 51.16  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  794 EEAREFFDAVPALARKLQTLMDvgltYIRlgQSATTLSGGEAQRVKLARELSKrgTGQTLyILDEPTTGLHFADIQQLLD 873
Cdd:PRK13645 121 ENKQEAYKKVPELLKLVQLPED----YVK--RSPFELSGGQKRRVALAGIIAM--DGNTL-VLDEPTGGLDPKGEEDFIN 191
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16131884  874 VLHKL-RDQGNTIVVIEHNLD-VIKTADWIV 902
Cdd:PRK13645 192 LFERLnKEYKKRIIMVTHNMDqVLRIADEVI 222
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
822-892 1.47e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 50.54  E-value: 1.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  822 RLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQgNTIVVIEHNL 892
Cdd:PRK14239 141 RLHDSALGLSGGQQQRVCIARVLA---TSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSM 207
cbiO PRK13637
energy-coupling factor transporter ATPase;
462-585 1.49e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 50.82  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  462 EIGDRLKFLVN-VGLNYLTLS-RSAETLSGGEAQRIRLAsqigaGLVGVM---YVLDEPSIGLHQRDNERLLGTLIHLRD 536
Cdd:PRK13637 118 EIENRVKRAMNiVGLDYEDYKdKSPFELSGGQKRRVAIA-----GVVAMEpkiLILDEPTAGLDPKGRDEILNKIKELHK 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884  537 -LGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGEVVAEGP----------LEAI-MAVPE 585
Cdd:PRK13637 193 eYNMTIILVSHSmEDVAKLADRIIVM------NKGKCELQGTprevfkevetLESIgLAVPQ 248
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
480-587 1.51e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.78  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIRLasqigAGLVGV---MYVLDEPSIGLHQRDNERLLGTLIHLRDLGN-TVIVVEHDEDAIRAAD 555
Cdd:PRK13635 134 LNREPHRLSGGQKQRVAI-----AGVLALqpdIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQAD 208
                         90       100       110
                 ....*....|....*....|....*....|..
gi 16131884  556 HVIDIgpgagvHGGEVVAEGPLEAIMAVPESL 587
Cdd:PRK13635 209 RVIVM------NKGEILEEGTPEEIFKSGHML 234
cbiO PRK13641
energy-coupling factor transporter ATPase;
467-624 1.52e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 50.98  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLAsqigaglvGVM------YVLDEPSIGLHQRDNERLLGTLIHLRDLGNT 540
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIA--------GVMayepeiLCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  541 VIVVEHDEDAI-RAADHVIDIGpgagvHGGEVVAEGPlEAIMAVPESLTGQYMSG------KRKIEVPKKRVPANPEKVL 613
Cdd:PRK13641 198 VILVTHNMDDVaEYADDVLVLE-----HGKLIKHASP-KEIFSDKEWLKKHYLDEpatsrfASKLEKGGFKFSEMPLTID 271
                        170
                 ....*....|.
gi 16131884  614 KLTGARGNNLK 624
Cdd:PRK13641 272 ELVDGIKNNLK 282
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
804-896 1.52e-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: 51.75  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   804 PALARKLQTLM-DVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQG 882
Cdd:TIGR02633 115 NAMYLRAKNLLrELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR---LLILDEPSSSLTEKETEILLDIIRDLKAHG 191
                          90
                  ....*....|....
gi 16131884   883 NTIVVIEHNLDVIK 896
Cdd:TIGR02633 192 VACVYISHKLNEVK 205
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
487-591 1.56e-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: 50.19  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 487 LSGGEAQRIRLASQIGAGLVGVMYvlDEPSIGLhqrD--NERLLGTLIH-LRD-LGNTVIVVEHDEDAIRA-ADHVidig 561
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLY--DEPTAGL---DpiASGVIDDLIRsLKKeLGLTSIMVTHDLDTAFAiADRI---- 207
                        90       100       110
                ....*....|....*....|....*....|
gi 16131884 562 pgAGVHGGEVVAEGPLEAIMAVPESLTGQY 591
Cdd:cd03261 208 --AVLYDGKIVAEGTPEELRASDDPLVRQF 235
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
811-932 1.97e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 50.52  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  811 QTLMDVGLtYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIE 889
Cdd:PRK13648 125 EALKQVDM-LERADYEPNALSGGQKQRVAIAGVLA---LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISIT 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 16131884  890 HNLDVIKTADWIVDLgpeggsGGGEILVSGTPETVAECEASHT 932
Cdd:PRK13648 201 HDLSEAMEADHVIVM------NKGTVYKEGTPTEIFDHAEELT 237
cbiO PRK13640
energy-coupling factor transporter ATPase;
811-924 2.11e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.57  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  811 QTLMDVGLT-YIRlgQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVI 888
Cdd:PRK13640 126 DVLADVGMLdYID--SEPANLSGGQKQRVAIAGILA---VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISI 200
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16131884  889 EHNLDVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13640 201 THDIDEANMADQVLVL------DDGKLLAQGSPVEI 230
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
822-904 2.58e-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: 49.54  E-value: 2.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHKLRdQGNTIVVIEHNLDVIKTADWI 901
Cdd:cd03253 130 IVGERGLKLSGGEKQRVAIARAILK---NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKI 205

                ...
gi 16131884 902 VDL 904
Cdd:cd03253 206 IVL 208
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
487-564 2.64e-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: 48.75  E-value: 2.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 487 LSGGEAQRIRLASqigaglvgVMY------VLDEPSIGLHQrDNERLLGTLI-HLRDLGNTVIVVEHDEDAIRAADHVID 559
Cdd:cd03246  97 LSGGQRQRLGLAR--------ALYgnprilVLDEPNSHLDV-EGERALNQAIaALKAAGATRIVIAHRPETLASADRILV 167

                ....*
gi 16131884 560 IGPGA 564
Cdd:cd03246 168 LEDGR 172
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
487-560 2.69e-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: 2.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884   487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLIHLRDlGNTVIVVEHDEDAIRAADHVIDI 560
Cdd:TIGR02857 459 LSGGQAQRLALARAFlrDAPLL----LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
830-902 2.92e-06

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 48.46  E-value: 2.92e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHK-LRDQgnTIVVIEHNLDVIKTADWIV 902
Cdd:cd03247  99 FSGGERQRLALARILLQDA---PIVLLDEPTVGLDPITERQLLSLIFEvLKDK--TLIWITHHLTGIEHMDKIL 167
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
805-893 3.06e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 49.98  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  805 ALARKLQTlmdVGLTYIRlGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGN 883
Cdd:PRK10253 123 AVTKAMQA---TGITHLA-DQSVDTLSGGQRQRAWIAMVLAQE---TAIMLLDEPTTWLDISHQIDLLELLSELnREKGY 195
                         90
                 ....*....|
gi 16131884  884 TIVVIEHNLD 893
Cdd:PRK10253 196 TLAAVLHDLN 205
cbiO PRK13646
energy-coupling factor transporter ATPase;
791-902 3.09e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 50.16  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  791 MTIEEAREffdavpalaRKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQ 870
Cdd:PRK13646 116 MNLDEVKN---------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA---MNPDIIVLDEPTAGLDPQSKRQ 183
                         90       100       110
                 ....*....|....*....|....*....|....
gi 16131884  871 LLDVLHKLR-DQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:PRK13646 184 VMRLLKSLQtDENKTIILVSHDMnEVARYADEVI 217
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
414-595 3.55e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 49.53  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  414 LRREARHVYVENTPLPAIS---DMSIGHAM--------EFFNNLKLAGQRAKIAEkilkEIGDRLkflvnvglnyltlSR 482
Cdd:PRK14247  80 LRRRVQMVFQIPNPIPNLSifeNVALGLKLnrlvkskkELQERVRWALEKAQLWD----EVKDRL-------------DA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  483 SAETLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVidigp 562
Cdd:PRK14247 143 PAGKLSGGQQQRLCIARAL--AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV----- 215
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16131884  563 gAGVHGGEVVAEGPLEAIMAVPE-SLTGQYMSGK 595
Cdd:PRK14247 216 -AFLYKGQIVEWGPTREVFTNPRhELTEKYVTGR 248
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
830-924 3.86e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 49.69  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKT-ADWIVDLgpeg 908
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMK---PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVM---- 210
                         90
                 ....*....|....*.
gi 16131884  909 gsGGGEILVSGTPETV 924
Cdd:PRK13639 211 --SDGKIIKEGTPKEV 224
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
480-558 3.97e-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: 48.67  E-value: 3.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 480 LSRSAETLSGGEAQRIRLASqigaGLV---GVMyVLDEPSIGLHQRDNERLLGTLIHL-RDLGNTVIVVEHD-EDAIRAA 554
Cdd:cd03259 124 LNRYPHELSGGQQQRVALAR----ALArepSLL-LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDqEEALALA 198

                ....
gi 16131884 555 DHVI 558
Cdd:cd03259 199 DRIA 202
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
830-904 4.13e-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: 4.13e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHKLRDqgnTIVVIEHNLDVI-KTADWIVDL 904
Cdd:cd03221  71 LSGGEKMRLALAKLLLENP---NLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLdQVATKIIEL 140
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
804-904 4.32e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 48.94  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  804 PALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELskrgtgQTL---YILDEPTTGLHFADIQQLLDVLHKL-R 879
Cdd:PRK10247 112 PDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL------QFMpkvLLLDEITSALDESNKHNVNEIIHRYvR 185
                         90       100
                 ....*....|....*....|....*
gi 16131884  880 DQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:PRK10247 186 EQNIAVLWVTHDKDEINHADKVITL 210
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
791-902 4.97e-06

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: 48.37  E-value: 4.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 791 MTIEEAREFFDAVPALARKL--QTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADI 868
Cdd:cd03268  87 LTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGN---PDLLILDEPTNGLDPDGI 162
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131884 869 QQLLDVLHKLRDQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLsEIQKVADRIG 197
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
487-558 5.06e-06

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: 47.76  E-value: 5.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 487 LSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrD--NERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVI 558
Cdd:cd03228  97 LSGGQRQRIAIArallrdPPI--------LILDEATSAL---DpeTEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
771-895 5.08e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 50.00  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  771 YNRETLEIKYKGKT----------------IHEVLD----MTIEE----AREFFDAVPALA-RKLQTLMDVGLTyiRLG- 824
Cdd:PRK10762  54 YTRDAGSILYLGKEvtfngpkssqeagigiIHQELNlipqLTIAEniflGREFVNRFGRIDwKKMYAEADKLLA--RLNl 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884  825 -----QSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:PRK10762 132 rfssdKLVGELSIGEQQMVEIAKVLS---FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
808-893 5.74e-06

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 48.86  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  808 RKLQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIV 886
Cdd:PRK09984 132 RALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQA---KVILADEPIASLDPESARIVMDTLRDInQNDGITVV 207

                 ....*..
gi 16131884  887 VIEHNLD 893
Cdd:PRK09984 208 VTLHQVD 214
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
783-896 5.97e-06

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 50.09  E-value: 5.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  783 KTIHEVLDMTIEEAREffdavPALARKLQTLMDVGLTYI--RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPT 860
Cdd:PRK15134 113 KQLYEVLSLHRGMRRE-----AARGEILNCLDRVGIRQAakRLTDYPHQLSGGERQRVMIAMALLTR---PELLIADEPT 184
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131884  861 TGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIK 896
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVR 221
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
805-890 6.36e-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: 48.58  E-value: 6.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGN 883
Cdd:COG4181 123 ARARARALLERVGLGH-RLDHYPAQLSGGEQQRVALARAFA---TEPAILFADEPTGNLDAATGEQIIDLLFELnRERGT 198

                ....*..
gi 16131884 884 TIVVIEH 890
Cdd:COG4181 199 TLVLVTH 205
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
829-896 6.83e-06

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: 47.87  E-value: 6.83e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884 829 TLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLDVIK 896
Cdd:cd03298 128 ELSGGERQRVALARVLVRD---KPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAK 193
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
468-549 7.44e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 48.93  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  468 KFLVNVGLNYLTLSRSAETLSGGEAQRIRLAsqigaGLVGV---MYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVV 544
Cdd:PRK13651 147 KYIELVGLDESYLQRSPFELSGGQKRRVALA-----GILAMepdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILV 221

                 ....*
gi 16131884  545 EHDED 549
Cdd:PRK13651 222 THDLD 226
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
486-581 8.39e-06

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: 48.16  E-value: 8.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 486 TLSGGEAQRIrlasQIGAGLVG--VMYVLDEPSIGL--HQRdnERLLGTLIHLRDLGNTVIV-VEHD-EDAIRAADHVID 559
Cdd:COG1119 142 TLSQGEQRRV----LIARALVKdpELLILDEPTAGLdlGAR--ELLLALLDKLAAEGAPTLVlVTHHvEEIPPGITHVLL 215
                        90       100
                ....*....|....*....|..
gi 16131884 560 IgpgagvHGGEVVAEGPLEAIM 581
Cdd:COG1119 216 L------KDGRVVAAGPKEEVL 231
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
788-902 8.65e-06

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 48.09  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  788 VLDMTIEEAREffdavpaLARKLqtlmdvgLTYIRLGQSATT----LSGGEAQRVKLARELSKRgtGQTLyILDEPTTGL 863
Cdd:PRK11124 110 VLGLSKDQALA-------RAEKL-------LERLRLKPYADRfplhLSGGQQQRVAIARALMME--PQVL-LFDEPTAAL 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 16131884  864 HFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVV 212
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
788-926 9.50e-06

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: 49.42  E-value: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   788 VLDMTIEEAREF-FDAVPALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHfa 866
Cdd:TIGR03269 127 VLDNVLEALEEIgYEGKEAVGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKE---PFLFLADEPTGTLD-- 200
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884   867 diQQLLDVLHKLRDQGntivVIEHNLDVIKTADW---IVDLGPEGG-SGGGEILVSGTPETVAE 926
Cdd:TIGR03269 201 --PQTAKLVHNALEEA----VKASGISMVLTSHWpevIEDLSDKAIwLENGEIKEEGTPDEVVA 258
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
809-903 9.67e-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: 9.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 809 KLQTLMDvgltyirlgQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHKLR----DQGNT 884
Cdd:cd03237 104 QIEQILD---------REVPELSGGELQRVAIAACLSKDA---DIYLLDEPSAYL---DVEQRLMASKVIRrfaeNNEKT 168
                        90
                ....*....|....*....
gi 16131884 885 IVVIEHnlDVIkTADWIVD 903
Cdd:cd03237 169 AFVVEH--DII-MIDYLAD 184
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
486-582 1.02e-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: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 486 TLSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrDNE---RLLGTLIHLRDlGNTVIVVEHDEDAIRAADH 556
Cdd:COG2274 611 NLSGGQRQRLAIArallrnPRI--------LILDEATSAL---DAEteaIILENLRRLLK-GRTVIIIAHRLSTIRLADR 678
                        90       100
                ....*....|....*....|....*.
gi 16131884 557 VIDIgpgagvHGGEVVAEGPLEAIMA 582
Cdd:COG2274 679 IIVL------DKGRIVEDGTHEELLA 698
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
791-890 1.05e-05

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: 47.49  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 791 MTIEEAREFFDAVPALARKLQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQ 870
Cdd:cd03231  88 LSVLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLL---SGRPLWILDEPTTALDKAGVAR 163
                        90       100
                ....*....|....*....|
gi 16131884 871 LLDVLHKLRDQGNTIVVIEH 890
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
623-904 1.10e-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: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqRQLNGATiaEPAPYRdiqgLEHFDKVIDIDQSPIGRTPRSNPA 702
Cdd:cd03256  17 LKDVSLSINPGEFVALIGPSGAGKSTLL---------RCLNGLV--EPTSGS----VLIDGTDINKLKGKALRQLRRQIG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 703 TytgVFtpvrELFAGVPESRARGytpgrfsfNVRGGRCEacqgdgvikvEMHFLPDIYvpcdqckgKRYNRETleikykg 782
Cdd:cd03256  82 M---IF----QQFNLIERLSVLE--------NVLSGRLG----------RRSTWRSLF--------GLFPKEE------- 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 783 ktihevldmtIEEAREffdavpALARklqtlmdVGLT---YIRlgqsATTLSGGEAQRVKLARELSKRgtgQTLYILDEP 859
Cdd:cd03256 122 ----------KQRALA------ALER-------VGLLdkaYQR----ADQLSGGQQQRVAIARALMQQ---PKLILADEP 171
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 16131884 860 TTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLDVIKT-ADWIVDL 904
Cdd:cd03256 172 VASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREyADRIVGL 218
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
825-940 1.12e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 48.08  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  825 QSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI-KTADWIVD 903
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQAR---YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYV 208
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131884  904 LgpeggsGGGEILVSGTP-ETVAECEASHTARFLKPML 940
Cdd:PRK13638 209 L------RQGQILTHGAPgEVFACTEAMEQAGLTQPWL 240
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
805-890 1.16e-05

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 47.52  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNT 884
Cdd:cd03262 112 AEERALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMN---PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMT 187

                ....*.
gi 16131884 885 IVVIEH 890
Cdd:cd03262 188 MVVVTH 193
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
793-904 1.19e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 48.12  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  793 IEEAREFFDAVPALARKLQTLMDVgltYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLL 872
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARALALK---PKVLLMDEPTSMIDIVNSQAIE 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16131884  873 DVLHKLRDQgNTIVVIEHN-LDVIKTADWIVDL 904
Cdd:PRK14246 194 KLITELKNE-IAIVIVSHNpQQVARVADYVAFL 225
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
824-904 1.39e-05

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: 47.47  E-value: 1.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 824 GQSATTLSGGEAQRVKLARELSKrgTGQTLyILDEPTTGLHfADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVD 903
Cdd:cd03248 145 GEKGSQLSGGQKQRVAIARALIR--NPQVL-ILDEATSALD-AESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILV 220

                .
gi 16131884 904 L 904
Cdd:cd03248 221 L 221
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
806-904 1.44e-05

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 48.95  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  806 LARKLQTLMDvGLtYIRLGQSATTLSGGEAQRVKLARELSKrgTGQTLyILDEPTTGLHFADIQQLLDVLHKLRDQgNTI 885
Cdd:PRK10790 455 LAELARSLPD-GL-YTPLGEQGNNLSVGQKQLLALARVLVQ--TPQIL-ILDEATANIDSGTEQAIQQALAAVREH-TTL 528
                         90
                 ....*....|....*....
gi 16131884  886 VVIEHNLDVIKTADWIVDL 904
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVL 547
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
830-896 1.59e-05

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 48.15  E-value: 1.59e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQ-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 1.67e-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: 47.23  E-value: 1.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 822 RLGQSATTLSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLhfaD------IQQLLDVLHKLRdqgnTIVVIEHNLDVI 895
Cdd:cd03251 131 VIGERGVKLSGGQRQRIAIARALLK---DPPILILDEATSAL---DteserlVQAALERLMKNR----TTFVIAHRLSTI 200

                ....*..
gi 16131884 896 KTADWIV 902
Cdd:cd03251 201 ENADRIV 207
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
811-890 1.72e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 48.50  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   811 QTLMDVGL-----TYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTI 885
Cdd:TIGR00955 143 EVLQALGLrkcanTRIGVPGRVKGLSGGERKRLAFASELL---TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTI 219

                  ....*
gi 16131884   886 VVIEH 890
Cdd:TIGR00955 220 ICTIH 224
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
775-903 1.74e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.65  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  775 TLEIKYKGKTIHEVLDMTIEEareFFDAVPA----------LARKLQ--TLMDvgltyirlgQSATTLSGGEAQRVKLAR 842
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVED---LLRSITDdlgssyykseIIKPLQleRLLD---------KNVKDLSGGELQRVAIAA 466
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884  843 ELSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHKLR----DQGNTIVVIEHNLDVIktaDWIVD 903
Cdd:PRK13409 467 CLSRDA---DLYLLDEPSAHL---DVEQRLAVAKAIRriaeEREATALVVDHDIYMI---DYISD 522
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
828-894 1.87e-05

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 47.23  E-value: 1.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884  828 TTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLDV 894
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLV---THPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAV 214
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
467-597 1.90e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 47.27  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  467 LKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEH 546
Cdd:PRK10619 133 VKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL--AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16131884  547 D-EDAIRAADHVIDIgpgagvHGGEVVAEGPLEAIMAVPES-LTGQYMSGKRK 597
Cdd:PRK10619 211 EmGFARHVSSHVIFL------HQGKIEEEGAPEQLFGNPQSpRLQQFLKGSLK 257
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
824-902 1.91e-05

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 48.57  E-value: 1.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884   824 GQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHfADIQQLLDVLHKLrdQGNTIVVIEHNLDVIKTADWIV 902
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRK---PRVLILDEATSALD-AECEQLLQESRSR--ASRTVLLIAHRLSTVERADQIL 684
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
794-895 1.91e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 47.80  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  794 EEAREFFDAV--PAlARKlqtlmdvgltyiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQL 871
Cdd:PRK09473 137 EESVRMLDAVkmPE-ARK------------RMKMYPHEFSGGMRQRVMIAMALLCR---PKLLIADEPTTALDVTVQAQI 200
                         90       100
                 ....*....|....*....|....*
gi 16131884  872 LDVLHKLRDQGNT-IVVIEHNLDVI 895
Cdd:PRK09473 201 MTLLNELKREFNTaIIMITHDLGVV 225
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
511-899 2.04e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 48.12  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  511 VLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVIDIGPGAGVHGGEVVAEGPLEAIMAVPESLTG 589
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDIIQAITPAARE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  590 QYMSGKRKI--EVP-KKRVPANPEKVLKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLInDTLFPIAQRQ----- 661
Cdd:PRK15439 243 KSLSASQKLwlELPgNRRQQAAGAPVLTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELA-ETLYGLRPARggrim 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  662 LNGATIAEPAPY-RDIQGLEHFDKviDIDQSpigrtprsnpatytgvftpvrELFAGVPES-RARGYTPGRFSFNVRGGR 739
Cdd:PRK15439 322 LNGKEINALSTAqRLARGLVYLPE--DRQSS---------------------GLYLDAPLAwNVCALTHNRRGFWIKPAR 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  740 CEAcqgdgviKVEmhflpdiyvpcdqckgkRYNReTLEIKYKGKTihevldmtieeareffdavpalarklqtlmdvglt 819
Cdd:PRK15439 379 ENA-------VLE-----------------RYRR-ALNIKFNHAE----------------------------------- 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  820 yirlgQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLHKlrdQGNTIVVIEHNLD-VI 895
Cdd:PRK15439 399 -----QAARTLSGGNQQKVLIAKCLEAS---PQLLIVDEPTRGVDVsarNDIYQLIRSIAA---QNVAVLFISSDLEeIE 467

                 ....
gi 16131884  896 KTAD 899
Cdd:PRK15439 468 QMAD 471
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
410-595 2.17e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 46.96  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  410 EGTRLRREARHVYVENTPLPAISDM-SIGHAMEFfNNLKLAGQRAKIAEKILKEIGDRLKFlvnvglnYLTLSRSAETLS 488
Cdd:PRK14246  84 DAIKLRKEVGMVFQQPNPFPHLSIYdNIAYPLKS-HGIKEKREIKKIVEECLRKVGLWKEV-------YDRLNSPASQLS 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  489 GGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVidigpgAGVHG 568
Cdd:PRK14246 156 GGQQQRLTIARAL--ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYV------AFLYN 227
                        170       180
                 ....*....|....*....|....*...
gi 16131884  569 GEVVAEGPLEAIMAVPES-LTGQYMSGK 595
Cdd:PRK14246 228 GELVEWGSSNEIFTSPKNeLTEKYVIGR 255
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
829-893 2.61e-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: 46.12  E-value: 2.61e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 829 TLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLD 893
Cdd:cd03269 128 ELSKGNQQKVQFIAAVIHD---PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
829-902 2.66e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 47.98  E-value: 2.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884  829 TLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:PRK11288 396 NLSGGNQQKAILGRWLS---EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIV 467
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
810-892 2.69e-05

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 47.90  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  810 LQTLMDVGLTYIR---------LGQSATTLSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLHFADIQQLLDVLHKLRd 880
Cdd:PRK11160 447 IEVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARALLHDA---PLLLLDEPTEGLDAETERQILELLAEHA- 522
                         90
                 ....*....|..
gi 16131884  881 QGNTIVVIEHNL 892
Cdd:PRK11160 523 QNKTVLMITHRL 534
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
480-562 2.81e-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: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 480 LSRSAETLSGGE------AQRIRLASQIGAGLvGVMyVLDEPSIGLhqrDNERLLGTLI-----HLRDLGNTVIVVEHDE 548
Cdd:cd03240 109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNL---DEENIEESLAeiieeRKSQKNFQLIVITHDE 183
                        90
                ....*....|....
gi 16131884 549 DAIRAADHVIDIGP 562
Cdd:cd03240 184 ELVDAADHIYRVEK 197
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
830-922 2.91e-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: 46.34  E-value: 2.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaD------IQQLldvLHKLRDQ-GNTIVVIEHNLD-VIKTADWI 901
Cdd:cd03261 137 LSGGMKKRVALARALA---LDPELLLYDEPTAGL---DpiasgvIDDL---IRSLKKElGLTSIMVTHDLDtAFAIADRI 207
                        90       100
                ....*....|....*....|.
gi 16131884 902 VDLgpeggsGGGEILVSGTPE 922
Cdd:cd03261 208 AVL------YDGKIVAEGTPE 222
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
801-925 3.40e-05

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 46.26  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  801 DAVPALAR-KLQTLMDvgltyirlgQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLR 879
Cdd:PRK09544 100 DILPALKRvQAGHLID---------APMQKLSGGETQRVLLARALLNR---PQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 16131884  880 DQGN-TIVVIEHNLD-VIKTADWIVDLgpeggsgGGEILVSGTPETVA 925
Cdd:PRK09544 168 RELDcAVLMVSHDLHlVMAKTDEVLCL-------NHHICCSGTPEVVS 208
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
446-585 3.72e-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: 46.04  E-value: 3.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 446 LKLAGQ-RAKIAEKILkeigDRLKFlvnVGLNYLTLSRSAEtLSGGEAQRIRLASqigaGLVGVMYVL--DEPSIGLHQR 522
Cdd:cd03258 107 LEIAGVpKAEIEERVL----ELLEL---VGLEDKADAYPAQ-LSGGQKQRVGIAR----ALANNPKVLlcDEATSALDPE 174
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 523 DNERLLGTLIHL-RDLGNTVIVVEHDEDAIRA-ADHVidigpgAGVHGGEVVAEGPLEAIMAVPE 585
Cdd:cd03258 175 TTQSILALLRDInRELGLTIVLITHEMEVVKRiCDRV------AVMEKGEVVEEGTVEEVFANPQ 233
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
774-903 4.43e-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: 47.09  E-value: 4.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 774 ETLEIKYKGKTIHEVLDMTIEE-----AREFFDAVPA---LARKLQ--TLMDvgltyirlgQSATTLSGGEAQRVKLARE 843
Cdd:COG1245 399 EDLKISYKPQYISPDYDGTVEEflrsaNTDDFGSSYYkteIIKPLGleKLLD---------KNVKDLSGGELQRVAIAAC 469
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884 844 LSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHKLR----DQGNTIVVIEHNLDVIktaDWIVD 903
Cdd:COG1245 470 LSRDA---DLYLLDEPSAHL---DVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLI---DYISD 524
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
774-923 4.71e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.33  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   774 ETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLmdvgltyirLGQSATTLSGGEAQRVKLARELSKrgtGQTL 853
Cdd:PTZ00265  533 ELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETL---------VGSNASKLSGGQKQRISIARAIIR---NPKI 600
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884   854 YILDEPTTGLHFADIQQLLDVLHKLRDQGNTI-VVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPET 923
Cdd:PTZ00265  601 LILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPT 671
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
482-582 4.88e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 46.13  E-value: 4.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  482 RSAETLSGGEAQRIRLAsQIGAGLVGVMyVLDEPSIGL---HQRDNERLLGTLIhlRDLGNTVIVVEHD-EDAIRAADHV 557
Cdd:PRK10253 139 QSVDTLSGGQRQRAWIA-MVLAQETAIM-LLDEPTTWLdisHQIDLLELLSELN--REKGYTLAAVLHDlNQACRYASHL 214
                         90       100
                 ....*....|....*....|....*.
gi 16131884  558 IdigpgaGVHGGEVVAEG-PLEAIMA 582
Cdd:PRK10253 215 I------ALREGKIVAQGaPKEIVTA 234
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
823-893 5.05e-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: 45.36  E-value: 5.05e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884 823 LGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLD 893
Cdd:cd03297 125 LNRYPAQLSGGEKQRVALARALAAQ---PELLLLDEPFSALDRALRLQLLPELKQIKKNLNiPVIFVTHDLS 193
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
788-896 5.11e-05

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 45.77  E-value: 5.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 788 VLDMTIEEAREffdavpaLARKLqtlmdvgLTYIRLGQSATT----LSGGEAQRVKLARELSKRgtGQTLyILDEPTTGL 863
Cdd:COG4161 110 VLGLSKEQARE-------KAMKL-------LARLRLTDKADRfplhLSGGQQQRVAIARALMME--PQVL-LFDEPTAAL 172
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131884 864 HFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIK 896
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIVTHEVEFAR 205
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
14-40 5.29e-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: 45.15  E-value: 5.29e-05
                        10        20
                ....*....|....*....|....*..
gi 16131884  14 LKNINLVIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd03250  21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
830-896 5.55e-05

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 46.33  E-value: 5.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  830 LSGGEAQRVKLARELSKRGTgqtlyIL--DEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLDVIK 896
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPK-----VLlcDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVK 205
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
791-924 5.85e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 45.65  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  791 MTIEEAREFFDAVPALARKLQTLMDVGLTYIR--LGQSattLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADI 868
Cdd:PRK10895 100 MAVLQIRDDLSAEQREDRANELMEEFHIEHLRdsMGQS---LSGGERRRVEIARALA---ANPKFILLDEPFAGVDPISV 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  869 QQLLDVLHKLRDQGNTIVVIEHN----LDVIKTAdWIVDlgpeggsgGGEILVSGTPETV 924
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNvretLAVCERA-YIVS--------QGHLIAHGTPTEI 224
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
446-584 5.89e-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: 45.75  E-value: 5.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 446 LKLAG-QRAKIAEKIlkeigDRLKFLVNVGLNYLtLSRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDN 524
Cdd:cd03295 100 PKLLKwPKEKIRERA-----DELLALVGLDPAEF-ADRYPHELSGGQQQRVGVARALAAD--PPLLLMDEPFGALDPITR 171
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884 525 ERLLGTLIHL-RDLGNTVIVVEHD-EDAIRAADHVidigpgAGVHGGEVVAEGPLEAIMAVP 584
Cdd:cd03295 172 DQLQEEFKRLqQELGKTIVFVTHDiDEAFRLADRI------AIMKNGEIVQVGTPDEILRSP 227
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
454-547 6.34e-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: 46.70  E-value: 6.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 454 KIAEK-ILKEIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIrlasQIGAGLV--GVMYVLDEPSIGL--HQRdnerlL 528
Cdd:COG1245 186 KVDERgKLDELAEKL------GLENI-LDRDISELSGGELQRV----AIAAALLrdADFYFFDEPSSYLdiYQR-----L 249
                        90       100
                ....*....|....*....|..
gi 16131884 529 GTLIHLRDL---GNTVIVVEHD 547
Cdd:COG1245 250 NVARLIRELaeeGKYVLVVEHD 271
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
623-902 6.85e-05

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: 45.29  E-value: 6.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtLfpiaqrqlngatiaepapyrdIQGL-EHFDKVIDIDQSPIGRTPRSNp 701
Cdd:cd03254  19 LKDINFSIKPGETVAIVGPTGAGKTTLIN--L---------------------LMRFyDPQKGQILIDGIDIRDISRKS- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 702 atytgvftpVRELFAGVPESrargytPGRFSfnvrggrceacqgdGVIKVEMHFlpdiyvpcdqckGKRYNRETLEIKyK 781
Cdd:cd03254  75 ---------LRSMIGVVLQD------TFLFS--------------GTIMENIRL------------GRPNATDEEVIE-A 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 782 GKTIHevldmtieeAREFFDAVPAlarklqtlmdvGLTYIrLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTT 861
Cdd:cd03254 113 AKEAG---------AHDFIMKLPN-----------GYDTV-LGENGGNLSQGERQLLAIARAMLRD---PKILILDEATS 168
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 16131884 862 GLHF---ADIQQLLDVLHKlrdqGNTIVVIEHNLDVIKTADWIV 902
Cdd:cd03254 169 NIDTeteKLIQEALEKLMK----GRTSIIIAHRLSTIKNADKIL 208
hmuV PRK13547
heme ABC transporter ATP-binding protein;
823-924 6.87e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 45.59  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  823 LGQSATTLSGGEAQRVKLARELSK------RGTGQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLDV- 894
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLAQlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLa 218
                         90       100       110
                 ....*....|....*....|....*....|
gi 16131884  895 IKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13547 219 ARHADRIAML------ADGAIVAHGAPADV 242
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
783-892 7.32e-05

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 45.45  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  783 KTIHEVLDmtiEEAREFFDAVPA--LARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPT 860
Cdd:PRK10419 106 KTVREIIR---EPLRHLLSLDKAerLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALA---VEPKLLILDEAV 179
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16131884  861 TGLHFADIQQLLDVLHKLRDQGNT-IVVIEHNL 892
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDL 212
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
796-888 7.67e-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: 44.88  E-value: 7.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 796 AREFFDAVPAL---------ARKLQTLMDVGLtYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfa 866
Cdd:cd03264  89 VREFLDYIAWLkgipskevkARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD---PSILIVDEPTAGL--- 161
                        90       100
                ....*....|....*....|..
gi 16131884 867 DIQQLLDVLHKLRDQGNTIVVI 888
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVI 183
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
805-896 7.95e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 45.19  E-value: 7.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  805 ALARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGN 883
Cdd:PRK11629 122 INSRALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNN---PRLVLADEPTGNLDARNADSIFQLLGELnRLQGT 197
                         90
                 ....*....|...
gi 16131884  884 TIVVIEHNLDVIK 896
Cdd:PRK11629 198 AFLVVTHDLQLAK 210
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
806-901 8.30e-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: 8.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 806 LARKLQTLMDVGLT-----YIRlgqsatTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLH---FADIQQLLDVLHk 877
Cdd:cd03294 138 EERAAEALELVGLEgwehkYPD------ELSGGMQQRVGLARALA---VDPDILLMDEAFSALDpliRREMQDELLRLQ- 207
                        90       100
                ....*....|....*....|....*
gi 16131884 878 lRDQGNTIVVIEHNLD-VIKTADWI 901
Cdd:cd03294 208 -AELQKTIVFITHDLDeALRLGDRI 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
822-892 8.38e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 45.41  E-value: 8.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884  822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNL 892
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVK---PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
hmuV PRK13547
heme ABC transporter ATP-binding protein;
480-607 8.44e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 45.59  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIRLA---SQI---GAGLVGVMY-VLDEPSIGLHQRDNERLLGTLIHL-RDLGNTVIVVEHDED-A 550
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFArvlAQLwppHDAAQPPRYlLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNlA 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884  551 IRAADHVidigpgAGVHGGEVVAEGPLEAIMAvPESLTGQYMSGKRKIEVPKKRVPA 607
Cdd:PRK13547 219 ARHADRI------AMLADGAIVAHGAPADVLT-PAHIARCYGFAVRLVDAGDGVPPV 268
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
825-892 9.47e-05

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: 44.86  E-value: 9.47e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 825 QSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQgNTIVVIEHNL 892
Cdd:cd03260 137 LHALGLSGGQQQRLCLARALANE---PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNM 200
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-576 9.62e-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: 45.09  E-value: 9.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 480 LSRSAETLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrDNE-RLLGTLIHLRDLGN---TVIVVEHD---EDA 550
Cdd:cd03237 109 LDREVPELSGGELQRVAIAACLSkdADI----YLLDEPSAYL---DVEqRLMASKVIRRFAENnekTAFVVEHDiimIDY 181
                        90       100
                ....*....|....*....|....*.
gi 16131884 551 IraADHVIDIGPGAGVHGgevVAEGP 576
Cdd:cd03237 182 L--ADRLIVFEGEPSVNG---VANPP 202
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 16131884  822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHN 891
Cdd:PRK10584 139 RLDHLPAQLSGGEQQRVALARAFNGR---PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
cbiO PRK13637
energy-coupling factor transporter ATPase;
816-924 1.04e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 45.42  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  816 VGLTYIRL-GQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQ-GNTIVVIEHNL- 892
Cdd:PRK13637 130 VGLDYEDYkDKSPFELSGGQKRRVAIAGVVAME---PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMe 206
                         90       100       110
                 ....*....|....*....|....*....|..
gi 16131884  893 DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13637 207 DVAKLADRIIVM------NKGKCELQGTPREV 232
PLN03211 PLN03211
ABC transporter G-25; Provisional
816-890 1.11e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.03  E-value: 1.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884  816 VGLTYIRlgqsatTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEH 890
Cdd:PLN03211 199 IGNSFIR------GISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
623-902 1.13e-04

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 44.60  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqRQLNGatiaepapyrdiqgLEHFDK-VIDIDQSPIGRTPRSnp 701
Cdd:COG1126  17 LKGISLDVEKGEVVVIIGPSGSGKSTLL---------RCINL--------------LEEPDSgTITVDGEDLTDSKKD-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 702 atytgvftpVRELfagvpesRARgytpgrfsfnvrggrceacqgdgvikVEMHFlpdiyvpcdQckgkRYNretLeikYK 781
Cdd:COG1126  72 ---------INKL-------RRK--------------------------VGMVF---------Q----QFN---L---FP 90
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 782 GKTIHE--------VLDMTIEEAREffdavpaLARKLqtLMDVGLTYiRLGQSATTLSGGEAQRVKLARELS---Krgtg 850
Cdd:COG1126  91 HLTVLEnvtlapikVKKMSKAEAEE-------RAMEL--LERVGLAD-KADAYPAQLSGGQQQRVAIARALAmepK---- 156
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 851 qtlYIL-DEPTTGLhfaD---IQQLLDVLHKLRDQGNTIVVIEHNL----DViktADWIV 902
Cdd:COG1126 157 ---VMLfDEPTSAL---DpelVGEVLDVMRDLAKEGMTMVVVTHEMgfarEV---ADRVV 207
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
782-902 1.20e-04

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: 45.83  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 782 GKTIHEVL----DMTIEEAReffdavpalARKLQTLMDVGLT--YIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYI 855
Cdd:COG4172 112 GKQIAEVLrlhrGLSGAAAR---------ARALELLERVGIPdpERRLDAYPHQLSGGQRQRVMIAMALA---NEPDLLI 179
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131884 856 LDEPTTGLhfaD--IQ-QLLDVLHKL-RDQGNTIVVIEHNLDVI-KTADWIV 902
Cdd:COG4172 180 ADEPTTAL---DvtVQaQILDLLKDLqRELGMALLLITHDLGVVrRFADRVA 228
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
446-560 1.21e-04

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 44.40  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 446 LKLAGQRAKIAEKILKEIGDRlkflvnVGLNYLtLSRSAETLSGGEAQRIRLASqigaGLVG-VMYVL-DEPSIGLHQRD 523
Cdd:cd03255 107 LLLAGVPKKERRERAEELLER------VGLGDR-LNHYPSELSGGQQQRVAIAR----ALANdPKIILaDEPTGNLDSET 175
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16131884 524 NERLLGTLIHL-RDLGNTVIVVEHDEDAIRAADHVIDI 560
Cdd:cd03255 176 GKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIEL 213
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
783-902 1.54e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 45.34  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  783 KTIHEVL-----DMTIEEAREFFDAVPAL---ARKLQTLMDVgltyirLGQSATTLSGGEAQRVKLARELSKRGtgqTLY 854
Cdd:PRK13657 423 RSIEDNIrvgrpDATDEEMRAAAERAQAHdfiERKPDGYDTV------VGERGRQLSGGERQRLAIARALLKDP---PIL 493
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131884  855 ILDEPTTGLHF---ADIQQLLDVLHKlrdqGNTIVVIEHNLDVIKTADWIV 902
Cdd:PRK13657 494 ILDEATSALDVeteAKVKAALDELMK----GRTTFIIAHRLSTVRNADRIL 540
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
613-902 1.55e-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: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   613 LKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLIndtlfpiaqrqlngatiaepapyRDIQGLEHFDKV-IDIDqs 691
Cdd:TIGR02142   3 ARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLI-----------------------RLIAGLTRPDEGeIVLN-- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   692 piGRTPRSNPAtytGVFTPvrelfagvPESRARGYTpgrfsFNvrggrceacqgdgvikvEMHFLPDIYVpcdqckgkry 771
Cdd:TIGR02142  58 --GRTLFDSRK---GIFLP--------PEKRRIGYV-----FQ-----------------EARLFPHLSV---------- 92
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   772 nRETLEIKYKgktihevlDMTIEEAREFFDAVPALarklqtlmdVGLTYIrLGQSATTLSGGEAQRVKLARELSkrgTGQ 851
Cdd:TIGR02142  93 -RGNLRYGMK--------RARPSERRISFERVIEL---------LGIGHL-LGRLPGRLSGGEKQRVAIGRALL---SSP 150
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16131884   852 TLYILDEPTTGLHFADIQQLLDVLHKLRDQGNT-IVVIEHNLD-VIKTADWIV 902
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQeVLRLADRVV 203
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
823-902 1.60e-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: 45.09  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 823 LGQSATTLSGGEAQRVKLAREL--SKRgtgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGNT-IVVIEHNLD-VIKTA 898
Cdd:COG4148 127 LDRRPATLSGGERQRVAIGRALlsSPR-----LLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDeVARLA 201

                ....
gi 16131884 899 DWIV 902
Cdd:COG4148 202 DHVV 205
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
830-895 1.83e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 45.01  E-value: 1.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884  830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:PRK10938 136 LSTGETRKTLLCQALM---SEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEI 198
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
829-904 1.88e-04

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 42.91  E-value: 1.88e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884 829 TLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaDIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDL 904
Cdd:cd03223  91 VLSGGEQQRLAFARLLLHK---PKFVFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL 160
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
807-893 1.90e-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: 43.66  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 807 ARKLQTLMDVGLTyIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTI 885
Cdd:cd03259 109 ARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALARE---PSLLLLDEPLSALDAKLREELREELKELqRELGITT 184

                ....*...
gi 16131884 886 VVIEHNLD 893
Cdd:cd03259 185 IYVTHDQE 192
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
458-547 2.06e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 45.18  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  458 KILKEIGDRLKfLVNVglnyltLSRSAETLSGGEAQRIRLAsqigAGLV--GVMYVLDEPSIGLHQRdnERL-LGTLIhl 534
Cdd:PRK13409 191 GKLDEVVERLG-LENI------LDRDISELSGGELQRVAIA----AALLrdADFYFFDEPTSYLDIR--QRLnVARLI-- 255
                         90
                 ....*....|....*
gi 16131884  535 RDL--GNTVIVVEHD 547
Cdd:PRK13409 256 RELaeGKYVLVVEHD 270
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
623-672 2.39e-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: 2.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfPIA--------QRQLNGATIAEPAP 672
Cdd:cd03293  20 LEDISLSVEEGEFVALVGPSGCGKSTLLR----IIAglerptsgEVLVDGEPVTGPGP 73
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
804-901 2.53e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 44.66  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  804 PALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGN 883
Cdd:PRK15439 115 QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR---ILILDEPTASLTPAETERLFSRIRELLAQGV 191
                         90
                 ....*....|....*....
gi 16131884  884 TIVVIEHNL-DVIKTADWI 901
Cdd:PRK15439 192 GIVFISHKLpEIRQLADRI 210
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
445-575 2.77e-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: 43.25  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 445 NLKLAGQRAKIAEKILKEigdrlkflvnVGLNYLtLSRSAETLSGGEAQRIRLASQigagLV---GVMyVLDEP--SIGL 519
Cdd:cd03298  98 GLKLTAEDRQAIEVALAR----------VGLAGL-EKRLPGELSGGERQRVALARV----LVrdkPVL-LLDEPfaALDP 161
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884 520 HQRDNERLLGTLIHlRDLGNTVIVVEHD-EDAIRAADHVIDIgpgagvHGGEVVAEG 575
Cdd:cd03298 162 ALRAEMLDLVLDLH-AETKMTVLMVTHQpEDAKRLAQRVVFL------DNGRIAAQG 211
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-41 2.90e-04

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 43.22  E-value: 2.90e-04
                        10        20
                ....*....|....*....|....*...
gi 16131884  14 LKNINLVIPRDKLIVVTGLSGSGKSSLA 41
Cdd:cd03225  17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
805-924 2.95e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 43.44  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  805 ALARKLQTLMDVGLTYIrLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLH---FADIQQLLDvlhKLRDQ 881
Cdd:PRK11300 130 ALDRAATWLERVGLLEH-ANRQAGNLAYGQQRRLEIARCMV---TQPEILMLDEPAAGLNpkeTKELDELIA---ELRNE 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16131884  882 -GNTIVVIEHNLD-VIKTADWIVDLGPEGGsgggeiLVSGTPETV 924
Cdd:PRK11300 203 hNVTVLLIEHDMKlVMGISDRIYVVNQGTP------LANGTPEEI 241
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
486-564 2.96e-04

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 43.19  E-value: 2.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 486 TLSGGEAQRIRLAsqigAGLVG---VMyVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVIDIG 561
Cdd:COG4778 152 TFSGGEQQRVNIA----RGFIAdppLL-LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226

                ...
gi 16131884 562 PGA 564
Cdd:COG4778 227 PFS 229
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-547 3.05e-04

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: 43.51  E-value: 3.05e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884 480 LSRSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPS--IGLHQRDNerlLGTLIH-LRDLGNTVIVVEHD 547
Cdd:cd03236 133 LDRNIDQLSGGELQRVAIAAALARD--ADFYFFDEPSsyLDIKQRLN---AARLIReLAEDDNYVLVVEHD 198
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
777-896 3.27e-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: 42.90  E-value: 3.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 777 EIKYKGKTIhevLDMTIEE-ARE-FFDA------VPALarklqTLMDVgLTYIRLGqsattLSGGEAQRVKLARELSKRg 848
Cdd:cd03217  58 EILFKGEDI---TDLPPEErARLgIFLAfqyppeIPGV-----KNADF-LRYVNEG-----FSGGEKKRNEILQLLLLE- 122
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 16131884 849 tgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHN---LDVIK 896
Cdd:cd03217 123 --PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK 171
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
481-594 3.39e-04

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 43.33  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  481 SRSAETLSGGEAQRIrlasQIGAGLVGV--MYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDED-AIRAADHv 557
Cdd:PRK11614 132 IQRAGTMSGGEQQML----AIGRALMSQprLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADR- 206
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131884  558 idigpGAGVHGGEVVAEGPLEAIMAvPESLTGQYMSG 594
Cdd:PRK11614 207 -----GYVLENGHVVLEDTGDALLA-NEAVRSAYLGG 237
cbiO PRK13641
energy-coupling factor transporter ATPase;
794-899 3.55e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 43.66  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  794 EEAREffdavpalaRKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLD 873
Cdd:PRK13641 119 DEAKE---------KALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYE---PEILCLDEPAAGLDPEGRKEMMQ 186
                         90       100
                 ....*....|....*....|....*..
gi 16131884  874 VLHKLRDQGNTIVVIEHNL-DVIKTAD 899
Cdd:PRK13641 187 LFKDYQKAGHTVILVTHNMdDVAEYAD 213
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
830-895 3.61e-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: 3.61e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 830 LSGGEAQRVKLARELSKRGtgqTLYILDEPTTGLhfaDIQQLLDVLHKLR----DQGNTIVVIEHNLDVI 895
Cdd:cd03222  72 LSGGELQRVAIAAALLRNA---TFYLFDEPSAYL---DIEQRLNAARAIRrlseEGKKTALVVEHDLAVL 135
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
830-902 3.70e-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: 44.43  E-value: 3.70e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLhfaDIQQLLDVLHKLRD--QGNTIVVIEHNLDVIKTADWIV 902
Cdd:COG5265 495 LSGGEKQRVAIARTLLKN---PPILIFDEATSAL---DSRTERAIQAALREvaRGRTTLVIAHRLSTIVDADEIL 563
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
3-113 3.86e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.43  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884     3 KIEVRgARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQrryveslsayarqflSLMEKPDvdhiEGLSPA 82
Cdd:PRK00635 1496 TLSVS-LSIHTIQNLNVSAPLHSLVAISGVSGSGKTSLLLEGFYKQAC---------------ALIEKGP----SVFSEI 1555
                          90       100       110
                  ....*....|....*....|....*....|.
gi 16131884    83 ISIEQKSTSHNPRSTVGTITEIHDYLRLLFA 113
Cdd:PRK00635 1556 IFLDSHPQISSQRSDISTYFDIAPSLRNFYA 1586
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
788-892 4.36e-04

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 43.20  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  788 VLDMTIE-------EAREffdAVPALARKLqtLMDVGLT-----YIRlgqsatTLSGGEAQRVKLARELSKRgtgQTLYI 855
Cdd:PRK11264 102 VLENIIEgpvivkgEPKE---EATARAREL--LAKVGLAgketsYPR------RLSGGQQQRVAIARALAMR---PEVIL 167
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131884  856 LDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNL 892
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
830-902 4.42e-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: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884   830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLDVIKTADWIV 902
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMR---PDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVLADRVI 207
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
830-893 4.64e-04

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 42.65  E-value: 4.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKL-RDQGNTIVVIEHNLD 893
Cdd:PRK10771 130 LSGGQRQRVALARCLVRE---QPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLE 191
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
487-558 4.81e-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: 41.92  E-value: 4.81e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLI-HLRDlgNTVIVVEHDEDAIRAADHVI 558
Cdd:cd03247  99 FSGGERQRLALARILlqDAPIV----LLDEPTVGLDPITERQLLSLIFeVLKD--KTLIWITHHLTGIEHMDKIL 167
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
487-558 4.85e-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: 41.65  E-value: 4.85e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVI 558
Cdd:cd03216  83 LSVGERQMVEIARALarNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVT 153
cbiO PRK13643
energy-coupling factor transporter ATPase;
807-924 5.20e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.18  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLQTlmdVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIV 886
Cdd:PRK13643 125 AEKLEM---VGLADEFWEKSPFELSGGQMRRVAIAGILAME---PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVV 198
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16131884  887 VIEHNL-DVIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:PRK13643 199 LVTHLMdDVADYADYVYLL------EKGHIISCGTPSDV 231
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
482-584 5.43e-04

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 43.29  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  482 RSAETLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDED-AIRAADHVidi 560
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARAL-AQATPVL-LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDEL--- 209
                         90       100
                 ....*....|....*....|....
gi 16131884  561 gpgAGVHGGEVVAEGPLEAIMAVP 584
Cdd:PRK09536 210 ---VLLADGRVRAAGPPADVLTAD 230
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
807-894 5.53e-04

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 42.74  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLQTLMDVGLTYiRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLhkLRDQGN 883
Cdd:PRK11247 112 DAALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHR---PGLLLLDEPLGALDAltrIEMQDLIESL--WQQHGF 185
                         90
                 ....*....|.
gi 16131884  884 TIVVIEHnlDV 894
Cdd:PRK11247 186 TVLLVTH--DV 194
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
830-893 5.54e-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: 42.46  E-value: 5.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 830 LSGGEAQRVKLARELSKRgtGQTLyILDEPttglhFA--DIQ---QLLDVLHKL-RDQGNTIVVIEHNLD 893
Cdd:cd03293 132 LSGGMRQRVALARALAVD--PDVL-LLDEP-----FSalDALtreQLQEELLDIwRETGKTVLLVTHDID 193
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
829-902 5.59e-04

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 43.32  E-value: 5.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884  829 TLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNT-IVVIEHNLD-VIKTADWIV 902
Cdd:PRK11144 128 SLSGGEKQRVAIGRALL---TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDeILRLADRVV 200
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
793-904 5.62e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 43.52  E-value: 5.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 793 IEEAREFFDAVPALARKLQTLMDV-----------------GLTYIRLGQSATTLSGGEAQRVKLARELSKRGtgqTLYI 855
Cdd:COG0488  99 LEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilsglGFPEEDLDRPVSELSGGWRRRVALARALLSEP---DLLL 175
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131884 856 LDEPTTGLHFADIQQLLDVLHKLRdqgNTIVVIEHN---LDviKTADWIVDL 904
Cdd:COG0488 176 LDEPTNHLDLESIEWLEEFLKNYP---GTVLVVSHDryfLD--RVATRILEL 222
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
435-574 5.74e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  435 SIGHAMEFFNNL--KLAGQRAKIAEKILKEIGD--------------------RLKFLVNVGLNYLTLSRSAETLSGGEa 492
Cdd:PRK03918 715 KLEKALERVEELreKVKKYKALLKERALSKVGEiaseifeeltegkysgvrvkAEENKVKLFVVYQGKERPLTFLSGGE- 793
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  493 qRI------RLA-SQIGAGLVGVMyVLDEPSIGLhqrDNERL--LGTLI--HLRDLGNtVIVVEHDEDAIRAADHVIDIG 561
Cdd:PRK03918 794 -RIalglafRLAlSLYLAGNIPLL-ILDEPTPFL---DEERRrkLVDIMerYLRKIPQ-VIIVSHDEELKDAADYVIRVS 867
                        170
                 ....*....|...
gi 16131884  562 PGAGVHGGEVVAE 574
Cdd:PRK03918 868 LEGGVSKVEVVSL 880
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
470-902 6.04e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 43.62  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  470 LVNVGLNyLTLSRSAETLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDED 549
Cdd:PRK09700 130 LLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM--LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  550 AIRA-ADHVIDIGPGAGVHGGEVvAEGPLEAI--MAVPESLTGQYMSGKRKIEVPKKRVPAnpeKVLKLTGARGNNLKDV 626
Cdd:PRK09700 207 EIRRiCDRYTVMKDGSSVCSGMV-SDVSNDDIvrLMVGRELQNRFNAMKENVSNLAHETVF---EVRNVTSRDRKKVRDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  627 TLTLPVGLFTCITGVSGSGKSTLINdTLFPIAQRQ-----LNGATIaepapyrdiqglehfdkvididqspigrTPRSNp 701
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMN-CLFGVDKRAggeirLNGKDI----------------------------SPRSP- 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  702 atytgvFTPVRELFAGVPESR-ARGYTPGrFSfnvrggrceacqgdgvIKVEMHFLPDIYVPcdqckgkrynretleiKY 780
Cdd:PRK09700 333 ------LDAVKKGMAYITESRrDNGFFPN-FS----------------IAQNMAISRSLKDG----------------GY 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  781 KGK--TIHEVLDM-TIEEAREFfdavpaLARKLQTLmdvgltyirlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILD 857
Cdd:PRK09700 374 KGAmgLFHEVDEQrTAENQREL------LALKCHSV----------NQNITELSGGNQQKVLISKWLC---CCPEVIIFD 434
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 16131884  858 EPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNL-DVIKTADWIV 902
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIA 480
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
807-890 6.12e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 43.28  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLQTLMDVGLTYIRLGQSATT----LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQG 882
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARALI---NDPQLLILDEPTTGLDPHARHLIWERLRSLLARG 222

                 ....*...
gi 16131884  883 NTIVVIEH 890
Cdd:PRK13536 223 KTILLTTH 230
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
14-41 6.39e-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: 41.60  E-value: 6.39e-04
                        10        20
                ....*....|....*....|....*...
gi 16131884  14 LKNINLVIPRDKLIVVTGLSGSGKSSLA 41
Cdd:cd03228  18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
822-892 6.81e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 42.46  E-value: 6.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  822 RLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQgNTIVVIEHNL 892
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQ---PEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNM 210
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
830-891 7.57e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 42.90  E-value: 7.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGL--HFADIQQL--LDVLHKLrdqGNTIVVIEHN 891
Cdd:PRK11607 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALdkKLRDRMQLevVDILERV---GVTCVMVTHD 209
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
434-575 7.88e-04

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 42.11  E-value: 7.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 434 MSIGH----AMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLvnvglnyltlSRSAETLSGGEAQRIRLASQIGAG--LVg 507
Cdd:cd03257  99 MTIGEqiaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEVL----------NRYPHELSGGQRQRVAIARALALNpkLL- 167
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884 508 vmyVLDEPSIGLHQRDNERLLGTLIHLRD-LGNTVIVVEHDEDAIRA-ADHVIdigpgagV-HGGEVVAEG 575
Cdd:cd03257 168 ---IADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKiADRVA-------VmYAGKIVEEG 228
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
482-578 8.19e-04

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 42.18  E-value: 8.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  482 RSAETLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVIDI 560
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAIAQQ--GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMV 215
                         90
                 ....*....|....*...
gi 16131884  561 gpgagvhGGEVVAEGPLE 578
Cdd:PRK15056 216 -------KGTVLASGPTE 226
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
377-594 8.47e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 42.14  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  377 VLHNMERRYKETESSAVREELAKFISNRPCASCEGTRLRREARHVYVENTPLPAIS---DMSIGhaMEFFNNLKLAGQRA 453
Cdd:PRK14267  46 LLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPFPHLTiydNVAIG--VKLNGLVKSKKELD 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  454 KIAEKILK------EIGDRLKflvnvglNYltlsrsAETLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERL 527
Cdd:PRK14267 124 ERVEWALKkaalwdEVKDRLN-------DY------PSNLSGGQRQRLVIARAL--AMKPKILLMDEPTANIDPVGTAKI 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884  528 LGTLIHLRDLGNTVIVVEHDEDAIRAADHVidigpgAGVHGGEVVAEGPLEAIMAVPE-SLTGQYMSG 594
Cdd:PRK14267 189 EELLFELKKEYTIVLVTHSPAQAARVSDYV------AFLYLGKLIEVGPTRKVFENPEhELTEKYVTG 250
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
484-548 8.77e-04

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 43.12  E-value: 8.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884   484 AETLSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNERLLGTLIHLRDlGNTVIVVEHDE 548
Cdd:TIGR02868 469 GARLSGGERQRLALARALlaDAPIL----LLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
487-607 8.91e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 42.06  E-value: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  487 LSGGEAQRIRLASQIGAGLVGVMYvlDEPSIGlhqrDNERLLGTLIHLRD-----LGNTVIVVEHD-EDAIRAADHVIDI 560
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMF--DEPFVG----QDPITMGVLVKLISelnsaLGVTCVVVSHDvPEVLSIADHAYIV 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 16131884  561 GpgagvhGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPkKRVPA 607
Cdd:PRK11831 218 A------DKKIVAHGSAQALQANPDPRVRQFLDGIADGPVP-FRYPA 257
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
791-924 9.91e-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: 9.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 791 MTIEEAREffdAVPAL---------ARKLQTLMDVGLTYIRLGQS-ATTLSGGEAQRVKLARELSkrgTGQTLYILDEPT 860
Cdd:cd03295  90 MTVEENIA---LVPKLlkwpkekirERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALA---ADPPLLLMDEPF 163
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131884 861 TGL----------HFADIQQLLdvlhklrdqGNTIVVIEHNLD-VIKTADWIVDLgpeggsGGGEILVSGTPETV 924
Cdd:cd03295 164 GALdpitrdqlqeEFKRLQQEL---------GKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEI 223
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
487-558 1.02e-03

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 41.02  E-value: 1.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 487 LSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLHQRDNERLLGTLIHLRD-LGNTVIVVEHD-EDAIRAADHVI 558
Cdd:cd03229 101 LSGGQQQRVALARAL------AMdpdvLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVV 172
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
795-904 1.06e-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: 42.61  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   795 EAREFFDAVPA--LARKLQTLMDVgltyIRL---GQSATTLSGGEAQRVKLAREL-SKrgtgQTLYILDEPTTGLhfaDI 868
Cdd:TIGR03719 126 ELQEIIDAADAwdLDSQLEIAMDA----LRCppwDADVTKLSGGERRRVALCRLLlSK----PDMLLLDEPTNHL---DA 194
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 16131884   869 QQLLDVLHKLRDQGNTIVVIEHN---LDVIktADWIVDL 904
Cdd:TIGR03719 195 ESVAWLERHLQEYPGTVVAVTHDryfLDNV--AGWILEL 231
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
487-587 1.11e-03

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 42.44  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 487 LSGGEAQRI---R-LASQIGAGLvgvmyvLDEPSIGL--HQRDN-ERLLGTLihLRDLGNTVIVVEHD-EDAIRAADHVI 558
Cdd:COG1118 134 LSGGQRQRValaRaLAVEPEVLL------LDEPFGALdaKVRKElRRWLRRL--HDELGGTTVFVTHDqEEALELADRVV 205
                        90       100       110
                ....*....|....*....|....*....|
gi 16131884 559 digpgagV-HGGEVVAEGPLEAIMAVPESL 587
Cdd:COG1118 206 -------VmNQGRIEQVGTPDEVYDRPATP 228
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
828-897 1.16e-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: 41.55  E-value: 1.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884 828 TTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVV-IEHNLDVIKT 897
Cdd:cd03299 128 ETLSGGEQQRVAIARALV---VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWA 195
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
811-904 1.18e-03

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 42.49  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 811 QTLMDVGLTYI--RLGQSA---TTLSGGEAQRVKLARELskrgtgqtLY-----ILDEPTTGLhfaDIQQLLDVLHKLRD 880
Cdd:COG4178 462 EALEAVGLGHLaeRLDEEAdwdQVLSLGEQQRLAFARLL--------LHkpdwlFLDEATSAL---DEENEAALYQLLRE 530
                        90       100
                ....*....|....*....|....*.
gi 16131884 881 Q--GNTIVVIEHNLDVIKTADWIVDL 904
Cdd:COG4178 531 ElpGTTVISVGHRSTLAAFHDRVLEL 556
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
462-547 1.33e-03

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 42.46  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 462 EIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrD-NERLLGTLI---HLR 535
Cdd:COG1245 438 EIIKPL------GLEKL-LDKNVKDLSGGELQRVAIAACLSrdADL----YLLDEPSAHL---DvEQRLAVAKAirrFAE 503
                        90
                ....*....|..
gi 16131884 536 DLGNTVIVVEHD 547
Cdd:COG1245 504 NRGKTAMVVDHD 515
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
487-548 1.39e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 41.30  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131884  487 LSGGEAQRIRLASQIgAGLVGVMYVlDEPSIGLHQRDNERLLGTLIHL-RDLGNTVIVVEHDE 548
Cdd:PRK10584 147 LSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
PLN03232 PLN03232
ABC transporter C family member; Provisional
795-902 1.40e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 42.66  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   795 EAREFFDAVPALArkLQTLMDV--GLTYIRLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLL 872
Cdd:PLN03232  706 ESERYWRAIDVTA--LQHDLDLlpGRDLTEIGERGVNISGGQKQRVSMARAVY---SNSDIYIFDDPLSALDAHVAHQVF 780
                          90       100       110
                  ....*....|....*....|....*....|
gi 16131884   873 DVLHKLRDQGNTIVVIEHNLDVIKTADWIV 902
Cdd:PLN03232  781 DSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
623-691 1.85e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 40.71  E-value: 1.85e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGA-TIAEPAPYRDIQGLEHFDKVIDIDQS 691
Cdd:COG2401  46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCvDVPDNQFGREASLIDAIGRKGDFKDA 115
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
823-902 2.00e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 42.32  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   823 LGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIKTADWI 901
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLRE---PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDKI 1428

                  .
gi 16131884   902 V 902
Cdd:PTZ00265 1429 V 1429
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
486-677 2.02e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 41.64  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  486 TLSGGEAQRIRLASQIG--AGLVgvmyVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIgpg 563
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSynAKIV----IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITI--- 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  564 agVHGGEVVAEGPLEAI-------MAVPESLTGQYmsgKRKIEVPKKRVpanpEKVLKLTGARGNNLKDVTLTLPVGLFT 636
Cdd:PRK10982 207 --LRDGQWIATQPLAGLtmdkiiaMMVGRSLTQRF---PDKENKPGEVI----LEVRNLTSLRQPSIRDVSFDLHKGEIL 277
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16131884  637 CITGVSGSgKSTLINDTLFPIAQR-----QLNGATIAEPAPYRDIQ 677
Cdd:PRK10982 278 GIAGLVGA-KRTDIVETLFGIREKsagtiTLHGKKINNHNANEAIN 322
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
791-896 2.08e-03

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 41.23  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  791 MTI-----EEAREFFdavPALAR-----KLQTLMD-VGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEP 859
Cdd:PRK15079 115 MTIgeiiaEPLRTYH---PKLSRqevkdRVKAMMLkVGLLPNLINRYPHEFSGGQCQRIGIARALILE---PKLIICDEP 188
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16131884  860 TTGLHFAdIQ-QLLDVLHKL-RDQGNTIVVIEHNLDVIK 896
Cdd:PRK15079 189 VSALDVS-IQaQVVNLLQQLqREMGLSLIFIAHDLAVVK 226
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
829-895 2.16e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 41.64  E-value: 2.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131884  829 TLSGGEAQRVKLARELSKRGTgqtLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSYNAK---IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
14-41 2.21e-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: 2.21e-03
                        10        20
                ....*....|....*....|....*...
gi 16131884  14 LKNINLVIPRDKLIVVTGLSGSGKSSLA 41
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
830-895 2.23e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 41.82  E-value: 2.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884  830 LSGGEAQRVKLARELSKrgtGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:PRK11288 141 LSIGQRQMVEIAKALAR---NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEI 203
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
12-40 2.26e-03

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: 39.54  E-value: 2.26e-03
                        10        20
                ....*....|....*....|....*....
gi 16131884  12 HNLKNINLVIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd00267  13 TALDNVSLTLKAGEIVALVGPNGSGKSTL 41
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
6-51 2.41e-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: 39.65  E-value: 2.41e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16131884   6 VRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQR 51
Cdd:cd03227   3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
487-589 2.43e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 40.83  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  487 LSGGEAQRIRLASqIGAGLVGVMyVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRA-ADHVIDIGpgag 565
Cdd:PRK13639 138 LSGGQKKRVAIAG-ILAMKPEII-VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMS---- 211
                         90       100
                 ....*....|....*....|....
gi 16131884  566 vhGGEVVAEGPLEAIMAVPESLTG 589
Cdd:PRK13639 212 --DGKIIKEGTPKEVFSDIETIRK 233
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
6-40 2.65e-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: 40.63  E-value: 2.65e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 16131884   6 VRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd03256   9 TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTL 43
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
830-895 2.76e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 41.38  E-value: 2.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHF---ADIQQLLDVLHKLRDQGntIVVIEHNLDVI 895
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVV 232
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
830-898 2.85e-03

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 40.88  E-value: 2.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIKTA 898
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACR---PKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEA 220
PTZ00243 PTZ00243
ABC transporter; Provisional
14-40 3.18e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 41.69  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|....*..
gi 16131884    14 LKNINLVIPRDKLIVVTGLSGSGKSSL 40
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTL 702
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
830-902 3.20e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 40.36  E-value: 3.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884  830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIKTADWIV 902
Cdd:PRK13632 143 LSGGQKQRVAIASVLA---LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVI 213
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
434-578 3.24e-03

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 40.78  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  434 MSIGHAMEFfnNLKLAGQRAKIAEKILKEIGDRLKflvnvgLNYLtLSRSAETLSGGeaQRIRLAsqIGAGLVG--VMYV 511
Cdd:PRK11000  90 LSVAENMSF--GLKLAGAKKEEINQRVNQVAEVLQ------LAHL-LDRKPKALSGG--QRQRVA--IGRTLVAepSVFL 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  512 LDEPSIGLHQ--RDNERLLGTLIHLRdLGNTVIVVEHDE-DAIRAADHVIDIgpgagvHGGEVVAEG-PLE 578
Cdd:PRK11000 157 LDEPLSNLDAalRVQMRIEISRLHKR-LGRTMIYVTHDQvEAMTLADKIVVL------DAGRVAQVGkPLE 220
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-40 3.38e-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: 40.18  E-value: 3.38e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16131884   4 IEVRGART-----HNLKNINLVIPRDKLIVVTGLSGSGKSSL 40
Cdd:cd03261   1 IELRGLTKsfggrTVLKGVDLDVRRGEILAIIGPSGSGKSTL 42
cbiO PRK13642
energy-coupling factor transporter ATPase;
830-902 3.49e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 40.46  E-value: 3.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIKTADWIV 902
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALR---PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRIL 211
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
623-893 3.51e-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: 40.46  E-value: 3.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 623 LKDVTLTLPVGLFTCITGVSGSGKSTLINdtlfpiaqrqlngaTIAepapyrdiqGLEHFDK-VIDIDQSPIGRTPRS-- 699
Cdd:COG1116  27 LDDVSLTVAAGEFVALVGPSGCGKSTLLR--------------LIA---------GLEKPTSgEVLVDGKPVTGPGPDrg 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 700 ----NPATYtgvftP---VRElfagvpesrargytpgrfsfNVRggrceacqgdgvikvemhfLPdiyvpcdqckgkryn 772
Cdd:COG1116  84 vvfqEPALL-----PwltVLD--------------------NVA-------------------LG--------------- 104
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 773 retLEIKYKGKtihevldmtiEEAREffdavpaLARKLqtLMDVGLT-----YIRlgqsatTLSGGEAQRVKLARELSkr 847
Cdd:COG1116 105 ---LELRGVPK----------AERRE-------RAREL--LELVGLAgfedaYPH------QLSGGMRQRVAIARALA-- 154
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131884 848 gTGQTLYILDEPttglhFA--DIQ---QLLDVLHKL-RDQGNTIVVIEHNLD 893
Cdd:COG1116 155 -NDPEVLLMDEP-----FGalDALtreRLQDELLRLwQETGKTVLFVTHDVD 200
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
829-895 3.52e-03

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 40.48  E-value: 3.52e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131884 829 TLSGGEAQRVKLArelskrgtgQT------LYILDEPTTGLhfaD---IQQLLDVLHKLRDQGNTIVVIEHNLDVI 895
Cdd:COG4152 129 ELSKGNQQKVQLI---------AAllhdpeLLILDEPFSGL---DpvnVELLKDVIRELAAKGTTVIFSSHQMELV 192
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
822-892 3.53e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 40.46  E-value: 3.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  822 RLGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQgNTIVVIEHNL 892
Cdd:PRK14271 156 RLSDSPFRLSGGQQQLLCLARTLA---VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNL 222
PLN03130 PLN03130
ABC transporter C family member; Provisional
803-902 4.09e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 41.26  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   803 VPALARKLQTLMDVGLTYIrlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGL--HFAdiQQLLDVLHKLRD 880
Cdd:PLN03130  716 VTALQHDLDLLPGGDLTEI--GERGVNISGGQKQRVSMARAVY---SNSDVYIFDDPLSALdaHVG--RQVFDKCIKDEL 788
                          90       100
                  ....*....|....*....|..
gi 16131884   881 QGNTIVVIEHNLDVIKTADWIV 902
Cdd:PLN03130  789 RGKTRVLVTNQLHFLSQVDRII 810
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
480-578 4.10e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 39.97  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGN-TVIVVEHDEDAIRAADHVI 558
Cdd:PRK13632 136 LDKEPQNLSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVI 213
                         90       100
                 ....*....|....*....|.
gi 16131884  559 DIGpgagvhGGEVVAEG-PLE 578
Cdd:PRK13632 214 VFS------EGKLIAQGkPKE 228
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
807-896 4.28e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.84  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  807 ARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TI 885
Cdd:PRK15134 403 QQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILK---PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAY 479
                         90
                 ....*....|.
gi 16131884  886 VVIEHNLDVIK 896
Cdd:PRK15134 480 LFISHDLHVVR 490
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
790-871 4.68e-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: 39.26  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   790 DMTIEEAREFFDAVPALARK--LQTLMDVGLTYIRlGQSATTLSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFAD 867
Cdd:TIGR01189  87 ELSALENLHFWAAIHGGAQRtiEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWL---SRRPLWILDEPTTALDKAG 162

                  ....
gi 16131884   868 IQQL 871
Cdd:TIGR01189 163 VALL 166
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
14-41 4.80e-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: 38.40  E-value: 4.80e-03
                          10        20
                  ....*....|....*....|....*...
gi 16131884    14 LKNINLVIPRDKLIVVTGLSGSGKSSLA 41
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
455-563 4.98e-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: 38.20  E-value: 4.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 455 IAEKILKEIGDrLKFLVNVGLNYLtlsrsaETLSGGEAQRIRLASqigAGLVGV-MYVLDEPSIGLhqrDNERLLgTLI- 532
Cdd:cd03221  46 IAGELEPDEGI-VTWGSTVKIGYF------EQLSGGEKMRLALAK---LLLENPnLLLLDEPTNHL---DLESIE-ALEe 111
                        90       100       110
                ....*....|....*....|....*....|..
gi 16131884 533 HLRDLGNTVIVVEHDEDAIRA-ADHVIDIGPG 563
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
790-893 5.68e-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: 39.37  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884   790 DMTIEEAREFFDavpalarklQTLMDVGLTYI---RLGQsattLSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFA 866
Cdd:TIGR01184  85 DLSKSERRAIVE---------EHIALVGLTEAadkRPGQ----LSGGMKQRVAIARALSIR---PKVLLLDEPFGALDAL 148
                          90       100
                  ....*....|....*....|....*...
gi 16131884   867 DIQQLLDVLHKL-RDQGNTIVVIEHNLD 893
Cdd:TIGR01184 149 TRGNLQEELMQIwEEHRVTVLMVTHDVD 176
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
467-580 5.75e-03

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 39.47  E-value: 5.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 467 LKFLVNVGLNYLTLSRsAETLSGGEAQRI---RLASQ----IGAglvgvmyvlDEPSIGLHQRDNERLLGTLIHL-RDLG 538
Cdd:cd03256 126 LAALERVGLLDKAYQR-ADQLSGGQQQRVaiaRALMQqpklILA---------DEPVASLDPASSRQVMDLLKRInREEG 195
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 16131884 539 NTVIVVEHDEDAIRA-ADHVIdigpgaGVHGGEVVAEGPLEAI 580
Cdd:cd03256 196 ITVIVSLHQVDLAREyADRIV------GLKDGRIVFDGPPAEL 232
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
480-584 5.82e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 39.86  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  480 LSRSAETLSGGEAQRIrlasQIGAGLVGV--MYVLDEP--SIGLhQRDNErLLGTLIHLRDLGNTVIV-VEHDEDAI-RA 553
Cdd:PRK11144 122 LDRYPGSLSGGEKQRV----AIGRALLTApeLLLMDEPlaSLDL-PRKRE-LLPYLERLAREINIPILyVSHSLDEIlRL 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16131884  554 ADHVIDIgpgagvHGGEVVAEGPLEAIMAVP 584
Cdd:PRK11144 196 ADRVVVL------EQGKVKAFGPLEEVWASS 220
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
462-547 6.06e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 40.18  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  462 EIGDRLkflvnvGLNYLtLSRSAETLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrD-NERLLGTLI---HLR 535
Cdd:PRK13409 436 EIIKPL------QLERL-LDKNVKDLSGGELQRVAIAACLSrdADL----YLLDEPSAHL---DvEQRLAVAKAirrIAE 501
                         90
                 ....*....|..
gi 16131884  536 DLGNTVIVVEHD 547
Cdd:PRK13409 502 EREATALVVDHD 513
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
830-901 6.18e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 39.79  E-value: 6.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131884  830 LSGGEAQRVKLARELSKRGtgQTLyILDEPTTGLHFADIQQLLDVLHKLRDQ-GNTIVVIEHNLDVI-KTADWI 901
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEP--QVL-VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVpEMADYI 208
cbiO PRK13650
energy-coupling factor transporter ATPase;
830-899 6.90e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 39.33  E-value: 6.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884  830 LSGGEAQRVKLARELSKRgtgQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGN-TIVVIEHNLDVIKTAD 899
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMR---PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVALSD 208
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
481-569 7.48e-03

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: 38.80  E-value: 7.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 481 SRSAETLSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLhqrD--NERLLGTLI-HLRDLGNTVIVVEHD-EDAIRAA 554
Cdd:cd03269 123 NKRVEELSKGNQQKVQFIAAVihDPELL----ILDEPFSGL---DpvNVELLKDVIrELARAGKTVILSTHQmELVEELC 195
                        90
                ....*....|....*
gi 16131884 555 DHVIDIGPGAGVHGG 569
Cdd:cd03269 196 DRVLLLNKGRAVLYG 210
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
830-891 8.33e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 38.70  E-value: 8.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131884  830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHN 891
Cdd:PRK13539 128 LSAGQKRRVALARLLV---SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
485-578 8.37e-03

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: 38.66  E-value: 8.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 485 ETLSGGEAQRIRLAsQIgAGLVGVMYVLDEPSIGLhQRDNERLLGTLI-HLRDLGNTVIVVEHDEdaiRAADHVI-DIgp 562
Cdd:cd03217 103 EGFSGGEKKRNEIL-QL-LLLEPDLAILDEPDSGL-DIDALRLVAEVInKLREEGKSVLIITHYQ---RLLDYIKpDR-- 174
                        90
                ....*....|....*....
gi 16131884 563 gagVH---GGEVVAEGPLE 578
Cdd:cd03217 175 ---VHvlyDGRIVKSGDKE 190
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
830-897 8.75e-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: 8.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131884   830 LSGGEAQRVKLARELSkrgTGQTLYILDEPTTGLhfaDIQQLLDVLHKLRDQGNTIVVIEHN---LDVIKT 897
Cdd:TIGR03719 444 LSGGERNRVHLAKTLK---SGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHDrwfLDRIAT 508
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
4-40 8.90e-03

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: 38.81  E-value: 8.90e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 16131884   4 IEVR------GARTHnLKNINLVIPRDKLIVVTGLSGSGKSSL 40
Cdd:COG1127   6 IEVRnltksfGDRVV-LDGVSLDVPRGEILAIIGGSGSGKSVL 47
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
8-41 8.93e-03

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 39.62  E-value: 8.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 16131884    8 GARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLA 41
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
479-546 8.95e-03

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: 38.30  E-value: 8.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131884 479 TLSRSAE--TLSGGEaqRIRLAsqIGAGLV---GVMYvLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEH 546
Cdd:cd03213 102 TLMFAAKlrGLSGGE--RKRVS--IALELVsnpSLLF-LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
443-576 9.38e-03

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 38.50  E-value: 9.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884 443 FNNLKLAgqrAKIAEKILKEIGDRLKF-LVNVGLNYLtLSRSAETLSGGEAQRIRLASqigaGLVG--VMYVLDEPSIGL 519
Cdd:COG2884  97 YENVALP---LRVTGKSRKEIRRRVREvLDLVGLSDK-AKALPHELSGGEQQRVAIAR----ALVNrpELLLADEPTGNL 168
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131884 520 HQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADH-VIDIgpgagvHGGEVVAEGP 576
Cdd:COG2884 169 DPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKrVLEL------EDGRLVRDEA 220
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
438-547 9.57e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 38.64  E-value: 9.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131884  438 HAMEFFNNLKLAGQRAKIAEKILKEIGDR-LKFLVNVGLNYLTLSRSAEtLSGGEAQRIRLASqigaGLVG--VMYVLDE 514
Cdd:PRK11629  97 HLLPDFTALENVAMPLLIGKKKPAEINSRaLEMLAAVGLEHRANHRPSE-LSGGERQRVAIAR----ALVNnpRLVLADE 171
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16131884  515 PSIGLHQRDNE---RLLGTLIhlRDLGNTVIVVEHD 547
Cdd:PRK11629 172 PTGNLDARNADsifQLLGELN--RLQGTAFLVVTHD 205
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH