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Conserved domains on  [gi|487747191|ref|WP_001829332|]
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MULTISPECIES: excinuclease ABC subunit UvrA [Staphylococcus]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 1000295)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UvrA super family cl33793
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-752 0e+00

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


The actual alignment was detected with superfamily member COG0178:

Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 740.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   1 MDFINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYI-QFhLNQQPRPKVKKIKNL 79
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYArQF-LGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  80 PVAMTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPF----------------V----------------------- 120
Cdd:COG0178   82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHcpicgrpvekqtvdqiVdrilalpegtrlqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 121 -------------GYS-------------------------------------------DA------------------- 125
Cdd:COG0178  162 gehkelleelrkqGFVrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsrlaDSvetalklgdglvivevvde 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 126 --------------------------YSFNSPKGMCKTCEGLGYIEDINLDeLL--DWDKSLNEGAI---DFPSFGPDKE 174
Cdd:COG0178  242 geellfsekfacpdcgisfeeleprlFSFNSPYGACPTCDGLGRVLEFDPD-LVipDPSLSLAEGAIapwSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 175 R----GKAYRdsglFDNNKKLKDYTKDELELFLY----QEPMTLKNPPKEWRKSAKYVGLIPRFSRIFLG-DKEFNKKRY 245
Cdd:COG0178  321 LlealAKHYG----FDLDTPWKDLPEEQRDLILYgsdeKIKFRYKNRGRRRTYEKPFEGVIPFLERRYREtYSEHVREEL 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 246 AKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLEDPT-----AKYIIDPLKKQLEALEYI 320
Cdd:COG0178  397 SRYM----SETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEreaeiAERILKEIRSRLGFLVDV 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 321 GLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:COG0178  473 GLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRA 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 401 GDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHN--LKENIREAN-HFYNIGPVTQNNLNNVKTSIPKHV 476
Cdd:COG0178  553 ADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSlTGQYLSGRKRipVPKKRRKGNgKFLTIKGARENNLKNVDVEIPLGV 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 477 LTVLTGVAGSGKSTLV-----KA-------------------GFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSVRSYF 532
Cdd:COG0178  633 LTCVTGVSGSGKSTLVndilyPAlarklngakekpgphdsieGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELF 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 533 -----SKETGLNKAMFSYNSKGA-CPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNLTVDE 606
Cdd:COG0178  713 aqtpeAKARGYKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEE 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 607 GIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIK-NSIFIFDEPTTGLHESDIPILMECF 685
Cdd:COG0178  793 ALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTgKTLYILDEPTTGLHFHDIRKLLEVL 872
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 686 DDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIDSSETLTSKHLKRYIKQ 752
Cdd:COG0178  873 HRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLEA 939
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-752 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 740.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   1 MDFINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYI-QFhLNQQPRPKVKKIKNL 79
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYArQF-LGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  80 PVAMTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPF----------------V----------------------- 120
Cdd:COG0178   82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHcpicgrpvekqtvdqiVdrilalpegtrlqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 121 -------------GYS-------------------------------------------DA------------------- 125
Cdd:COG0178  162 gehkelleelrkqGFVrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsrlaDSvetalklgdglvivevvde 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 126 --------------------------YSFNSPKGMCKTCEGLGYIEDINLDeLL--DWDKSLNEGAI---DFPSFGPDKE 174
Cdd:COG0178  242 geellfsekfacpdcgisfeeleprlFSFNSPYGACPTCDGLGRVLEFDPD-LVipDPSLSLAEGAIapwSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 175 R----GKAYRdsglFDNNKKLKDYTKDELELFLY----QEPMTLKNPPKEWRKSAKYVGLIPRFSRIFLG-DKEFNKKRY 245
Cdd:COG0178  321 LlealAKHYG----FDLDTPWKDLPEEQRDLILYgsdeKIKFRYKNRGRRRTYEKPFEGVIPFLERRYREtYSEHVREEL 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 246 AKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLEDPT-----AKYIIDPLKKQLEALEYI 320
Cdd:COG0178  397 SRYM----SETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEreaeiAERILKEIRSRLGFLVDV 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 321 GLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:COG0178  473 GLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRA 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 401 GDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHN--LKENIREAN-HFYNIGPVTQNNLNNVKTSIPKHV 476
Cdd:COG0178  553 ADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSlTGQYLSGRKRipVPKKRRKGNgKFLTIKGARENNLKNVDVEIPLGV 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 477 LTVLTGVAGSGKSTLV-----KA-------------------GFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSVRSYF 532
Cdd:COG0178  633 LTCVTGVSGSGKSTLVndilyPAlarklngakekpgphdsieGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELF 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 533 -----SKETGLNKAMFSYNSKGA-CPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNLTVDE 606
Cdd:COG0178  713 aqtpeAKARGYKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEE 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 607 GIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIK-NSIFIFDEPTTGLHESDIPILMECF 685
Cdd:COG0178  793 ALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTgKTLYILDEPTTGLHFHDIRKLLEVL 872
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 686 DDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIDSSETLTSKHLKRYIKQ 752
Cdd:COG0178  873 HRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLEA 939
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-731 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: 626.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191    3 FINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYIQFHLNQQPRPKVKKIKNLPVA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   83 MTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPFV------------------------------------------ 120
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgef 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  121 ----------GYS------------------------------------------------------------------- 123
Cdd:TIGR00630 161 rklleklrkqGFArvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeev 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  124 --------------------------DAYSFNSPKGMCKTCEGLGYIEDINLDELLDWDKSLNEGAIDFPSfgpDKERGK 177
Cdd:TIGR00630 241 aeskeelfsekfacpecgfslpelepRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPF---KKSTTS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  178 AYRD--SGL-----FDNNKKLKDYTKDELELFLY-----QEPMTLKNPPKE-WRKSAKYVGLIPRFSRIFL-GDKEFNKK 243
Cdd:TIGR00630 318 YYRQmfASLaehlgFDLDTPWKDLPEEAQKAILYgsgeeVIVVKYRNGGGEtFRYHKPFEGVIPELERRYLeTESESMRE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  244 RYAKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLE-DPTAKYIIDP-LKKQLEALEY-- 319
Cdd:TIGR00630 398 YLEKFM----SERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTlTPEEKKIAEEvLKEIRERLGFli 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  320 -IGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVI 398
Cdd:TIGR00630 474 dVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  399 KEGDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHNLK--ENIREAN-HFYNIGPVTQNNLNNVKTSIPK 474
Cdd:TIGR00630 554 RAADYVIDIGPGAGEHGGEVVASGTPEEILANPDSlTGQYLSGRKKIEvpAERRPGNgKFLTLKGARENNLKNITVSIPL 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  475 HVLTVLTGVAGSGKSTLVK------------------------AGFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSVRS 530
Cdd:TIGR00630 634 GLFTCITGVSGSGKSTLINdtlypalanrlngaktvpgrytsiEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRE 713
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  531 YF-----SKETGLNKAMFSYNSK-GACPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNLTV 604
Cdd:TIGR00630 714 LFaetpeAKVRGYTPGRFSFNVKgGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTV 793
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  605 DEGIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKN-SIFIFDEPTTGLHESDIPILME 683
Cdd:TIGR00630 794 EEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKLLE 873
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*...
gi 487747191  684 CFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTP 731
Cdd:TIGR00630 874 VLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTP 921
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-752 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 615.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   1 MDFINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYI-QFhLNQQPRPKVKKIKNL 79
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYArQF-LGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  80 PVAMTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPFV--------------------------------------- 120
Cdd:PRK00349  82 SPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCpncgrpieaqtvsqmvdrvlelpegtrlqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 121 -------------GYSDA-------------------------------------------------------------- 125
Cdd:PRK00349 162 gehkkllenlrkqGFVRVrvdgevydldeppkldknkkhtievvvdrlvvkedirqrladsietalklsdglvvvevmdd 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 126 ----------------------------YSFNSPKGMCKTCEGLGYIEDINLDELL-DWDKSLNEGAIDfpsfgPDKERG 176
Cdd:PRK00349 242 peaeellfsekfacpvcgfsipeleprlFSFNSPYGACPTCDGLGVKLEFDPDLVVpDPELSLAEGAIA-----PWSRSS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 177 KAYRDSGL--------FDNNKKLKDYTKDELELFLY-----QEPMTLKNPPKEWRK-SAKYVGLIPRFSRIFL-GDKEFN 241
Cdd:PRK00349 317 SSYYFQMLkslaehygFDLDTPWKDLPEEVQDIILYgsgdeEIEFRYKNDRGRTRErKHPFEGVIPNLERRYReTESEYV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 242 KKRYAKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLE-DPTAKYIIDPLKKQLEA---- 316
Cdd:PRK00349 397 REELEKYM----SERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKlSEQEAKIAEPILKEIRErlkf 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 317 LEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPD 396
Cdd:PRK00349 473 LVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDED 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 397 VIKEGDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHNL---KENIREANHFYNIGPVTQNNLNNVKTSI 472
Cdd:PRK00349 553 TIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSlTGQYLSGKKKIevpKERRKGNGKFLKLKGARENNLKNVDVEI 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 473 PKHVLTVLTGVAGSGKSTLV-----KA-------------------GFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSV 528
Cdd:PRK00349 633 PLGKFTCVTGVSGSGKSTLInetlyKAlarklngakkvpgkhkeieGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPI 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 529 RSYF-----SKETGLNKAMFSYNSKGA-CPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNL 602
Cdd:PRK00349 713 RELFagtpeAKARGYKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDM 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 603 TVDEGIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDeeiK----NSIFIFDEPTTGLHESDI 678
Cdd:PRK00349 793 TVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELS---KrstgKTLYILDEPTTGLHFEDI 869
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191 679 PILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIDSSETLTSKHLKRYIKQ 752
Cdd:PRK00349 870 RKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-422 3.43e-77

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: 247.94  E-value: 3.43e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYIQFHLNQQPRPKVKKIKNLPVAM 83
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  84 TINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGepfvgysdaysfnspkgmcktceglgyiedinldelldwdkslnega 163
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG----------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 164 idfpsfgpdkergkayrdsglfdnnkklkdytkdelelflyqepmtlknppkewrksakyvgliprfsriflgdkefnkk 243
Cdd:cd03270      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 244 ryakhlknvvnnkicstckgqrlnskilsskimsknisdftqmtIKENLEFLNKledptakyiidplkkqlealeyIGLS 323
Cdd:cd03270  114 --------------------------------------------IRERLGFLVD----------------------VGLG 127
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 324 YLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDY 403
Cdd:cd03270  128 YLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADH 207
                        410
                 ....*....|....*....
gi 487747191 404 IIDMGPGSGKNGGEITFEG 422
Cdd:cd03270  208 VIDIGPGAGVHGGEIVAQG 226
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
315-407 5.64e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 56.47  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSSlSDLvYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD 394
Cdd:NF040873 102 DALERVGLADL-AGRQLGELSGGQRQRALLAQGLAQE-ADL-LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHD 178
                         90
                 ....*....|...
gi 487747191 395 PDVIKEGDYIIDM 407
Cdd:NF040873 179 LELVRRADPCVLL 191
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
260-362 1.36e-05

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: 45.72  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  260 TCKGQRLNSKILssKIMSKNISDFTQ-------MTIKENLEFLNKLEDPTAKYIIDPLKKQLEALEYIGLSYLTLNRVTT 332
Cdd:pfam00005  43 LLDGQDLTDDER--KSLRKEIGYVFQdpqlfprLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPG 120
                          90       100       110
                  ....*....|....*....|....*....|
gi 487747191  333 TLSGGEAQRLKLIRHLNSSlSDlVYIIDEP 362
Cdd:pfam00005 121 TLSGGQRQRVAIARALLTK-PK-LLLLDEP 148
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-752 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 740.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   1 MDFINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYI-QFhLNQQPRPKVKKIKNL 79
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYArQF-LGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  80 PVAMTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPF----------------V----------------------- 120
Cdd:COG0178   82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHcpicgrpvekqtvdqiVdrilalpegtrlqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 121 -------------GYS-------------------------------------------DA------------------- 125
Cdd:COG0178  162 gehkelleelrkqGFVrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsrlaDSvetalklgdglvivevvde 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 126 --------------------------YSFNSPKGMCKTCEGLGYIEDINLDeLL--DWDKSLNEGAI---DFPSFGPDKE 174
Cdd:COG0178  242 geellfsekfacpdcgisfeeleprlFSFNSPYGACPTCDGLGRVLEFDPD-LVipDPSLSLAEGAIapwSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 175 R----GKAYRdsglFDNNKKLKDYTKDELELFLY----QEPMTLKNPPKEWRKSAKYVGLIPRFSRIFLG-DKEFNKKRY 245
Cdd:COG0178  321 LlealAKHYG----FDLDTPWKDLPEEQRDLILYgsdeKIKFRYKNRGRRRTYEKPFEGVIPFLERRYREtYSEHVREEL 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 246 AKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLEDPT-----AKYIIDPLKKQLEALEYI 320
Cdd:COG0178  397 SRYM----SETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEreaeiAERILKEIRSRLGFLVDV 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 321 GLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:COG0178  473 GLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRA 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 401 GDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHN--LKENIREAN-HFYNIGPVTQNNLNNVKTSIPKHV 476
Cdd:COG0178  553 ADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSlTGQYLSGRKRipVPKKRRKGNgKFLTIKGARENNLKNVDVEIPLGV 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 477 LTVLTGVAGSGKSTLV-----KA-------------------GFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSVRSYF 532
Cdd:COG0178  633 LTCVTGVSGSGKSTLVndilyPAlarklngakekpgphdsieGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELF 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 533 -----SKETGLNKAMFSYNSKGA-CPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNLTVDE 606
Cdd:COG0178  713 aqtpeAKARGYKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEE 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 607 GIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIK-NSIFIFDEPTTGLHESDIPILMECF 685
Cdd:COG0178  793 ALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTgKTLYILDEPTTGLHFHDIRKLLEVL 872
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 686 DDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIDSSETLTSKHLKRYIKQ 752
Cdd:COG0178  873 HRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLEA 939
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-731 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: 626.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191    3 FINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYIQFHLNQQPRPKVKKIKNLPVA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   83 MTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPFV------------------------------------------ 120
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgef 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  121 ----------GYS------------------------------------------------------------------- 123
Cdd:TIGR00630 161 rklleklrkqGFArvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeev 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  124 --------------------------DAYSFNSPKGMCKTCEGLGYIEDINLDELLDWDKSLNEGAIDFPSfgpDKERGK 177
Cdd:TIGR00630 241 aeskeelfsekfacpecgfslpelepRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPF---KKSTTS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  178 AYRD--SGL-----FDNNKKLKDYTKDELELFLY-----QEPMTLKNPPKE-WRKSAKYVGLIPRFSRIFL-GDKEFNKK 243
Cdd:TIGR00630 318 YYRQmfASLaehlgFDLDTPWKDLPEEAQKAILYgsgeeVIVVKYRNGGGEtFRYHKPFEGVIPELERRYLeTESESMRE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  244 RYAKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLE-DPTAKYIIDP-LKKQLEALEY-- 319
Cdd:TIGR00630 398 YLEKFM----SERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTlTPEEKKIAEEvLKEIRERLGFli 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  320 -IGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVI 398
Cdd:TIGR00630 474 dVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  399 KEGDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHNLK--ENIREAN-HFYNIGPVTQNNLNNVKTSIPK 474
Cdd:TIGR00630 554 RAADYVIDIGPGAGEHGGEVVASGTPEEILANPDSlTGQYLSGRKKIEvpAERRPGNgKFLTLKGARENNLKNITVSIPL 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  475 HVLTVLTGVAGSGKSTLVK------------------------AGFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSVRS 530
Cdd:TIGR00630 634 GLFTCITGVSGSGKSTLINdtlypalanrlngaktvpgrytsiEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRE 713
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  531 YF-----SKETGLNKAMFSYNSK-GACPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNLTV 604
Cdd:TIGR00630 714 LFaetpeAKVRGYTPGRFSFNVKgGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTV 793
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  605 DEGIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKN-SIFIFDEPTTGLHESDIPILME 683
Cdd:TIGR00630 794 EEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKLLE 873
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*...
gi 487747191  684 CFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTP 731
Cdd:TIGR00630 874 VLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTP 921
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-752 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 615.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   1 MDFINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYI-QFhLNQQPRPKVKKIKNL 79
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYArQF-LGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  80 PVAMTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPFV--------------------------------------- 120
Cdd:PRK00349  82 SPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCpncgrpieaqtvsqmvdrvlelpegtrlqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 121 -------------GYSDA-------------------------------------------------------------- 125
Cdd:PRK00349 162 gehkkllenlrkqGFVRVrvdgevydldeppkldknkkhtievvvdrlvvkedirqrladsietalklsdglvvvevmdd 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 126 ----------------------------YSFNSPKGMCKTCEGLGYIEDINLDELL-DWDKSLNEGAIDfpsfgPDKERG 176
Cdd:PRK00349 242 peaeellfsekfacpvcgfsipeleprlFSFNSPYGACPTCDGLGVKLEFDPDLVVpDPELSLAEGAIA-----PWSRSS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 177 KAYRDSGL--------FDNNKKLKDYTKDELELFLY-----QEPMTLKNPPKEWRK-SAKYVGLIPRFSRIFL-GDKEFN 241
Cdd:PRK00349 317 SSYYFQMLkslaehygFDLDTPWKDLPEEVQDIILYgsgdeEIEFRYKNDRGRTRErKHPFEGVIPNLERRYReTESEYV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 242 KKRYAKHLknvvNNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKLE-DPTAKYIIDPLKKQLEA---- 316
Cdd:PRK00349 397 REELEKYM----SERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKlSEQEAKIAEPILKEIRErlkf 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 317 LEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPD 396
Cdd:PRK00349 473 LVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDED 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 397 VIKEGDYIIDMGPGSGKNGGEITFEGTYNELLSSNTS-TGNALRNKHNL---KENIREANHFYNIGPVTQNNLNNVKTSI 472
Cdd:PRK00349 553 TIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSlTGQYLSGKKKIevpKERRKGNGKFLKLKGARENNLKNVDVEI 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 473 PKHVLTVLTGVAGSGKSTLV-----KA-------------------GFENNDHTIFIDQKAVQGSNRSNLLTYLGVFDSV 528
Cdd:PRK00349 633 PLGKFTCVTGVSGSGKSTLInetlyKAlarklngakkvpgkhkeieGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPI 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 529 RSYF-----SKETGLNKAMFSYNSKGA-CPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNL 602
Cdd:PRK00349 713 RELFagtpeAKARGYKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDM 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 603 TVDEGIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDeeiK----NSIFIFDEPTTGLHESDI 678
Cdd:PRK00349 793 TVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELS---KrstgKTLYILDEPTTGLHFEDI 869
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191 679 PILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIDSSETLTSKHLKRYIKQ 752
Cdd:PRK00349 870 RKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-752 8.83e-121

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 398.82  E-value: 8.83e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191    4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYIQFHLNQQPRPKVKKIKNLPVAM 83
Cdd:PRK00635    6 VRLSGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEGLSPTI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   84 TINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGE--------PFVGYS-------------------------------- 123
Cdd:PRK00635   86 AVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQardpvtlhPLTLYSkekilstiaaipdgtqitllaplpakdilair 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191      --------------------------------------------------------------------------------
Cdd:PRK00635  166 eclrqgftkvridgeispiykfltsgipedvpvdivvdtliknesntarlkvslftaldighgecslhfdnqkrtfstqa 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  124 --------------DAYSFNSPKGMCKTCEGLGYIEDINLDELLDWDKSLNEGAIDFP---SFGPDKERGKAYRDSGLFD 186
Cdd:PRK00635  246 tipetqqtytpltpQLFSPHSLEDRCPQCQGSGIFISIDDPSLIQQNLSIEENCCPFAgncSTYLYHTIYQSLADSLGFS 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  187 NNKKLKDYTKDELELFLYQE-----PMTLKNPP--------KEWRKSAKYVGLIPRFSriflgdkefNKKryAKHLKNVV 253
Cdd:PRK00635  326 LSTPWKDLSPEIQNIFLYGKeglvlPVRLFDGTlgkktlthKVWRGVLNEIGEKVRYS---------NKP--SRYLPKGT 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  254 NNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKL--EDPTAKYIIDPLKKQLEALEYIGLSYLTLNRVT 331
Cdd:PRK00635  395 SATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLpsKSLSIEEVLQGLKSRLSILIDLGLPYLTPERAL 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  332 TTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDMGPGS 411
Cdd:PRK00635  475 ATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGA 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  412 GKNGGEITFEGTYNELL-SSNTSTGNALRNKHNLKENIREANHFYNI--GPVTQNNLNNVKTSIPKHVLTVLTGVAGSGK 488
Cdd:PRK00635  555 GIFGGEVLFNGSPREFLaKSDSLTAKYLRQELTIPIPEKRTNSLGTLtlSKATKHNLKDLTISLPLGRLTVVTGVSGSGK 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  489 STLV------------KAGFENNDH--------TIFIDQKAVQGSNRSNLLTYLGVFDSVRSYF-----SKETGLNKAMF 543
Cdd:PRK00635  635 SSLIndtlvpaveefiEQGFCSNLSiqwgaisrLVHITRDLPGRSQRSIPLTYIKAFDDLRELFaeqprSKRLGLTKSHF 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  544 SYN-SKGACPNCGGKGYIKTElafMGDFSQTCEVCHGKRYKQEVLDATIDGYSIADVLNLTVDEGIIFFDKKNDIKSKLQ 622
Cdd:PRK00635  715 SFNtPLGACAECQGLGSITTT---DNRTSIPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLDEPSIHEKIH 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  623 SVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKN-SIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHN 701
Cdd:PRK00635  792 ALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN 871
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|.
gi 487747191  702 LSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIdSSETLTSKHLKRYIKQ 752
Cdd:PRK00635  872 MHVVKVADYVLELGPEGGNLGGYLLASCSPEELI-HLHTPTAKALRPYLSS 921
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-748 5.83e-85

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 295.20  E-value: 5.83e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191    4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYI-QFHLNQQPRPKVKKIKNLPVA 82
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIrQALIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   83 MTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEP---------------------FVGYSDAY-SFNSP-------KG 133
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPysplsgdalrkitpqtiaeelLTHYTKGYvTITSPipkeedlFI 1100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  134 MCKTCEGLGYIEDINLDELLDWDKSLNEGAIDfP---------------------------------------------- 167
Cdd:PRK00635 1101 YLQEKLKEGFLKLYANEQFYDLDEPLPTSLEN-Paiviqhtkiseknlssllssltlafslsssiclhieyagtslslty 1179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  168 ------SFG---PDKERGKAYRD-----------SG------LFDNNKKLKDYTKDEL-ELFLYQEPMT--------LKN 212
Cdd:PRK00635 1180 rlgwqdSSGnlyPNITTPLLSRDheeglcplchgKGfilkcsLLPHKEKIAHYTPLSLfTLFFPNQDPKpvypllkeLGI 1259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  213 PPKEWRKSAKyvglIPRFSRIFLGDKEF-----------NKKRYAKHLKNVVNNKICSTCKGQRLNSKILSSKIMSKNIS 281
Cdd:PRK00635 1260 PSIALFQELD----TLSFESLCLGTQQHpglnallmeamLMESEEPLPPPLISKTPCNQCQGLGVYTYAHCVRIHNTSLS 1335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  282 DFTQMTIKENLEFLNKLEDPTAKYIIDPLKKQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDE 361
Cdd:PRK00635 1336 DIYQEDVTFLKKFLLTIHDDEEPSIIQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLED 1415
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  362 PSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDMGPGSGKNGGEITfegTYNELLSSNTSTGNALRNK 441
Cdd:PRK00635 1416 PLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGGYLL---STSALKQSQPDLHNTRSSE 1492
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  442 HNLKENIReanhfynigpVTQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVKAGF--------ENNDHT----IFIDQKA 509
Cdd:PRK00635 1493 ETPTLSVS----------LSIHTIQNLNVSAPLHSLVAISGVSGSGKTSLLLEGFykqacaliEKGPSVfseiIFLDSHP 1562
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  510 VQGSNRSNLLTYLGVFDSVRSYFSKET---GLN--KAMFSYNSK-GACPNCGGKGYIKTELAFMGDFSQTCEVCHGKRYK 583
Cdd:PRK00635 1563 QISSQRSDISTYFDIAPSLRNFYASLTqakALNisASMFSTNTKqGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQ 1642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  584 QEVLDATIDGYSIADVLNLTVDEGIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKN-S 662
Cdd:PRK00635 1643 PLAQEVVYEGKHFGQLLQTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHpT 1722
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  663 IFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTPKNFIDSSETLT 742
Cdd:PRK00635 1723 LFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLL 1802

                  ....*.
gi 487747191  743 SKHLKR 748
Cdd:PRK00635 1803 KTYMCN 1808
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-422 3.43e-77

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: 247.94  E-value: 3.43e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYIQFHLNQQPRPKVKKIKNLPVAM 83
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  84 TINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGepfvgysdaysfnspkgmcktceglgyiedinldelldwdkslnega 163
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG----------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 164 idfpsfgpdkergkayrdsglfdnnkklkdytkdelelflyqepmtlknppkewrksakyvgliprfsriflgdkefnkk 243
Cdd:cd03270      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 244 ryakhlknvvnnkicstckgqrlnskilsskimsknisdftqmtIKENLEFLNKledptakyiidplkkqlealeyIGLS 323
Cdd:cd03270  114 --------------------------------------------IRERLGFLVD----------------------VGLG 127
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 324 YLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDY 403
Cdd:cd03270  128 YLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADH 207
                        410
                 ....*....|....*....
gi 487747191 404 IIDMGPGSGKNGGEITFEG 422
Cdd:cd03270  208 VIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
460-731 1.75e-75

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: 244.83  E-value: 1.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 460 VTQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVK------------------------AGFENNDHTIFIDQKAVQGSNR 515
Cdd:cd03271    6 ARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrlhlkkeqpgnhdriEGLEHIDKVIVIDQSPIGRTPR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 516 SNLLTYLGVFDSVRSYFsketglnkamfsynskgacpncggkgyiktelafmgdfsqtCEVCHGKRYKQEVLDATIDGYS 595
Cdd:cd03271   86 SNPATYTGVFDEIRELF-----------------------------------------CEVCKGKRYNRETLEVRYKGKS 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 596 IADVLNLTVDEGIIFFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDE-EIKNSIFIFDEPTTGLH 674
Cdd:cd03271  125 IADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKrSTGKTLYILDEPTTGLH 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 675 ESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSGTP 731
Cdd:cd03271  205 FHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
455-729 6.82e-60

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: 199.86  E-value: 6.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 455 YNIGPVTQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVKAGFenndhtifidqkavqgsnrsnlltylgvfdsvrsYFSK 534
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------------------------------YASG 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 535 ETGLNKAM--FSYNSkgacpncggkgyiktelafmgdfsqtcevchgkrykqevldatidgysiadvlnltvdegIIFFD 612
Cdd:cd03238   47 KARLISFLpkFSRNK------------------------------------------------------------LIFID 66
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KkndikskLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQN 692
Cdd:cd03238   67 Q-------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLG 139
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 487747191 693 NTVILIEHNLSIMCEADWIIDVGPGPGLDGGKVQFSG 729
Cdd:cd03238  140 NTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-427 1.56e-56

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: 208.33  E-value: 1.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191    3 FINITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNesyssyiQFHLNQQPRPKVKKIKNLPVA 82
Cdd:TIGR00630 613 FLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRLN-------GAKTVPGRYTSIEGLEHLDKV 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   83 MTINQKRFNGNSRSTVGTVSDIYASVRLLWSRIGEPFV-GYSDA-YSFNSPKGMCKTCEGLGYI--EDinldelldwdks 158
Cdd:TIGR00630 686 IHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPEAKVrGYTPGrFSFNVKGGRCEACQGDGVIkiEM------------ 753
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  159 lnegaidfpSFGPDkergkayrdsglfdnnkklkdytkdelelfLYqepmtlknppkewrksakyvglIPrfsriflgdk 238
Cdd:TIGR00630 754 ---------HFLPD------------------------------VY----------------------VP---------- 762
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  239 efnkkryakhlknvvnnkiCSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKledptakyiIDPLKKQLEALE 318
Cdd:TIGR00630 763 -------------------CEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFFEA---------VPSISRKLQTLC 814
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  319 YIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNS-SLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDV 397
Cdd:TIGR00630 815 DVGLGYIRLGQPATTLSGGEAQRIKLAKELSKrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDV 894
                         410       420       430
                  ....*....|....*....|....*....|
gi 487747191  398 IKEGDYIIDMGPGSGKNGGEITFEGTYNEL 427
Cdd:TIGR00630 895 IKTADYIIDLGPEGGDGGGTVVASGTPEEV 924
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
4-423 3.45e-51

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 179.35  E-value: 3.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLnesyssyiqfHLNQQPRPKVKKIknlpvam 83
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRL----------HLKKEQPGNHDRI------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  84 tinqkrfngnsrstvgtvsdiyasvrllwsrigepfvgysdaysfnspkgmcktcEGLGYIedinlDELLDWDKSLnega 163
Cdd:cd03271   64 -------------------------------------------------------EGLEHI-----DKVIVIDQSP---- 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 164 IdfpsfgpdkerGKAYRdsglfdnnkklkdytkdelelflyqepmtlKNPpkewrksAKYVGLiprfsriflgdkeFNKK 243
Cdd:cd03271   80 I-----------GRTPR------------------------------SNP-------ATYTGV-------------FDEI 98
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 244 RyakhlknvvnNKICSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLNKledptakyiIDPLKKQLEALEYIGLS 323
Cdd:cd03271   99 R----------ELFCEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFEN---------IPKIARKLQTLCDVGLG 159
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 324 YLTLNRVTTTLSGGEAQRLKLIRHL-NSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGD 402
Cdd:cd03271  160 YIKLGQPATTLSGGEAQRIKLAKELsKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCAD 239
                        410       420
                 ....*....|....*....|.
gi 487747191 403 YIIDMGPGSGKNGGEITFEGT 423
Cdd:cd03271  240 WIIDLGPEGGDGGGQVVASGT 260
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-752 1.23e-46

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 180.02  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191    4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSYIQFHLNQQPRpKVKKIKNLPvam 83
Cdd:PRK00635  601 LTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQGFCSNLSIQWGAISR-LVHITRDLP--- 676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   84 tinqkrfnGNS-RSTVGTVSDIYASVRLLWSRigEP---FVGYSDA-YSFNSPKGMCKTCEGLGYIEdinldelldwdks 158
Cdd:PRK00635  677 --------GRSqRSIPLTYIKAFDDLRELFAE--QPrskRLGLTKShFSFNTPLGACAECQGLGSIT------------- 733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  159 lnegaidfpsfgpdkergkayrdsgLFDNNKklkdytkdelelflyqepmtlknppkewrksakyvgLIPrfsriflgdk 238
Cdd:PRK00635  734 -------------------------TTDNRT------------------------------------SIP---------- 742
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  239 efnkkryakhlknvvnnkiCSTCKGQRLNSKILSSKIMSKNISDFTQMTIKENLEFLnkLEDPTakyiidpLKKQLEALE 318
Cdd:PRK00635  743 -------------------CPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF--LDEPS-------IHEKIHALC 794
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  319 YIGLSYLTLNRVTTTLSGGEAQRLKLIRHL-NSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDV 397
Cdd:PRK00635  795 SLGLDYLPLGRPLSSLSGGEIQRLKLAYELlAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV 874
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  398 IKEGDYIIDMGPGSGKNGGEITFEGTYNELLSSNTSTGNALR-----------------NKHNLKE-NIREANHfynigp 459
Cdd:PRK00635  875 VKVADYVLELGPEGGNLGGYLLASCSPEELIHLHTPTAKALRpylsspqelpylpdpspKPPVPADiTIKNAYQ------ 948
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  460 vtqNNLNNVKTSIPKHVLTVLTGVAGSGKSTLV----------------------------------------------K 493
Cdd:PRK00635  949 ---HNLKHIDLSLPRNALTAVTGPSASGKHSLVfdilyaagniayaelfppyirqalikktplpsvdkvtglspviaieK 1025
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  494 AGFENN-----------------------------------------------------------------DHTIFIDQK 508
Cdd:PRK00635 1026 TSASKNsnhsvasaleisngleklfarlghpysplsgdalrkitpqtiaeellthytkgyvtitspipkeeDLFIYLQEK 1105
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  509 AVQG-----------------------------------SNRSNLL--------------------------TY-LGVFD 526
Cdd:PRK00635 1106 LKEGflklyaneqfydldeplptslenpaiviqhtkiseKNLSSLLssltlafslsssiclhieyagtslslTYrLGWQD 1185
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  527 SV-RSYFSKETglnKAMFSYNSKGACPNCGGKGYI--------------KTELAFMGDF--------------------- 570
Cdd:PRK00635 1186 SSgNLYPNITT---PLLSRDHEEGLCPLCHGKGFIlkcsllphkekiahYTPLSLFTLFfpnqdpkpvypllkelgipsi 1262
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  571 ----------------------------------------------SQTCEVCHG---KRYKQEVldaTIDGYSIADVLN 601
Cdd:PRK00635 1263 alfqeldtlsfeslclgtqqhpglnallmeamlmeseeplppplisKTPCNQCQGlgvYTYAHCV---RIHNTSLSDIYQ 1339
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  602 LTVD-----EGIIFFDKKNDIKSKLQS----VSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKNSIFIFDEPTTG 672
Cdd:PRK00635 1340 EDVTflkkfLLTIHDDEEPSIIQDLLNrltfIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSG 1419
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  673 LHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPGPGLDGGkvqFSGTPKNFIDSSETLTSKHLKRYIKQ 752
Cdd:PRK00635 1420 LHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGG---YLLSTSALKQSQPDLHNTRSSEETPT 1496
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
312-422 5.06e-40

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: 145.16  E-value: 5.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 312 KQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIV 391
Cdd:cd03238   66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                         90       100       110
                 ....*....|....*....|....*....|.
gi 487747191 392 EHDPDVIKEGDYIIDMGPGSGKNGGEITFEG 422
Cdd:cd03238  146 EHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
461-729 2.07e-35

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: 133.92  E-value: 2.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 461 TQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVkagFEnndhTIFID-QKAVQGSNRSNLLTYLGVFDsvRSYFSKETGLN 539
Cdd:cd03270    7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLA---FD----TIYAEgQRRYVESLSAYARQFLGQMD--KPDVDSIEGLS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 540 KAMfSYNSKGACPNCGGKGYIKTElafmgdfsqtcevchgkrykqevldatidgysIADVLNLtvdegiIFfdKKNDIKS 619
Cdd:cd03270   78 PAI-AIDQKTTSRNPRSTVGTVTE--------------------------------IYDYLRL------LF--ARVGIRE 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 620 KLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIE 699
Cdd:cd03270  117 RLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
                        250       260       270
                 ....*....|....*....|....*....|
gi 487747191 700 HNLSIMCEADWIIDVGPGPGLDGGKVQFSG 729
Cdd:cd03270  197 HDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
461-746 7.72e-25

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: 110.87  E-value: 7.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  461 TQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLvkaGFE----------------------------NNDH------TIFID 506
Cdd:TIGR00630   8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL---AFDtiyaegqrryveslsayarqflgvmdkpDVDSieglspAISID 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  507 QKAVQGSNRSNLLTYLGVFDSVRSYFSK---------------------------------------------------- 534
Cdd:TIGR00630  85 QKTTSHNPRSTVGTITEIYDYLRLLFARvgtpycptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgefrkll 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  535 -------------------------------------------------------ETGLNKA------------------ 541
Cdd:TIGR00630 165 eklrkqgfarvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvETALRLGdgllevefdddeevaesk 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  542 -----------------------MFSYNS-KGACPNCGGKGYIK----------TELAFMGD----------------FS 571
Cdd:TIGR00630 245 eelfsekfacpecgfslpeleprLFSFNSpYGACPECSGLGIKQefdpeliipdPLLSLNGGaivpfkksttsyyrqmFA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  572 QTCE--------------------VCHGK--------------------------------RYKQE-------------- 585
Cdd:TIGR00630 325 SLAEhlgfdldtpwkdlpeeaqkaILYGSgeevivvkyrngggetfryhkpfegvipelerRYLETesesmreylekfms 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  586 ---------------VLDATIDGYSIADVLNLTVDEGIIFFDKKN--------------DIKSKLQSVSKTGLNYMSLGQ 636
Cdd:TIGR00630 405 erpcpscggtrlkpeALAVTVGGKSIADVSELSIREAHEFFNQLTltpeekkiaeevlkEIRERLGFLIDVGLDYLSLSR 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  637 PLSTLSGGEIQRVKLGQHLDEEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGP 716
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGP 564
                         570       580       590
                  ....*....|....*....|....*....|
gi 487747191  717 GPGLDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:TIGR00630 565 GAGEHGGEVVASGTPEEILANPDSLTGQYL 594
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
286-410 3.01e-17

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 81.02  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEFLNKLedptAKYIIDPlKKQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVG 365
Cdd:COG4619   88 GTVRDNLPFPFQL----RERKFDR-ERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL--LLQPDVLLLDEPTSA 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 487747191 366 LHPEDIAKINEILKSL-KEKGNTVLIVEHDPDVIKE-GDYIIDMGPG 410
Cdd:COG4619  161 LDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
287-407 4.35e-16

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 77.66  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  287 TIKENLEFLNKLEDPTAKyiiDPLKKQLEALEYIGLsYLTLNRVTTTLSGGEAQRLKLIRHLnssLSDLVYII-DEPSVG 365
Cdd:TIGR03608  92 TVEENLDLGLKYKKLSKK---EKREKKKEALEKVGL-NLKLKQKIYELSGGEQQRVALARAI---LKPPPLILaDEPTGS 164
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 487747191  366 LHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDM 407
Cdd:TIGR03608 165 LDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
334-410 1.48e-15

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: 74.59  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHL--NSSLsdlvYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMGPG 410
Cdd:cd00267   81 LSGGQRQRVALARALllNPDL----LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDG 156
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
465-712 6.54e-15

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 74.04  E-value: 6.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 465 LNNVKTSIPKHVLTVLTGVAGSGKSTLVK--AGFEN-NDHTIFIDQKAVQGSNRSNLLTYLG-VFDSVRSYFSKETglnk 540
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRllNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGlVFQNPDDQFFGPT---- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 541 amfsynskgacpncggkgyIKTELAFmgdfsqTCEvchgkrykqevldatidgysiadvlNLTVDEGIIffdkKNDIKSK 620
Cdd:cd03225   93 -------------------VEEEVAF------GLE-------------------------NLGLPEEEI----EERVEEA 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 621 LQSVSKTGLnymsLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEH 700
Cdd:cd03225  119 LELVGLEGL----RDRSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTH 192
                        250
                 ....*....|...
gi 487747191 701 NLSIMCE-ADWII 712
Cdd:cd03225  193 DLDLLLElADRVI 205
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
286-430 7.66e-15

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 74.71  E-value: 7.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEF---LNKLEDPTAKYIIDplkkqlEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLnssLSD-LVYIIDE 361
Cdd:COG1131   88 LTVRENLRFfarLYGLPRKEARERID------ELLELFGLTDA-ADRKVGTLSGGMKQRLGLALAL---LHDpELLILDE 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 362 PSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMgpgsgkNGGEITFEGTYNELLSS 430
Cdd:COG1131  158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAII------DKGRIVADGTPDELKAR 221
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
315-429 5.19e-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: 71.98  E-value: 5.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLtLNRVTTTLSGGEAQRL----------KLIrhlnsslsdlvyIIDEPSVGLHPEDIAKINEILKSLKEK 384
Cdd:COG1122  117 EALELVGLEHL-ADRPPHELSGGQKQRVaiagvlamepEVL------------VLDEPTAGLDPRGRRELLELLKRLNKE 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487747191 385 GNTVLIVEHDPD-VIKEGDYIIDMgpgsgkNGGEITFEGTYNELLS 429
Cdd:COG1122  184 GKTVIIVTHDLDlVAELADRVIVL------DDGRIVADGTPREVFS 223
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
318-409 5.29e-14

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 70.47  E-value: 5.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 318 EYIGLSYLTLNRVTTTLSGGEAQRLKL--IRHLNSSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDP 395
Cdd:cd03227   62 CIVAAVSAELIFTRLQLSGGEKELSALalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
                         90
                 ....*....|....
gi 487747191 396 DVIKEGDYIIDMGP 409
Cdd:cd03227  142 ELAELADKLIHIKK 155
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
311-410 7.04e-14

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: 71.34  E-value: 7.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 311 KKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIrhlnSSLS---DlVYIIDEPSVGLHPEDIAKINEILKSLKEKGNT 387
Cdd:cd03225  113 ERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAIA----GVLAmdpD-ILLLDEPTAGLDPAGRRELLELLKKLKAEGKT 186
                         90       100
                 ....*....|....*....|....
gi 487747191 388 VLIVEHDPDVIKE-GDYIIDMGPG 410
Cdd:cd03225  187 IIIVTHDLDLLLElADRVIVLEDG 210
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
311-405 9.48e-13

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: 67.94  E-value: 9.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 311 KKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHL--NSSLsdlvYIIDEPSVGLHPEDIAKINEILKSLKEKGNTV 388
Cdd:cd03235  111 AKVDEALERVGLSEL-ADRQIGELSGGQQQRVLLARALvqDPDL----LLLDEPFAGVDPKTQEDIYELLRELRREGMTI 185
                         90
                 ....*....|....*...
gi 487747191 389 LIVEHDPD-VIKEGDYII 405
Cdd:cd03235  186 LVVTHDLGlVLEYFDRVL 203
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
334-431 1.02e-12

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 71.33  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpgsg 412
Cdd:COG4988  474 LSGGQAQRLALARAL---LRDApLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVL----- 544
                         90
                 ....*....|....*....
gi 487747191 413 kNGGEITFEGTYNELLSSN 431
Cdd:COG4988  545 -DDGRIVEQGTHEELLAKN 562
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
279-430 1.30e-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: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 279 NISDFTQMTIKENLE-------FLNKLEDPTAKYIIDPLKKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSS 351
Cdd:cd03219   83 IPRLFPELTVLENVMvaaqartGSGLLLARARREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATD 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 352 lSDLVyIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMgpgsgkNGGEITFEGTYNELLSS 430
Cdd:cd03219  162 -PKLL-LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVL------DQGRVIAEGTPDEVRNN 233
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
283-429 4.34e-12

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 66.30  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEF-LNKLEDPTAKYIID------PLKKQLealeyiglsyltLNRVTTTLSGGEAQRLKLIRHLNSSlSDL 355
Cdd:cd03224   87 FPELTVEENLLLgAYARRRAKRKARLErvyelfPRLKER------------RKQLAGTLSGGEQQMLAIARALMSR-PKL 153
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 356 VyIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GD--YIIDmgpgsgknGGEITFEGTYNELLS 429
Cdd:cd03224  154 L-LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADraYVLE--------RGRVVLEGTAAELLA 221
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
602-717 8.79e-12

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: 63.80  E-value: 8.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 602 LTVDEGIIFFDKKNDIKSKLQSVsktgLNYMSLgqpLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLHESDIPI 680
Cdd:cd00267   49 LKPTSGEILIDGKDIAKLPLEEL----RRRIGY---VPQLSGGQRQRVALARAL---LLNpDLLLLDEPTSGLDPASRER 118
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 487747191 681 LMECFDDLIDQNNTVILIEHNLS-IMCEADWIIDVGPG 717
Cdd:cd00267  119 LLELLRELAEEGRTVIIVTHDPElAELAADRVIVLKDG 156
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
286-407 1.59e-11

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: 64.43  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLE---FLNKLEDPTAKyiidplKKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSSlSDLVyIIDEP 362
Cdd:cd03255   97 LTALENVElplLLAGVPKKERR------ERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALAND-PKII-LADEP 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487747191 363 SVGLHPEDIAKINEILKSL-KEKGNTVLIVEHDPDVIKEGDYIIDM 407
Cdd:cd03255  168 TGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIEL 213
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
314-731 2.35e-11

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: 66.85  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 314 LEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSL-KEKGNTVLIVE 392
Cdd:COG1123  124 LELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL--ALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLIT 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 393 HDPDVIKEG-DYIIDMgpgsgkNGGEITFEGTYNELLSSNTSTGNALRNKHNLKENIREAN-------------HFYNIG 458
Cdd:COG1123  201 HDLGVVAEIaDRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAaaepllevrnlskRYPVRG 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 459 PVTQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVK--AGFENNDH-TIFIDQKAVQGSNRSNLLTYLG----VF-DSVRS 530
Cdd:COG1123  275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARllLGLLRPTSgSILFDGKDLTKLSRRSLRELRRrvqmVFqDPYSS 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 531 yfsketgLNKAMFsynskgacpncggkgyIKTELAFmgdfsqtCEVCHGKRYKQEVLDAtidgysIADVLNLtvdegiif 610
Cdd:COG1123  355 -------LNPRMT----------------VGDIIAE-------PLRLHGLLSRAERRER------VAELLER-------- 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 611 fdkkndiksklqsvskTGLNYMSLGQPLSTLSGGEIQRVklgqhldeeiknSI----------FIFDEPTTGLhesDIPI 680
Cdd:COG1123  391 ----------------VGLPPDLADRYPHELSGGQRQRV------------AIaralalepklLILDEPTSAL---DVSV 439
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 487747191 681 ---LMECFDDLIDQNN-TVILIEHNLSIMCE-ADWIIdVgpgpgLDGGKVQFSGTP 731
Cdd:COG1123  440 qaqILNLLRDLQRELGlTYLFISHDLAVVRYiADRVA-V-----MYDGRIVEDGPT 489
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
4-60 2.61e-11

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: 62.73  E-value: 2.61e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191   4 INITGASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLVFNTVAAESEQLLNESYSSY 60
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKF 57
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
287-493 6.78e-11

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: 65.59  E-value: 6.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  287 TIKEN-LEFLNKLEDPTAkyiiDPLKKQLEALEYIGLSYlTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVG 365
Cdd:TIGR03269 126 TVLDNvLEALEEIGYEGK----EAVGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQL--AKEPFLFLADEPTGT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  366 LHPEdIAKI--NEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMgpgsgkNGGEITFEGTYNELLSSNTSTGNALRNKH 442
Cdd:TIGR03269 199 LDPQ-TAKLvhNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWL------ENGEIKEEGTPDEVVAVFMEGVSEVEKEC 271
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191  443 NL---KENIREAN---HFYNIGPVTQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVK 493
Cdd:TIGR03269 272 EVevgEPIIKVRNvskRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSK 328
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
634-741 8.16e-11

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: 62.74  E-value: 8.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVklgqhldeEI------KNSIFIFDEPTTGLhesDIP---ILMECFDDLIDQNNTVILIEHNLSI 704
Cdd:COG1122  128 ADRPPHELSGGQKQRV--------AIagvlamEPEVLVLDEPTAGL---DPRgrrELLELLKRLNKEGKTVIIVTHDLDL 196
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 487747191 705 MCE-ADWIIdVgpgpgLDGGKVQFSGTPKNFIDSSETL 741
Cdd:COG1122  197 VAElADRVI-V-----LDDGRIVADGTPREVFSDYELL 228
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
636-748 1.97e-10

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 61.64  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 636 QPLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLhesDIP---ILMECFDDLIDQNNTVILIEHNLSIMCE-ADW 710
Cdd:COG1121  135 RPIGELSGGQQQRVLLARAL---AQDpDLLLLDEPFAGV---DAAteeALYELLRELRREGKTILVVTHDLGAVREyFDR 208
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 487747191 711 IIdvgpgpGLDGGKVqFSGTPKnfidssETLTSKHLKR 748
Cdd:COG1121  209 VL------LLNRGLV-AHGPPE------EVLTPENLSR 233
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
638-716 2.81e-10

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: 59.68  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 638 LSTLSGGEIQRVKLGQHLDEEIKN--SIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVG 715
Cdd:cd03227   75 RLQLSGGEKELSALALILALASLKprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154

                 .
gi 487747191 716 P 716
Cdd:cd03227  155 K 155
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
308-423 4.98e-10

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 60.11  E-value: 4.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 308 DPlKKQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNssLSDLVYIIDEPSVGLHPEDIAKINEILKSL-KEKGN 386
Cdd:PRK10247 113 DP-AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQ--FMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNI 189
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 487747191 387 TVLIVEHDPDVIKEGDYIIDMGPgSGKNGGEITFEGT 423
Cdd:PRK10247 190 AVLWVTHDKDEINHADKVITLQP-HAGEMQEARYELA 225
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
283-430 9.37e-10

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 59.44  E-value: 9.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEFL----NKLEDPTakyiIDplKKQLEALEYIGLSYlTLNRVTTTLSGGEAQRLKLIRHLnssLSDLVYI 358
Cdd:cd03261   89 FDSLTVFENVAFPlrehTRLSEEE----IR--EIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVALARAL---ALDPELL 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 359 I-DEPSVGLHPEDIAKINEILKSLK-EKGNTVLIVEHD-PDVIKEGDYIIDMGpgsgknGGEITFEGTYNELLSS 430
Cdd:cd03261  159 LyDEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDlDTAFAIADRIAVLY------DGKIVAEGTPEELRAS 227
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
283-409 1.22e-09

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 58.64  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEFLNKL--EDPTAKYIidplkkqLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLnssLSD--LVyI 358
Cdd:COG4133   87 KPELTVRENLRFWAALygLRADREAI-------DEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLL---LSPapLW-L 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487747191 359 IDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIkEGDYIIDMGP 409
Cdd:COG4133  155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL-AAARVLDLGD 204
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
334-407 2.45e-09

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: 57.23  E-value: 2.45e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191 334 LSGGEAQRLKLIRHLNSSLSDLVyiIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDM 407
Cdd:cd03246   97 LSGGQRQRLGLARALYGNPRILV--LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
641-737 2.77e-09

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 58.45  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQH--LDEEIknsIFiFDEPTTGLhesDiPILMECFDDLI----DQNN-TVILIEHNLSIMCE-ADWII 712
Cdd:COG1127  142 LSGGMRKRVALARAlaLDPEI---LL-YDEPTAGL---D-PITSAVIDELIrelrDELGlTSVVVTHDLDSAFAiADRVA 213
                         90       100
                 ....*....|....*....|....*
gi 487747191 713 dVgpgpgLDGGKVQFSGTPKNFIDS 737
Cdd:COG1127  214 -V-----LADGKIIAEGTPEELLAS 232
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
636-748 2.77e-09

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: 58.52  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 636 QPLSTLSGGEIQRVKLGQHL--DEEiknsIFIFDEPTTGLhesDIP---ILMECFDDLI-DQNNTVILIEHNLSIMCE-A 708
Cdd:COG1120  133 RPVDELSGGERQRVLIARALaqEPP----LLLLDEPTSHL---DLAhqlEVLELLRRLArERGRTVVMVLHDLNLAARyA 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 487747191 709 DWIIdvgpgpGLDGGKVQFSGTPKnfidssETLTSKHLKR 748
Cdd:COG1120  206 DRLV------LLKDGRIVAQGPPE------EVLTPELLEE 233
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
316-422 3.58e-09

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


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 56.67  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 316 ALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHL--NSSlsdlVYIIDEPSVGLhpeDIAKINEILKSLK----EKGNTVL 389
Cdd:cd03214   81 ALELLGLAHL-ADRPFNELSGGERQRVLLARALaqEPP----ILLLDEPTSHL---DIAHQIELLELLRrlarERGKTVV 152
                         90       100       110
                 ....*....|....*....|....*....|....
gi 487747191 390 IVEHDPD-VIKEGDYIIDMgpgsgkNGGEITFEG 422
Cdd:cd03214  153 MVLHDLNlAARYADRVILL------KDGRIVAQG 180
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
641-737 4.23e-09

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 57.51  E-value: 4.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQH--LDEEIknsIFiFDEPTTGLhesDiPILMECFDDLI-----DQNNTVILIEHNLSIMCE-ADWII 712
Cdd:cd03261  137 LSGGMKKRVALARAlaLDPEL---LL-YDEPTAGL---D-PIASGVIDDLIrslkkELGLTSIMVTHDLDTAFAiADRIA 208
                         90       100
                 ....*....|....*....|....*
gi 487747191 713 dvgpgpGLDGGKVQFSGTPKNFIDS 737
Cdd:cd03261  209 ------VLYDGKIVAEGTPEELRAS 227
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
315-407 5.64e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 56.47  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSSlSDLvYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD 394
Cdd:NF040873 102 DALERVGLADL-AGRQLGELSGGQRQRALLAQGLAQE-ADL-LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHD 178
                         90
                 ....*....|...
gi 487747191 395 PDVIKEGDYIIDM 407
Cdd:NF040873 179 LELVRRADPCVLL 191
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
601-737 6.68e-09

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 57.00  E-value: 6.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 601 NLTVDEGIIFF-----DKKNDIKSKLQSV-SKTGLNYmSLGQPLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL 673
Cdd:COG1131   87 DLTVRENLRFFarlygLPRKEARERIDELlELFGLTD-AADRKVGTLSGGMKQRLGLALAL---LHDpELLILDEPTSGL 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 674 hesDIP---ILMECFDDLIDQNNTVILIEHNLSimcEADWIID---VgpgpgLDGGKVQFSGTPKNFIDS 737
Cdd:COG1131  163 ---DPEarrELWELLRELAAEGKTVLLSTHYLE---EAERLCDrvaI-----IDKGRIVADGTPDELKAR 221
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
636-704 7.86e-09

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 56.39  E-value: 7.86e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747191 636 QPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSI 704
Cdd:cd03235  128 RQIGELSGGQQQRVLLARALVQDPD--LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL 194
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
281-430 8.65e-09

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: 56.78  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 281 SDFTQMTIKENLE-FLNKLEDPTAKyiidpLKKQLEA-LEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSSLSDLvyI 358
Cdd:cd03218   85 SIFRKLTVEENILaVLEIRGLSKKE-----REEKLEElLEEFHITHL-RKSKASSLSGGERRRVEIARALATNPKFL--L 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 359 IDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD-PDVIKEGD--YIIdmgpgsgkNGGEITFEGTYNELLSS 430
Cdd:cd03218  157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvRETLSITDraYII--------YEGKVLAEGTPEEIAAN 223
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
334-407 1.13e-08

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: 58.45  E-value: 1.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191  334 LSGGEAQRLKLIRHLnSSLSDLVyIIDEPSVGLHPEDIAKINEILKSLKEkGNTVLIVEHDPDVIKEGDYIIDM 407
Cdd:TIGR02857 459 LSGGQAQRLALARAF-LRDAPLL-LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
288-422 2.00e-08

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: 55.59  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 288 IKENLEFLNKLEDPTAKyiidpLKKQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLS-DLVyIIDEPSVGL 366
Cdd:cd03257  105 IAEPLRIHGKLSKKEAR-----KEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL--ALNpKLL-IADEPTSAL 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487747191 367 hpeDI---AKINEILKSLK-EKGNTVLIVEHDPDVIKE-GDYIIDMgpgsgkNGGEITFEG 422
Cdd:cd03257  177 ---DVsvqAQILDLLKKLQeELGLTLLFITHDLGVVAKiADRVAVM------YAGKIVEEG 228
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
283-394 3.47e-08

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 55.03  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEF-LNKLEDPTAKyiIDplKKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDE 361
Cdd:cd03299   83 FPHMTVYKNIAYgLKKRKVDKKE--IE--RKVLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARAL--VVNPKILLLDE 155
                         90       100       110
                 ....*....|....*....|....*....|....
gi 487747191 362 PSVGLHPEDIAKINEILKSL-KEKGNTVLIVEHD 394
Cdd:cd03299  156 PFSALDVRTKEKLREELKKIrKEFGVTVLHVTHD 189
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
613-731 3.59e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 56.01  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KKNDIKSKLQ-SVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQ 691
Cdd:PRK13631 148 KKSEAKKLAKfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL--AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 487747191 692 NNTVILIEHNLSIMCE-ADWIIdvgpgpGLDGGKVQFSGTP 731
Cdd:PRK13631 226 NKTVFVITHTMEHVLEvADEVI------VMDKGKILKTGTP 260
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
308-413 3.78e-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: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 308 DPLKKQLEALEYIGLSYLTLnRVTTTLSGGEAQRLKLIrhlNSSLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKEKGN 386
Cdd:cd03226  102 AGNEQAETVLKDLDLYALKE-RHPLSLSGGQKQRLAIA---AALLSGKdLLIFDEPTSGLDYKNMERVGELIRELAAQGK 177
                         90       100
                 ....*....|....*....|....*...
gi 487747191 387 TVLIVEHDPDVIKE-GDYIIDMGPGSGK 413
Cdd:cd03226  178 AVIVITHDYEFLAKvCDRVLLLANGAIV 205
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
639-732 3.92e-08

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: 56.69  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 639 STLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL---HESDIpilMECFDDLIdQNNTVILIEHNLSIMCEADWIIDv 714
Cdd:COG4988  472 RGLSGGQAQRLALARAL---LRDaPLLLLDEPTAHLdaeTEAEI---LQALRRLA-KGRTVILITHRLALLAQADRILV- 543
                         90
                 ....*....|....*...
gi 487747191 715 gpgpgLDGGKVQFSGTPK 732
Cdd:COG4988  544 -----LDDGRIVEQGTHE 556
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
602-729 4.52e-08

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: 53.59  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 602 LTVDEGIIFFDKKN--DIKSK---------LQSVSKTGLNYMSlGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPT 670
Cdd:cd03214   49 LKPSSGEILLDGKDlaSLSPKelarkiayvPQALELLGLAHLA-DRPFNELSGGERQRVLLARALAQEPP--ILLLDEPT 125
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191 671 TGLhesDIP---ILMECFDDLIDQNN-TVILIEHNLSI-MCEADWIIdvgpgpGLDGGKVQFSG 729
Cdd:cd03214  126 SHL---DIAhqiELLELLRRLARERGkTVVMVLHDLNLaARYADRVI------LLKDGRIVAQG 180
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
287-431 5.48e-08

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: 56.38  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 287 TIKENLeflnKLEDPTAkyiidPLKKQLEALEYIGLS---------YLTLnrVT---TTLSGGEAQRLKLIRHL--NSSl 352
Cdd:COG2274  564 TIRENI----TLGDPDA-----TDEEIIEAARLAGLHdfiealpmgYDTV--VGeggSNLSGGQRQRLAIARALlrNPR- 631
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747191 353 sdlVYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLSSN 431
Cdd:COG2274  632 ---ILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVL------DKGRIVEDGTHEELLARK 700
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
311-398 6.53e-08

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: 53.95  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 311 KKQLEALEYIGLSYlTLNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLI 390
Cdd:cd03292  115 KRVPAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV 191

                 ....*...
gi 487747191 391 VEHDPDVI 398
Cdd:cd03292  192 ATHAKELV 199
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
286-393 6.86e-08

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: 53.76  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEFLnkledptAKYIIDPLKKQLEALEYIGLSYLTLNRVTTtLSGGEAQRLKLIRHLnssLS--DLVyIIDEPS 363
Cdd:cd03268   87 LTARENLRLL-------ARLLGIRKKRIDEVLDVVGLKDSAKKKVKG-FSLGMKQRLGIALAL---LGnpDLL-ILDEPT 154
                         90       100       110
                 ....*....|....*....|....*....|
gi 487747191 364 VGLHPEDIAKINEILKSLKEKGNTVLIVEH 393
Cdd:cd03268  155 NGLDPDGIKELRELILSLRDQGITVLISSH 184
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
275-712 7.87e-08

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 55.56  E-value: 7.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 275 IMSKNISDFTQMTIKENLeFLNKLedPTAKY----IIDPLKKQLEA---LEYIGLSyLTLNRVTTTLSGGEAQRLKLIRH 347
Cdd:PRK09700  84 IIYQELSVIDELTVLENL-YIGRH--LTKKVcgvnIIDWREMRVRAammLLRVGLK-VDLDEKVANLSISHKQMLEIAKT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 348 LNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMGPGSGKNGGEITfEGTYNE 426
Cdd:PRK09700 160 LMLDAK--VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVS-DVSNDD 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 427 LLSsnTSTGNALRNKHN-LKENIREANH-----FYNIGPVTQNNLNNVKTSIPKHVLTVLTGVAGSGKSTLVKAgfennd 500
Cdd:PRK09700 237 IVR--LMVGRELQNRFNaMKENVSNLAHetvfeVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNC------ 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 501 htIFIDQKAVQGSNRSNlltylGVFDSVRSYFSketGLNKAMfsynskgacpncggkGYI---KTELAFMGDFSqtcevc 577
Cdd:PRK09700 309 --LFGVDKRAGGEIRLN-----GKDISPRSPLD---AVKKGM---------------AYItesRRDNGFFPNFS------ 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 578 hgkrYKQEVldatidgySIADVLNLTVDEGII-FFDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLD 656
Cdd:PRK09700 358 ----IAQNM--------AISRSLKDGGYKGAMgLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLC 425
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 657 EEIKnsIFIFDEPTTGLH---ESDIPILMEcfdDLIDQNNTVILIEHNL-SIMCEADWII 712
Cdd:PRK09700 426 CCPE--VIIFDEPTRGIDvgaKAEIYKVMR---QLADDGKVILMVSSELpEIITVCDRIA 480
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
334-435 1.06e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 55.50  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLNSSlsDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDMGPGS-- 411
Cdd:PRK10535 145 LSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEiv 222
                         90       100
                 ....*....|....*....|....
gi 487747191 412 GKNGGEITFEGTYNELLSSNTSTG 435
Cdd:PRK10535 223 RNPPAQEKVNVAGGTEPVVNTASG 246
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
634-743 1.08e-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: 55.29  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILIEHNLSIMCE-ADWI 711
Cdd:COG1123  136 LDRYPHQLSGGQRQRVAIAMALALDPD--LLIADEPTTALDVTTQAEILDLLRELQRERGtTVLLITHDLGVVAEiADRV 213
                         90       100       110
                 ....*....|....*....|....*....|..
gi 487747191 712 IdvgpgpGLDGGKVQFSGTPKNFIDSSETLTS 743
Cdd:COG1123  214 V------VMDDGRIVEDGPPEEILAAPQALAA 239
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
641-724 1.37e-07

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: 52.00  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL-HESDIpILMECFDDLIdQNNTVILIEHNLSIMCEADWIIDvgpgp 718
Cdd:cd03228   97 LSGGQRQRIAIARAL---LRDpPILILDEATSALdPETEA-LILEALRALA-KGKTVIVIAHRLSTIRDADRIIV----- 166

                 ....*.
gi 487747191 719 gLDGGK 724
Cdd:cd03228  167 -LDDGR 171
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
280-407 2.28e-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: 54.41  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 280 ISDFTQMTIKENLEFLNKLEDPTAKY---IIDPLkkQLEALeyiglsyltLNRVTTTLSGGEAQRLKLIrhlnSSLS--- 353
Cdd:COG1245  410 ISPDYDGTVEEFLRSANTDDFGSSYYkteIIKPL--GLEKL---------LDKNVKDLSGGELQRVAIA----ACLSrda 474
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 354 DLvYIIDEPSVGLHPED---IAKIneILKSLKEKGNTVLIVEHDpdvIkegdYIIDM 407
Cdd:COG1245  475 DL-YLLDEPSAHLDVEQrlaVAKA--IRRFAENRGKTAMVVDHD---I----YLIDY 521
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
327-446 2.47e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 52.61  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 327 LNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIID 406
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARAL--AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAF 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 487747191 407 MgpgsgkNGGEITFEGTYNELLSsntstgnalRNKHNLKE 446
Cdd:PRK14247 218 L------YKGQIVEWGPTREVFT---------NPRHELTE 242
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
310-406 2.61e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.17  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 310 LKKQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVYiiDEPSVGLHPEDIAKINEILKSLKEKGNTVL 389
Cdd:PRK13651 142 KKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVF--DEPTAGLDPQGVKEILEIFDNLNKQGKTII 219
                         90       100
                 ....*....|....*....|....*..
gi 487747191 390 IVEHDPD----------VIKEGDYIID 406
Cdd:PRK13651 220 LVTHDLDnvlewtkrtiFFKDGKIIKD 246
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
283-430 2.98e-07

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 52.34  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKEN----LEFLNKledpTAKYIidplKKQLEAL-EYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSSLSdlvY 357
Cdd:COG1137   90 FRKLTVEDNilavLELRKL----SKKER----EERLEELlEEFGITHL-RKSKAYSLSGGERRRVEIARALATNPK---F 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747191 358 II-DEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHdpDV-----IKEGDYIIdmgpgsgkNGGEITFEGTYNELLSS 430
Cdd:COG1137  158 ILlDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH--NVretlgICDRAYII--------SEGKVLAEGTPEEILNN 226
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
306-406 3.83e-07

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 52.03  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 306 IIDPLkkQLEALeyiglsyltLNRVTTTLSGGEAQRLKLIRHLnSSLSDLvYIIDEPSVGLHPEDIAKINEILKSLKEKG 385
Cdd:cd03237   99 IAKPL--QIEQI---------LDREVPELSGGELQRVAIAACL-SKDADI-YLLDEPSAYLDVEQRLMASKVIRRFAENN 165
                         90       100
                 ....*....|....*....|..
gi 487747191 386 N-TVLIVEHDpdvIKEGDYIID 406
Cdd:cd03237  166 EkTAFVVEHD---IIMIDYLAD 184
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
334-408 4.40e-07

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 51.55  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIK---------EGDYI 404
Cdd:PRK11124 142 LSGGQQQRVAIARAL--MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARktasrvvymENGHI 219

                 ....
gi 487747191 405 IDMG 408
Cdd:PRK11124 220 VEQG 223
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
641-732 5.06e-07

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: 51.46  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLHESDIPILMECFDDLIdQNNTVILIEHNLSIMCEADWIIdVgpgpg 719
Cdd:cd03253  138 LSGGEKQRVAIARAI---LKNpPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKII-V----- 207
                         90
                 ....*....|...
gi 487747191 720 LDGGKVQFSGTPK 732
Cdd:cd03253  208 LKDGRIVERGTHE 220
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
334-410 5.62e-07

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: 50.07  E-value: 5.62e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747191 334 LSGGEAQRLKLIRHL--NSSlsdlVYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMGPG 410
Cdd:cd03228   97 LSGGQRQRIAIARALlrDPP----ILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVLDDG 170
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
327-422 6.75e-07

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: 50.00  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 327 LNRVTTTLSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKI-NEILKSLKEKgnTVLIVEHDPDVIKEGDYI 404
Cdd:cd03247   92 RNNLGRRFSGGERQRLALARIL---LQDApIVLLDEPTVGLDPITERQLlSLIFEVLKDK--TLIWITHHLTGIEHMDKI 166
                         90
                 ....*....|....*...
gi 487747191 405 IDMgpgsgKNgGEITFEG 422
Cdd:cd03247  167 LFL-----EN-GKIIMQG 178
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
334-400 7.51e-07

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: 49.70  E-value: 7.51e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747191 334 LSGGEAQRLKLIRHLnssLSD-LVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:cd03230   96 LSGGMKQRLALAQAL---LHDpELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAER 160
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
292-410 8.73e-07

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: 49.88  E-value: 8.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 292 LEFLNKLEDPTAKYI------IDPLKKQLEAL---------EYIGLSYLT-LNRVTTTLSGGEAQRLKLIRHLNSSLSdl 355
Cdd:cd03229   43 LRCIAGLEEPDSGSIlidgedLTDLEDELPPLrrrigmvfqDFALFPHLTvLENIALGLSGGQQQRVALARALAMDPD-- 120
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 356 VYIIDEPSVGLHPEDIAKINEILKSLKEK-GNTVLIVEHDPD-VIKEGDYIIDMGPG 410
Cdd:cd03229  121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDeAARLADRVVVLRDG 177
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
634-737 9.11e-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: 50.56  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL-HESDIPILMECFDdlIDQNNTVILIEHNLSIMCEADWI 711
Cdd:cd03252  132 VGEQGAGLSGGQRQRIAIARAL---IHNpRILIFDEATSALdYESEHAIMRNMHD--ICAGRTVIIIAHRLSTVKNADRI 206
                         90       100
                 ....*....|....*....|....*.
gi 487747191 712 IdvgpgpGLDGGKVQFSGTPKNFIDS 737
Cdd:cd03252  207 I------VMEKGRIVEQGSHDELLAE 226
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
285-427 1.13e-06

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 50.06  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 285 QMTIKENLEFLNKLedptAKYIIDPLKKQL-EALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLNSSLSDLVyiIDEPS 363
Cdd:cd03265   87 ELTGWENLYIHARL----YGVPGAERRERIdELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLF--LDEPT 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487747191 364 VGLHPEDIAKINEILKSLKEK-GNTVLIVEHDPDvikEGDY------IIDMgpgsgkngGEITFEGTYNEL 427
Cdd:cd03265  160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYME---EAEQlcdrvaIIDH--------GRIIAEGTPEEL 219
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
272-437 1.20e-06

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 50.26  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 272 SSKIMSKNISD-------FTQMTIKENLEFLNKLEDptakyiidplKKQLEalEYIGLSYLTLNRV-------TTTLSGG 337
Cdd:PRK11614  74 TAKIMREAVAIvpegrrvFSRMTVEENLAMGGFFAE----------RDQFQ--ERIKWVYELFPRLherriqrAGTMSGG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 338 EAQRLKLIRHLNSSLSDLvyIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPD-VIKEGD--YIIDmgpgsgkn 414
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLL--LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrgYVLE-------- 211
                        170       180
                 ....*....|....*....|...
gi 487747191 415 GGEITFEGTYNELLsSNTSTGNA 437
Cdd:PRK11614 212 NGHVVLEDTGDALL-ANEAVRSA 233
PTZ00243 PTZ00243
ABC transporter; Provisional
406-743 1.26e-06

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.09  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  406 DMGPGSGKNGGEI-TFEGTYNEllSSNTSTGNAlrnkhnlKENIREANHFYNIGPvtQNNLNNVKTSIPKHVLTVLTGVA 484
Cdd:PTZ00243  627 DYGSPSSASRHIVeGGTGGGHE--ATPTSERSA-------KTPKMKTDDFFELEP--KVLLRDVSVSVPRGKLTVVLGAT 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  485 GSGKSTLVKAgfenndhtifidqkavqgsnrsnlltylgvfdsvrsyfsketglnkamfsynskgacpncggkgyiktel 564
Cdd:PTZ00243  696 GSGKSTLLQS---------------------------------------------------------------------- 705
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  565 aFMGDFsqtcEVCHGKRYKQEvldatidgySIADV------LNLTVDEGIIFFDKKNdiKSKLQS---VSKTGLNYMSLG 635
Cdd:PTZ00243  706 -LLSQF----EISEGRVWAER---------SIAYVpqqawiMNATVRGNILFFDEED--AARLADavrVSQLEADLAQLG 769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  636 QPLST--------LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGL--HESDIpILMECFDDLIdQNNTVILIEHNLSIM 705
Cdd:PTZ00243  770 GGLETeigekgvnLSGGQKARVSLARAV--YANRDVYLLDDPLSALdaHVGER-VVEECFLGAL-AGKTRVLATHQVHVV 845
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 487747191  706 CEADWIIdvgpgpGLDGGKVQFSGTPKNFIDSS--ETLTS 743
Cdd:PTZ00243  846 PRADYVV------ALGDGRVEFSGSSADFMRTSlyATLAA 879
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
286-410 1.49e-06

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: 49.87  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEFLNKLEDPTAKYIIDPLKKqlEALEYIGLSYLTLNR-VTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSV 364
Cdd:cd03260   95 GSIYDNVAYGLRLHGIKLKEELDERVE--EALRKAALWDEVKDRlHALGLSGGQQQRLCLARAL--ANEPEVLLLDEPTS 170
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 487747191 365 GLHPEDIAKINEILKSLKEKgNTVLIVEHDP-DVIKEGDYIIDMGPG 410
Cdd:cd03260  171 ALDPISTAKIEELIAELKKE-YTIVIVTHNMqQAARVADRTAFLLNG 216
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
287-431 1.73e-06

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: 49.92  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 287 TIKENLEFLNklEDPTAKYIIDpLKKQLEALEYI-----GLsYLTLNRVTTTLSGGEAQRLKLIRHL--NSSlsdlVYII 359
Cdd:cd03254   92 TIMENIRLGR--PNATDEEVIE-AAKEAGAHDFImklpnGY-DTVLGENGGNLSQGERQLLAIARAMlrDPK----ILIL 163
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747191 360 DEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLSSN 431
Cdd:cd03254  164 DEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVL------DDGKIIEEGTHDELLAKK 228
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
638-703 1.77e-06

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: 49.09  E-value: 1.77e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 638 LSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLS 703
Cdd:cd03213  109 LRGLSGGERKRVSIALEL---VSNpSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPS 172
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
315-432 1.80e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.40  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVEH 393
Cdd:PRK13635 123 QALRQVGMEDF-LNREPHRLSGGQKQRVAIAGVL--ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITH 199
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 487747191 394 DPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLSSNT 432
Cdd:PRK13635 200 DLDEAAQADRVIVM------NKGEILEEGTPEEIFKSGH 232
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
641-741 1.82e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 50.09  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILIEHNLSIMCEADWIIDvgpgpg 719
Cdd:PRK13633 145 LSGGQKQRVAIAGIL--AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVEADRIIV------ 216
                         90       100
                 ....*....|....*....|..
gi 487747191 720 LDGGKVQFSGTPKNFIDSSETL 741
Cdd:PRK13633 217 MDSGKVVMEGTPKEIFKEVEMM 238
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
283-394 2.28e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 49.58  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLeflnkLEDPTAKYIIDPLKKQLEALEY---IGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYII 359
Cdd:PRK10619 104 WSHMTVLENV-----MEAPIQVLGLSKQEARERAVKYlakVGIDERAQGKYPVHLSGGQQQRVSIARAL--AMEPEVLLF 176
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 487747191 360 DEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD 394
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
311-452 2.30e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 50.08  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 311 KKQLEALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLI 390
Cdd:PRK13639 116 KRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGIL--AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIII 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 391 VEHDPDVI---KEGDYIIdmgpgsgkNGGEITFEGTYNELLSSntstgnalrnkhnlKENIREAN 452
Cdd:PRK13639 193 STHDVDLVpvyADKVYVM--------SDGKIIKEGTPKEVFSD--------------IETIRKAN 235
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
465-743 2.73e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 49.75  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 465 LNNVKTSIPKHVLTVLTGVAGSGKSTLVK--AGFEN-NDHTIFIDQKAVQGSNRSNLLTYLG-VFDSVRSYFSKETglnk 540
Cdd:PRK13648  25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKlmIGIEKvKSGEIFYNNQAITDDNFEKLRKHIGiVFQNPDNQFVGSI---- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 541 amfsynskgacpncggkgyIKTELAF-MGDFSQTCEVCHgkRYKQEVLDaTIDGYSIADvlnltvdegiiffdkkndikS 619
Cdd:PRK13648 101 -------------------VKYDVAFgLENHAVPYDEMH--RRVSEALK-QVDMLERAD--------------------Y 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 620 KLQSvsktglnymslgqplstLSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILI 698
Cdd:PRK13648 139 EPNA-----------------LSGGQKQRVAIAGVL--ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISI 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 487747191 699 EHNLSIMCEADWIIdvgpgpGLDGGKVQFSGTPKNFIDSSETLTS 743
Cdd:PRK13648 200 THDLSEAMEADHVI------VMNKGTVYKEGTPTEIFDHAEELTR 238
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
636-731 2.84e-06

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: 49.36  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 636 QPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCE-ADWIIdV 714
Cdd:cd03219  139 RPAGELSYGQQRRLEIARALATDPK--LLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVT-V 215
                         90
                 ....*....|....*..
gi 487747191 715 gpgpgLDGGKVQFSGTP 731
Cdd:cd03219  216 -----LDQGRVIAEGTP 227
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
639-731 2.99e-06

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: 50.60  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 639 STLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL-HESDIpILMECFDDLIdQNNTVILIEHNLSIMCEADWIIdVgp 716
Cdd:COG2274  610 SNLSGGQRQRLAIARAL---LRNpRILILDEATSALdAETEA-IILENLRRLL-KGRTVIIIAHRLSTIRLADRII-V-- 681
                         90
                 ....*....|....*
gi 487747191 717 gpgLDGGKVQFSGTP 731
Cdd:COG2274  682 ---LDKGRIVEDGTH 693
cbiO PRK13637
energy-coupling factor transporter ATPase;
315-426 3.55e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 49.28  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLTL-NRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHP---EDIakINEILKSLKEKGNTVLI 390
Cdd:PRK13637 125 RAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVV--AMEPKILILDEPTAGLDPkgrDEI--LNKIKELHKEYNMTIIL 200
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 487747191 391 VEHD-PDVIKEGDYIIDMgpgsgkNGGEITFEGTYNE 426
Cdd:PRK13637 201 VSHSmEDVAKLADRIIVM------NKGKCELQGTPRE 231
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
634-736 4.40e-06

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: 48.58  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCE-ADWII 712
Cdd:cd03224  126 RKQLAGTLSGGEQQMLAIARALMSRPK--LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAY 203
                         90       100
                 ....*....|....*....|....
gi 487747191 713 dVgpgpgLDGGKVQFSGTPKNFID 736
Cdd:cd03224  204 -V-----LERGRVVLEGTAAELLA 221
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
641-746 4.77e-06

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: 48.97  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLhesDiPI----LMECFDDLIDQNN-TVILIEHNLSIMCEADWIIdVg 715
Cdd:TIGR04520 137 LSGGQKQRVAIAGVL--AMRPDIIILDEATSML---D-PKgrkeVLETIRKLNKEEGiTVISITHDMEEAVLADRVI-V- 208
                          90       100       110
                  ....*....|....*....|....*....|.
gi 487747191  716 pgpgLDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:TIGR04520 209 ----MNKGKIVAEGTPREIFSQVELLKEIGL 235
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
308-409 5.17e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 49.08  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 308 DPLKKQLE-ALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSL-KEKG 385
Cdd:PRK13636 116 DEVRKRVDnALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVL--VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELG 192
                         90       100       110
                 ....*....|....*....|....*....|....
gi 487747191 386 NTVLIVEHDPD----------VIKEGDYIIDMGP 409
Cdd:PRK13636 193 LTIIIATHDIDivplycdnvfVMKEGRVILQGNP 226
cbiO PRK13643
energy-coupling factor transporter ATPase;
315-404 5.93e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 48.96  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEH- 393
Cdd:PRK13643 126 EKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL--AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHl 203
                         90
                 ....*....|.
gi 487747191 394 DPDVIKEGDYI 404
Cdd:PRK13643 204 MDDVADYADYV 214
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
622-714 5.95e-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: 49.59  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  622 QSVSKTGLNYM--SLGQPLST--------LSGGEIQRVKLGQHLdeeIKNS-IFIFDEPTTGLHESDIPILMECFDDLId 690
Cdd:TIGR02857 430 EALERAGLDEFvaALPQGLDTpigeggagLSGGQAQRLALARAF---LRDApLLLLDEPTAHLDAETEAEVLEALRALA- 505
                          90       100
                  ....*....|....*....|....
gi 487747191  691 QNNTVILIEHNLSIMCEADWIIDV 714
Cdd:TIGR02857 506 QGRTVLLVTHRLALAALADRIVVL 529
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
309-396 6.29e-06

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 48.47  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 309 PLKKQ--LEALEYIGLSYLTLNRVTTtLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSLKEK-G 385
Cdd:PRK09984 127 REQKQraLQALTRVGMVHFAHQRVST-LSGGQQQRVAIARALMQQAK--VILADEPIASLDPESARIVMDTLRDINQNdG 203
                         90
                 ....*....|.
gi 487747191 386 NTVLIVEHDPD 396
Cdd:PRK09984 204 ITVVVTLHQVD 214
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
626-702 7.63e-06

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 47.64  E-value: 7.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 626 KTGLNYMSLGQPLStLSGGEIQRVKLGQHLDEeiKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:cd03226  113 DLDLYALKERHPLS-LSGGQKQRLAIAAALLS--GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY 186
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
306-406 8.21e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.04  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 306 IIDPLkkQLEALeyiglsyltLNRVTTTLSGGEAQRLKLIrhlnSSLS---DLvYIIDEPSVGLHPED---IAKIneILK 379
Cdd:PRK13409 437 IIKPL--QLERL---------LDKNVKDLSGGELQRVAIA----ACLSrdaDL-YLLDEPSAHLDVEQrlaVAKA--IRR 498
                         90       100
                 ....*....|....*....|....*..
gi 487747191 380 SLKEKGNTVLIVEHDPDVIkegDYIID 406
Cdd:PRK13409 499 IAEEREATALVVDHDIYMI---DYISD 522
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
308-410 8.46e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 48.09  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 308 DPLKKQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSL-KEKGN 386
Cdd:PRK13634 120 DAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVL--AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGL 197
                         90       100
                 ....*....|....*....|....*
gi 487747191 387 TVLIVEHD-PDVIKEGDYIIDMGPG 410
Cdd:PRK13634 198 TTVLVTHSmEDAARYADQIVVMHKG 222
cbiO PRK13649
energy-coupling factor transporter ATPase;
641-746 8.46e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 48.20  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCE-ADWIIDvgpgpg 719
Cdd:PRK13649 146 LSGGQMRRVAIAGILAME--PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYV------ 217
                         90       100
                 ....*....|....*....|....*..
gi 487747191 720 LDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:PRK13649 218 LEKGKLVLSGKPKDIFQDVDFLEEKQL 244
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
286-400 8.58e-06

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 47.28  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEFLNKLEDPTAKYIidpLKKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIrhlnSSL---SDLVyIIDEP 362
Cdd:cd03269   85 MKVIDQLVYLAQLKGLKKEEA---RRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFI----AAVihdPELL-ILDEP 155
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 487747191 363 SVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:cd03269  156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEE 193
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
283-427 8.85e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 47.91  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEF---LNKLEDPTakyiiDPLKKQLE-ALEYIGLSYLTLNRVT---TTLSGGEAQRLKLIRHLnsSLSDL 355
Cdd:PRK14267  97 FPHLTIYDNVAIgvkLNGLVKSK-----KELDERVEwALKKAALWDEVKDRLNdypSNLSGGQRQRLVIARAL--AMKPK 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 356 VYIIDEPSVGLHPEDIAKINEILKSLKEKgNTVLIVEHDP-DVIKEGDY--------IIDMGPgsgkngGEITFEGTYNE 426
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPaQAARVSDYvaflylgkLIEVGP------TRKVFENPEHE 242

                 .
gi 487747191 427 L 427
Cdd:PRK14267 243 L 243
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
613-735 9.66e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 48.06  E-value: 9.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KKNDIKSKLQSVSKTGLNYMSlGQPLSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGLHESDIPILMECFDDL-IDQ 691
Cdd:PRK10253 117 RKEDEEAVTKAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQE--TAIMLLDEPTTWLDISHQIDLLELLSELnREK 193
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 487747191 692 NNTVILIEHNLSIMCE-ADWIIdvgpgpGLDGGKVQFSGTPKNFI 735
Cdd:PRK10253 194 GYTLAAVLHDLNQACRyASHLI------ALREGKIVAQGAPKEIV 232
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
622-748 1.00e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 47.70  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 622 QSVSKTGLNYMSlGQPLSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGL---HESDipiLMECFDDLIDQNNTVILI 698
Cdd:PRK11231 121 QAMEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQD--TPVVLLDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTV 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487747191 699 EHNLSIMCE-ADWIIdvgpgpGLDGGKVQFSGTPknfidsSETLTSKHLKR 748
Cdd:PRK11231 195 LHDLNQASRyCDHLV------VLANGHVMAQGTP------EEVMTPGLLRT 233
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
307-394 1.05e-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: 49.01  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 307 IDPLKKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLK----LIRHLNsslsdlVYIIDEPSVGLhpeDI---AKINEILK 379
Cdd:COG1245  187 VDERGKLDELAEKLGLENI-LDRDISELSGGELQRVAiaaaLLRDAD------FYFFDEPSSYL---DIyqrLNVARLIR 256
                         90
                 ....*....|....*
gi 487747191 380 SLKEKGNTVLIVEHD 394
Cdd:COG1245  257 ELAEEGKYVLVVEHD 271
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
287-440 1.18e-05

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 49.17  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   287 TIKENLEFLNKLEDPTAKYIIDP--LKKQLEALEyiGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSlSDlVYIIDEP-- 362
Cdd:TIGR00957  714 SLRENILFGKALNEKYYQQVLEAcaLLPDLEILP--SGDRTEIGEKGVNLSGGQKQRVSLARAVYSN-AD-IYLFDDPls 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   363 ----SVGLHP-EDIAKINEILKslkekGNTVLIVEHDPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLSSNTSTGNA 437
Cdd:TIGR00957  790 avdaHVGKHIfEHVIGPEGVLK-----NKTRILVTHGISYLPQVDVIIVM------SGGKISEMGSYQELLQRDGAFAEF 858

                   ...
gi 487747191   438 LRN 440
Cdd:TIGR00957  859 LRT 861
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
260-362 1.36e-05

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: 45.72  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  260 TCKGQRLNSKILssKIMSKNISDFTQ-------MTIKENLEFLNKLEDPTAKYIIDPLKKQLEALEYIGLSYLTLNRVTT 332
Cdd:pfam00005  43 LLDGQDLTDDER--KSLRKEIGYVFQdpqlfprLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPG 120
                          90       100       110
                  ....*....|....*....|....*....|
gi 487747191  333 TLSGGEAQRLKLIRHLNSSlSDlVYIIDEP 362
Cdd:pfam00005 121 TLSGGQRQRVAIARALLTK-PK-LLLLDEP 148
cbiO PRK13646
energy-coupling factor transporter ATPase;
334-442 1.38e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 47.47  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVEHD-PDVIKEGDYIIDMgpgs 411
Cdd:PRK13646 146 MSGGQMRKIAIVSIL--AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENkTIILVSHDmNEVARYADEVIVM---- 219
                         90       100       110
                 ....*....|....*....|....*....|.
gi 487747191 412 gkNGGEITFEGTYNELLSSntstGNALRNKH 442
Cdd:PRK13646 220 --KEGSIVSQTSPKELFKD----KKKLADWH 244
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
601-703 1.40e-05

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 46.90  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 601 NLTVDEGIIFFDKKNDIKSKLQSVSKTgLNYMSLGQ----PLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHES 676
Cdd:cd03297   89 HLNVRENLAFGLKRKRNREDRISVDEL-LDLLGLDHllnrYPAQLSGGEKQRVALARALAAQPE--LLLLDEPFSALDRA 165
                         90       100
                 ....*....|....*....|....*...
gi 487747191 677 DIPILMECFDDLIDQ-NNTVILIEHNLS 703
Cdd:cd03297  166 LRLQLLPELKQIKKNlNIPVIFVTHDLS 193
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
278-394 1.43e-05

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 47.29  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 278 KNISDFTQMTIKENL----------EFLNKLEDpTAKYiidpLKKQLEALEY-------IGLSYLTlNRVTTTLSGGEAQ 340
Cdd:PRK11300  87 QHVRLFREMTVIENLlvaqhqqlktGLFSGLLK-TPAF----RRAESEALDRaatwlerVGLLEHA-NRQAGNLAYGQQR 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 341 RLKLIRHLNSSLSDLvyIIDEPSVGLHPEDIAKINEILKSLK-EKGNTVLIVEHD 394
Cdd:PRK11300 161 RLEIARCMVTQPEIL--MLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHD 213
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
286-394 1.60e-05

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 46.48  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEFLNKLEDpTAKYIIDplKKQLEALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVG 365
Cdd:cd03301   87 MTVYDNIAFGLKLRK-VPKDEID--ERVREVAELLQIEHL-LDRKPKQLSGGQRQRVALGRAIVREPK--VFLMDEPLSN 160
                         90       100       110
                 ....*....|....*....|....*....|....
gi 487747191 366 LHpediAKI-----NEILKSLKEKGNTVLIVEHD 394
Cdd:cd03301  161 LD----AKLrvqmrAELKRLQQRLGTTTIYVTHD 190
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
596-714 1.80e-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: 48.24  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 596 IADVLNLTVDEGIiffdKKNDIKSKLQS-VSKTGLNYMsLGQPLSTLSGGEIQRVKLGQHLdeeIKNS-IFIFDEPTTGL 673
Cdd:COG1245  172 IPKVFKGTVRELL----EKVDERGKLDElAEKLGLENI-LDRDISELSGGELQRVAIAAAL---LRDAdFYFFDEPSSYL 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 487747191 674 hesDI-------PILMEcfddLIDQNNTVILIEHNLSIMceaDWIIDV 714
Cdd:COG1245  244 ---DIyqrlnvaRLIRE----LAEEGKYVLVVEHDLAIL---DYLADY 281
cbiO PRK13644
energy-coupling factor transporter ATPase;
281-429 1.92e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 46.90  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 281 SDFTQMTIKENLEF--LNKLEDPTAkyiidpLKKQLE-ALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLNSSLSDLVY 357
Cdd:PRK13644  88 TQFVGRTVEEDLAFgpENLCLPPIE------IRKRVDrALAEIGLEKYR-HRSPKTLSGGQGQCVALAGILTMEPECLIF 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747191 358 iiDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLS 429
Cdd:PRK13644 161 --DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM------DRGKIVLEGEPENVLS 224
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
641-702 2.05e-05

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: 45.50  E-value: 2.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:cd03216   83 LSVGERQMVEIARALARNAR--LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRL 142
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
599-717 2.34e-05

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


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 46.17  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 599 VLNLTVDEGIIF---FDKKNdIKSKLQSVS-KTGLNYMSLGQPLS------TLSGGEIQRVKLGQHLDEEiKNSIFIfDE 668
Cdd:cd03290   90 LLNATVEENITFgspFNKQR-YKAVTDACSlQPDIDLLPFGDQTEigergiNLSGGQRQRICVARALYQN-TNIVFL-DD 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487747191 669 PTTGL--HESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVGPG 717
Cdd:cd03290  167 PFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
634-748 2.43e-05

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 46.37  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKL--------------GQHLdeeiknsifIFDEPTTGLhesDIP-------ILMEcfddLIDQN 692
Cdd:COG4138  120 LSRPLTQLSGGEWQRVRLaavllqvwptinpeGQLL---------LLDEPMNSL---DVAqqaaldrLLRE----LCQQG 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 487747191 693 NTVILIEHNLSIMC-EAD--WIidvgpgpgLDGGKVQFSGTPKnfidssETLTSKHLKR 748
Cdd:COG4138  184 ITVVMSSHDLNHTLrHADrvWL--------LKQGKLVASGETA------EVMTPENLSE 228
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
603-702 2.70e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.00  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 603 TVDEGIIF------FDKKNDIKSKLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHES 676
Cdd:PRK13651 122 TIEKDIIFgpvsmgVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPD--FLVFDEPTAGLDPQ 199
                         90       100
                 ....*....|....*....|....*.
gi 487747191 677 DIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:PRK13651 200 GVKEILEIFDNLNKQGKTIILVTHDL 225
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
287-431 2.92e-05

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 47.53  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 287 TIKENLEFLNKLEDPTAkyiIDPLKKQLEALEYI-----GLSYLTLNRvTTTLSGGEAQRLKLIRHLNSSlSDLvYIIDE 361
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQ---LQQALENAWVSEFLpllpqGLDTPIGDQ-AAGLSVGQAQRLALARALLQP-CQL-LLLDE 511
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191 362 PSVGL--HPEdiakiNEILKSLKE--KGNTVLIVEHDPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLSSN 431
Cdd:PRK11174 512 PTASLdaHSE-----QLVMQALNAasRRQTTLMVTHQLEDLAQWDQIWVM------QDGQIVQQGDYAELSQAG 574
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
292-406 3.72e-05

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 45.82  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 292 LEFLNKLEDPTAKyiiDPLKKQLEaLEYIglsyltLNRVTTTLSGGEAQRLKL----IRHLNsslsdlVYIIDEPSVGLH 367
Cdd:cd03236  108 GELLKKKDERGKL---DELVDQLE-LRHV------LDRNIDQLSGGELQRVAIaaalARDAD------FYFFDEPSSYLD 171
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 487747191 368 PEDIAKINEILKSLKEKGNTVLIVEHDPDVIkegDYIID 406
Cdd:cd03236  172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVL---DYLSD 207
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
640-748 3.98e-05

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 45.88  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 640 TLSGGEIQRVKLG-------QHLDEEIKnsiFIF-DEPTTGLhesDIP---ILMECFDDLIDQNNTVILIEH--NLSIMC 706
Cdd:COG4559  133 TLSGGEQQRVQLArvlaqlwEPVDGGPR---WLFlDEPTSAL---DLAhqhAVLRLARQLARRGGGVVAVLHdlNLAAQY 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 487747191 707 eADWIIdvgpgpGLDGGKVQFSGTPknfidsSETLTSKHLKR 748
Cdd:COG4559  207 -ADRIL------LLHQGRLVAQGTP------EEVLTDELLER 235
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
605-712 4.22e-05

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: 44.70  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 605 DEGIIFFDKKNDIKSKLQSVSKTGL--------NYMSLGQPLStLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLhe 675
Cdd:cd03230   53 DSGEIKVLGKDIKKEPEEVKRRIGYlpeepslyENLTVRENLK-LSGGMKQRLALAQAL---LHDpELLILDEPTSGL-- 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 487747191 676 sDIP---ILMECFDDLIDQNNTVILIEHNLSIMCE-ADWII 712
Cdd:cd03230  127 -DPEsrrEFWELLRELKKEGKTILLSSHILEEAERlCDRVA 166
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
334-431 5.19e-05

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 46.63  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  334 LSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKEkGNTVLIVEHDPDVIKEGDYIIDMgpgsg 412
Cdd:TIGR02203 470 LSGGQRQRLAIARAL---LKDApILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEKADRIVVM----- 540
                          90
                  ....*....|....*....
gi 487747191  413 kNGGEITFEGTYNELLSSN 431
Cdd:TIGR02203 541 -DDGRIVERGTHNELLARN 558
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
333-405 5.23e-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: 44.91  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 333 TLSGGE------AQRLKLIRHLNSSLSDLvyIIDEPSVGLHPEDIA-KINEILKSLKEKGN-TVLIVEHDPDVIKEGDYI 404
Cdd:cd03240  115 RCSGGEkvlaslIIRLALAETFGSNCGIL--ALDEPTTNLDEENIEeSLAEIIEERKSQKNfQLIVITHDEELVDAADHI 192

                 .
gi 487747191 405 I 405
Cdd:cd03240  193 Y 193
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
334-431 5.28e-05

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: 45.30  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLnssLSD-LVYIIDEPSVGLhpeDIAKINEILKSLKE--KGNTVLIVEHDPDVIKEGDYIIDMgpg 410
Cdd:cd03253  138 LSGGEKQRVAIARAI---LKNpPILLLDEATSAL---DTHTEREIQAALRDvsKGRTTIVIAHRLSTIVNADKIIVL--- 208
                         90       100
                 ....*....|....*....|.
gi 487747191 411 sgkNGGEITFEGTYNELLSSN 431
Cdd:cd03253  209 ---KDGRIVERGTHEELLAKG 226
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
601-702 5.36e-05

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 46.56  E-value: 5.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 601 NLTVDEGII---------FFDKKnDIKSKLQSVSKT-GLNyMSLGQPLSTLSGGEIQRVklgqhldeEI------KNSIF 664
Cdd:COG3845   94 NLTVAENIVlgleptkggRLDRK-AARARIRELSERyGLD-VDPDAKVEDLSVGEQQRV--------EIlkalyrGARIL 163
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 487747191 665 IFDEPTTGL--HESDipILMECFDDLIDQNNTVILIEHNL 702
Cdd:COG3845  164 ILDEPTAVLtpQEAD--ELFEILRRLAAEGKSIIFITHKL 201
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
621-702 5.69e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 45.39  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 621 LQSVSKTGLNYMSlGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDlIDQNN--TVILI 698
Cdd:PRK09984 134 LQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQAK--VILADEPIASLDPESARIVMDTLRD-INQNDgiTVVVT 209

                 ....
gi 487747191 699 EHNL 702
Cdd:PRK09984 210 LHQV 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
641-713 5.96e-05

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: 44.49  E-value: 5.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747191 641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLhesDiPILMECFDDLIDQNN-----TVILIEHNLSimcEADWIID 713
Cdd:cd03229  101 LSGGQQQRVALARAL--AMDPDVLLLDEPTSAL---D-PITRREVRALLKSLQaqlgiTVVLVTHDLD---EAARLAD 169
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
613-714 6.23e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 46.34  E-value: 6.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KKNDIKSKLQS-VSKTGLNYMsLGQPLSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGLhesDIPILMECfDDLI-- 689
Cdd:PRK13409 185 KKVDERGKLDEvVERLGLENI-LDRDISELSGGELQRVAIAAALLRD--ADFYFFDEPTSYL---DIRQRLNV-ARLIre 257
                         90       100
                 ....*....|....*....|....*.
gi 487747191 690 -DQNNTVILIEHNLSIMceaDWIIDV 714
Cdd:PRK13409 258 lAEGKYVLVVEHDLAVL---DYLADN 280
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
316-399 6.40e-05

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 44.79  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 316 ALEYIGLSYLtLNRVTTTLSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPediAKINE----ILKSLKEKGNTVLI 390
Cdd:cd03298  112 ALARVGLAGL-EKRLPGELSGGERQRVALARVL---VRDKpVLLLDEPFAALDP---ALRAEmldlVLDLHAETKMTVLM 184

                 ....*....
gi 487747191 391 VEHDPDVIK 399
Cdd:cd03298  185 VTHQPEDAK 193
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
613-736 6.50e-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: 45.25  E-value: 6.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KKNDIKSKLQSVSKTGLNYMSLgQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDL-IDQ 691
Cdd:cd03256  118 PKEEKQRALAALERVGLLDKAY-QRADQLSGGQQQRVAIARALMQQPK--LILADEPVASLDPASSRQVMDLLKRInREE 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487747191 692 NNTVILIEHNLSIMCE-ADWIIdvgpgpGLDGGKVQFSGTPKNFID 736
Cdd:cd03256  195 GITVIVSLHQVDLAREyADRIV------GLKDGRIVFDGPPAELTD 234
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
282-393 6.93e-05

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 45.57  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 282 DFTqmtIKENLEFLNK---LEDPTAKYIIDPLkkqleaLEYIGLSYLTLNRVTTtLSGGEAQRLKLIRHLnssLSDL-VY 357
Cdd:PRK13537  94 DFT---VRENLLVFGRyfgLSAAAARALVPPL------LEFAKLENKADAKVGE-LSGGMKRRLTLARAL---VNDPdVL 160
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 487747191 358 IIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEH 393
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
332-395 8.53e-05

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: 45.81  E-value: 8.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191  332 TTLSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKEkGNTVLIVEHDP 395
Cdd:TIGR02868 470 ARLSGGERQRLALARAL---LADApILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
641-730 8.65e-05

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 45.97  E-value: 8.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLH---ESDIpilMECFDDlIDQNNTVILIEHNLSIMCEADWIIdVgp 716
Cdd:COG5265  495 LSGGEKQRVAIARTL---LKNpPILIFDEATSALDsrtERAI---QAALRE-VARGRTTLVIAHRLSTIVDADEIL-V-- 564
                         90
                 ....*....|....
gi 487747191 717 gpgLDGGKVQFSGT 730
Cdd:COG5265  565 ---LEAGRIVERGT 575
cbiO PRK13644
energy-coupling factor transporter ATPase;
622-735 8.81e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 44.98  E-value: 8.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 622 QSVSKTGLNYMSLGQPlSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHN 701
Cdd:PRK13644 119 RALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTME--PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN 195
                         90       100       110
                 ....*....|....*....|....*....|....
gi 487747191 702 LSIMCEADWIIdvgpgpGLDGGKVQFSGTPKNFI 735
Cdd:PRK13644 196 LEELHDADRII------VMDRGKIVLEGEPENVL 223
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
281-408 1.02e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 44.50  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 281 SDFTQMTIKENL-EFLNKLEDPTAKYIIDplkKQLEALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLNSSLSDLvyII 359
Cdd:PRK10895  88 SIFRRLSVYDNLmAVLQIRDDLSAEQRED---RANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFI--LL 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487747191 360 DEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDP----DVIkEGDYIIDMG 408
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVretlAVC-ERAYIVSQG 213
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
334-431 1.07e-04

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: 44.40  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpgsgk 413
Cdd:cd03252  139 LSGGQRQRIAIARALIHNPR--ILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRIIVM------ 209
                         90
                 ....*....|....*...
gi 487747191 414 NGGEITFEGTYNELLSSN 431
Cdd:cd03252  210 EKGRIVEQGSHDELLAEN 227
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
137-398 1.24e-04

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 44.69  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  137 TCEGLGYIEDINLDELLDWDKSLNEGAIDFPSFGPDKERGKAYRDSGLFDNNKKLKDYTKDELELFLYQEPMTLKNPPKE 216
Cdd:pfam13304  33 TDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  217 WR----------KSAKYVGLIPRFSRIFLGDKEFNKKRYAKHLKNVVNNkicstckGQRLNSKILSSKIMSKNISDFTQM 286
Cdd:pfam13304 113 PEaeelrlgldvEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGL-------LLEDWAVLDLAADLALFPDLKELL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  287 TIKENLEFLNKLEDPTAKYIIDPLKKQLEALEYIGLSYLTLNRVTTT----LSGGEAQRLKLIRHLNSSLSDL-VYIIDE 361
Cdd:pfam13304 186 QRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELpafeLSDGTKRLLALLAALLSALPKGgLLLIDE 265
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 487747191  362 PSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVI 398
Cdd:pfam13304 266 PESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
634-732 1.28e-04

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: 44.07  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL-HESDIpILMECFDDLIdQNNTVILIEHNLSIMCEADWI 711
Cdd:cd03249  133 VGERGSQLSGGQKQRIAIARAL---LRNpKILLLDEATSALdAESEK-LVQEALDRAM-KGRTTIVIAHRLSTIRNADLI 207
                         90       100
                 ....*....|....*....|.
gi 487747191 712 IdvgpgpGLDGGKVQFSGTPK 732
Cdd:cd03249  208 A------VLQNGQVVEQGTHD 222
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
283-429 1.33e-04

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 44.31  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEFLNKLEDPTAKYiiDPLKKQLEALEYIGLSYlTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEP 362
Cdd:PRK09493  89 FPHLTALENVMFGPLRVRGASKE--EAEKQARELLAKVGLAE-RAHHYPSELSGGQQQRVAIARAL--AVKPKLMLFDEP 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747191 363 SVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMgpgsgkNGGEITFEGTYNELLS 429
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFI------DKGRIAEDGDPQVLIK 225
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
266-422 1.33e-04

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: 44.18  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 266 LNSKILSSKIMSKNISDFTQ-------MTIKENLEFLNKLEDPTAKYiiDPLKKQLEALEYIGLSYLTL--NRVTTTLSG 336
Cdd:cd03234   69 FNGQPRKPDQFQKCVAYVRQddillpgLTVRETLTYTAILRLPRKSS--DAIRKKRVEDVLLRDLALTRigGNLVKGISG 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 337 GEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDP--DVIKEGDYIIDMgpgsgk 413
Cdd:cd03234  147 GERRRVSIAVQL---LWDPkVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPrsDLFRLFDRILLL------ 217

                 ....*....
gi 487747191 414 NGGEITFEG 422
Cdd:cd03234  218 SSGEIVYSG 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
610-746 1.47e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 44.43  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 610 FFDKKNDIKSkLQSVSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLI 689
Cdd:PRK13641 116 FSEDEAKEKA-LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE--ILCLDEPAAGLDPEGRKEMMQLFKDYQ 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 690 DQNNTVILIEHNLSIMceADWIIDVgpgPGLDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:PRK13641 193 KAGHTVILVTHNMDDV--AEYADDV---LVLEHGKLIKHASPKEIFSDKEWLKKHYL 244
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
632-702 1.58e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 44.92  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487747191 632 MSLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:PRK13549 135 INPATPVGNLGLGQQQLVEIAKALNKQAR--LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKL 203
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
283-411 1.64e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 44.69  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEF----LNKLEDPTAKYIidpLKKQLEALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYI 358
Cdd:PRK10851  86 FRHMTVFDNIAFgltvLPRRERPNAAAI---KAKVTQLLEMVQLAHLA-DRYPAQLSGGQKQRVALARAL--AVEPQILL 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 359 IDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVEHDPDVIKE-GDYIIDMGPGS 411
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEvADRVVVMSQGN 214
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
327-430 1.74e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 43.87  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 327 LNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVEHD-PDVIKEGDYI 404
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARAL--AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlHQVSRLSDFT 221
                         90       100
                 ....*....|....*....|....*.
gi 487747191 405 IDMGPGSGKNGGEITFeGTYNELLSS 430
Cdd:PRK14258 222 AFFKGNENRIGQLVEF-GLTKKIFNS 246
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
285-510 1.77e-04

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 44.82  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  285 QMTIKENLEFLNKLEDPTAKYIIDPLKKQLEAL-EYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLvyIIDEPS 363
Cdd:TIGR02633  92 ELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLlRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL--ILDEPS 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  364 VGLHPEDIAKINEILKSLKEKGNTVLIVEHDPD----------VIKEGDYIiDMGPGSGKNGGEITFEGTYNELLSSNTs 433
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISHKLNevkavcdticVIRDGQHV-ATKDMSTMSEDDIITMMVGREITSLYP- 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  434 tgnalRNKHNLKENIREANHFYNIGPVTQN--NLNNVKTSIPKHVLTVLTGVAGSGKSTLVKAGF----ENNDHTIFIDQ 507
Cdd:TIGR02633 248 -----HEPHEIGDVILEARNLTCWDVINPHrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFgaypGKFEGNVFING 322

                  ...
gi 487747191  508 KAV 510
Cdd:TIGR02633 323 KPV 325
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
641-741 1.93e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 43.85  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILIEHNLSIMCEADWIIdvgpgpG 719
Cdd:PRK13635 141 LSGGQKQRVAIAGVL--ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI------V 212
                         90       100
                 ....*....|....*....|..
gi 487747191 720 LDGGKVQFSGTPKNFIDSSETL 741
Cdd:PRK13635 213 MNKGEILEEGTPEEIFKSGHML 234
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
283-442 2.04e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 43.88  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEFLNKLEDPTAKYIIDPLKKqlEALEYIGL---SYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYII 359
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVE--ECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARAL--ALKPKVLLM 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 360 DEPSVGLHPEDIAKINEILKSLKEKgNTVLIVEHDP-DVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLssnTSTGNAL 438
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPqQVARVADYVAFL------YNGELVEWGSSNEIF---TSPKNEL 247

                 ....
gi 487747191 439 RNKH 442
Cdd:PRK14246 248 TEKY 251
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
613-705 2.16e-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: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KKNDIKSKLQS-VSKTGLNYMsLGQPLSTLSGGEIQRVKLGQHLDEeiKNSIFIFDEPTTGLhesDIPILMEC---FDDL 688
Cdd:cd03236  112 KKKDERGKLDElVDQLELRHV-LDRNIDQLSGGELQRVAIAAALAR--DADFYFFDEPSSYL---DIKQRLNAarlIREL 185
                         90
                 ....*....|....*..
gi 487747191 689 IDQNNTVILIEHNLSIM 705
Cdd:cd03236  186 AEDDNYVLVVEHDLAVL 202
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
327-394 2.17e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 43.62  E-value: 2.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747191 327 LNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKgNTVLIVEHD 394
Cdd:PRK14243 145 LKQSGLSLSGGQQQRLCIARAI--AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHN 209
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
332-411 2.20e-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: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 332 TTLSGGEAQRLKLIRHLNSSLSDLvyIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYIIDMGPG 410
Cdd:COG4778  151 ATFSGGEQQRVNIARGFIADPPLL--LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228

                 .
gi 487747191 411 S 411
Cdd:COG4778  229 S 229
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
635-725 2.20e-04

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: 43.23  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 635 GQPLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLH-ESDIPILMECFDDLidQNNTVILIEHNLSIMCEADWII 712
Cdd:cd03248  145 GEKGSQLSGGQKQRVAIARAL---IRNpQVLILDEATSALDaESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQIL 219
                         90
                 ....*....|...
gi 487747191 713 dvgpgpGLDGGKV 725
Cdd:cd03248  220 ------VLDGGRI 226
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
613-709 2.39e-04

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 43.56  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 613 KKNDIKSKLQSVSKTGLnymsLGQPLSTLSGGEIQRVKLGQHLDEeiKNSIFIFDEPTTGLhesDIPILMECFdDLIDQ- 691
Cdd:PRK09544  97 KKEDILPALKRVQAGHL----IDAPMQKLSGGETQRVLLARALLN--RPQLLVLDEPTQGV---DVNGQVALY-DLIDQl 166
                         90       100
                 ....*....|....*....|...
gi 487747191 692 ----NNTVILIEHNLS-IMCEAD 709
Cdd:PRK09544 167 rrelDCAVLMVSHDLHlVMAKTD 189
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
332-431 2.71e-04

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 44.39  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 332 TTLSGGEAQRLKLIRHLnssLSD-LVYIIDEPSVGLHPEdiakiNE--ILKSLKE--KGNTVLIVEHDPDVIKEGDYIID 406
Cdd:COG1132  475 VNLSGGQRQRIAIARAL---LKDpPILILDEATSALDTE-----TEalIQEALERlmKGRTTIVIAHRLSTIRNADRILV 546
                         90       100
                 ....*....|....*....|....*
gi 487747191 407 MgpgsgkNGGEITFEGTYNELLSSN 431
Cdd:COG1132  547 L------DDGRIVEQGTHEELLARG 565
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
334-431 2.72e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 44.18  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpgsg 412
Cdd:PRK13657 472 LSGGERQRLAIARAL---LKDPpILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRILVF----- 542
                         90
                 ....*....|....*....
gi 487747191 413 kNGGEITFEGTYNELLSSN 431
Cdd:PRK13657 543 -DNGRVVESGSFDELVARG 560
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
306-406 2.95e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.03  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 306 IIDPLKKQLEaLEYIglsyltLNRVTTTLSGGEAQRLK----LIRHLNsslsdlVYIIDEPSVGLhpeDIA---KINEIL 378
Cdd:PRK13409 192 KLDEVVERLG-LENI------LDRDISELSGGELQRVAiaaaLLRDAD------FYFFDEPTSYL---DIRqrlNVARLI 255
                         90       100
                 ....*....|....*....|....*...
gi 487747191 379 KSLKEkGNTVLIVEHDPDVIkegDYIID 406
Cdd:PRK13409 256 RELAE-GKYVLVVEHDLAVL---DYLAD 279
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
636-702 3.09e-04

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: 42.65  E-value: 3.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 636 QPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:cd03269  124 KRVEELSKGNQQKVQFIAAVIHDPE--LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQM 188
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
641-746 3.10e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 43.47  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILIEHNLSIMCE-ADWIIdVgpgp 718
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPE--VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARyADQIV-V---- 218
                         90       100
                 ....*....|....*....|....*...
gi 487747191 719 gLDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:PRK13634 219 -MHKGTVFLQGTPREIFADPDELEAIGL 245
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
333-430 3.29e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 43.20  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 333 TLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVEHDPDVIKEGDYIIDMgpgs 411
Cdd:PRK13648 142 ALSGGQKQRVAIAGVL--ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVM---- 215
                         90
                 ....*....|....*....
gi 487747191 412 gkNGGEITFEGTYNELLSS 430
Cdd:PRK13648 216 --NKGTVYKEGTPTEIFDH 232
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
641-746 3.33e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 43.25  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILIEHNLSIMCE-ADWIIdvgpgp 718
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQ--VLVLDEPTAGLDPQGVKELIDFLNDLPETYGmTVIFSTHQLDLVPEmADYIY------ 209
                         90       100
                 ....*....|....*....|....*...
gi 487747191 719 GLDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:PRK13652 210 VMDKGRIVAYGTVEEIFLQPDLLARVHL 237
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
284-408 3.37e-04

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: 42.48  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 284 TQMTIKENLEFLNKLEDPTAKyiidplkkqLEALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPS 363
Cdd:cd03231   86 TTLSVLENLRFWHADHSDEQV---------EEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRP--LWILDEPT 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487747191 364 VGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDY-IIDMG 408
Cdd:cd03231  154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGArELDLG 199
cbiO PRK13646
energy-coupling factor transporter ATPase;
641-746 3.79e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 43.23  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDL-IDQNNTVILIEHNLS-IMCEADWIIDvgpgp 718
Cdd:PRK13646 146 MSGGQMRKIAIVSIL--AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNeVARYADEVIV----- 218
                         90       100
                 ....*....|....*....|....*...
gi 487747191 719 gLDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:PRK13646 219 -MKEGSIVSQTSPKELFKDKKKLADWHI 245
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
465-671 3.81e-04

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 41.48  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  465 LNNVKTSIPKHVLTVLTGVAGSGKSTLVK--AGFENNDH-TIFIDQKAVQGSNRSNLLTYLGVFDSVRSYFSKETGLNKA 541
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKliAGLLSPTEgTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  542 MFSYNSKGacpncggkgyiktelafmgdfsqtcevchgkrykqevLDATIDGYSIADVLNLTvdeGIIFFDKKndikskl 621
Cdd:pfam00005  81 RLGLLLKG-------------------------------------LSKREKDARAEEALEKL---GLGDLADR------- 113
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 487747191  622 qsvsktglnymSLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTT 671
Cdd:pfam00005 114 -----------PVGERPGTLSGGQRQRVAIARALLTKPK--LLLLDEPTA 150
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
327-400 4.05e-04

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: 43.64  E-value: 4.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191  327 LNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPedIAKI---NEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPR--IVILDEPTGTMDP--ITKVdvtHSILKAREEMEQTFIIVSHDMDFVLD 493
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
629-702 4.09e-04

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 43.66  E-value: 4.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191  629 LNYMSLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:TIGR02633 130 LDADNVTRPVGDYGGGQQQLVEIAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKL 201
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
332-431 4.99e-04

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 43.47  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 332 TTLSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpg 410
Cdd:PRK11176 479 VLLSGGQRQRIAIARAL---LRDSpILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEKADEILVV--- 551
                         90       100
                 ....*....|....*....|.
gi 487747191 411 sgkNGGEITFEGTYNELLSSN 431
Cdd:PRK11176 552 ---EDGEIVERGTHAELLAQN 569
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
633-712 5.54e-04

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 43.36  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 633 SLGQPLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLhesDIPILMECFD---DLIDQNNTVILIEHNL-SIMCEA 708
Cdd:PRK11288 389 SREQLIMNLSGGNQQKAILGRWLSEDMK--VILLDEPTRGI---DVGAKHEIYNviyELAAQGVAVLFVSSDLpEVLGVA 463

                 ....
gi 487747191 709 DWII 712
Cdd:PRK11288 464 DRIV 467
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
628-701 5.60e-04

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 5.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 628 GLNYMSLGQPLSTLSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNN-TVILIEHN 701
Cdd:COG4619  118 GLPPDILDKPVERLSGGERQRLALIRAL--LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGrAVLWVSHD 190
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
332-431 5.67e-04

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: 42.22  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 332 TTLSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKeKGNTVLIVEHDPDVIKEGDYIIDMgpg 410
Cdd:cd03251  137 VKLSGGQRQRIAIARAL---LKDPpILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVVL--- 209
                         90       100
                 ....*....|....*....|.
gi 487747191 411 sgkNGGEITFEGTYNELLSSN 431
Cdd:cd03251  210 ---EDGKIVERGTHEELLAQG 227
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
636-741 5.95e-04

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 42.91  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 636 QPLSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVg 715
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQA--TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVL- 211
                         90       100
                 ....*....|....*....|....*.
gi 487747191 716 pgpgLDGGKVQFSGTPKNFIdSSETL 741
Cdd:PRK09536 212 ----LADGRVRAAGPPADVL-TADTL 232
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
641-725 6.13e-04

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 42.11  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLhesDIPI---LMECFDDLIDQNN-TVILIEHNLSIMCE-ADWIIdVg 715
Cdd:cd03257  146 LSGGQRQRVAIARALALNPK--LLIADEPTSAL---DVSVqaqILDLLKKLQEELGlTLLFITHDLGVVAKiADRVA-V- 218
                         90
                 ....*....|
gi 487747191 716 pgpgLDGGKV 725
Cdd:cd03257  219 ----MYAGKI 224
cbiO PRK13641
energy-coupling factor transporter ATPase;
312-407 6.26e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 42.51  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 312 KQLEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIV 391
Cdd:PRK13641 124 KALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM--AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILV 201
                         90
                 ....*....|....*.
gi 487747191 392 EHDPDVIKEgdYIIDM 407
Cdd:PRK13641 202 THNMDDVAE--YADDV 215
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
602-736 6.52e-04

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 43.11  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  602 LTVDEGIIF---FDKKNDI--KSKLQSVSKTgLNYMSL--------GQP--LSTLSGGEIQRVKLGqhldEEIKN--SIF 664
Cdd:TIGR00955 114 LTVREHLMFqahLRMPRRVtkKEKRERVDEV-LQALGLrkcantriGVPgrVKGLSGGERKRLAFA----SELLTdpPLL 188
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191  665 IFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLS--IMCEADWIIdvgpgpGLDGGKVQFSGTPKNFID 736
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSseLFELFDKII------LMAEGRVAYLGSPDQAVP 256
cbiO PRK13637
energy-coupling factor transporter ATPase;
641-743 6.55e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 42.34  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQ-NNTVILIEHNLSIMCE-ADWIIdvgpgp 718
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPK--ILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKlADRII------ 216
                         90       100
                 ....*....|....*....|....*
gi 487747191 719 GLDGGKVQFSGTPKNFIDSSETLTS 743
Cdd:PRK13637 217 VMNKGKCELQGTPREVFKEVETLES 241
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
285-406 7.11e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 42.51  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 285 QMTIKENLEFLNK---LEDPTAKYIIDPLkkqleaLEYIGLSYLTLNRVTTtLSGGEAQRLKLIRHLnssLSD-LVYIID 360
Cdd:PRK13536 128 EFTVRENLLVFGRyfgMSTREIEAVIPSL------LEFARLESKADARVSD-LSGGMKRRLTLARAL---INDpQLLILD 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487747191 361 EPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHdpdVIKEGDYIID 406
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTH---FMEEAERLCD 240
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
287-411 7.16e-04

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: 41.93  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 287 TIKENLEFLNKLEDPTAKYIIDP--LKKQLEALEYIGLSylTLNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEP-- 362
Cdd:cd03290   94 TVEENITFGSPFNKQRYKAVTDAcsLQPDIDLLPFGDQT--EIGERGINLSGGQRQRICVARALYQNTN--IVFLDDPfs 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 487747191 363 SVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDYIIDMGPGS 411
Cdd:cd03290  170 ALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
480-726 7.53e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 42.74  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 480 LTGVAGSGKSTLVK--AGFE---------NNDHTI-FIDQKAVQGSNRSnlltylgVFDSVRSYFSKETGLNKAMFSYNS 547
Cdd:COG0488   29 LVGRNGAGKSTLLKilAGELepdsgevsiPKGLRIgYLPQEPPLDDDLT-------VLDTVLDGDAELRALEAELEELEA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 548 KGACPNCGGKGYikTELafmgdfsqtcevchgkrykQEVLDAtIDGYsiadvlnltvdegiiffdkknDIKSKLQSV-SK 626
Cdd:COG0488  102 KLAEPDEDLERL--AEL-------------------QEEFEA-LGGW---------------------EAEARAEEIlSG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 627 TGLNYMSLGQPLSTLSGGEIQRVKLGQHLdeeIKNS-IFIFDEPTTGLhesDIP-IL-MECFddLIDQNNTVILIEH--- 700
Cdd:COG0488  139 LGFPEEDLDRPVSELSGGWRRRVALARAL---LSEPdLLLLDEPTNHL---DLEsIEwLEEF--LKNYPGTVLVVSHdry 210
                        250       260
                 ....*....|....*....|....*....
gi 487747191 701 ---NLsimceADWIIDvgpgpgLDGGKVQ 726
Cdd:COG0488  211 fldRV-----ATRILE------LDRGKLT 228
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
640-747 7.59e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.09  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  640 TLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQ-NNTVILIEHNLSIMCEADWIIdVGPGP 718
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPK--ILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASIKRSDKIV-VFNNP 1434
                          90       100
                  ....*....|....*....|....*....
gi 487747191  719 GLDGGKVQFSGTPKNFIDSSETLTSKHLK 747
Cdd:PTZ00265 1435 DRTGSFVQAHGTHEELLSVQDGVYKKYVK 1463
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
334-400 7.70e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 41.92  E-value: 7.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 334 LSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:PRK13638 137 LSHGQKKRVAIAGAL--VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYE 201
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
334-394 8.24e-04

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 41.66  E-value: 8.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487747191 334 LSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD 394
Cdd:PRK11264 145 LSGGQQQRVAIARAL--AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
327-400 8.70e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.49  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 327 LNRVTTTLSGGEAQRLKLirHLNSSLSDLV----------YIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPD 396
Cdd:cd03279  117 LARPVSTLSGGETFLASL--SLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEE 194

                 ....
gi 487747191 397 vIKE 400
Cdd:cd03279  195 -LKE 197
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
551-580 9.84e-04

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 38.01  E-value: 9.84e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 487747191 551 CPNCGGKGYIKTELAFMGDF---SQTCEVCHGK 580
Cdd:cd10719   18 CPTCGGSGQVRQVQGTGFGFfqtQTTCPTCGGT 50
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
641-714 9.93e-04

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 40.66  E-value: 9.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 641 LSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDV 714
Cdd:cd03246   97 LSGGQRQRLGLARAL---YGNpRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
639-731 1.06e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 42.46  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 639 STLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL---HESDIpilMECFDDLIdQNNTVILIEHNLS-IMcEADWIId 713
Cdd:COG1132  475 VNLSGGQRQRIAIARAL---LKDpPILILDEATSALdteTEALI---QEALERLM-KGRTTIVIAHRLStIR-NADRIL- 545
                         90
                 ....*....|....*...
gi 487747191 714 VgpgpgLDGGKVQFSGTP 731
Cdd:COG1132  546 V-----LDDGRIVEQGTH 558
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
551-589 1.07e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 42.06  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 487747191 551 CPNCGGKGYIKTELAFMgDFSQTCEVCHGKRYKQEVLDA 589
Cdd:PRK14291 176 CPTCGGSGEIYQRGGFF-RISQTCPTCGGEGVLREPCSK 213
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
315-395 1.14e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 41.30  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYlTLNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSL-KEKGNTVLIVEH 393
Cdd:PRK10584 129 ALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPD--VLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205

                 ..
gi 487747191 394 DP 395
Cdd:PRK10584 206 DL 207
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
285-422 1.25e-03

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: 41.02  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 285 QMTIKENLEF---LNKLEDPTAKYIIDplkkqlEALEYIGLsYLTLNRVTTTLSGGEAQRLKLIRHLnssLSD-LVYIID 360
Cdd:cd03264   86 NFTVREFLDYiawLKGIPSKEVKARVD------EVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQAL---VGDpSILIVD 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747191 361 EPSVGLHPEDIAKINEILKSLKEkGNTVLIVEHD-PDVIKEGDYIIDMgpgsgkNGGEITFEG 422
Cdd:cd03264  156 EPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIvEDVESLCNQVAVL------NKGKLVFEG 211
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
314-399 1.31e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 42.00  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 314 LEALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVE 392
Cdd:PRK15134 406 IAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARAL--ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFIS 483

                 ....*..
gi 487747191 393 HDPDVIK 399
Cdd:PRK15134 484 HDLHVVR 490
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
315-430 1.37e-03

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: 41.81  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLnsSLS-DLVyIIDEPSVGLHPEDIAKINEILKSLKEKGN-TVLIVE 392
Cdd:COG1123  386 ELLERVGLPPDLADRYPHELSGGQRQRVAIARAL--ALEpKLL-ILDEPTSALDVSVQAQILNLLRDLQRELGlTYLFIS 462
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 487747191 393 HDPDVIKE-GDYIIDMgpgsgkNGGEITFEGTYNELLSS 430
Cdd:COG1123  463 HDLAVVRYiADRVAVM------YDGRIVEDGPTEEVFAN 495
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
296-430 1.41e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 41.13  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 296 NKLEDPTA-KYIIDPLKKQLEALEYiglsyltLNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKI 374
Cdd:PRK13632 111 NKKVPPKKmKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDPKGKREI 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487747191 375 NEILKSLKEKGNTVLI-VEHDPDVIKEGDYIIDMgpgsgkNGGEITFEGTYNELLSS 430
Cdd:PRK13632 182 KKIMVDLRKTRKKTLIsITHDMDEAILADKVIVF------SEGKLIAQGKPKEILNN 232
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
636-717 1.48e-03

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 42.02  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 636 QPlSTLSGGEIQRVKLGQHLDEeiKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEADWIIDVG 715
Cdd:PRK10535 141 QP-SQLSGGQQQRVSIARALMN--GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIR 217

                 ..
gi 487747191 716 PG 717
Cdd:PRK10535 218 DG 219
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
594-747 1.61e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 40.99  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 594 YSIADVLNLTVDEGIIFFDKKNDI--KSKLQSVS----------------------KTGLNYMSlGQPLSTLSGGEIQRV 649
Cdd:PRK13636  72 YSRKGLMKLRESVGMVFQDPDNQLfsASVYQDVSfgavnlklpedevrkrvdnalkRTGIEHLK-DKPTHCLSFGQKKRV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 650 KLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILI-EHNLSIM---CEADWIidvgpgpgLDGGKV 725
Cdd:PRK13636 151 AIAGVLVMEPK--VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVplyCDNVFV--------MKEGRV 220
                        170       180
                 ....*....|....*....|..
gi 487747191 726 QFSGTPKNFIDSSETLTSKHLK 747
Cdd:PRK13636 221 ILQGNPKEVFAEKEMLRKVNLR 242
cbiO PRK13643
energy-coupling factor transporter ATPase;
641-746 1.69e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 41.26  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCE-ADWIIdvgpgpG 719
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPE--VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVY------L 216
                         90       100
                 ....*....|....*....|....*..
gi 487747191 720 LDGGKVQFSGTPKNFIDSSETLTSKHL 746
Cdd:PRK13643 217 LEKGHIISCGTPSDVFQEVDFLKAHEL 243
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
327-394 1.74e-03

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 40.69  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747191 327 LNRVTTTLSGGEAQRLKLI-------RHLNSSlSDLVyIIDEPSVGLhpeDIAKIN---EILKSLKEKGNTVLIVEHD 394
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAavvlqvwPDINPA-GQLL-LLDEPMNSL---DVAQQAaldRLLSELCQQGIAVVMSSHD 192
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
614-747 1.79e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 40.83  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 614 KNDIKSKLQSVSKTGLNymslGQPLSTLSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNN 693
Cdd:PRK13639 115 EKRVKEALKAVGMEGFE----NKPPHHLSGGQKKRVAIAGIL--AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGI 188
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 487747191 694 TVILIEHNLSIMCEADWIIDVgpgpgLDGGKVQFSGTPKNFIDSSETLTSKHLK 747
Cdd:PRK13639 189 TIIISTHDVDLVPVYADKVYV-----MSDGKIIKEGTPKEVFSDIETIRKANLR 237
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
283-411 1.80e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 41.69  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLEFLNKLEDptAKY-----IIDPLKKQL---EALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSd 354
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKD--GGYkgamgLFHEVDEQRtaeNQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE- 429
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 487747191 355 lVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD-PDVIKEGDYIIDMGPGS 411
Cdd:PRK09700 430 -VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGR 486
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
600-736 1.98e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 40.97  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 600 LNLTVDEGIIFFDKKNDIKSK-LQSVSKTGLNYMSLGQ----PLSTLSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLH 674
Cdd:PRK13536 127 LEFTVRENLLVFGRYFGMSTReIEAVIPSLLEFARLESkadaRVSDLSGGMKRRLTLARALINDPQ--LLILDEPTTGLD 204
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 675 ESDIPILMECFDDLIDQNNTVILIEHnlsIMCEADWIID---VgpgpgLDGGKVQFSGTPKNFID 736
Cdd:PRK13536 205 PHARHLIWERLRSLLARGKTILLTTH---FMEEAERLCDrlcV-----LEAGRKIAEGRPHALID 261
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
8-41 1.99e-03

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: 39.67  E-value: 1.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 487747191   8 GASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLV 41
Cdd:cd03228   12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
601-733 2.08e-03

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 40.40  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 601 NLTVDEGIIF------FDKKNDIKSKLQSVSKTGLNYMsLGQPLSTLSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGL- 673
Cdd:cd03299   85 HMTVYKNIAYglkkrkVDKKEIERKVLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARAL--VVNPKILLLDEPFSALd 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747191 674 ---HESdipiLMECFDDLIDQNN-TVILIEHNLSimcEADWIID-VGPgpgLDGGKVQFSGTPKN 733
Cdd:cd03299  162 vrtKEK----LREELKKIRKEFGvTVLHVTHDFE---EAWALADkVAI---MLNGKLIQVGKPEE 216
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
328-397 2.11e-03

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 41.37  E-value: 2.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 328 NRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDV 397
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATP--VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
636-673 2.19e-03

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: 40.25  E-value: 2.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 487747191 636 QPLSTLSGGEIQRVKLGQHLdeeIKN-SIFIFDEPTTGL 673
Cdd:cd03264  126 KKIGSLSGGMRRRVGIAQAL---VGDpSILIVDEPTAGL 161
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
332-431 2.25e-03

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 41.26  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  332 TTLSGGEAQRLKLIRHLnssLSDL-VYIIDEPSVGLHPEDIAKINEILKSLKEKgnTVLIVEHDPDVIKEGDYIIDMgpg 410
Cdd:TIGR01193 610 SSISGGQKQRIALARAL---LTDSkVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDKIIVL--- 681
                          90       100
                  ....*....|....*....|.
gi 487747191  411 sgkNGGEITFEGTYNELLSSN 431
Cdd:TIGR01193 682 ---DHGKIIEQGSHDELLDRN 699
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
300-393 2.61e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 41.17  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 300 DPTAKYIIDP--LKKQLEAL--EYiGLSyLTLNRVTTTLSGGEAQR---LK-LIRHlnsslSDLVyIIDEPSVGLHPEDI 371
Cdd:COG3845  106 EPTKGGRLDRkaARARIRELseRY-GLD-VDPDAKVEDLSVGEQQRveiLKaLYRG-----ARIL-ILDEPTAVLTPQEA 177
                         90       100
                 ....*....|....*....|..
gi 487747191 372 AKINEILKSLKEKGNTVLIVEH 393
Cdd:COG3845  178 DELFEILRRLAAEGKSIIFITH 199
cbiO PRK13649
energy-coupling factor transporter ATPase;
315-413 2.62e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 40.50  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSDLVyiIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEH- 393
Cdd:PRK13649 127 EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILV--LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHl 204
                         90       100
                 ....*....|....*....|....*
gi 487747191 394 -DpDVIKEGDYIIDMGPG----SGK 413
Cdd:PRK13649 205 mD-DVANYADFVYVLEKGklvlSGK 228
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
634-730 2.64e-03

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: 40.89  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKL-----GqhldeeiKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNLSIMCEA 708
Cdd:COG4618  461 IGEGGARLSGGQRQRIGLaralyG-------DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV 533
                         90       100
                 ....*....|....*....|..
gi 487747191 709 DWIIdVgpgpgLDGGKVQFSGT 730
Cdd:COG4618  534 DKLL-V-----LRDGRVQAFGP 549
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
286-409 2.68e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 39.86  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 286 MTIKENLEFLNKLEDPTAKYIidplkkqLEALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVG 365
Cdd:PRK13539  88 LTVAENLEFWAAFLGGEELDI-------AAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRP--IWILDEPTAA 157
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 487747191 366 LHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKEGDyIIDMGP 409
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPGAR-ELDLGP 200
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
154-247 2.89e-03

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 37.84  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191  154 DWDKSLNEGAIdfPSFGPDKER---------GKAYRdsglFDNNKKLKDYTKDELELFLY-----QEPMTLKNPPKEWRK 219
Cdd:pfam17755   8 DPSLSLAEGAI--APWGKKRSSyyfqllealAKHYG----FDLDTPFKDLPEEQQDIILYgsgeeIIVFYYSRGGRTRTY 81
                          90       100
                  ....*....|....*....|....*....
gi 487747191  220 SAKYVGLIPRFSRIFL-GDKEFNKKRYAK 247
Cdd:pfam17755  82 TKPFEGVIPNLERRYReTDSESVREELEK 110
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
639-738 3.00e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 40.08  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 639 STLSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGL-----HEsdipiLMECFDDLIDQNNTVILIEHnlsimcEADWIID 713
Cdd:PRK09493 135 SELSGGQQQRVAIARAL--AVKPKLMLFDEPTSALdpelrHE-----VLKVMQDLAEEGMTMVIVTH------EIGFAEK 201
                         90       100
                 ....*....|....*....|....*.
gi 487747191 714 VGPG-PGLDGGKVQFSGTPKNFIDSS 738
Cdd:PRK09493 202 VASRlIFIDKGRIAEDGDPQVLIKNP 227
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
641-707 3.27e-03

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: 39.79  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747191 641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLhesDIPI---LMECFDDLIDQNN-TVILIEHNLSI---MCE 707
Cdd:COG1124  139 LSGGQRQRVAIARAL--ILEPELLLLDEPTSAL---DVSVqaeILNLLKDLREERGlTYLFVSHDLAVvahLCD 207
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
283-391 3.62e-03

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 40.39  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKENLeFLNKLEDPTAKYIIDPLKKQLEALEYI---GLSYLTLNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYII 359
Cdd:COG1129  342 VLDLSIRENI-TLASLDRLSRGGLLDRRRERALAEEYIkrlRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPK--VLIL 418
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 487747191 360 DEPSVGLhpeDI-AK--INEILKSLKEKGNTVLIV 391
Cdd:COG1129  419 DEPTRGI---DVgAKaeIYRLIRELAAEGKAVIVI 450
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
641-741 3.70e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 39.97  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 641 LSGGEIQRVKLGQHLdeEIKNSIFIFDEPTTGLH---ESDIPILMecfDDLIDQNN-TVILIEHNLSIMCEADWIIdvgp 716
Cdd:PRK13632 143 LSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDpkgKREIKKIM---VDLRKTRKkTLISITHDMDEAILADKVI---- 213
                         90       100
                 ....*....|....*....|....*
gi 487747191 717 gpGLDGGKVQFSGTPKNFIDSSETL 741
Cdd:PRK13632 214 --VFSEGKLIAQGKPKEILNNKEIL 236
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
639-712 3.85e-03

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: 39.40  E-value: 3.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747191 639 STLSGGEIQRVKLGQHLdeeIKNSIFIF-DEPTTGLHESDIPILMECFDDLIDQ-NNTVILIEHNLSIMCEADWII 712
Cdd:cd03255  139 SELSGGQQQRVAIARAL---ANDPKIILaDEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRII 211
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
356-400 3.85e-03

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 39.68  E-value: 3.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 487747191 356 VYIIDEP-SVGlhpeDIA---KINEILKSLKEKGNTVLIVEHDPDVIKE 400
Cdd:COG1134  167 ILLVDEVlAVG----DAAfqkKCLARIRELRESGRTVIFVSHSMGAVRR 211
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
311-394 4.04e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 39.41  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 311 KKQLEALEYIGLSYLTLNRvTTTLSGGEAQRLKLIRHLNSSLSdLVyIIDEPSVGLHPEDIAKINEILKSL-KEKGNTVL 389
Cdd:PRK11629 124 SRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPR-LV-LADEPTGNLDARNADSIFQLLGELnRLQGTAFL 200

                 ....*
gi 487747191 390 IVEHD 394
Cdd:PRK11629 201 VVTHD 205
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
634-730 4.23e-03

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: 39.52  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 634 LGQPLSTLSGGEIQRVKLGQHLdeeIKNS-IFIFDEPTTGL-HESDIPIlMECFDDLIdQNNTVILIEHNLSIMCEADWI 711
Cdd:cd03251  132 IGERGVKLSGGQRQRIAIARAL---LKDPpILILDEATSALdTESERLV-QAALERLM-KNRTTFVIAHRLSTIENADRI 206
                         90
                 ....*....|....*....
gi 487747191 712 IdVgpgpgLDGGKVQFSGT 730
Cdd:cd03251  207 V-V-----LEDGKIVERGT 219
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
334-393 4.46e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 39.76  E-value: 4.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 334 LSGGEAQRLKLIRHLnsSLSDLVYIIDEPSVGLHPEDIAKINEILKSLKEKgNTVLIVEH 393
Cdd:PRK14239 149 LSGGQQQRVCIARVL--ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTR 205
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
332-411 5.36e-03

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 38.99  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 332 TTLSGGEAQRLKLIRHLNSSlSDlVYIIDEP------SVGLHpedIAKiNEILKSLKeKGNTVLIVEHDPDVIKEGDYII 405
Cdd:cd03250  126 INLSGGQKQRISLARAVYSD-AD-IYLLDDPlsavdaHVGRH---IFE-NCILGLLL-NNKTRILVTHQLQLLPHADQIV 198

                 ....*.
gi 487747191 406 DMGPGS 411
Cdd:cd03250  199 VLDNGR 204
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
634-736 5.69e-03

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 40.31  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191   634 LGQPLSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPttgLHESDIPILMECFDDLID-----QNNTVILIEHNLSIMCEA 708
Cdd:TIGR00957  754 IGEKGVNLSGGQKQRVSLARAVYSN--ADIYLFDDP---LSAVDAHVGKHIFEHVIGpegvlKNKTRILVTHGISYLPQV 828
                           90       100
                   ....*....|....*....|....*...
gi 487747191   709 DWIIdvgpgpGLDGGKVQFSGTPKNFID 736
Cdd:TIGR00957  829 DVII------VMSGGKISEMGSYQELLQ 850
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
283-394 6.28e-03

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


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 38.86  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 283 FTQMTIKEN----LEFLNKLEDPTAKYIidpLKKQLEALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLnsSLSDLVYI 358
Cdd:cd03296   86 FRHMTVFDNvafgLRVKPRSERPPEAEI---RAKVHELLKLVQLDWLA-DRYPAQLSGGQRQRVALARAL--AVEPKVLL 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 487747191 359 IDEPSVGLHpediAKINEILKSL-----KEKGNTVLIVEHD 394
Cdd:cd03296  160 LDEPFGALD----AKVRKELRRWlrrlhDELHVTTVFVTHD 196
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
624-702 6.47e-03

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 39.18  E-value: 6.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747191 624 VSKTGLNYMSLGQPLSTLSGGEIQRVKLGQHLDEEikNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHNL 702
Cdd:PRK10619 136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME--PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
356-405 6.78e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 39.33  E-value: 6.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487747191 356 VYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHDPDVIKE-GDYII 405
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVI 209
DUF5351 pfam17302
Family of unknown function (DUF5351); This family of unknown function is found in Bacillales.
551-580 7.49e-03

Family of unknown function (DUF5351); This family of unknown function is found in Bacillales.


Pssm-ID: 435851 [Multi-domain]  Cd Length: 29  Bit Score: 34.49  E-value: 7.49e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 487747191  551 CPNCGGKGYIKTELafmgDFSQTCEVCHGK 580
Cdd:pfam17302   1 CPYCKGKGYVQLLL----GGSETCPNCEGT 26
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
8-41 7.62e-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: 39.82  E-value: 7.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 487747191   8 GASQNNLKNIDVNIPKHLVTVFTGRSGSGKSSLV 41
Cdd:COG2274  485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
315-405 9.80e-03

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 38.71  E-value: 9.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 315 EALEYIGLSYLTlNRVTTTLSGGEAQRLKLIRHLNSSLSdlVYIIDEPSVGLHPEDIAKINEILKSLKEKGNTVLIVEHD 394
Cdd:PRK15056 125 AALARVDMVEFR-HRQIGELSGGQKKRVFLARAIAQQGQ--VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
                         90
                 ....*....|..
gi 487747191 395 PDVIKE-GDYII 405
Cdd:PRK15056 202 LGSVTEfCDYTV 213
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
641-708 9.92e-03

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 38.95  E-value: 9.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747191 641 LSGGEIQRVKLGQHLDEEIKnsIFIFDEPTTGLhesDIPILMECFDDLID----QNNTVILIEHNLSIMCEA 708
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPK--LLIADEPTTAL---DVTIQAQIIELLLElqqkENMALVLITHDLALVAEA 220
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
593-701 9.99e-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: 37.89  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747191 593 GYSIADVLNLTVDEGIIFFDKKNDIKSKLQSVSKTGLnYMSLGQPLS---------------TLSGGEIQRVKLGQHLde 657
Cdd:cd03217   43 AKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGI-FLAFQYPPEipgvknadflryvneGFSGGEKKRNEILQLL-- 119
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 487747191 658 EIKNSIFIFDEPTTGLHESDIPILMECFDDLIDQNNTVILIEHN 701
Cdd:cd03217  120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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