|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
46-649 |
7.43e-145 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 434.47 E-value: 7.43e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 46 VKVKSGFLPGRKPvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARkDPSGL--SGDVLINGalRPTNFKC--- 119
Cdd:TIGR00955 24 VSRLRGCFCRERP-RKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFR-SPKGVkgSGSVLLNG--MPIDAKEmra 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 120 NSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQ-FIRGVSGGERKRTSIGM 198
Cdd:TIGR00955 100 ISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFE 278
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 279 SAGYHCEAYNNPADFFLDIIngdstAVALNREEDFKATeiiepskrdkplIEKLAEIYVDSSFYKETKAELHQLSGGEKK 358
Cdd:TIGR00955 260 DLGHPCPENYNPADFYVQVL-----AVIPGSENESRER------------IEKICDSFAVSDIGRDMLVNTNLWSGKAGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 359 --KKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVILGLVIGAIYFGLNNDSTGIQNRAGVLFFLTTN 436
Cdd:TIGR00955 323 lvKDSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 437 QCFSSV-SAVELFVVEKKLFIHEYISGYYRVSSYFFGKLLSDLLPMRMLPsIIFTCIVYFMLGLKPTADAFFIMMFTLMM 515
Cdd:TIGR00955 403 MTFQNVfPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILP-ALFTSITYWMIGLRSGATHFLTFLFLVTL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 516 VAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGL 595
Cdd:TIGR00955 482 VANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECT 561
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 596 NATVNNTCNYatcTGEEYLTKQGIDLSPwgLWKNHVALACMIVIFLTIAYLKLL 649
Cdd:TIGR00955 562 SANTTGPCPS---SGEVILETLSFRNAD--LYLDLIGLVILIFFFRLLAYFALR 610
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-652 |
5.84e-93 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 301.03 E-value: 5.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRVKVKSGF--------LPGRKPV---------EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKD 98
Cdd:PLN03211 40 LKFMDVCYRVKFENMKnkgsnikrILGHKPKisdetrqiqERTILNGVTGMASPGeILAVLGPSGSGKSTLLNALAGRIQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 99 PSGLSGDVLINGALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKV 178
Cdd:PLN03211 120 GNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTII 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 179 GTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTL 258
Cdd:PLN03211 200 GNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 259 LASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGdstavalnreedfkATEIIEPSKRDKPLIEKLAEIYVD 338
Cdd:PLN03211 280 LSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANG--------------VCQTDGVSEREKPNVKQSLVASYN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 339 SSFYKETKAELHQLSGGEKKKKITV---FKE------ISYTTSFcHQLRWVSKRSFK-------NLLgnpqaSIAQIIVT 402
Cdd:PLN03211 346 TLLAPKVKAAIEMSHFPQANARFVGsasTKEhrssdrISISTWF-NQFSILLQRSLKerkhesfNTL-----RVFQVIAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 403 VILGlviGAIYFglNNDSTGIQNRAGVLFFLTTN-QCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKLLSDlLPM 481
Cdd:PLN03211 420 ALLA---GLMWW--HSDFRDVQDRLGLLFFISIFwGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGD-LPM 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 482 RMLPSIIFTCIVYFMLGLKPTADAFFIMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNltTI 561
Cdd:PLN03211 494 ELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVH--KL 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 562 ASWLSWLQYFSIPRYGFTAL---QHNEflGQNFCPGLNATVNNTCNYATCTGEEylTKQGIDLSPwglWKNHVALACMIV 638
Cdd:PLN03211 572 PSCMAWIKYISTTFYSYRLLinvQYGE--GKRISSLLGCSLPHGSDRASCKFVE--EDVAGQISP---ATSVSVLIFMFV 644
|
650
....*....|....
gi 1622936545 639 IFLTIAYLKLLFLK 652
Cdd:PLN03211 645 GYRLLAYLALRRIK 658
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-568 |
1.89e-86 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 295.48 E-value: 1.89e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 26 NDRK---AFTEGAVLSFHNICYRVKVKSGflpgrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDpSG 101
Cdd:TIGR00956 746 NDEKdmeKESGEDIFHWRNLTYEVKIKKE--------KRVILNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVT-TG 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 102 L--SGDVLINGALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVG 179
Cdd:TIGR00956 817 VitGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVG 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 180 TQFIrGVSGGERKRTSIGMELITDP-SILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTL 258
Cdd:TIGR00956 897 VPGE-GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLL 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 259 LASG-RLMFHGP----AQEALGYFESAGYH-CEAYNNPADFFLDIINGDSTAVAlnrEEDFkateiiepskrdkpliekl 332
Cdd:TIGR00956 976 LQKGgQTVYFGDlgenSHTIINYFEKHGAPkCPEDANPAEWMLEVIGAAPGAHA---NQDY------------------- 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 333 AEIYVDSSFYKETKAELHQ----LSGGEKKKKITVFKEisYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVILGLV 408
Cdd:TIGR00956 1034 HEVWRNSSEYQAVKNELDRleaeLSKAEDDNDPDALSK--YAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALF 1111
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 409 IGAIYFGLNNDSTGIQNRAG-----VLFFLTTNQcfssvSAVELFVVEKKLF-IHEYISGYYRVSSYFFGKLLSDlLPMR 482
Cdd:TIGR00956 1112 IGFTFFKVGTSLQGLQNQMFavfmaTVLFNPLIQ-----QYLPPFVAQRDLYeVRERPSRTFSWLAFIAAQITVE-IPYN 1185
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 483 MLPSIIFTCIVYFMLGLKPTA-------DAFFIMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLL 555
Cdd:TIGR00956 1186 LVAGTIFFFIWYYPVGFYWNAsktgqvhERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVL 1265
|
570
....*....|...
gi 1622936545 556 VNLTTIASWLSWL 568
Cdd:TIGR00956 1266 APPSRMPGFWIFM 1278
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-268 |
3.80e-86 |
|
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: 267.88 E-value: 3.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 34 GAVLSFHNICYRVKvksgflPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGA- 111
Cdd:cd03213 1 GVTLSFRNLTVTVK------SSPSKSGKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 LRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlpttmtnheknerinrviqelgldkvadskvgtqfirGVSGGER 191
Cdd:cd03213 75 LDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGER 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 192 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
51-652 |
1.35e-81 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 281.61 E-value: 1.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 51 GFLPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPS--GLSGDVLINGaLRPTNFK----CNSGY 123
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASNTDGFhiGVEGVITYDG-ITPEEIKkhyrGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 124 VVQDDVVMGTLTVRENLQFSAALRLPTT-MTNHEKNERINRV----IQELGLDKVADSKVGTQFIRGVSGGERKRTSIGM 198
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKTPQNrPDGVSREEYAKHIadvyMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF-SIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYF 277
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 278 ESAGYHCEAYNNPADFFldiingdsTAVALNREE----DFKATEIIEPSK-----RDKP----LIEKLAEIYVDSSFY-- 342
Cdd:TIGR00956 303 EKMGFKCPDRQTTADFL--------TSLTSPAERqikpGYEKKVPRTPQEfetywRNSPeyaqLMKEIDEYLDRCSESdt 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 343 KETKAELHQlsgGEKKKKITVFKeiSYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVILGLVIGAIYFGLNNDSTG 422
Cdd:TIGR00956 375 KEAYRESHV---AKQSKRTRPSS--PYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 423 IQNRAGVLFFLTTNQCFSSVSavELFVVEKKLFIHEYISGY--YRVSSYFFGKLLSDlLPMRMLPSIIFTCIVYFMLGLK 500
Cdd:TIGR00956 450 FYSRGGALFFAILFNAFSSLL--EIASMYEARPIVEKHRKYalYHPSADAIASIISE-IPFKIIESVVFNIILYFMVNFR 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 501 PTADAFFIMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTA 580
Cdd:TIGR00956 527 RTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFES 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 581 LQHNEFLG-----QNFCPGLNATVNNTCNYATCT------------GEEYLtKQGIDLSPWGLWKNHVALACMIVIFLTI 643
Cdd:TIGR00956 607 LMVNEFHGrrfecSQYVPSGGGYDNLGVTNKVCTvvgaepgqdyvdGDDYL-KLSFQYYNSHKWRNFGIIIGFTVFFFFV 685
|
....*....
gi 1622936545 644 AYLKLLFLK 652
Cdd:TIGR00956 686 YILLTEFNK 694
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
56-268 |
9.32e-67 |
|
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: 218.29 E-value: 9.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 56 RKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSG-LSGDVLING-ALRPTNFKCNSGYVVQDDVVMG 132
Cdd:cd03234 15 NWNKYARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGqPRKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSAALRLPttmtNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:cd03234 95 GLTVRETLTYTAILRLP----RKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 213 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-262 |
1.83e-63 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 208.25 E-value: 1.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 34 GAVLSFHNICYRVKVKSGflpgrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAL 112
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG--------KRQLLNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 113 RPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALrlpttmtnheknerinrviqelgldkvadskvgtqfiRGVSGGERK 192
Cdd:cd03232 73 LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALL-------------------------------------RGLSVEQRK 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 193 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASG 262
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
62-573 |
4.65e-58 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 212.40 E-value: 4.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLING-ALRPTNFKCNSGYVVQDDVVMGTLTVREN 139
Cdd:PLN03140 894 QLLREVTGAFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGfPKKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 140 LQFSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:PLN03140 974 LIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 220 TANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLA-SGRLMFHGP----AQEALGYFES---AGYHCEAYnNPA 291
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPlgrnSHKIIEYFEAipgVPKIKEKY-NPA 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 292 DFFLDIingDSTAVALNREEDFkateiiepskrdkplieklAEIYVDSSFYKETKAELHQLSGGEKKKKITVFkEISYTT 371
Cdd:PLN03140 1133 TWMLEV---SSLAAEVKLGIDF-------------------AEHYKSSSLYQRNKALVKELSTPPPGASDLYF-ATQYSQ 1189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 372 SFCHQLR-------WVSKRSfknllgnPQASIAQIIVTVILGLVIGAIYF--GLNNDSTG-----IQNRAGVLFFLTTNQ 437
Cdd:PLN03140 1190 STWGQFKsclwkqwWTYWRS-------PDYNLVRFFFTLAAALMVGTIFWkvGTKRSNANdltmvIGAMYAAVLFVGINN 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 438 CfSSVSAVelFVVEKKLFIHEYISGYYRVSSYFFGKLLSDlLPMRMLPSIIFTCIVYFMLGLKPTADAF----FIMMFTL 513
Cdd:PLN03140 1263 C-STVQPM--VAVERTVFYRERAAGMYSALPYAIAQVVCE-IPYVLIQTTYYTLIVYAMVAFEWTAAKFfwfyFISFFSF 1338
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 514 MMVAYSAsSMALAIAAGQsvvSVATLLMTICFVFMMIFSGLLVNLTTIASWlsWLQYFSI 573
Cdd:PLN03140 1339 LYFTYYG-MMTVSLTPNQ---QVAAIFAAAFYGLFNLFSGFFIPRPKIPKW--WVWYYWI 1392
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
63-651 |
2.92e-48 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 183.12 E-value: 2.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPS-GLSGDVLINGaLRPTNF--KCNSGYVVQDDVVMGTLTVRE 138
Cdd:PLN03140 180 ILKDASGIIKPSrMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNG-YRLNEFvpRKTSAYISQNDVHVGVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 139 NLQFSAALR-------LPTTMTNHEKNERI------------------------NRVIQELGLDKVADSKVGTQFIRGVS 187
Cdd:PLN03140 259 TLDFSARCQgvgtrydLLSELARREKDAGIfpeaevdlfmkatamegvksslitDYTLKILGLDICKDTIVGDEMIRGIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 188 GGERKRTSIGmELITDPS-ILFLDEPTTGLDSSTANAVLLLLKRMSKQGR-TIIFSIHQPRYSIFKLFDSLTLLASGRLM 265
Cdd:PLN03140 339 GGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQIV 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 266 FHGPAQEALGYFESAGYHCEAYNNPADFFLDIIN-GDSTAVALNREEDFKATEIIEPSKRDKplieklaeiyvdsSFYKE 344
Cdd:PLN03140 418 YQGPRDHILEFFESCGFKCPERKGTADFLQEVTSkKDQEQYWADRNKPYRYISVSEFAERFK-------------SFHVG 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 345 TKAElHQLS----GGEKKKKITVFKEISYTTS----FCHQLRWVSKRsfKNLLGNPQASIAQIIVTVILGLVIGAIYFGL 416
Cdd:PLN03140 485 MQLE-NELSvpfdKSQSHKAALVFSKYSVPKMellkACWDKEWLLMK--RNAFVYVFKTVQIIIVAAIASTVFLRTEMHT 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 417 NNDSTGIQNRAGVLFFLTTNQcFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKLLSDlLPMRMLPSIIFTCIVYFM 496
Cdd:PLN03140 562 RNEEDGALYIGALLFSMIINM-FNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLG-IPISIIESVVWVVITYYS 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 497 LGLKPTADAFFIMMFTLMMVAYSASSMALAIAAGQSVVSVATL--LMTICFVFMMifSGLLVNLTTIASWLSWLQYFSIP 574
Cdd:PLN03140 640 IGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTggALVLLLVFLL--GGFILPKGEIPNWWEWAYWVSPL 717
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 575 RYGFTALQHNEFLGQNFcpgLNatvNNTCNYATCTGEEYLTKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFL 651
Cdd:PLN03140 718 SYGFNALAVNEMFAPRW---MN---KMASDNSTRLGTAVLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALTYL 788
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
380-584 |
1.91e-45 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 160.52 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 380 VSKRSFKNLLGNPQASIAQIIVTVILGLVIGAIYFGLNNdSTGIQNRAGVLFFLTTNQCFSSVSAVEL-FVVEKKLFIHE 458
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN-QQGGLNRPGLLFFSILFNAFSALSGISPvFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 459 YISGYYRVSSYFFGKLLSDLlPMRMLPSIIFTCIVYFMLGLKPTADAFFIMMFTLMMVAYSASSMALAIAAGQSVVSVAT 538
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSEL-PLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622936545 539 LLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHN 584
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
61-302 |
7.53e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.45 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---ALRPTNFKCNSGYVVQDDVVMGTLTV 136
Cdd:COG1131 13 KTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPT--SGEVRVLGedvARDPAEVRRRIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEAL-GYFEsagyhceaynnpaDFFL 295
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELKaRLLE-------------DVFL 228
|
....*..
gi 1622936545 296 DIINGDS 302
Cdd:COG1131 229 ELTGEEA 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
60-301 |
1.10e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 148.47 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---ALRPTNFKCNSGYVVQDDVVMGTLT 135
Cdd:COG4555 13 KVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGedvRKEPREARRQIGVLPDERGLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQFSAALRLpttMTNHEKNERINRVIQELGLDKVADSKVGtqfirGVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:COG4555 91 VRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQPrYSIFKLFDSLTLLASGRLMFHGPAQEalgyfesagyHCEAYNNP--ADF 293
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE----------LREEIGEEnlEDA 231
|
....*...
gi 1622936545 294 FLDIINGD 301
Cdd:COG4555 232 FVALIGSE 239
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
52-268 |
2.68e-40 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 146.25 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 52 FLPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSG-LSGDVLING---ALRPTNFKCNSGYVVQ 126
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGipyKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 DDVVMGTLTVRENLQFSAALRlpttmtnheknerinrviqelgldkvadskvGTQFIRGVSGGERKRTSIGMELITDPSI 206
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 207 LFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
77-272 |
1.39e-32 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 125.31 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-LRPTNFKC--NSGYVVQDDVVMGTLTVRENLQFSAALR-LPttm 152
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGYsIRTDRKAArqSLGYCPQFDALFDELTVREHLRFYARLKgLP--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 153 tNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMs 232
Cdd:cd03263 107 -KSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622936545 233 KQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03263 180 RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
61-268 |
5.89e-32 |
|
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: 123.07 E-value: 5.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---ALRPTNFKCNSGYVVQDDVVMGTLTVR 137
Cdd:cd03264 13 KRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPS--SGTIRIDGqdvLKQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 ENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:cd03264 91 EFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 218 SSTANAVLLLLKRMSKqGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03264 163 PEERIRFRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
36-274 |
2.04e-31 |
|
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: 122.84 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 36 VLSFHNICYRVKvksgflpgrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---- 110
Cdd:COG1120 1 MLEAENLSVGYG------------GRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPS--SGEVLLDGrdla 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ALRPTNFKCNSGYVVQDDVVMGTLTVREnlqfSAAL-RLPTT----MTNHEKNERINRVIQELGLDKVADSKVGTqfirg 185
Cdd:COG1120 67 SLSRRELARRIAYVPQEPPAPFGLTVRE----LVALgRYPHLglfgRPSAEDREAVEEALERTGLEHLADRPVDE----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQP----RYSifklfDSLTLLA 260
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLnlaaRYA-----DRLVLLK 212
|
250
....*....|....
gi 1622936545 261 SGRLMFHGPAQEAL 274
Cdd:COG1120 213 DGRIVAQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
38-263 |
4.03e-31 |
|
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: 120.65 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 38 SFHNICYRVKVKsgflpgrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----AL 112
Cdd:cd03225 1 ELKNLSFSYPDG----------ARPALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLLGPT--SGEVLVDGkdltKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 113 RPTNFKCNSGYVVQD-DVVMGTLTVRENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGER 191
Cdd:cd03225 69 SLKELRRKVGLVFQNpDDQFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRD-----RSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 192 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGR 263
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
35-264 |
4.29e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 121.30 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 35 AVLSFHNICYRVkvksgflpGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--- 110
Cdd:COG1136 3 PLLELRNLTKSY--------GTGEGEVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVLIDGqdi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ---------ALRPTNFkcnsGYVVQDDVVMGTLTVRENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADSKVGTq 181
Cdd:COG1136 73 sslserelaRLRRRHI----GFVFQFFNLLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPSQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 182 firgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRysIFKLFDSLTLLA 260
Cdd:COG1136 145 ----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLR 218
|
....
gi 1622936545 261 SGRL 264
Cdd:COG1136 219 DGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
55-264 |
1.15e-30 |
|
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: 119.52 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 55 GRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING------------ALRPTNFkcns 121
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGeFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVRVDGtdisklsekelaAFRRRHI---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 122 GYVVQDDVVMGTLTVRENLqfsaalRLPTTMTNHEKNERINRVIQ---ELGLDKVADSKVGTqfirgVSGGERKRTSIGM 198
Cdd:cd03255 85 GFVFQSFNLLPDLTALENV------ELPLLLAGVPKKERRERAEElleRVGLGDRLNHYPSE-----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRysIFKLFDSLTLLASGRL 264
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE--LAEYADRIIELRDGKI 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-274 |
1.94e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 32 TEGAVLSFHNICYRVkvksgflpGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDV 106
Cdd:COG1121 2 MMMPAIELENLTVSY--------GGRPV----LEDVSLTIPPGeFVAIVGPNGAGKSTLLKAIL------GLlpptSGTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 107 LINGAlRPTNFKCNSGYVVQD------------DVVMGTLTVRENLqfsaaLRLPTtmtnHEKNERINRVIQELGLDKVA 174
Cdd:COG1121 64 RLFGK-PPRRARRRIGYVPQRaevdwdfpitvrDVVLMGRYGRRGL-----FRRPS----RADREAVDEALERVGLEDLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 175 DSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFD 254
Cdd:COG1121 134 DRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFD 207
|
250 260
....*....|....*....|
gi 1622936545 255 SLTLLAsGRLMFHGPAQEAL 274
Cdd:COG1121 208 RVLLLN-RGLVAHGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
64-214 |
1.24e-28 |
|
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: 111.59 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTLTVRE 138
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPT--EGTILLDGqdltDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 139 NLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADSKVGtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:pfam00005 79 NLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVG-ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
61-264 |
2.09e-28 |
|
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: 111.72 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---ALRPTNFKCNSGYVVQDDVVMGTLTV 136
Cdd:cd03230 13 KTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPD--SGEIKVLGkdiKKEPEEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSaalrlpttmtnheknerinrviqelgldkvadskvgtqfirgvsGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:cd03230 91 RENLKLS--------------------------------------------GGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622936545 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
60-245 |
4.97e-28 |
|
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: 111.80 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING---ALRPTNFKCNSGYVVQDDVVM 131
Cdd:COG4133 14 ERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILA------GLlppsAGEVLWNGepiRDAREDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFSAALRlpttmTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG4133 88 PELTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1622936545 212 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
61-268 |
1.06e-27 |
|
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: 111.09 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGaLRPTNFKCNSGYVVQDDVVMGT-- 133
Cdd:cd03235 12 HPVLEDVSFEVKPGeFLAIVGPNGAGKSTLLKAIL------GLlkptSGSIRVFG-KPLEKERKRIGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRE-----NLQFSAALRLPTtmtnHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILF 208
Cdd:cd03235 85 ISVRDvvlmgLYGHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLAsGRLMFHG 268
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLN-RTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
37-278 |
1.13e-27 |
|
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: 111.66 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRVkvksgflPGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRP 114
Cdd:COG1122 1 IELENLSFSY-------PGGTPA----LDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLNGLLKPT--SGEVLVDGkDITK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 115 TNFK---CNSGYVVQD-D--VVMGTltVRENLQFS-AALRLPTTmtnhEKNERINRVIQELGLDKVADSKVGTqfirgVS 187
Cdd:COG1122 68 KNLRelrRKVGLVFQNpDdqLFAPT--VEEDVAFGpENLGLPRE----EIRERVEEALELVGLEHLADRPPHE-----LS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 188 GGERKRTSI-GMeLITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMF 266
Cdd:COG1122 137 GGQKQRVAIaGV-LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVA 214
|
250
....*....|..
gi 1622936545 267 HGPAQEALGYFE 278
Cdd:COG1122 215 DGTPREVFSDYE 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
72-268 |
1.29e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 110.92 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 72 KPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---ALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALR 147
Cdd:cd03266 29 KPGeVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGfdvVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 lptTMTNHEKNERINRVIQELGLDKVADSKVGtqfirGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 227
Cdd:cd03266 107 ---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622936545 228 LKRMSKQGRTIIFSIHQpRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03266 179 IRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
60-272 |
4.33e-27 |
|
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: 109.90 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPT---NFKCNSGYVVQDDVVM 131
Cdd:cd03261 12 GRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPD--SGEVLIDGedisGLSEAelyRLRRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFSaaLRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:cd03261 90 DSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 212 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQpRYSIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
60-268 |
1.82e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 107.61 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAL---RPTNfKCNSGYVVQDDVVMGTLT 135
Cdd:cd03259 12 SVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPD--SGEILIDGRDvtgVPPE-RRNIGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:cd03259 89 VAENIAF--GLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 216 LDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03259 161 LDAKLREELREELKELQRElGITTIYVTHDQE-EALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
60-274 |
2.70e-26 |
|
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: 107.76 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING---------ALRPTNFKCnsGYVV 125
Cdd:COG1127 17 DRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLII------GLlrpdSGEILVDGqditglsekELYELRRRI--GMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 QDDVVMGTLTVRENLQFsaALRLPTTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPS 205
Cdd:COG1127 89 QGGALFDSLTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAAD-----KMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLD-SAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
64-272 |
3.57e-26 |
|
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: 107.52 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTNFkCNSGyVV---QDDVVMGTLT 135
Cdd:cd03219 16 LDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPT--SGSVLFDGEditgLPPHEI-ARLG-IGrtfQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQFSAALRLPTTM-------TNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILF 208
Cdd:cd03219 92 VLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD-VVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
77-272 |
4.65e-26 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 109.02 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--ALR-PTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlptTMT 153
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRMLTTLLRPT--SGTARVAGydVVRePRKVRRSIGIVPQYASVDEDLTGRENLEMMGRLY---GLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:TIGR01188 98 KDEAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622936545 234 QGRTIIFSIHQpRYSIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:TIGR01188 173 EGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
37-243 |
9.33e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 105.63 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRvkvksgFLPGRKPVEkeILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-LRP 114
Cdd:cd03293 1 LEVRNVSKT------YGGGGGAVT--ALEDISLSVEEGeFVALVGPSGCGKSTLLRIIAGLERPT--SGEVLVDGEpVTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 115 TNFKCnsGYVVQDDVVMGTLTVRENLQFSAALRLpttMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRT 194
Cdd:cd03293 71 PGPDR--GYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENA-----YPHQLSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622936545 195 SIGMELITDPSILFLDEPTTGLDSSTANAV-LLLLKRMSKQGRTIIFSIH 243
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTH 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-274 |
2.60e-25 |
|
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: 110.62 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 16 NTNGFPTTTSNDRKAFTEGAVLSFHNICYRvkvksgfLPGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLA 94
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFS-------YPGGRPA----LDGLSLTIPPGeRVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 95 ARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTlTVRENLQFSAAlrlpttmtnHEKNERINRVIQELGL 170
Cdd:COG4988 385 GFLPPY--SGSILINGvdlsDLDPASWRRQIAWVPQNPYLFAG-TIRENLRLGRP---------DASDEELEAALEAAGL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 171 DKVA-------DSKVGTQFiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIH 243
Cdd:COG4988 453 DEFVaalpdglDTPLGEGG-RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITH 530
|
250 260 270
....*....|....*....|....*....|.
gi 1622936545 244 QPrySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4988 531 RL--ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
60-268 |
4.58e-25 |
|
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: 103.45 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPTNFKCNS--GYVVQDDVVMGTLTV 136
Cdd:cd03268 12 KKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPD--SGEITFDGKSYQKNIEALRriGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSAALRLpttmtnhEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:cd03268 90 RENLRLLARLLG-------IRKKRIDEVLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
77-272 |
6.37e-25 |
|
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: 103.22 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--ALR-PTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALR-LPttm 152
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPT--SGRATVAGhdVVRePREVRRRIGIVFQDLSVDDELTGWENLYIHARLYgVP--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 153 tNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS 232
Cdd:cd03265 105 -GAERRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622936545 233 K-QGRTIIFSIHqprY--SIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03265 179 EeFGMTILLTTH---YmeEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
60-263 |
9.18e-25 |
|
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: 100.78 E-value: 9.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalrptnfkcnsgyvvqddvvmgtltvre 138
Cdd:cd00267 11 GRTALDNVSlTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT--SGEILIDG---------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 139 nlqfsaalrlpttmtnheknERINRVIQELGLDKVAdskvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:cd00267 61 --------------------KDIAKLPLEELRRRIG-------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622936545 219 STANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGR 263
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-274 |
1.34e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 108.31 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 21 PTTTSNDRKAFTEGAVLSFHNICYRvkvksgFLPGRKPVekeiLSNINGIMKPG--LnAILGPTGGGKSSLLDVLAARKD 98
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFR------YPGAGRPV----LDGLSLTLPPGerV-AIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 99 PSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTlTVRENLQFsAALRLPttmtnhekNERINRVIQELGLDKVA 174
Cdd:COG4987 387 PQ--SGSITLGGvdlrDLDEDDLRRRIAVVPQRPHLFDT-TLRENLRL-ARPDAT--------DEELWAALERVGLGDWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 175 -------DSKVGTQFiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHQPry 247
Cdd:COG4987 455 aalpdglDTWLGEGG-RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRL-- 530
|
250 260
....*....|....*....|....*..
gi 1622936545 248 SIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
60-263 |
2.16e-24 |
|
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: 100.34 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA------LRPTNFKCNSGYVVQDDVVMG 132
Cdd:cd03229 12 QKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPD--SGSILIDGEdltdleDELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFsaalrlpttmtnheknerinrviqelgldkvadskvgtqfirGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:cd03229 90 HLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 213 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGR 263
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
61-264 |
3.95e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.90 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING------------ALRPtnfkcNSGYVVQD 127
Cdd:COG2884 15 REALSDVSLEIEKGeFVFLTGPSGAGKSTLLKLLYGEERPT--SGQVLVNGqdlsrlkrreipYLRR-----RIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 128 -----DvvmgtLTVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELIT 202
Cdd:COG2884 88 frllpD-----RTVYENVAL--PLRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 203 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTL-LASGRL 264
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD--LELVDRMPKRVLeLEDGRL 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
60-268 |
4.10e-24 |
|
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: 99.82 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING----ALRPTNFKCNSGYVVQddvv 130
Cdd:cd03214 11 GRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLA------GLlkpsSGEILLDGkdlaSLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 mgtltvrenlqfsaalrlpttmtnheknerinrVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:cd03214 81 ---------------------------------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP----RYSifklfDSLTLLASGRLMFHG 268
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLnlaaRYA-----DRVILLKDGRIVAQG 180
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
74-268 |
5.20e-24 |
|
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: 100.45 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 74 GLNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGA-LRPTNFKCNS-------GYVVQDDVVMGTLTVRENLQFsaA 145
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDG--GTIVLNGTvLFDSRKKINLppqqrkiGLVFQQYALFPHLNVRENLAF--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 146 LRlptTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:cd03297 100 LK---RKRNREDRISVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622936545 226 LLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
44-268 |
8.30e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 100.48 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 44 YRVKVKSGFLPG-------RKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGaLRPt 115
Cdd:cd03267 10 YRVYSKEPGLIGslkslfkRKYREVEALKGISfTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT--SGEVRVAG-LVP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 116 nFKCNSGYVVQDDVVMGT-------LTVRENLQFSAAL-RLPTTmtnhEKNERINRVIQELGLDKVADSKVgtqfiRGVS 187
Cdd:cd03267 86 -WKRRKKFLRRIGVVFGQktqlwwdLPVIDSFYLLAAIyDLPPA----RFKKRLDELSELLDLEELLDTPV-----RQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 188 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMF 266
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMK-DIEALARRVLVIDKGRLLY 234
|
..
gi 1622936545 267 HG 268
Cdd:cd03267 235 DG 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
61-272 |
8.83e-24 |
|
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: 100.72 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------ALRptNFKCNSGYVVQDDVV 130
Cdd:cd03256 14 KKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPT--SGSVLIDGtdinklkgkALR--QLRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 MGTLTVRENLQFSAALRLPT--TMTNHEKNERINRVIQEL---GLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:cd03256 90 IERLSVLENVLSGRLGRRSTwrSLFGLFPKEEKQRALAALervGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKDGRIVFDGPPAE 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
37-274 |
1.08e-23 |
|
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: 106.07 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRvkvksgFLPGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING- 110
Cdd:COG2274 474 IELENVSFR------YPGDSPPV----LDNISLTIKPGeRVAIVGRSGSGKSTLLKLLL------GLyeptSGRILIDGi 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ---ALRPTNFKCNSGYVVQDDVVMGTlTVRENLQFSAALrlpTTMtnheknERINRVIQELGLDKVA-------DSKVGT 180
Cdd:COG2274 538 dlrQIDPASLRRQIGVVLQDVFLFSG-TIRENITLGDPD---ATD------EEIIEAARLAGLHDFIealpmgyDTVVGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 181 QFiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHqpRYSIFKLFDSLTLLA 260
Cdd:COG2274 608 GG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAH--RLSTIRLADRIIVLD 683
|
250
....*....|....
gi 1622936545 261 SGRLMFHGPAQEAL 274
Cdd:COG2274 684 KGRIVEDGTHEELL 697
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
57-264 |
1.20e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.59 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 57 KPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTNFKCNSGYVVQDdVVM 131
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKvAIIGRVGSGKSTLLKLLAGLYKPT--SGSVLLDGTdirqLDPADLRRNIGYVPQD-VTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLqfsaALRLPttmtnHEKNERINRVIQELGLDKVA-------DSKVGTQFiRGVSGGERKRTSIGMELITDP 204
Cdd:cd03245 90 FYGTLRDNI----TLGAP-----LADDERILRAAELAGVTDFVnkhpnglDLQIGERG-RGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 205 SILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRL 264
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITH--RPSLLDLVDRIIVMDSGRI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
37-264 |
1.41e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.12 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRVKvksgflpgrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING- 110
Cdd:COG4619 1 LELEGLSFRVG------------GKPILSPVSLTLEAGeCVAITGPSGSGKSTLLRALA------DLdpptSGEIYLDGk 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ---ALRPTNFKCNSGYVVQDdVVMGTLTVRENLQFSAALRlpttmTNHEKNERINRVIQELGLDK-VADSKVGTqfirgV 186
Cdd:COG4619 63 plsAMPPPEWRRQVAYVPQE-PALWGGTVRDNLPFPFQLR-----ERKFDRERALELLERLGLPPdILDKPVER-----L 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRL 264
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQ-IERVADRVLTLEAGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
77-274 |
2.65e-23 |
|
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: 98.95 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAlRPTNF---KCNSGYVVQDDVVMGTLTVRENLQFsaALRLPTTMt 153
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPD--SGKILLNGK-DITNLppeKRDISYVPQNYALFPHMTVYKNIAY--GLKKRKVD- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:cd03299 103 KKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622936545 234 QGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
37-263 |
4.79e-23 |
|
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: 96.30 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRvkvksgfLPGRkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----A 111
Cdd:cd03228 1 IEFKNVSFS-------YPGR---PKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPT--SGEILIDGvdlrD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 LRPTNFKCNSGYVVQDDVVMGTlTVRENLqfsaalrlpttmtnheknerinrviqelgldkvadskvgtqfirgVSGGER 191
Cdd:cd03228 69 LDLESLRKNIAYVPQDPFLFSG-TIRENI---------------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 192 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGR 263
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
64-245 |
5.87e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPtnfkcnsGYVVQDDVVMGTL--TVRENL 140
Cdd:NF040873 8 LHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPT--SGTVRRAGGARV-------AYVPQRSEVPDSLplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 141 QFSA-ALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:NF040873 79 AMGRwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*.
gi 1622936545 220 TANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDL 179
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
32-240 |
5.96e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.62 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 32 TEGAVLSFHNICYRvkvksgFLPGRKPVEkeILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDV 106
Cdd:COG1116 3 AAAPALELRGVSKR------FPTGGGGVT--ALDDVSLTVAAGeFVALVGPSGCGKSTLLRLIA------GLekptSGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 107 LINGAlRPTNFKCNSGYVVQDDVVMGTLTVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgV 186
Cdd:COG1116 69 LVDGK-PVTGPGPDRGVVFQEPALLPWLTVLDNVAL--GLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQ-----L 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAnAVL--LLLKRMSKQGRTIIF 240
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTR-ERLqdELLRLWQETGKTVLF 194
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
55-280 |
2.52e-22 |
|
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: 96.41 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 55 GRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAL----RPTNFKCNSGYVV 125
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESfGLVGESGSGKSTLLRALA------GLerpwSGEVTFDGRPvtrrRRKAFRRRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 QDdvVMGTL----TVRENLqfSAALRLpTTMTNHEknERINRVIQELGLDkvadSKVGTQFIRGVSGGERKRTSIGMELI 201
Cdd:COG1124 86 QD--PYASLhprhTVDRIL--AEPLRI-HGLPDRE--ERIAELLEQVGLP----PSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 202 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEALGYFESA 280
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAV-VAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
64-243 |
2.69e-22 |
|
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: 95.55 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTN---------FKCNSGYVVQDDVVMGT 133
Cdd:cd03292 17 LDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPT--SGTIRVNG--QDVSdlrgraipyLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:cd03292 93 RNVYENVAF--ALEV-TGVPPREIRKRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|
gi 1622936545 214 TGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
48-274 |
4.45e-22 |
|
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: 95.37 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 48 VKSGFLPGRKpvekeILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAlRPTNFKCNS----- 121
Cdd:cd03253 6 VTFAYDPGRP-----VLKDVSFTIPAGKKvAIVGPSGSGKSTILRLLFRFYDVS--SGSILIDGQ-DIREVTLDSlrrai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 122 GYVVQDDVVMGTlTVRENLQFSaalRLPTT---MTNHEKNERINRVIqeLGLDKVADSKVGTqfiRGV--SGGERKRTSI 196
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYG---RPDATdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGE---RGLklSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 197 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH--RLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
77-268 |
1.33e-21 |
|
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: 93.33 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--------ALRPTNFkcnsgyVVQDDVVMGTLTVREN--LQFSAAL 146
Cdd:cd03298 28 AIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGvdvtaappADRPVSM------LFQENNLFAHLTVEQNvgLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 RLpttmtNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL- 225
Cdd:cd03298 100 KL-----TAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLd 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622936545 226 LLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-275 |
1.57e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.44 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 35 AVLSFHNICYRvkvksgFLPGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSG-LSGDVLING-- 110
Cdd:COG1123 3 PLLEVRDLSVR------YPGGDVPA----VDGVSLTIAPGeTVALVGESGSGKSTLALALMGLLPHGGrISGEVLLDGrd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 --ALRPTNFKCNSGYVVQD-DVVMGTLTVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVS 187
Cdd:COG1123 73 llELSEALRGRRIGMVFQDpMTQLNPVTVGDQIAE--ALEN-LGLSRAEARARVLELLEAVGLERRLD-----RYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 188 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMF 266
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGV-VAEIADRVVVMDDGRIVE 223
|
....*....
gi 1622936545 267 HGPAQEALG 275
Cdd:COG1123 224 DGPPEEILA 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
54-243 |
2.33e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.16 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 54 PGRKPvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRP-TNFKCNSGYVVQDDVVM 131
Cdd:COG4525 14 PGGGQ-PQPALQDVSLTIESGeFVVALGASGCGKTTLLNLIAGFLAPS--SGEITLDG--VPvTGPGADRGVVFQKDALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG4525 89 PWLNVLDNVAF--GLRL-RGVPKAERRARAEELLALVGLADFAR-----RRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190
....*....|....*....|....*....|...
gi 1622936545 212 PTTGLDSSTANAV-LLLLKRMSKQGRTIIFSIH 243
Cdd:COG4525 161 PFGALDALTREQMqELLLDVWQRTGKGVFLITH 193
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
36-240 |
4.15e-21 |
|
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: 92.57 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 36 VLSFHNicyrVKVKsgFLPGRKPVEkeILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---- 110
Cdd:cd03257 1 LLEVKN----LSVS--FPTGGGSVK--ALDDVSFSIKKGETlGLVGESGSGKSTLARAILGLLKPT--SGSIIFDGkdll 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ----ALRPTNFKcNSGYVVQDdvVMGTL----TVREnlQFSAALRLPTTMTNHEKNERInrviQELGLDKV-ADSKVGTQ 181
Cdd:cd03257 71 klsrRLRKIRRK-EIQMVFQD--PMSSLnprmTIGE--QIAEPLRIHGKLSKKEARKEA----VLLLLVGVgLPEEVLNR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 182 FIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 240
Cdd:cd03257 142 YPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLF 201
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
74-275 |
8.53e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 94.41 E-value: 8.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 74 GLNAILGPTGGGKSSLLDVLAARKDPSG----LSGDVLINGALR---PTNfKCNSGYVVQDDVVMGTLTVRENLQFSAal 146
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEgeivLNGRTLFDSRKGiflPPE-KRRIGYVFQEARLFPHLSVRGNLRYGM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 rlpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:TIGR02142 101 ---KRARPSERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622936545 227 LLKRMSKQGRT-IIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQ-EVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
37-264 |
1.15e-20 |
|
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: 89.58 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRvkvksgfLPGRKPvekEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA---- 111
Cdd:cd03246 1 LEVENVSFR-------YPGAEP---PVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPT--SGRVRLDGAdisq 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 LRPTNFKCNSGYVVQDDVVMGTlTVRENLqfsaalrlpttmtnheknerinrviqelgldkvadskvgtqfirgVSGGER 191
Cdd:cd03246 69 WDPNELGDHVGYLPQDDELFSG-SIAENI---------------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 192 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPrySIFKLFDSLTLLASGRL 264
Cdd:cd03246 103 QRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
56-245 |
2.10e-20 |
|
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: 95.12 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 56 RKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPsgLSGDVLING----ALRPTNFKCNSGYVVQDDVV 130
Cdd:TIGR02868 343 GYPGAPPVLDGVSLDLPPGERvAILGPSGSGKSTLLATLAGLLDP--LQGEVTLDGvpvsSLDQDEVRRRVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 MGTlTVRENLQFSAAlrlptTMTNHEKNERINRV-----IQEL--GLDkvadSKVGTQFIRgVSGGERKRTSIGMELITD 203
Cdd:TIGR02868 421 FDT-TVRENLRLARP-----DATDEELWAALERVgladwLRALpdGLD----TVLGEGGAR-LSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622936545 204 PSILFLDEPTTGLDSSTANAVL-LLLKRMSkqGRTIIFSIHQP 245
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLeDLLAALS--GRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
37-268 |
3.16e-20 |
|
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: 88.52 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYrvkvksgflpGRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPT 115
Cdd:cd03247 1 LSINNVSF----------SYPEQEQQVLKNLSLELKQGEKiALLGRSGSGKSTLLQLLTGDLKPQ--QGEITLDGVPVSD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 116 NFKCNSGYvvqddvvMGTLTVRENLqFSAALRlpttmtnheknerinrviqelgldkvadSKVGTQFirgvSGGERKRTS 195
Cdd:cd03247 69 LEKALSSL-------ISVLNQRPYL-FDTTLR----------------------------NNLGRRF----SGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 196 IGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH--HLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
60-274 |
5.60e-20 |
|
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: 89.21 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------ALRPtnfkcNSGYVVQDDV 129
Cdd:cd03254 15 KKPVLKDINFSIKPGeTVAIVGPTGAGKTTLINLLMRFYDPQ--KGQILIDGidirdisrkSLRS-----MIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 130 VMGTlTVRENLQFSaalrlpttmTNHEKNERINRVIQELGLDkvadskvgtQFIR---------------GVSGGERKRT 194
Cdd:cd03254 88 LFSG-TIMENIRLG---------RPNATDEEVIEAAKEAGAH---------DFIMklpngydtvlgenggNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 195 SIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH--RLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
37-274 |
5.98e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.12 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYrvkvksGFLPGRKPVekeiLSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLING----- 110
Cdd:PRK11160 339 LTLNNVSF------TYPDQPQPV----LKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQ--QGEILLNGqpiad 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ----ALRptnfkcNSGYVVQDDVVMGTLTVRENLQFSAAlrlpttmtnHEKNERINRVIQELGLDKVADSKVG-TQFI-- 183
Cdd:PRK11160 407 yseaALR------QAISVVSQRVHLFSATLRDNLLLAAP---------NASDEALIEVLQQVGLEKLLEDDKGlNAWLge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 184 --RGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLAS 261
Cdd:PRK11160 472 ggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH--RLTGLEQFDRICVMDN 548
|
250
....*....|...
gi 1622936545 262 GRLMFHGPAQEAL 274
Cdd:PRK11160 549 GQIIEQGTHQELL 561
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
61-262 |
6.01e-20 |
|
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: 88.47 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRP--TNFKCnSGYVVQD-DVVMGTLTV 136
Cdd:cd03226 13 TEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKES--SGSILLNGKPIKakERRKS-IGYVMQDvDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSAalrlpttMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:cd03226 90 REELLLGL-------KELDAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622936545 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASG 262
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANG 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
73-274 |
6.42e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 91.70 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 73 PGLNAILGPTGGGKSSLLDVLA--ARKDpSG---LSGDVLINGALR---PTNfKCNSGYVVQDDVVMGTLTVRENLQFSA 144
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAglERPD-SGrirLGGEVLQDSARGiflPPH-RRRIGYVFQEARLFPHLSVRGNLLYGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 145 AlRLPTtmtnHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 224
Cdd:COG4148 103 K-RAPR----AERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 225 LLLLKRMSKQGRT-IIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4148 173 LPYLERLRDELDIpILYVSHSLD-EVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
77-274 |
9.38e-20 |
|
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: 88.26 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLaarkdpSGL----SGDVLING---ALRPTNFKCNSG--YVVQDDVVMGTLTVRENLQFSAALR 147
Cdd:cd03224 30 ALLGRNGAGKTTLLKTI------MGLlpprSGSIRFDGrdiTGLPPHERARAGigYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 lpttmTNHEKNERINRVIQEL-GLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:cd03224 104 -----RRAKRKARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622936545 227 LLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03224 174 AIRELRDEGVTILLVEQNAR-FALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
56-264 |
1.22e-19 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 88.18 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 56 RKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING------------ALRPTNFkcnsG 122
Cdd:TIGR02211 13 EGKLDTRVLKGVSlSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT--SGEVLFNGqslsklssneraKLRNKKL----G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 123 YVVQDDVVMGTLTVRENLQFSAalrLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELIT 202
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 203 DPSILFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIFSIHQPRYSifKLFDSLTLLASGRL 264
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFdLMLELNRELNTSFLVVTHDLELA--KKLDRVLEMKDGQL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
60-274 |
2.17e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.22 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDvlaarkdpsglsgdvLINGALRPTnfkcnSGYVVQddvVMGTLTVRE 138
Cdd:COG1119 15 GKTILDDISWTVKPGEHwAILGPNGAGKSTLLS---------------LITGDLPPT-----YGNDVR---LFGERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 139 NLQ--------FSAAL--RLPTTMT-------------------NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGG 189
Cdd:COG1119 72 DVWelrkriglVSPALqlRFPRDETvldvvlsgffdsiglyrepTDEQRERARELLELLGLAHLADRPFGT-----LSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 190 ERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQG-RTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHG 268
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAG 225
|
....*.
gi 1622936545 269 PAQEAL 274
Cdd:COG1119 226 PKEEVL 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
60-272 |
2.47e-19 |
|
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: 87.24 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLL-------DVLAARKDpsglSGDVLINGA------LRPTNFKCNSGYVV 125
Cdd:cd03260 12 DKHALKDISLDIPKGeITALIGPSGCGKSTLLrllnrlnDLIPGAPD----EGEVLLDGKdiydldVDVLELRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 QDDVVMgTLTVRENLqfSAALRLPTTMTNHEKNERINRVIQELGL-DKVADSKVGtqfiRGVSGGERKRTSIGMELITDP 204
Cdd:cd03260 88 QKPNPF-PGSIYDNV--AYGLRLHGIKLKEELDERVEEALRKAALwDEVKDRLHA----LGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 205 SILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ-QAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
35-246 |
2.93e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 87.10 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 35 AVLSFHNICYRVKVKSGFLpgrkpvekEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--- 110
Cdd:COG4181 7 PIIELRGLTKTVGTGAGEL--------TILKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPT--SGTVRLAGqdl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 ---------ALRPTNFkcnsGYVVQDDVVMGTLTVRENLQfsaalrLPTTMTNH-EKNERINRVIQELGLDKVADskvgt 180
Cdd:COG4181 77 faldedaraRLRARHV----GFVFQSFQLLPTLTALENVM------LPLELAGRrDARARARALLERVGLGHRLD----- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 181 QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPR 246
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
60-245 |
6.54e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING-ALRPTNFKCNSGYVVQDDVVMGT 133
Cdd:PRK13539 14 GRVLFSGLSFTLAAGeALVLTGPNGSGKTTLLRLIA------GLlppaAGTIKLDGgDIDDPDVAEACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRENLQFSAALRlpttmtnHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:PRK13539 88 LTVAENLEFWAAFL-------GGEELDIAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1622936545 214 TGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
77-274 |
8.09e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.96 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--------ALRP--TNFkcnsgyvvQDDVVMGTLTVREN--LQFSA 144
Cdd:COG3840 29 AILGPSGAGKSTLLNLIAGFLPPD--SGRILWNGqdltalppAERPvsMLF--------QENNLFPHLTVAQNigLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 145 ALRLpttmtNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 224
Cdd:COG3840 99 GLKL-----TAEQRAQVEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 225 LLLLKRMSK-QGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG3840 169 LDLVDELCReRGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
78-243 |
9.81e-19 |
|
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: 85.38 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTnfKCNSGYVVQDDVVMGTLTVRENLQFSAALRlptTMT 153
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEEPT--SGRIYIGGRdvtdLPPK--DRDIAMVFQNYALYPHMTVYDNIAFGLKLR---KVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 154 NHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:cd03301 104 KDEIDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQ 178
|
170
....*....|.
gi 1622936545 234 Q-GRTIIFSIH 243
Cdd:cd03301 179 RlGTTTIYVTH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
62-272 |
1.12e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 85.71 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------ALRptNFKCNSGYVVQDDVVM 131
Cdd:cd03258 19 TALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPT--SGSVLVDGtdltllsgkELR--KARRRIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:cd03258 95 SSRTVFENVAL--PLEI-AGVPKAEIEERVLELLELVGLEDKADA-----YPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 212 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRElGLTIVLITHEME-VVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
57-274 |
1.15e-18 |
|
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: 85.62 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 57 KPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVM 131
Cdd:cd03252 11 KPDGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPE--NGRVLVDGhdlaLADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTlTVRENLQfsaalrLPTTMTNHEKNERINRV------IQEL--GLDKVadskVGTQFIrGVSGGERKRTSIGMELITD 203
Cdd:cd03252 89 NR-SIRDNIA------LADPGMSMERVIEAAKLagahdfISELpeGYDTI----VGEQGA-GLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 204 PSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
77-272 |
1.18e-18 |
|
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: 85.29 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGaLRPTNFKCNS------GYVVQDDVVMGTLTVRENLqfSAALRLpT 150
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVGLVKPD--SGKILLDG-QDITKLPMHKrarlgiGYLPQEASIFRKLTVEENI--LAVLEI-R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 151 TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKR 230
Cdd:cd03218 104 GLSKKEREEKLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622936545 231 MSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03218 179 LKDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
60-274 |
1.43e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTL 134
Cdd:PRK11231 14 TKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTP--QSGTVFLGDkpisMLSSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENLQF--SAALRLPTTMTNHEKnERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK11231 92 TVRELVAYgrSPWLSLWGRLSAEDN-ARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 213 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGKTVVTVLHDlnqaSRYC-----DHLVVLANGHVMAQGTPEEVM 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
37-274 |
2.04e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.55 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRVkvksgflpGRKPvekeILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----A 111
Cdd:COG4559 2 LEAENLSVRL--------GGRT----LLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPS--SGEVRLNGrplaA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 LRPT---------------NFkcnsGYVVQDDVVMGtltvrenlqfsaalRLPTTMTNHEKNERINRVIQELGLDKVADs 176
Cdd:COG4559 68 WSPWelarrravlpqhsslAF----PFTVEEVVALG--------------RAPHGSSAAQDRQIVREALALVGLAHLAG- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 177 kvgtQFIRGVSGGERKRTSIGMELI-------TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP---- 245
Cdd:COG4559 129 ----RSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLnlaa 204
|
250 260
....*....|....*....|....*....
gi 1622936545 246 RYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4559 205 QYA-----DRILLLHQGRLVAQGTPEEVL 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
54-245 |
2.11e-18 |
|
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: 88.88 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 54 PGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGA----LRPTNFKCNSGYVVQDD 128
Cdd:TIGR02857 332 PGRRPA----LRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTE--GSIAVNGVpladADADSWRDQIAWVPQHP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVMGTlTVRENLQFSaalrlpttmTNHEKNERINRVIQELGLDK-VADSKVGTQFI-----RGVSGGERKRTSIGMELIT 202
Cdd:TIGR02857 406 FLFAG-TIAENIRLA---------RPDASDAEIREALERAGLDEfVAALPQGLDTPigeggAGLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622936545 203 DPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHQP 245
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL 517
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
36-274 |
2.17e-18 |
|
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: 88.81 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 36 VLSFHNICYRvkvksgfLPGRKPVEKEILSNINGIMKPG--LnAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--- 110
Cdd:COG1123 260 LLEVRNLSKR-------YPVRGKGGVRAVDDVSLTLRRGetL-GLVGESGSGKSTLARLLLGLLRPT--SGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 -ALRPTNFKCNS---GYVVQDdvVMGTL----TVRENLQFsaALRLPTTMTNHEKNERINRVIQELGLDkvadSKVGTQF 182
Cdd:COG1123 330 tKLSRRSLRELRrrvQMVFQD--PYSSLnprmTVGDIIAE--PLRLHGLLSRAERRERVAELLERVGLP----PDLADRY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 183 IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQ----PRYSifklfDSLT 257
Cdd:COG1123 402 PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlavvRYIA-----DRVA 476
|
250
....*....|....*..
gi 1622936545 258 LLASGRLMFHGPAQEAL 274
Cdd:COG1123 477 VMYDGRIVEDGPTEEVF 493
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
61-217 |
3.18e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPS-GLSGDVLING---ALRPTNFKcNSGYVVQDDVVMGTLT 135
Cdd:COG4136 14 RPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGrrlTALPAEQR-RIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQFSaalrLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:COG4136 93 VGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 1622936545 216 LD 217
Cdd:COG4136 164 LD 165
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
77-243 |
3.22e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 83.24 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNFKCNS--------GYVVQ--DDVVMGTlTVRENLQFSaal 146
Cdd:TIGR01166 22 ALLGANGAGKSTLLLHLNGLLRPQ--SGAVLIDG--EPLDYSRKGllerrqrvGLVFQdpDDQLFAA-DVDQDVAFG--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 rlPTTMTNHEknERINRVIQElGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:TIGR01166 94 --PLNLGLSE--AEVERRVRE-ALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLA 168
|
170
....*....|....*..
gi 1622936545 227 LLKRMSKQGRTIIFSIH 243
Cdd:TIGR01166 169 ILRRLRAEGMTVVISTH 185
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
60-294 |
5.28e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.90 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTnfKCNSGYVVQDDVVMGTL 134
Cdd:COG3839 15 GVEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIAGLEDPT--SGEILIGGrdvtDLPPK--DRNIAMVFQSYALYPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENLQFsaALRLpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:COG3839 91 TVYENIAF--PLKL-RKVPKAEIDRRVREAAELLGLEDLLDRKPKQ-----LSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 215 GLDsstanAVL-----LLLKRMSKQ-GRTIIFSIHQPRysifklfDSLTL------LASGRLMFHGPAQealgyfesagy 282
Cdd:COG3839 163 NLD-----AKLrvemrAEIKRLHRRlGTTTIYVTHDQV-------EAMTLadriavMNDGRIQQVGTPE----------- 219
|
250
....*....|..
gi 1622936545 283 hcEAYNNPADFF 294
Cdd:COG3839 220 --ELYDRPANLF 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
63-246 |
9.13e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 9.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDpsGLSGDVLING------------ALRPTNFkcnsGYVVQDDV 129
Cdd:PRK10584 25 ILTGVELVVKRGETiALIGESGSGKSTLLAILAGLDD--GSSGEVSLVGqplhqmdeearaKLRAKHV----GFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 130 VMGTLTVRENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADsKVGTQfirgVSGGERKRTSIGMELITDPSILFL 209
Cdd:PRK10584 99 LIPTLNALENVELPALLR---GESSRQSRNGAKALLEQLGLGKRLD-HLPAQ----LSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 210 DEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPR 246
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQ 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
77-240 |
1.63e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 84.38 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING----ALRPtnFKCNSGYVVQDDVVMGTLTVRENLQFSaaLRL 148
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIA------GFetpdSGRILLDGrdvtGLPP--EKRNVGMVFQDYALFPHLTVAENVAFG--LRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 149 pTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:COG3842 105 -RGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL 178
|
170
....*....|...
gi 1622936545 229 KRMSKQ-GRTIIF 240
Cdd:COG3842 179 RRLQRElGITFIY 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
60-244 |
2.99e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 81.04 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGaLRPTNFKCNS-------GYVVQDDVVM 131
Cdd:cd03262 12 DFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDG-LKLTDDKKNInelrqkvGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFsaALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:cd03262 89 PHLTVLENITL--APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190
....*....|....*....|....*....|...
gi 1622936545 212 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
37-288 |
4.58e-17 |
|
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: 84.77 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRvkvksgfLPGRkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRP 114
Cdd:TIGR02203 331 VEFRNVTFR-------YPGR---DRPALDSISLVIEPGeTVALVGRSGSGKSTLVNLIPRFYEPD--SGQILLDGhDLAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 115 TNFKCNSGYV--VQDDVVMGTLTVRENLQFSAALRLPttmtnhekNERINRVIQEL-------GLDKVADSKVGTQFIRg 185
Cdd:TIGR02203 399 YTLASLRRQValVSQDVVLFNDTIANNIAYGRTEQAD--------RAEIERALAAAyaqdfvdKLPLGLDTPIGENGVL- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLM 265
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAH--RLSTIEKADRIVVMDDGRIV 546
|
250 260
....*....|....*....|...
gi 1622936545 266 FHGPAQEALgyfESAGYHCEAYN 288
Cdd:TIGR02203 547 ERGTHNELL---ARNGLYAQLHN 566
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
62-272 |
6.54e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.43 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPT--------NFKCNSGYVVQD-DVVM 131
Cdd:PRK13636 20 HALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPS--SGRILFDG--KPIdysrkglmKLRESVGMVFQDpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFSAA-LRLPttmtNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK13636 96 FSASVYQDVSFGAVnLKLP----EDEVRKRVDNALKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQprYSIFKLF-DSLTLLASGRLMFHGPAQE 272
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHD--IDIVPLYcDNVFVMKEGRVILQGNPKE 228
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
64-239 |
8.58e-17 |
|
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274568 [Multi-domain] Cd Length: 242 Bit Score: 80.29 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalrpTNFkcnSGYVVQDDVVMG---------- 132
Cdd:TIGR03411 18 LNDLSLYVDPGeLRVIIGPNGAGKTTMMDVITGKTRPD--EGSVLFGG----TDL---TGLPEHQIARAGigrkfqkptv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 --TLTVRENLQFSAAL--RLPTTMT---NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:TIGR03411 89 feNLTVFENLELALPRdkSVFASLFfrlSAEEKDRIEEVLETIGLADEADRLAGL-----LSHGQKQWLEIGMLLMQDPK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 206 ILFLDEPTTGLD----SSTANavllLLKRMSKqGRTII 239
Cdd:TIGR03411 164 LLLLDEPVAGMTdeetEKTAE----LLKSLAG-KHSVV 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
60-276 |
8.66e-17 |
|
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: 79.97 E-value: 8.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRptNFKCNS-----GYVVQDdVVMG 132
Cdd:cd03251 14 GPPVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVD--SGRILIDGhDVR--DYTLASlrrqiGLVSQD-VFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSaalRLPTTMTNHEKNERI---NRVIQELglDKVADSKVGTqfiRGV--SGGERKRTSIGMELITDPSIL 207
Cdd:cd03251 89 NDTVAENIAYG---RPGATREEVEEAARAanaHEFIMEL--PEGYDTVIGE---RGVklSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 208 FLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEALGY 276
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMK-NRTTFVIAH--RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
55-275 |
1.21e-16 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 79.63 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 55 GRKPVEKEILSNINGIMKPGLnaiLGPTGGGKSSLLDVLAA--RKDpsglSGDVLING---ALRPTNFKCNSG--YVVQD 127
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGL---LGPNGAGKTTSFYMIVGlvRPD----AGKILIDGqdiTHLPMHERARLGigYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 128 DVVMGTLTVRENLQfsAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSIL 207
Cdd:TIGR04406 85 ASIFRKLTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 208 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
58-239 |
1.23e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.68 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDdVVMG 132
Cdd:COG1132 350 PGDRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPT--SGRILIDGvdirDLTLESLRRQIGVVPQD-TFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSaalRLPTTMtnheknERINRVIQELGLDKVA-------DSKVGTqfiRGV--SGGERKRTSIGMELITD 203
Cdd:COG1132 427 SGTIRENIRYG---RPDATD------EEVEEAAKAAQAHEFIealpdgyDTVVGE---RGVnlSGGQRQRIAIARALLKD 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622936545 204 PSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTII 239
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK-GRTTI 529
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
78-245 |
1.99e-16 |
|
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: 78.30 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGalRPTNFKCNSG-----YVVQDDVVMGTLTVRENLQFSAALrlpttm 152
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPP--LAGRVLLNG--GPLDFQRDSIargllYLGHAPGIKTTLSVLENLRFWHAD------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 153 tnhEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMS 232
Cdd:cd03231 101 ---HSDEQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGVARFAEAMA 169
|
170
....*....|....*.
gi 1622936545 233 ---KQGRTIIFSIHQP 245
Cdd:cd03231 170 ghcARGGMVVLTTHQD 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
77-268 |
2.43e-16 |
|
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: 78.09 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlptTMTNHE 156
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPD--SGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLK---GLKKEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 157 KNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR 236
Cdd:cd03269 105 ARRRIDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1622936545 237 TIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03269 180 TVILSTHQME-LVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
58-272 |
4.73e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.97 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNFKCNS--------GYVVQ-- 126
Cdd:PRK13639 12 PDGTEALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPT--SGEVLIKG--EPIKYDKKSllevrktvGIVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 DDVVMGTlTVRENLQFSAA-LRLPttmtNHEKNERINRVIQELGLDKVaDSKVGTQFirgvSGGERKRTSIGMELITDPS 205
Cdd:PRK13639 88 DDQLFAP-TVEEDVAFGPLnLGLS----KEEVEKRVKEALKAVGMEGF-ENKPPHHL----SGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPVYA-----DKVYVMSDGKIIKEGTPKE 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
64-294 |
5.33e-16 |
|
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: 77.76 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--ALRPTNFKCNSGYVVQDDVVMGTLTVRENL 140
Cdd:cd03296 18 LDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGedATDVPVQERNVGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 141 QFSAALRLPTTMTNH-EKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:cd03296 96 AFGLRVKPRSERPPEaEIRAKVHELLKLVQLDWLADR-----YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 220 TANAVLLLLKRM-SKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLmfhgpaqealgyfESAGYHCEAYNNPADFF 294
Cdd:cd03296 171 VRKELRRWLRRLhDELHVTTVFVTHDQEEAL-EVADRVVVMNKGRI-------------EQVGTPDEVYDHPASPF 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
77-272 |
7.45e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.61 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSL----LDVLAArkDpsglSGDVLINGA-LRPTNFKcNSGYvvqddvvM----G---TLTVRENLQFSA 144
Cdd:COG4152 31 GLLGPNGAGKTTTiriiLGILAP--D----SGEVLWDGEpLDPEDRR-RIGY-------LpeerGlypKMKVGEQLVYLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 145 ALRlptTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 224
Cdd:COG4152 97 RLK---GLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622936545 225 LLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:COG4152 169 KDVIRELAAKGTTVIFSSHQME-LVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
77-272 |
7.72e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTLTVREnlqFSAALRLP--- 149
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAqpleSWSSKAFARKVAYLPQQLPAAEGMTVRE---LVAIGRYPwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 150 -TTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:PRK10575 116 aLGRFGAADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622936545 229 KRMSKQ-GRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQE 272
Cdd:PRK10575 191 HRLSQErGLTVIAVLHDinmaARYC-----DYLVALRGGEMIAQGTPAE 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
122-217 |
1.40e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 122 GYVVQDDVVMGTLTVRENLQfsAALRLpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELI 201
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNIL--AVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAYS-----LSGGERRRVEIARALA 152
|
90
....*....|....*.
gi 1622936545 202 TDPSILFLDEPTTGLD 217
Cdd:COG1137 153 TNPKFILLDEPFAGVD 168
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
64-239 |
1.82e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.69 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA--LR-----------------PTNFKcnsgy 123
Cdd:COG4674 26 LNDLSLYVDPGeLRVIIGPNGAGKTTLMDVITGKTRPD--SGSVLFGGTdlTGldeheiarlgigrkfqkPTVFE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 124 vvqddvvmgTLTVRENLQFSAA-----LRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGM 198
Cdd:COG4674 99 ---------ELTVFENLELALKgdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGL-----LSHGQKQWLEIGM 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622936545 199 ELITDPSILFLDEPTTGL-DSSTANAVlLLLKRMSKQgRTII 239
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGMtDAETERTA-ELLKSLAGK-HSVV 204
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
60-272 |
2.14e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.28 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLA--ARKDpsglSGDVLING-----------A-----LRptnfkcn 120
Cdd:COG4604 13 GKVVLDDVSlTIPKGGITALIGPNGAGKSTLLSMISrlLPPD----SGEVLVDGldvattpsrelAkrlaiLR------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 121 sgyvvQDDVVMGTLTVRENLQFSaalRLPTT---MTNhEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIG 197
Cdd:COG4604 82 -----QENHINSRLTVRELVAFG---RFPYSkgrLTA-EDREIIDEAIAYLDLEDLAD-----RYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 198 MELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQE 272
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDinfaSCYA-----DHIVAMKDGRVVAQGTPEE 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
77-246 |
2.36e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.09 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGALRPTNFKC---NSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMT 153
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGLLRP--DSGEVRWNGTPLAEQRDEpheNILYLGHLPGLKPELSALENLHFWAAIHGGAQRT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 154 NHEKNERInrviqelGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMS- 232
Cdd:TIGR01189 108 IEDALAAV-------GLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALD---KAGVALLAGLLRa 172
|
170
....*....|....*.
gi 1622936545 233 --KQGRTIIFSIHQPR 246
Cdd:TIGR01189 173 hlARGGIVLLTTHQDL 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
61-262 |
3.32e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.89 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGaLRPTNFKCNSGYVVQDDVVMGTLTVREN 139
Cdd:PRK11248 14 KPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDG-KPVEGPGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 140 LQFSAALRlpttmtNHEKNERINRVIQELGldKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:PRK11248 91 VAFGLQLA------GVEKMQRLEIAHQMLK--KVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622936545 220 TANAV-LLLLKRMSKQGRTIIFSIHQPRYSIFkLFDSLTLLASG 262
Cdd:PRK11248 163 TREQMqTLLLKLWQETGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
59-243 |
3.92e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 75.35 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 59 VEKE-----ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPtnFKCNSGYVVQDD 128
Cdd:cd03300 6 VSKFyggfvALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAGFETPT--SGEILLDGkditNLPP--HKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVMGTLTVRENLQFsaALRLPTTMTNhEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILF 208
Cdd:cd03300 82 ALFPHLTVFENIAF--GLRLKKLPKA-EIKERVAEALDLVQLEGYANRK-----PSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622936545 209 LDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-272 |
4.08e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPTNFKCNS---GYVVQDDVVMGTLTVRENLQ-FSAALRlpttMT 153
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPARARLARariGVVPQFDNLDLEFTVRENLLvFGRYFG----MS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA 220
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622936545 234 QGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13536 221 RGKTILLTTHFMEEAE-RLCDRLCVLEAGRKIAEGRPHA 258
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-272 |
4.59e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPT---NFKCNSGYVVQDDVVMGTLTVRENLQ-FSAALRLPTtmt 153
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPVPSrarHARQRVGVVPQFDNLDPDFTVRENLLvFGRYFGLSA--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 154 nHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:PRK13537 113 -AAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622936545 234 QGRTIIFSIHqprysiF-----KLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13537 187 RGKTILLTTH------FmeeaeRLCDRLCVIEEGRKIAEGAPHA 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
35-274 |
5.18e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.19 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 35 AVLSFHNICYRVkvksgflpGRKPvekeILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--- 110
Cdd:PRK13548 1 AMLEARNLSVRL--------GGRT----LLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGrpl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 --------ALR----PTNFKCNSGYVVQDDVVMGtltvrenlqfsaalRLPTTMTNHEKNERINRVIQELGLDKVADSkv 178
Cdd:PRK13548 67 adwspaelARRravlPQHSSLSFPFTVEEVVAMG--------------RAPHGLSRAEDDALVAAALAQVDLAHLAGR-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 179 gtqFIRGVSGGERKRTSIGMELI------TDPSILFLDEPTTGLDSSTANAVLLLLKRM-SKQGRTIIFSIHQ----PRY 247
Cdd:PRK13548 131 ---DYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDlnlaARY 207
|
250 260
....*....|....*....|....*..
gi 1622936545 248 SifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13548 208 A-----DRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
61-272 |
6.28e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIM-KPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRPTNFK---CNSGYVVQ--DDVVMGT 133
Cdd:PRK13652 17 KEALNNINFIApRNSRIAVIGPNGAGKSTLFRHFNGILKPT--SGSVLIRGePITKENIRevrKFVGLVFQnpDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 lTVRENLQFSAA-LRLPTTMTNHekneRINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK13652 95 -TVEQDIAFGPInLGLDEETVAH----RVSSALHMLGLEELRD-----RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 213 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
74-272 |
6.30e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 74 GLNAILGPTGGGKSSLLDVLAARKDP-SG---LSGDVLI---NGALRPTNfKCNSGYVVQDDVVMGTLTVRENLQFSAAl 146
Cdd:PRK11144 25 GITAIFGRSGAGKTSLINAISGLTRPqKGrivLNGRVLFdaeKGICLPPE-KRRIGYVFQDARLFPHYKVRGNLRYGMA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 rlpttmtnHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:PRK11144 103 --------KSMVAQFDKIVALLGIEPLLD-----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622936545 227 LLKRMSKQGRT-IIFSIHqpryS---IFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK11144 170 YLERLAREINIpILYVSH----SldeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
54-264 |
6.84e-15 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 74.64 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 54 PGRKPVekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDD 128
Cdd:cd03295 11 GGGKKA----VNNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEPT--SGEIFIDGedirEQDPVELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVMGTLTVRENLQFSAALrlpttmtNHEKNERINRVIQEL----GLDkvaDSKVGTQFIRGVSGGERKRTSIGMELITDP 204
Cdd:cd03295 85 GLFPHMTVEENIALVPKL-------LKWPKEKIRERADELlalvGLD---PAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 205 SILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSiFKLFDSLTLLASGRL 264
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEA-FRLADRIAIMKNGEI 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
77-294 |
1.05e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.95 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGALRPTNFKC---NSGYVVQDDVVMGTLTVRENLQFSAALRLP 149
Cdd:COG1118 32 ALLGPSGSGKTTLLRIIA------GLetpdSGRIVLNGRDLFTNLPPrerRVGFVFQHYALFPHMTVAENIAFGLRVRPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 150 TtmtNHEKNERINRVIQELGLDKVADSKVgTQfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLK 229
Cdd:COG1118 106 S---KAEIRARVEELLELVQLEGLADRYP-SQ----LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 230 RM-SKQGRTIIFSIHQP----RYSifklfDSLTLLASGRLMFHGPAQealgyfesagyhcEAYNNPADFF 294
Cdd:COG1118 178 RLhDELGGTTVFVTHDQeealELA-----DRVVVMNQGRIEQVGTPD-------------EVYDRPATPF 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
59-243 |
1.06e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.08 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 59 VEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNfKCNS-----------GYVVQ 126
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPT--SGDVIFNG--QPMS-KLSSaakaelrnqklGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 DDVVMGTLTVRENLqfsAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSI 206
Cdd:PRK11629 95 FHHLLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSE-----LSGGERQRVAIARALVNNPRL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 207 LFLDEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 243
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTH 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
78-297 |
1.12e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 74.60 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLING------------ALRPTNFkcnsGYVVQDDVVMGTLTVRENLQFSAA 145
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPT--SGKVLIDGqdiaamsrkelrELRRKKI----SMVFQSFALLPHRTVLENVAFGLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 146 LRlptTMTNHEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSstanavL 225
Cdd:cd03294 129 VQ---GVPRAEREERAAEALELVGLEGWEHKY-----PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP------L 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 226 -------LLLKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQEALgyfesagyhceayNNPAD-----F 293
Cdd:cd03294 195 irremqdELLRLQAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTPEEIL-------------TNPANdyvreF 260
|
....
gi 1622936545 294 FLDI 297
Cdd:cd03294 261 FRGV 264
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
77-272 |
1.19e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTNFKCNSGYVVQDDVVMGTLTVREnlqFSAALRLPT-- 150
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPA--HGHVWLDGEhiqhYASKEVARRIGLLAQNATTPGDITVQE---LVARGRYPHqp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 151 --TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:PRK10253 112 lfTRWRKEDEEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622936545 229 KRMSK-QGRTIIFSIHQ----PRYSIfklfdSLTLLASGRLMFHGPAQE 272
Cdd:PRK10253 187 SELNReKGYTLAAVLHDlnqaCRYAS-----HLIALREGKIVAQGAPKE 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-269 |
1.33e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 44 YRVKVK-SGFLPG------RKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLaarkdpSGL----SGDVLINGa 111
Cdd:COG4586 11 YRVYEKePGLKGAlkglfrREYREVEAVDDISFTIEPGeIVGFIGPNGAGKSTTIKML------TGIlvptSGEVRVLG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 LRPtnFKCNSGYVVQDDVVMGT-------LTVRENLQFSAAL-RLPTTmtnhEKNERINRVIQELGLDKVADskvgtQFI 183
Cdd:COG4586 84 YVP--FKRRKEFARRIGVVFGQrsqlwwdLPAIDSFRLLKAIyRIPDA----EYKKRLDELVELLDLGELLD-----TPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 184 RGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHqprYS--IFKLFDSLTLLA 260
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSH---DMddIEALCDRVIVID 229
|
....*....
gi 1622936545 261 SGRLMFHGP 269
Cdd:COG4586 230 HGRIIYDGS 238
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
63-263 |
1.51e-14 |
|
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: 72.89 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGALrptnfkcnsGYVVQDDVVMGTlTVRENLQ 141
Cdd:cd03250 20 TLKDINLEVPKGeLVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPGSI---------AYVSQEPWIQNG-TIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 142 FSAALRlpttmtnhekNERINRVIQELGLDKvaDSK---------VGtqfIRGV--SGGERKRTSIGMELITDPSILFLD 210
Cdd:cd03250 88 FGKPFD----------EERYEKVIKACALEP--DLEilpdgdlteIG---EKGInlSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622936545 211 EPTTGLDSSTANAVL--LLLKRMsKQGRTIIFSIHQPRYsiFKLFDSLTLLASGR 263
Cdd:cd03250 153 DPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQLQL--LPHADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
71-243 |
1.72e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.75 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 71 MKPG-LNAILGPTGGGKSSLLDVLAArkDPSGLSGDVLINGALRPTNFK---CNSGYVVQDDVVMGTLTVRENLQFSAAL 146
Cdd:TIGR01257 1962 VRPGeCFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTNISdvhQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 R-LPTtmtnhEKNERI-NRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 224
Cdd:TIGR01257 2040 RgVPA-----EEIEKVaNWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170
....*....|....*....
gi 1622936545 225 LLLLKRMSKQGRTIIFSIH 243
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSH 2128
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
62-245 |
2.00e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.69 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLA------------ARKDPSGLSGDVLinGALRPTNFkcnsGYVVQDD 128
Cdd:PRK10535 22 EVLKGISLDIYAGeMVAIVGASGSGKSTLMNILGcldkptsgtyrvAGQDVATLDADAL--AQLRREHF----GFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVMGTLTVRENLQfsaalrLPTTMTNHEKNERINRVI---QELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:PRK10535 96 HLLSHLTAAQNVE------VPAVYAGLERKQRLLRAQellQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
54-243 |
2.65e-14 |
|
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: 72.96 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 54 PGRKPVEkeILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPsgLSGDVLING----ALRPTNFKCNSGYVVQDD 128
Cdd:cd03249 11 PSRPDVP--ILKGLSLTIPPGKTvALVGSSGCGKSTVVSLLERFYDP--TSGEILLDGvdirDLNLRWLRSQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVMGTlTVRENLQFSaalRLPTTMTNHEKNER---INRVIQEL--GLDKVADSKvGTQfirgVSGGERKRTSIGMELITD 203
Cdd:cd03249 87 VLFDG-TIAENIRYG---KPDATDEEVEEAAKkanIHDFIMSLpdGYDTLVGER-GSQ----LSGGQKQRIAIARALLRN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622936545 204 PSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIH 243
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
37-268 |
3.16e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.18 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNIC--YRVKVKSGFL--------PGRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGD 105
Cdd:cd03220 1 IELENVSksYPTYKGGSSSlkklgilgRKGEVGEFWALKDVSFEVPRGERiGLIGRNGAGKSTLLRLLAGIYPPD--SGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 106 VLINGALRPTnFKCNSGyvvqddvVMGTLTVRENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADSKVGTqfirg 185
Cdd:cd03220 79 VTVRGRVSSL-LGLGGG-------FNPELTGRENIYLNGRLL---GLSRKEIDEKIDEIIEFSELGDFIDLPVKT----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLM 265
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS-SIKRLCDRALVLEKGKIR 221
|
...
gi 1622936545 266 FHG 268
Cdd:cd03220 222 FDG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
60-246 |
3.30e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLING----ALRPTNfKCNSG--YVVQDDVVMG 132
Cdd:COG0396 12 GKEILKGVNLTIKPGeVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGedilELSPDE-RARAGifLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSAALRLPTTMTNHEKNERINRVIQELGLDKvadskvgtQFI-RGV----SGGERKRTSIGMELITDPSIL 207
Cdd:COG0396 91 GVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDE--------DFLdRYVnegfSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622936545 208 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPR 246
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQR 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
77-274 |
3.84e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--------ALRPTNFkcnsgyVVQDDVVMGTLTVREN--LQFSAAL 146
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGqdhtttppSRRPVSM------LFQENNLFSHLTVAQNigLGLNPGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 RLpttmtNHEKNERINRVIQELGLDKVADsKVGTQfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:PRK10771 101 KL-----NAAQREKLHAIARQMGIEDLLA-RLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 227 LLKRMSKQGR-TIIFSIHQ--------PRysifklfdSLtLLASGRLMFHGPAQEAL 274
Cdd:PRK10771 171 LVSQVCQERQlTLLMVSHSledaariaPR--------SL-VVADGRIAWDGPTDELL 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
75-268 |
4.49e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.21 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 75 LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPTNF---KCNSGYVVQDDVVMGTLTVRENLQFSAALRlptT 151
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPT--SGTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQLK---G 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 152 MTNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLKR 230
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWdLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 231 MSkqGRTIIFSIHQPRYSIFkLFDSLTLLASGRLMFHG 268
Cdd:TIGR01257 1108 RS--GRTIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-272 |
5.48e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 33 EGAVlSFHNICYRvkvksgfLPGRKPVekeiLSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA 111
Cdd:PRK13657 332 KGAV-EFDDVSFS-------YDNSRQG----VEDVSFEAKPGQTvAIVGPTGAGKSTLINLLQRVFDPQ--SGRILIDGT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 -LRPTNFKC---NSGYVVQDDVVMGTlTVRENLQFSAALRLPTTMtnHEKNER------INRviQELGLDKVadskVGTq 181
Cdd:PRK13657 398 dIRTVTRASlrrNIAVVFQDAGLFNR-SIEDNIRVGRPDATDEEM--RAAAERaqahdfIER--KPDGYDTV----VGE- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 182 fiRG--VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLL 259
Cdd:PRK13657 468 --RGrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAH--RLSTVRNADRILVF 542
|
250
....*....|...
gi 1622936545 260 ASGRLMFHGPAQE 272
Cdd:PRK13657 543 DNGRVVESGSFDE 555
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
52-272 |
5.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 52 FLPGrKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGaLRPTNFKCN-------SGY 123
Cdd:PRK13637 12 YMEG-TPFEKKALDNVNIEIEDGeFVGLIGHTGSGKSTLIQHLNGLLKPT--SGKIIIDG-VDITDKKVKlsdirkkVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 124 VVQ-DDVVMGTLTVRENLQFSaalrlPTTM--TNHEKNERINRVIQELGLDKvADSKVGTQFirGVSGGERKRTSIGMEL 200
Cdd:PRK13637 88 VFQyPEYQLFEETIEKDIAFG-----PINLglSEEEIENRVKRAMNIVGLDY-EDYKDKSPF--ELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 201 ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME-DVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
60-282 |
6.79e-14 |
|
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: 70.63 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGalrptnfkcnsgyvvqddvvmgtltvrE 138
Cdd:cd03217 12 GKEILKGVNLTIKKGeVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG---------------------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 139 NLqfsaalrlpttmTNHEKNERINRVI----QE----LGLdKVADskvgtqFIRGV----SGGERKRTSIGMELITDPSI 206
Cdd:cd03217 65 DI------------TDLPPEERARLGIflafQYppeiPGV-KNAD------FLRYVnegfSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 207 LFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysIFKLF--DSLTLLASGRLMFHGPAQEALgYFESAGY 282
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQR--LLDYIkpDRVHVLYDGRIVKSGDKELAL-EIEKKGY 200
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
60-273 |
7.90e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTl 134
Cdd:PRK10247 19 DAKILNNISFSLRAGeFKLITGPSGCGKSTLLKIVASLISPT--SGTLLFEGedisTLKPEIYRQQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENLQFSAALRlpttmTNHEKNERINRVIQELGLDKvadsKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:PRK10247 96 TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALPD----TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGrlmfhGPAQEA 273
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA-----GEMQEA 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
62-244 |
8.66e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------------ALRPtnfkcNSGYVV 125
Cdd:COG4161 16 QALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPD--SGQLNIAGhqfdfsqkpsekairLLRQ-----KVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 QDDVVMGTLTVRENLqFSAALRLpTTMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPS 205
Cdd:COG4161 89 QQYNLWPHLTVMENL-IEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADR-----FPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
52-231 |
8.67e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.04 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 52 FLPGrKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA--LRPTNFKCNS--GYVVQ 126
Cdd:COG1101 11 FNPG-TVNEKRALDGLNLTIEEGdFVTVIGSNGAGKSTLLNAIAGSLPPD--SGSILIDGKdvTKLPEYKRAKyiGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 DdVVMGT---LTVRENLQFsAALR-----LPTTMTNHEKN---ERINRViqELGLDKVADSKVGTqfirgVSGGERKRTS 195
Cdd:COG1101 88 D-PMMGTapsMTIEENLAL-AYRRgkrrgLRRGLTKKRRElfrELLATL--GLGLENRLDTKVGL-----LSGGQRQALS 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622936545 196 IGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 231
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
77-274 |
9.53e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 71.17 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLaarkdpSGL----SGDVLING---ALRPTNFKCNSG--YVVQDDVVMGTLTVRENLQFSAALR 147
Cdd:COG0410 33 ALLGRNGAGKTTLLKAI------SGLlpprSGSIRFDGediTGLPPHRIARLGigYVPEGRRIFPSLTVEENLLLGAYAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 LPTtmtnHEKNERINRV------IQELgldkvADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTA 221
Cdd:COG0410 107 RDR----AEVRADLERVyelfprLKER-----RRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 222 NAVLLLLKRMSKQGRTIIFS---IHQprysIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG0410 173 EEIFEIIRRLNREGVTILLVeqnARF----ALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
60-217 |
1.67e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPGlN--AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRptnfkcnSGYVVQDDVVMGTLTVR 137
Cdd:COG0488 10 GRPLLDDVSLSINPG-DriGLVGRNGAGKSTLLKILAGELEPD--SGEVSIPKGLR-------IGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 ENL------------QFSAALRLPTTMTN--------HEKNE---------RINRVIQELGLDKV-ADSKVGTqfirgVS 187
Cdd:COG0488 80 DTVldgdaelraleaELEELEAKLAEPDEdlerlaelQEEFEalggweaeaRAEEILSGLGFPEEdLDRPVSE-----LS 154
|
170 180 190
....*....|....*....|....*....|
gi 1622936545 188 GGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
80-243 |
2.31e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 80 GPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTnfKCNSGYVVQDDVVMGTLTVRENLQFsaALRLPTTMTNh 155
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDIT--SGDLFIGEKrmndVPPA--ERGVGMVFQSYALYPHLSVAENMSF--GLKLAGAKKE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 156 EKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ- 234
Cdd:PRK11000 109 EINQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRl 183
|
....*....
gi 1622936545 235 GRTIIFSIH 243
Cdd:PRK11000 184 GRTMIYVTH 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
78-245 |
2.42e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPsgLSGDVLING----ALRPTnFKCNSGYV-----VQDDvvmgtLTVRENLQFSAALRL 148
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARP--DAGEVLWQGepirRQRDE-YHQDLLYLghqpgIKTE-----LTALENLRFYQRLHG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 149 PTTmtnhekNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLL 228
Cdd:PRK13538 104 PGD------DEALWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAID---KQGVARLE 169
|
170 180
....*....|....*....|
gi 1622936545 229 KRMS---KQGRTIIFSIHQP 245
Cdd:PRK13538 170 ALLAqhaEQGGMVILTTHQD 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-264 |
2.54e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 34 GAVLSFHNIcyrvkvkSGFLPGRKPvekeiLSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGal 112
Cdd:PRK11288 2 SPYLSFDGI-------GKTFPGVKA-----LDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 113 RPTNFK-----CNSGYVV--QDDVVMGTLTVRENLQFSaalRLPTT--MTNHEK-NERINRVIQELGLDKVADSKVGTqf 182
Cdd:PRK11288 66 QEMRFAsttaaLAAGVAIiyQELHLVPEMTVAENLYLG---QLPHKggIVNRRLlNYEAREQLEHLGVDIDPDTPLKY-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 183 irgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASG 262
Cdd:PRK11288 141 ---LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDG 216
|
..
gi 1622936545 263 RL 264
Cdd:PRK11288 217 RY 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
60-280 |
2.58e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.38 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTN-------------FKCNS 121
Cdd:PRK10619 17 EHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPS--EGSIVVNGQtinlVRDKDgqlkvadknqlrlLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 122 GYVVQDDVVMGTLTVRENLQFSAALRLptTMTNHEKNERINRVIQELGLDKVADSKVGTQfirgVSGGERKRTSIGMELI 201
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQGKYPVH----LSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 202 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQEALGYFESA 280
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA-RHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
36-280 |
3.46e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 36 VLSFHNI--CYRV------KVKSGFLPGRKP--VEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpsglsg 104
Cdd:COG1134 4 MIEVENVskSYRLyhepsrSLKELLLRRRRTrrEEFWALKDVSFEVERGESvGIIGRNGAGKSTLLKLIA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 105 dvlinGALRPTnfkcnSGYV-VQDDVV----MGT-----LTVRENLQFSAALRlptTMTNHEKNERINRVIQ--ELGldK 172
Cdd:COG1134 74 -----GILEPT-----SGRVeVNGRVSalleLGAgfhpeLTGRENIYLNGRLL---GLSRKEIDEKFDEIVEfaELG--D 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 173 VADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPT-TGlDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFK 251
Cdd:COG1134 139 FIDQPVKT-----YSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMG-AVRR 211
|
250 260
....*....|....*....|....*....
gi 1622936545 252 LFDSLTLLASGRLMFHGPAQEALGYFESA 280
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
77-272 |
3.83e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLaarkdpSGL-SGD--------VLINGALRPTNF-------KCNSGYVVQDDVVMGTLTVRENL 140
Cdd:PRK09984 34 ALLGPSGSGKSTLLRHL------SGLiTGDksagshieLLGRTVQREGRLardirksRANTGYIFQQFNLVNRLSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 141 QFSAALRLPTTMT-----NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK09984 108 LIGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 216 LDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQ 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
77-269 |
4.03e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------ALRptNFKCNSGYVVQDDVVMGTLTVRENLQFsaALR 147
Cdd:COG1135 35 GIIGYSGAGKSTLIRCINLLERPT--SGSVLVDGvdltalserELR--AARRKIGMIFQHFNLLSSRTVAENVAL--PLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 LpttmTNHEKNERINRViQEL----GL-DKvADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:COG1135 109 I----AGVPKAEIRKRV-AELlelvGLsDK-ADA-----YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 223 AVLLLLKRMSKQ-GRTIIFSIHQP---RysifKLFDSLTLLASGRLMFHGP 269
Cdd:COG1135 178 SILDLLKDINRElGLTIVLITHEMdvvR----RICDRVAVLENGRIVEQGP 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
77-274 |
8.72e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.64 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLPTTM 152
Cdd:PRK09536 33 GLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAGddveALSARAASRRVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 153 TNHEKNER-INRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 231
Cdd:PRK09536 111 TWTETDRAaVERAMERTGVAQFADRPVTS-----LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622936545 232 SKQGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK09536 186 VDDGKTAVAAIHDldlaARYC-----DELVLLADGRVRAAGPPADVL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
61-272 |
8.96e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLS---GDVLINGAlRPTN--------FKCNSGYVVQDD 128
Cdd:PRK11264 16 QTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvGDITIDTA-RSLSqqkglirqLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVMGTLTVRENLqfsaaLRLPTTMTNHEKNERINRViQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILF 208
Cdd:PRK11264 95 NLFPHRTVLENI-----IEGPVIVKGEPKEEATARA-REL-LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA-RDVADRAIFMDQGRIVEQGPAKA 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
78-274 |
2.35e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAarkdpsGL---SGDVLINGA----LRPTNFKCNSGYVVQDDVVMGTLTVRENLqfsaALRLPT 150
Cdd:PRK03695 27 LVGPNGAGKSTLLARMA------GLlpgSGSIQFAGQpleaWSAAELARHRAYLSQQQTPPFAMPVFQYL----TLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 151 TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSI-GMELITDPSI------LFLDEPTTGLDSSTANA 223
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRLaAVVLQVWPDInpagqlLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 224 VLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK03695 172 LDRLLSELCQQGIAVVMSSHDLNHT-LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
48-243 |
3.05e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 48 VKSGFLPgRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSS----LLDVLAARkdpsglsGDVLING---------ALR 113
Cdd:PRK15134 287 IRKGILK-RTVDHNVVVKNISFTLRPGETlGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGqplhnlnrrQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 114 PtnFKCNSGYVVQDDvvMGTLTVRENLQ--FSAALRL-PTTMTNHEKNERINRVIQELGLDKVADSKVGTQFirgvSGGE 190
Cdd:PRK15134 359 P--VRHRIQVVFQDP--NSSLNPRLNVLqiIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQ 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 191 RKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR-TIIFSIH 243
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISH 484
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
64-262 |
4.37e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 66.34 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNFKCNSGYVV-QDDVVMGTLTVRENLQ 141
Cdd:TIGR01184 1 LKGVNLTIQQGeFISLIGHSGCGKSTLLNLISGLAQPT--SGGVILEG--KQITEPGPDRMVVfQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 142 FSAALRLPTtMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST- 220
Cdd:TIGR01184 77 LAVDRVLPD-LSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTr 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622936545 221 ANAVLLLLKRMSKQGRTIIFSIHQPRYSIFkLFDSLTLLASG 262
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
78-244 |
4.46e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAL----RPTNFKC------NSGYVVQDDVVMGTLTVRENLqFSAALR 147
Cdd:PRK11124 33 LLGPSGAGKSSLLRVLNLLEMPR--SGTLNIAGNHfdfsKTPSDKAirelrrNVGMVFQQYNLWPHLTVQQNL-IEAPCR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 LpTTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 227
Cdd:PRK11124 110 V-LGLSKDQALARAEKLLERLRLKPYAD-----RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
170
....*....|....*..
gi 1622936545 228 LKRMSKQGRTIIFSIHQ 244
Cdd:PRK11124 184 IRELAETGITQVIVTHE 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
61-243 |
4.50e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.05 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA--------LRPTNfkcnsgYVVQDDVVM 131
Cdd:PRK09452 27 KEVISNLDLTINNGeFLTLLGPSGCGKTTVLRLIAGFETPD--SGRIMLDGQdithvpaeNRHVN------TVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFsaALRLPTTmTNHEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK09452 99 PHMTVFENVAF--GLRMQKT-PAAEITPRVMEALRMVQLEEFAQRK-----PHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190
....*....|....*....|....*....|...
gi 1622936545 212 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKlGITFVFVTH 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
58-243 |
4.62e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPTNFKCNSGYVVQDDVVMGtLTV 136
Cdd:PRK13651 17 PTELKALDNVSVEINQGeFIAIIGQTGSGKTTFIEHLNALLLPD--TGTIEWIFKDEKNKKKTKEKEKVLEKLVIQ-KTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSAALRL-------------------------PTTM--TNHEKNERINRVIQELGLDKVADSKvgTQFirGVSGG 189
Cdd:PRK13651 94 FKKIKKIKEIRRrvgvvfqfaeyqlfeqtiekdiifgPVSMgvSKEEAKKRAAKYIELVGLDESYLQR--SPF--ELSGG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 190 ERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
77-240 |
7.24e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 67.00 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKS----SLLDVLaarKDPSGLSGDVLING------------ALRPTNFkcnsGYVVQDdvVMGTL----TV 136
Cdd:COG0444 35 GLVGESGSGKStlarAILGLL---PPPGITSGEILFDGedllklsekelrKIRGREI----QMIFQD--PMTSLnpvmTV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 REnlQFSAALRLPTTMTNHEKNERINRVIQELGLD---KVADSKVGtQFirgvSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:COG0444 106 GD--QIAEPLRIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPH-EL----SGGMRQRVMIARALALEPKLLIADEPT 178
|
170 180
....*....|....*....|....*...
gi 1622936545 214 TGLDSSTANAVLLLLKRMSKQ-GRTIIF 240
Cdd:COG0444 179 TALDVTIQAQILNLLKDLQRElGLAILF 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
55-274 |
8.10e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 55 GRKPVEkeilsNINGIMKPG-LNAILGPTGGGKSSLLDVLAA--RKDpsglSGDVLING---ALRPTNFKCNSG--YVVQ 126
Cdd:PRK10895 15 GRRVVE-----DVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGivPRD----AGNIIIDDediSLLPLHARARRGigYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 DDVVMGTLTVRENLQfsAALRLPTTMTNHEKNERINRVIQELGLDKVADSkVGtqfiRGVSGGERKRTSIGMELITDPSI 206
Cdd:PRK10895 86 EASIFRRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDS-MG----QSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 207 LFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
77-240 |
1.00e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLaarkdpSGL----SGDVLINGalRPTNFKcnS---------GYVVQDDVVMGTLTVRENLqfs 143
Cdd:COG3845 35 ALLGENGAGKSTLMKIL------YGLyqpdSGEILIDG--KPVRIR--SprdaialgiGMVHQHFMLVPNLTVAENI--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 144 aAL---RLPTTMTNHEK-NERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:COG3845 102 -VLglePTKGGRLDRKAaRARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEPTAVLTPQ 175
|
170 180
....*....|....*....|.
gi 1622936545 220 TANAVLLLLKRMSKQGRTIIF 240
Cdd:COG3845 176 EADELFEILRRLAAEGKSIIF 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
63-274 |
1.02e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLS------GDVLING----ALRPTNFKCNSGYVVQDDVVM 131
Cdd:PRK13547 16 ILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvtGDVTLNGeplaAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENL---QFSAALRlpTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMEL-------- 200
Cdd:PRK13547 96 FAFSAREIVllgRYPHARR--AGALTHRDGEIAWQALALAGATALVGRDVTT-----LSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 201 -ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI-HQP----RYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPnlaaRHA-----DRIAMLADGAIVAHGAPADVL 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
54-274 |
1.16e-11 |
|
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: 67.47 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 54 PGRKpveKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGA----LRPTNFKCNSGYV 124
Cdd:COG4618 341 PGSK---RPILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLV------GVwpptAGSVRLDGAdlsqWDREELGRHIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 125 VQDdvVmgTL---TVRENL-QFS---------AA---------LRLPttmtnheknerinrviqeLGLD-KVADSkvGTq 181
Cdd:COG4618 412 PQD--V--ELfdgTIAENIaRFGdadpekvvaAAklagvhemiLRLP------------------DGYDtRIGEG--GA- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 182 firGVSGGERKRtsIGME--LITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHqpRYSIFKLFDSLTLL 259
Cdd:COG4618 467 ---RLSGGQRQR--IGLAraLYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH--RPSLLAAVDKLLVL 539
|
250
....*....|....*
gi 1622936545 260 ASGRLMFHGPAQEAL 274
Cdd:COG4618 540 RDGRVQAFGPRDEVL 554
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
64-262 |
1.24e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPT-----NFKCNSGYVVQDDVVMGTLTVR 137
Cdd:PRK09700 21 LKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPT--KGTITINNINYNKldhklAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 ENLQFSaalRLPT-------TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK09700 99 ENLYIG---RHLTkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASG 262
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDG 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
77-272 |
1.31e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAA--RKDpsglSGDVLINGalRPTNFK-----CNSGYVV--QDDVVMGTLTVRENLqfsaAL- 146
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvyQPD----SGEILLDG--EPVRFRsprdaQAAGIAIihQELNLVPNLSVAENI----FLg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 RLPTT--MTNHEK-NERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:COG1129 104 REPRRggLIDWRAmRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 224 VLLLLKRMSKQGRTIIFsIhqpryS-----IFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:COG1129 179 LFRIIRRLKAQGVAIIY-I-----ShrldeVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
60-244 |
1.38e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.83 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGAlRPTNFKCNS-----GYVVQDDVVMGT 133
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTG--GQVLLDGV-PLVQYDHHYlhrqvALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 lTVRENLQFSAALRLPTTMTNHEKNERINRVIQEL--GLDKVADSKvGTQfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEK-GSQ----LSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190
....*....|....*....|....*....|...
gi 1622936545 212 PTTGLDsstANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:TIGR00958 644 ATSALD---AECEQLLQESRSRASRTVLLIAHR 673
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
64-274 |
1.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--ALRPTNF---KCNSGYVVQD-DVVMGTLTV 136
Cdd:PRK13644 18 LENINlVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGidTGDFSKLqgiRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSAA-LRLPTTmtnhEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK13644 96 EEDLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKT-----LSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHN--LEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
60-282 |
2.19e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.20 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLING----ALRPtNFKCNSGYVV--QDDVVMG 132
Cdd:TIGR01978 12 DKEILKGVNLTVKKGeIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGqdllELEP-DERARAGLFLafQYPEEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSA----ALRLPTTMTNHEKNERINRVIQELGLDK-VADSKVGTQFirgvSGGERKRTSIGMELITDPSIL 207
Cdd:TIGR01978 91 GVSNLEFLRSALnarrSARGEEPLDLLDFEKLLKEKLALLDMDEeFLNRSVNEGF----SGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 208 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysIFKLF--DSLTLLASGRLMFHGPAQEALgYFESAGY 282
Cdd:TIGR01978 167 ILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR--LLNYIkpDYVHVLLDGRIVKSGDVELAK-ELEAKGY 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
62-272 |
2.38e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTNFKCNSGYVV-QDDVVMGTLT 135
Cdd:PRK15439 25 EVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNpcarLTPAKAHQLGIYLVpQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQFsaalRLPTTMtnhEKNERINRVIQELGLDKVADSKVGTQFIrgvsgGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK15439 103 VKENILF----GLPKRQ---ASMQKMKQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGKTAD 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
61-277 |
2.43e-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: 66.36 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAL--------RPTNF-----KCNSGYVVQ 126
Cdd:TIGR03269 13 KEVLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALcekcgyveRPSKVgepcpVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 D-DVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINRVIQ---ELG-------------LDKVADSKVGTQFIRGVSGG 189
Cdd:TIGR03269 93 EvDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEaleEIGyegkeavgravdlIEMVQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 190 ERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHG 268
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEV-IEDLSDKAIWLENGEIKEEG 251
|
....*....
gi 1622936545 269 PAQEALGYF 277
Cdd:TIGR03269 252 TPDEVVAVF 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
47-243 |
3.33e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 47 KVKSGFLPGRkpvekEILSNINGIMKPGLNAIL-GPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTN---FK 118
Cdd:PRK10908 6 HVSKAYLGGR-----QALQGVTFHMRPGEMAFLtGHSGAGKSTLLKLICGIERPS--AGKIWFSGhditRLKNREvpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 119 CNSGYVVQDDVVMGTLTVRENLQfsaalrLPTTMTNhEKNERINRVIQElGLDKVADSKVGTQFIRGVSGGERKRTSIGM 198
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVA------IPLIIAG-ASGDDIRRRVSA-ALDKVGLLDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622936545 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
63-264 |
3.45e-11 |
|
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: 63.64 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGalrptnfKCNSGY-----------VVQDDVV 130
Cdd:cd03248 29 VLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQG--GQVLLDG-------KPISQYehkylhskvslVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 MGTlTVRENLQFSAALRLPTTMTNHEKNERINRVIQEL--GLDKVADSKvGTQfirgVSGGERKRTSIGMELITDPSILF 208
Cdd:cd03248 100 FAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELasGYDTEVGEK-GSQ----LSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 209 LDEPTTGLDSSTANAVLLLLkRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRL 264
Cdd:cd03248 174 LDEATSALDAESEQQVQQAL-YDWPERRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
58-243 |
4.41e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.03 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDvlaarkdpsglsgdvLINGALRPTNfkcnsGYVVQDDVVMGTLT- 135
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGkYYAIVGQTGSGKSTLIQ---------------NINALLKPTT-----GTVTVDDITITHKTk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 ------VRENL----QFSAALRLPTT-------------MTNHEKNERINRVIQELGLDKVADSKVGTQfirgVSGGERK 192
Cdd:PRK13646 77 dkyirpVRKRIgmvfQFPESQLFEDTvereiifgpknfkMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQ----MSGGQMR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 193 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 243
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
60-239 |
4.91e-11 |
|
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: 65.61 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------ALRPTnfkcnSGYVVQDdV 129
Cdd:COG5265 370 ERPILKGVSFEVPAGKTvAIVGPSGAGKSTLARLLFRFYDVT--SGRILIDGqdirdvtqaSLRAA-----IGIVPQD-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 130 VMGTLTVRENLQFS----------AALRLPttmtnhekneRINRVIQEL--GLDkvadSKVGTqfiRGV--SGGERKRTS 195
Cdd:COG5265 442 VLFNDTIAYNIAYGrpdaseeeveAAARAA----------QIHDFIESLpdGYD----TRVGE---RGLklSGGEKQRVA 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622936545 196 IGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTII 239
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTL 547
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
58-220 |
5.59e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpsGLSGDvlINGALRPT-NFKCnsGYVVQDDVVMGTLT 135
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKiGVLGLNGAGKSTLLRIMA------GVDKD--FNGEARPQpGIKV--GYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENL---------------QFSAALRLPTTMTNH--EKNERINRVIQELG-------LDKVADS---KVGTQFIRGVSG 188
Cdd:TIGR03719 85 VRENVeegvaeikdaldrfnEISAKYAEPDADFDKlaAEQAELQEIIDAADawdldsqLEIAMDAlrcPPWDADVTKLSG 164
|
170 180 190
....*....|....*....|....*....|..
gi 1622936545 189 GERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
77-243 |
5.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRPTNFK---CNSGYVVQD-DVVMGTLTVRENLQFSaalrlPTT 151
Cdd:PRK13647 35 ALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMGrEVNAENEKwvrSKVGLVFQDpDDQVFSSTVWDDVAFG-----PVN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 152 M--TNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLK 229
Cdd:PRK13647 108 MglDKDEVERRVEEALKAVRMWDFRDKPP-----YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD 182
|
170
....*....|....
gi 1622936545 230 RMSKQGRTIIFSIH 243
Cdd:PRK13647 183 RLHNQGKTVIVATH 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
60-287 |
6.89e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.12 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQDDVVMGTl 134
Cdd:PRK10789 327 DHPALENVNFTLKPGqMLGICGPTGSGKSTLLSLIQRHFDVS--EGDIRFHDipltKLQLDSWRSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENLqfsaALRLPT-TMTNHEKNERINRVIQE-LGLDKVADSKVGTqfiRGV--SGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK10789 404 TVANNI----ALGRPDaTQQEIEHVARLASVHDDiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEALgyfESAGYHCEAY 287
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWG-EGRTVIISAH--RLSALTEASEILVMQHGHIAQRGNHDQLA---QQSGWYRDMY 547
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
62-274 |
1.22e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.03 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLING------ALRPTNFKCNSGYVVQDDVVMGTL 134
Cdd:PRK09493 15 QVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITS--GDLIVDGlkvndpKVDERLIRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENLQFSaalrlPTTMTNHEKNErINRVIQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:PRK09493 93 TALENVMFG-----PLRVRGASKEE-AEKQAREL-LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFA-EKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-272 |
3.06e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.08 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDV---LAARKDPSGLSGDVLING----ALRPTNFKCNSGYVVQDDVVMGT 133
Cdd:PRK14247 17 EVLDGVNLEIPDNtITALMGPSGSGKSTLLRVfnrLIELYPEARVSGEVYLDGqdifKMDVIELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRENLQFSAAL-RLptTMTNHEKNERINRVIQELGL-DKVADsKVGTQFIRgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK14247 97 LSIFENVALGLKLnRL--VKSKKELQERVRWALEKAQLwDEVKD-RLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 212 PTTGLD-SSTANAVLLLLKRmsKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14247 173 PTANLDpENTAKIESLFLEL--KKDMTIVLVTHFPQQAA-RISDYVAFLYKGQIVEWGPTRE 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
77-244 |
3.07e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.33 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLaarkdpSGL---SGDVLING----ALRPTNFKCNSGYVVQDDVVM-GTLtvRENLqfsaalrl 148
Cdd:PRK11174 380 ALVGPSGAGKTSLLNAL------LGFlpyQGSLKINGielrELDPESWRKHLSWVGQNPQLPhGTL--RDNV-------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 149 ptTMTNHEKN-ERINRVI-----------QELGLDkvadSKVGTQFIrGVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:PRK11174 444 --LLGNPDASdEQLQQALenawvseflplLPQGLD----TPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180
....*....|....*....|....*...
gi 1622936545 217 DSSTANAVLLLLKRMSkQGRTIIFSIHQ 244
Cdd:PRK11174 517 DAHSEQLVMQALNAAS-RRQTTLMVTHQ 543
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
35-265 |
4.38e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 60.97 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 35 AVLSFHNICYRVKvKSGFLpgRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-- 111
Cdd:TIGR02769 1 SLLEVRDVTHTYR-TGGLF--GAKQRAPVLTNVSLSIEEGETvGLLGRSGCGKSTLARLLLGLEKPA--QGTVSFRGQdl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 --LRPTN---FKCNSGYVVQD--DVVMGTLTVRENLqfSAALRLPTTMTNHEKNERINRVIQELGLDkvadSKVGTQFIR 184
Cdd:TIGR02769 76 yqLDRKQrraFRRDVQLVFQDspSAVNPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLR----SEDADKLPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 185 GVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGR 263
Cdd:TIGR02769 150 QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLR-LVQSFCQRVAVMDKGQ 228
|
..
gi 1622936545 264 LM 265
Cdd:TIGR02769 229 IV 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
37-272 |
5.80e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRvkvksgFLPGrKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLI------- 108
Cdd:PRK13641 3 IKFENVDYI------YSPG-TPMEKKGLDNISfELEEGSFVALVGHTGSGKSTLMQHFNALLKPS--SGTITIagyhitp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 109 ---NGALRPTNFKCnsGYVVQ-DDVVMGTLTVRENLQFSAalrLPTTMTNHEKNERINRVIQELGLDKVADSKvgTQFir 184
Cdd:PRK13641 74 etgNKNLKKLRKKV--SLVFQfPEAQLFENTVLKDVEFGP---KNFGFSEDEAKEKALKWLKKVGLSEDLISK--SPF-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 185 GVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:PRK13641 145 ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKL 223
|
....*...
gi 1622936545 265 MFHGPAQE 272
Cdd:PRK13641 224 IKHASPKE 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
60-284 |
7.23e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGA----LRPTNfKCNSG------YVVQDD 128
Cdd:CHL00131 19 ENEILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGEsildLEPEE-RAHLGiflafqYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 129 VVmgtltvrENLQFsaaLRLPTTMTNHEKN----------ERINRVIQELGLDKVadskvgtqFI-----RGVSGGERKR 193
Cdd:CHL00131 98 GV-------SNADF---LRLAYNSKRKFQGlpeldpleflEIINEKLKLVGMDPS--------FLsrnvnEGFSGGEKKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 194 TSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEA 273
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELA 239
|
250
....*....|.
gi 1622936545 274 LgYFESAGYHC 284
Cdd:CHL00131 240 K-ELEKKGYDW 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-272 |
1.41e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNIN-GIMKPGLNAILGPTGGGKSSLL---DVLAARKDPSGLSGDVLINGA------LRPTNFKCNSGYVVQDDVVM 131
Cdd:PRK14267 18 HVIKGVDlKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGRniyspdVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFSAALRlPTTMTNHEKNERINRVIQELGL-DKVADSKvgTQFIRGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK14267 98 PHLTIYDNVAIGVKLN-GLVKSKKELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAA-RVSDYVAFLYLGKLIEVGPTRK 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
181-278 |
1.46e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 181 QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLA 260
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLR 210
|
90
....*....|....*...
gi 1622936545 261 SGRLMFHGPAQEALGYFE 278
Cdd:PRK13638 211 QGQILTHGAPGEVFACTE 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-272 |
1.96e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVL----AARKDPSGLSGDVLINGA----LRPTNFKCNSGYVVQDDVV 130
Cdd:PRK14246 22 DKAILKDITiKIPNNSIFGIMGPSGSGKSTLLKVLnrliEIYDSKIKVDGKVLYFGKdifqIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 MGTLTVRENLQFSaaLRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK14246 102 FPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ-QVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
60-229 |
2.09e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.63 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKP-GLNAILGPTGGGKSSLLDVLAARKDpsgLSGDVLINGALrptNFKCNSGYVVQDDVV-----MGT 133
Cdd:PRK14239 17 KKKALNSVSLDFYPnEITALIGPSGSGKSTLLRSINRMND---LNPEVTITGSI---VYNGHNIYSPRTDTVdlrkeIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 ---------LTVRENLQFsaALRLPTTMTNHEKNERINRVIQELGL-----DKVADSKVGtqfirgVSGGERKRTSIGME 199
Cdd:PRK14239 91 vfqqpnpfpMSIYENVVY--GLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG------LSGGQQQRVCIARV 162
|
170 180 190
....*....|....*....|....*....|...
gi 1622936545 200 LITDPSILFLDEPTTGLDSSTANAV---LLLLK 229
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIeetLLGLK 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-272 |
2.34e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.95 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDP-SGL--SGDVLINGA-------------------LRPTNF 117
Cdd:PRK14271 34 KTVLDQVSmGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYrySGDVLLGGRsifnyrdvlefrrrvgmlfQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 118 KCNsgyvVQDDVVMGT----LTVRENLQFSAALRLpttmtnheknerinrviQELGL-DKVADSKVGTQFirGVSGGERK 192
Cdd:PRK14271 114 PMS----IMDNVLAGVrahkLVPRKEFRGVAQARL-----------------TEVGLwDAVKDRLSDSPF--RLSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 193 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSifKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAA--RISDRAALFFDGRLVEEGPTEQ 248
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-272 |
2.94e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 46 VKVKSGFLPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGdVLINGALrptnfkcnsGYV 124
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGsLVAIVGGTGEGKTSLISAMLGELSHAETSS-VVIRGSV---------AYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 125 VQDDVVMGTlTVRENLQFSAALrlpttmtnheKNERINRVIQELGLDKVADSKVGTQFI----RGV--SGGERKRTSIGM 198
Cdd:PLN03232 685 PQVSWIFNA-TVRENILFGSDF----------ESERYWRAIDVTALQHDLDLLPGRDLTeigeRGVniSGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsiFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEGMIKEEGTFAE 825
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
77-264 |
3.12e-09 |
|
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: 56.28 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNFkcnsgyvvqddvvmgtLTVREnlqfsaALRLpttmtnhe 156
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPD--SGEILVDG--KEVSF----------------ASPRD------ARRA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 157 kneRINRVIQelgldkvadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR 236
Cdd:cd03216 76 ---GIAMVYQ-------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGV 133
|
170 180
....*....|....*....|....*...
gi 1622936545 237 TIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:cd03216 134 AVIFISHRLD-EVFEIADRVTVLRDGRV 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
70-217 |
3.38e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 70 IMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA--------LRPTNFkcnsgyVVQDDVVMGTLTVRENLQ 141
Cdd:PRK11607 42 IYKGEIFALLGASGCGKSTLLRMLAGFEQPT--AGQIMLDGVdlshvppyQRPINM------MFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 142 FSAAL-RLPttmtnheKNERINRVIQELGLdkVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11607 114 FGLKQdKLP-------KAEIASRVNEMLGL--VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
187-271 |
3.81e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLM 265
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLS-IVRKLADRVAVMQNGRCV 236
|
....*.
gi 1622936545 266 FHGPAQ 271
Cdd:PRK15134 237 EQNRAA 242
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
185-272 |
3.99e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 185 GVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKI 254
|
....*...
gi 1622936545 265 MFHGPAQE 272
Cdd:PRK13631 255 LKTGTPYE 262
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
37-243 |
4.48e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C 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-resistance 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: 213211 [Multi-domain] Cd Length: 221 Bit Score: 57.12 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNIC--YRvkvksgflPGRKPVEKEILSNINGIMKPGlnaILGPTGGGKSSLLDVLAARKDPSglSGDVLING---- 110
Cdd:cd03244 3 IEFKNVSlrYR--------PNLPPVLKNISFSIKPGEKVG---IVGRTGSGKSSLLLALFRLVELS--SGSILIDGvdis 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 -----ALRpTNFKCnsgyVVQDDVVMgTLTVRENL----QFSaalrlpttmtnhekNERINRVIQELGLDKVADSKVG-- 179
Cdd:cd03244 70 kiglhDLR-SRISI----IPQDPVLF-SGTIRSNLdpfgEYS--------------DEELWQALERVGLKEFVESLPGgl 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 180 -TQFIRG---VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIH 243
Cdd:cd03244 130 dTVVEEGgenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAH 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
77-231 |
4.88e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLI---NGALRPTN----------FKCNSGYVVQDDvvmgtltvRENL--Q 141
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPD--AGEVHYrmrDGQLRDLYalseaerrrlLRTEWGFVHQHP--------RDGLrmQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 142 FSA----ALRLPTTMTNHEKNER------INRViqELGLDKVADskVGTQFirgvSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK11701 106 VSAggniGERLMAVGARHYGDIRatagdwLERV--EIDAARIDD--LPTTF----SGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180
....*....|....*....|
gi 1622936545 212 PTTGLDSSTANAVLLLLKRM 231
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGL 197
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
243-300 |
5.15e-09 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 58.76 E-value: 5.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 243 HQPRYSIFKLFDSLTLLASGRLM-FHGPAQEALGYFESAGYHCEAYNNPADFFLDIING 300
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
64-247 |
5.53e-09 |
|
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: 56.96 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLdvLAARKDPSGLSGDVLINGALRPTNFKCNS--------GYVVQDDVVMGTl 134
Cdd:cd03290 17 LSNINIRIPTGqLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNKNESEPSFEATrsrnrysvAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENLQFSAALrlpttmtnheKNERINRVIQELGLDKVAD-------SKVGTQFIrGVSGGERKRTSIGMELITDPSIL 207
Cdd:cd03290 94 TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGERGI-NLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622936545 208 FLDEPTTGLDSSTANAVLL--LLKRMSKQGRTIIFSIHQPRY 247
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
77-217 |
5.95e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLA-ARKDPSG----LSGDvLINGALRptnfkcnsgyvvqDDVV-----M----G-----TLTVR 137
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAgARKIQQGrvevLGGD-MADARHR-------------RAVCpriayMpqglGknlypTLSVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 ENLQFSAALRlptTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:NF033858 97 ENLDFFGRLF---GQDAAERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
56-272 |
6.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.72 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 56 RKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLaarkdpsglsgdvliNGALRPTnfkcnSGYVVQDDVVMGTL 134
Cdd:PRK13634 15 KTPFERRALYDVNVSIPSGsYVAIIGHTGSGKSTLLQHL---------------NGLLQPT-----SGTVTIGERVITAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 135 TVRENL-----------QFSAALRLPTT-------------MTNHEKNERINRVIQELGLDKvadsKVGTQFIRGVSGGE 190
Cdd:PRK13634 75 KKNKKLkplrkkvgivfQFPEHQLFEETvekdicfgpmnfgVSEEDAKQKAREMIELVGLPE----ELLARSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 191 RKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQ----PRYSifklfDSLTLLASGRLM 265
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSmedaARYA-----DQIVVMHKGTVF 225
|
....*..
gi 1622936545 266 FHGPAQE 272
Cdd:PRK13634 226 LQGTPRE 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
187-272 |
8.12e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIhQPRYSIFKLFDSLTLLASGRLMF 266
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIA 224
|
....*.
gi 1622936545 267 HGPAQE 272
Cdd:NF000106 225 DGKVDE 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
63-303 |
8.14e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAlrptNFKCNSgyVVQDDVVM--------GT 133
Cdd:PRK11432 21 VIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPT--EGQIFIDGE----DVTHRS--IQQRDICMvfqsyalfPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRENLQFsaALRlpttMTNHEKNERINRVIQELGLdkVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:PRK11432 93 MSLGENVGY--GLK----MLGVPKEERKQRVKEALEL--VDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 214 TGLDsstANavllLLKRMSKQGRTIifsihQPRYSIFKLF------------DSLTLLASGRLMFHGPAQealgyfesag 281
Cdd:PRK11432 165 SNLD---AN----LRRSMREKIREL-----QQQFNITSLYvthdqseafavsDTVIVMNKGKIMQIGSPQ---------- 222
|
250 260
....*....|....*....|..
gi 1622936545 282 yhcEAYNNPADFFLDIINGDST 303
Cdd:PRK11432 223 ---ELYRQPASRFMASFMGDAN 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
78-239 |
8.37e-09 |
|
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: 58.64 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSG--LSGDVLIngALRPTnfkcnsgYVVQDdvvmGTLTVRENLQFSAALRLPTTMTNH 155
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEgeVDEDLKI--SYKPQ-------YISPD----YDGTVEEFLRSANTDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 156 EknerinrVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS-KQ 234
Cdd:COG1245 438 E-------IIKPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNR 505
|
....*
gi 1622936545 235 GRTII 239
Cdd:COG1245 506 GKTAM 510
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
78-295 |
9.00e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.12 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA---------LRPTNFKcNSGYVVQDDVVMGTLTVRENLQFSAALrl 148
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPT--RGQVLIDGVdiakisdaeLREVRRK-KIAMVFQSFALMPHMTVLDNTAFGMEL-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 149 pTTMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LL 227
Cdd:PRK10070 134 -AGINAEERREKALDALRQVGLENYAHS-----YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdEL 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 228 LKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQEALgyfesagyhceayNNPADFFL 295
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL-------------NNPANDYV 261
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
187-239 |
1.11e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.90 E-value: 1.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
47-243 |
1.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 47 KVKSGFLPGrKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLaarkdpsglsgdvliNGALRPTNfkcnsGYVV 125
Cdd:PRK13643 6 KVNYTYQPN-SPFASRALFDIDLEVKKGsYTALIGHTGSGKSTLLQHL---------------NGLLQPTE-----GKVT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 QDDVVMGTLTVRENLQ-----FSAALRLPTTMTNHEKNER-INRVIQELGLDKVADSKVGTQFIRGV------------- 186
Cdd:PRK13643 65 VGDIVVSSTSKQKEIKpvrkkVGVVFQFPESQLFEETVLKdVAFGPQNFGIPKEKAEKIAAEKLEMVgladefwekspfe 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 187 -SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13643 145 lSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
77-240 |
1.19e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 55.13 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNFKCNS-------GYVVQD---DVVMGTLTVRENLQFSAAL 146
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLRPPA--SGEITLDG--KPVTRRSPRdairagiAYVPEDrkrEGLVLDLSVAENIALSSLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 rlpttmtnheknerinrviqelgldkvadskvgtqfirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:cd03215 106 ----------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170
....*....|....
gi 1622936545 227 LLKRMSKQGRTIIF 240
Cdd:cd03215 146 LIRELADAGKAVLL 159
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
58-243 |
1.20e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDvlaarkdpsglsgdvLINGALRPTnfkcnSGYVVQDDVVMgtltv 136
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGsYTAFIGHTGSGKSTIMQ---------------LLNGLHVPT-----QGSVRVDDTLI----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 renlqfsaalrlpttmTNHEKNERINRVIQELGL--------------------------------DKVADSK---VGTQ 181
Cdd:PRK13649 72 ----------------TSTSKNKDIKQIRKKVGLvfqfpesqlfeetvlkdvafgpqnfgvsqeeaEALAREKlalVGIS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 182 ---FIRG---VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13649 136 eslFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
60-268 |
2.03e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLING----ALRPTNfKCNSGYVV--QDDVVMG 132
Cdd:PRK09580 13 DKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGkdllELSPED-RAGEGIFMafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSA-ALRlpttmtNHEKNERINRV-IQELGLDKVADSKVGTQFIR-----GVSGGERKRTSIGMELITDPS 205
Cdd:PRK09580 92 GVSNQFFLQTALnAVR------SYRGQEPLDRFdFQDLMEEKIALLKMPEDLLTrsvnvGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
62-279 |
2.22e-08 |
|
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: 57.44 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----LRPTNFKCNSGYVVQDDVVMgTLTV 136
Cdd:TIGR01193 488 NILSDISlTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR--SGEILLNGFslkdIDRHTLRQFINYLPQEPYIF-SGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQFSA-----------ALRLPTTMTNHEKnerinrviQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:TIGR01193 565 LENLLLGAkenvsqdeiwaACEIAEIKDDIEN--------MPLGYQTELSEEGSS-----ISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMskQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL---GYFES 279
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQGSHDELLdrnGFYAS 704
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-230 |
2.42e-08 |
|
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: 55.49 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSGlsGDVLIngALRPTNFKcnSGYVVQDDvvmgTLTVRENLqfSAALRLPTTmTNHEK 157
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDE--GDIEI--ELDTVSYK--PQYIKADY----EGTVRDLL--SSITKDFYT-HPYFK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 158 NErinrVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKR 230
Cdd:cd03237 97 TE----IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
78-266 |
3.00e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAArkDPSGLSGDVLINGAlRPTNFKcnSGYVVQDDV--------VMGTLTVRENLQFSAALrlp 149
Cdd:PRK11614 36 LIGANGAGKTTLLGTLCG--DPRATSGRIVFDGK-DITDWQ--TAKIMREAVaivpegrrVFSRMTVEENLAMGGFF--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 150 ttMTNHEKNERINRVIQELG-LDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:PRK11614 108 --AERDQFQERIKWVYELFPrLHERRIQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTI 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 229 KRMSKQGRTiIFSIHQPRYSIFKLFDSLTLLASGRLMF 266
Cdd:PRK11614 181 EQLREQGMT-IFLVEQNANQALKLADRGYVLENGHVVL 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-224 |
4.36e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 46 VKVKSGFLPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDV----LAARKDpsglsGDVLINGALrptnfkcn 120
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGsLVAIVGSTGEGKTSLISAmlgeLPPRSD-----ASVVIRGTV-------- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 121 sGYVVQDDVVMGTlTVRENLQFSAALrlpttmtnheKNERINRVIQELGLDKVADSKVGTQFI----RGV--SGGERKRT 194
Cdd:PLN03130 682 -AYVPQVSWIFNA-TVRDNILFGSPF----------DPERYERAIDVTALQHDLDLLPGGDLTeigeRGVniSGGQKQRV 749
|
170 180 190
....*....|....*....|....*....|
gi 1622936545 195 SIGMELITDPSILFLDEPTTGLDSSTANAV 224
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
70-274 |
4.66e-08 |
|
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: 56.49 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 70 IMKPGLNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGALrptnfkcnsGYVVQDDVVMGTlTVRENLQFSAALRLP 149
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVHMKGSV---------AYVPQQAWIQND-SLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 150 ttmtnhekneRINRVIQELGLdkVAD---------SKVGTQFIRgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:TIGR00957 729 ----------YYQQVLEACAL--LPDleilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622936545 221 ANAVL--LLLKRMSKQGRTIIFSIHQPRYsiFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:TIGR00957 796 GKHIFehVIGPEGVLKNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
78-244 |
4.93e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLdvlaaRkdpsglsgdvLINGALRPTnfkcnSGYVVQDDVVMGTLTVRE---------------NLQF 142
Cdd:PRK11153 36 VIGASGAGKSTLI-----R----------CINLLERPT-----SGRVLVDGQDLTALSEKElrkarrqigmifqhfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 143 S------AALrlPTTMTNHEKNErINRVIQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:PRK11153 96 SrtvfdnVAL--PLELAGTPKAE-IKARVTEL-LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
170 180
....*....|....*....|....*....
gi 1622936545 217 DSSTANAVLLLLKRMSKQ-GRTIIFSIHQ 244
Cdd:PRK11153 172 DPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
78-240 |
4.96e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTG--G-GKSSLLDVL--AARKDpsglSGDVLINGalRPTNFKCNS-------GYVVQD---DVVMGTLTVRENLQF 142
Cdd:COG1129 280 ILGIAGlvGaGRTELARALfgADPAD----SGEIRLDG--KPVRIRSPRdairagiAYVPEDrkgEGLVLDLSIRENITL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 143 SAALRLPTTMTNHEKNER--INRVIQELGLdKVADSKvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:COG1129 354 ASLDRLSRGGLLDRRRERalAEEYIKRLRI-KTPSPE---QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170 180
....*....|....*....|
gi 1622936545 221 ANAVLLLLKRMSKQGRTIIF 240
Cdd:COG1129 430 KAEIYRLIRELAAEGKAVIV 449
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
60-229 |
6.34e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG--LnAILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGALRPtnfkcnsGYVVQD-DVVMGTLTV 136
Cdd:COG0488 327 DKTLLDDLSLRIDRGdrI-GLIGPNGAGKSTLLKLLAGELEP--DSGTVKLGETVKI-------GYFDQHqEELDPDKTV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLQfsaalRLPTTMTNHEknerinrVIQELGL-----DKVaDSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG0488 397 LDELR-----DGAPGGTEQE-------VRGYLGRflfsgDDA-FKPVGV-----LSGGEKARLALAKLLLSPPNVLLLDE 458
|
170
....*....|....*...
gi 1622936545 212 PTTGLDSSTANAVLLLLK 229
Cdd:COG0488 459 PTNHLDIETLEALEEALD 476
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
69-242 |
8.71e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 69 GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRPTNFK---CNSGYVVQ--DDVVMGTLtvrenLQF 142
Cdd:PRK13648 31 NIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK--SGEIFYNNqAITDDNFEklrKHIGIVFQnpDNQFVGSI-----VKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 143 SAALRLPTTMTNHEK-NERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTA 221
Cdd:PRK13648 104 DVAFGLENHAVPYDEmHRRVSEALKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180
....*....|....*....|.
gi 1622936545 222 NAVLLLLKRMSKQGRTIIFSI 242
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISI 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
62-218 |
8.84e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--ALRPTNFKCNSGYVVQDDVVMGTLTVRE 138
Cdd:PRK10851 16 QVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQT--SGHIRFHGtdVSRLHARDRKVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 139 NLQFSAalrlpTTMTNHEKNER--INRVIQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:PRK10851 94 NIAFGL-----TVLPRRERPNAaaIKAKVTQL-LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
..
gi 1622936545 217 DS 218
Cdd:PRK10851 168 DA 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
77-240 |
9.22e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTNFKcNSGY-------VVQDDVVmgTLTVRENLQ--FSAALR 147
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPT--SGELLIDD--HPLHFG-DYSYrsqrirmIFQDPST--SLNPRQRISqiLDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 LPTTMTNHEKNERINRVIQELGLdkVADSkvGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-L 226
Cdd:PRK15112 116 LNTDLEPEQREKQIIETLRQVGL--LPDH--ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLInL 191
|
170
....*....|....
gi 1622936545 227 LLKRMSKQGRTIIF 240
Cdd:PRK15112 192 MLELQEKQGISYIY 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
58-332 |
1.01e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.84 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLING-ALRPTNFK---CNSGYVVQ--DDVV 130
Cdd:PRK13632 19 NSENNALKNVSFEINEGeYVAILGHNGSGKSTISKILTGLLKP--QSGEIKIDGiTISKENLKeirKKIGIIFQnpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 MGtLTVRENLQFSaalrLPTTMTNHEK-NERINRVIQELGLDKVADSKvgTQFIrgvSGGERKRTSIGMELITDPSILFL 209
Cdd:PRK13632 97 IG-ATVEDDIAFG----LENKKVPPKKmKDIIDDLAKKVGMEDYLDKE--PQNL---SGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 210 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI-HQPRYSIfkLFDSLTLLASGRLMFHGPAQEALgyfesagyhceayN 288
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAI--LADKVIVFSEGKLIAQGKPKEIL-------------N 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622936545 289 NPAdfFLDIINGDSTAVALNREEdfkaTEIIEPSKRDKPLIEKL 332
Cdd:PRK13632 232 NKE--ILEKAKIDSPFIYKLSKK----LKGIDPTYNEEELIEQI 269
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
37-237 |
1.18e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 37 LSFHNICYRVKvkSGFLPGRKPvEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSGlsGDVLING----A 111
Cdd:PRK10419 4 LNVSGLSHHYA--HGGLSGKHQ-HQTVLNNVSLSLKSGETvALLGRSGCGKSTLARLLVGLESPSQ--GNVSWRGeplaK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 LRPTN---FKCNSGYVVQDDV--VMGTLTVRENLqfSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQfirgV 186
Cdd:PRK10419 79 LNRAQrkaFRRDIQMVFQDSIsaVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----L 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRT 237
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGT 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
58-217 |
1.24e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 58 PVEKEILSNINGIMKPGlnA---ILGPTGGGKSSLLDVLAarkdpsGLsgDVLINGALRPT-NFKCnsGYVVQDDVVMGT 133
Cdd:PRK11819 17 PPKKQILKDISLSFFPG--AkigVLGLNGAGKSTLLRIMA------GV--DKEFEGEARPApGIKV--GYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRENLQ---------------FSAALRLPTTMTNH--EKNERINRVIQELG---LD---KVA---------DSKVGTq 181
Cdd:PRK11819 85 KTVRENVEegvaevkaaldrfneIYAAYAEPDADFDAlaAEQGELQEIIDAADawdLDsqlEIAmdalrcppwDAKVTK- 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622936545 182 firgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11819 164 ----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
64-263 |
1.25e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAA--RKDpsglSGDVLINGalRPTNFKcNSGYVVQDDVVM--------G 132
Cdd:PRK10982 14 LDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGiyQKD----SGSILFQG--KEIDFK-SSKEALENGISMvhqelnlvL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TLTVRENLQFSaalRLPTT--MTNHEKNERINRVI-QELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFL 209
Cdd:PRK10982 87 QRSVMDNMWLG---RYPTKgmFVDQDKMYRDTKAIfDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 210 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGR 263
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITILRDGQ 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
60-217 |
1.47e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRptnfkcnSGYVVQD---DVVMgTLT 135
Cdd:PRK09544 16 QRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIKRNGKLR-------IGYVPQKlylDTTL-PLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQFSAALR----LPTtmtnheknerinrviqelgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK09544 86 VNRFLRLRPGTKkediLPA-------------------LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
....*.
gi 1622936545 212 PTTGLD 217
Cdd:PRK09544 147 PTQGVD 152
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
132-243 |
1.96e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 132 GTLTVRENLQFSAAL-RLPTTmtnhEKNERINRVIQELGLDKVADSKVGtqfirGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:NF033858 352 GELTVRQNLELHARLfHLPAA----EIAARVAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110
....*....|....*....|....*....|....
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 243
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTH 456
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
56-268 |
4.17e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 56 RKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDV---LAARKDPSGLSGDVLINGALRP----TNFKCNSGYVVQ- 126
Cdd:PRK13645 19 KTPFEFKALNNTSlTFKKNKVTCVIGTTGSGKSTMIQLtngLIISETGQTIVGDYAIPANLKKikevKRLRKEIGLVFQf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 DDVVMGTLTVRENLQFSaalrlPTTMtNHEKNERINRVIQELGLDKVADSKVGTQFIRgVSGGERKRTSIGMELITDPSI 206
Cdd:PRK13645 99 PEYQLFQETIEKDIAFG-----PVNL-GENKQEAYKKVPELLKLVQLPEDYVKRSPFE-LSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936545 207 LFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
156-234 |
5.13e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.76 E-value: 5.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 156 EKNERINRVIQELGLDKVADSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 234
Cdd:COG4172 400 ERRARVAEALEEVGLDPAARHRYPHEF----SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
63-289 |
8.28e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLdvlaarkdpsglsgdVLINGALRPTNFKC-NSG---YVVQDDVVMGTlTVR 137
Cdd:TIGR01271 441 VLKNISFKLEKGqLLAVAGSTGSGKSSLL---------------MMIMGELEPSEGKIkHSGrisFSPQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 ENLQFSAA---LRLPTTMTNHEKNERINRVIQElglDKVADSKVGTQfirgVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:TIGR01271 505 DNIIFGLSydeYRYTSVIKACQLEEDIALFPEK---DKTVLGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 215 GLDSSTANAVL--LLLKRMSKQGRTIIFSihqpRYSIFKLFDSLTLLASGRLMFHGPAQEALGY---FESAGYHCEAYNN 289
Cdd:TIGR01271 578 HLDVVTEKEIFesCLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTFSELQAKrpdFSSLLLGLEAFDN 653
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
66-245 |
8.84e-07 |
|
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: 49.28 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 66 NINGIMKPGLNAILGPTGGGKSSLLD----VLAARKDPSGLSGDVLINgalrptnfkCNSGYVvqddvvmgtltvrenlq 141
Cdd:cd03227 14 NDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSATRRRSGVKAG---------CIVAAV----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 142 fSAALRLpttmtnheknerinrviqelgldkvadskvgtqFIRGVSGGERKRTSIGMEL----ITDPSILFLDEPTTGLD 217
Cdd:cd03227 68 -SAELIF---------------------------------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLD 113
|
170 180
....*....|....*....|....*...
gi 1622936545 218 SSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
63-254 |
8.86e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.46 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPGLNA-ILGPTGGGKSSLLDVLAarkdpsGL----SGDVLingalRPTnfKCNSGYVVQDDVvMGTLTVR 137
Cdd:cd03223 16 LLKDLSFEIKPGDRLlITGPSGTGKSSLFRALA------GLwpwgSGRIG-----MPE--GEDLLFLPQRPY-LPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 EnlqfsaALRLPttmtnheknerinrviqelgLDKVadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:cd03223 82 E------QLIYP--------------------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 218 SSTANAVLLLLKRMSkqgrTIIFSI-HQPrySIFKLFD 254
Cdd:cd03223 124 EESEDRLYQLLKELG----ITVISVgHRP--SLWKFHD 155
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
77-271 |
9.99e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLI-----NGALR-------PTNFKCNSGY--VVQDDVVMGtltvreNLQF 142
Cdd:PRK15056 37 ALVGVNGSGKSTLFKALMGFVRLA--SGKISIlgqptRQALQknlvayvPQSEEVDWSFpvLVEDVVMMG------RYGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 143 SAALRLPTTMtnhekneriNRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:PRK15056 109 MGWLRRAKKR---------DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622936545 223 AVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTLLASGRLMFHGPAQ 271
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHN--LGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
428-648 |
1.11e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 49.81 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 428 GVLFFLTTNQCFSSVSAVelFVVEKKL-FIHEYISGYYRVSSYFFGKLLSDLLPMrMLPSIIFTCIVYFMLGLKPTADAF 506
Cdd:COG0842 8 GLLAMSLLFTALMLTALS--IAREREQgTLERLLVTPVSRLEILLGKVLAYLLRG-LLQALLVLLVALLFFGVPLRGLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 507 FIMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQhNEF 586
Cdd:COG0842 85 LLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALR-ALF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 587 LGQnfcpglnatvnntcnyatctgeeyltkqgidLSPWGLWKNHVALACMIVIFLTIAYLKL 648
Cdd:COG0842 164 LGG-------------------------------AGLADVWPSLLVLLAFAVVLLALALRLF 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
77-242 |
1.11e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.78 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING-ALRPTN---FKCNSGYVVQ--DDVVMGTlTVRENLQFSaalrlpt 150
Cdd:PRK13635 37 AIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGmVLSEETvwdVRRQVGMVFQnpDNQFVGA-TVQDDVAFG------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 151 tMTNH-----EKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:PRK13635 107 -LENIgvpreEMVERVDQALRQVGMEDFLNREPHR-----LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL 180
|
170
....*....|....*..
gi 1622936545 226 LLLKRMSKQGRTIIFSI 242
Cdd:PRK13635 181 ETVRQLKEQKGITVLSI 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
187-272 |
1.23e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMF 266
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
....*.
gi 1622936545 267 HGPAQE 272
Cdd:PRK09473 243 YGNARD 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
78-217 |
1.30e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGALRPTnfkcnsgYVvQDDVVMgtlTVRENLqFSAALRLPTTMTNHEk 157
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ-------YI-KPDYDG---TVEDLL-RSITDDLGSSYYKSE- 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 158 nerinrVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13409 437 ------IIKPLQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
59-268 |
1.33e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 59 VEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALrptnfkcnsGYVVQDDVVMGTlTVR 137
Cdd:PTZ00243 671 EPKVLLRDVSvSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS--EGRVWAERSI---------AYVPQQAWIMNA-TVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 138 ENLQFsaalrlpttmTNHEKNERINRVIQELGLDkvAD---------SKVGTqfiRGV--SGGERKRTSIGMELITDPSI 206
Cdd:PTZ00243 739 GNILF----------FDEEDAARLADAVRVSQLE--ADlaqlgggleTEIGE---KGVnlSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 207 LFLDEPTTGLDSSTANAVL--LLLKRMSkqGRTIIFSIHQprYSIFKLFDSLTLLASGRLMFHG 268
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVeeCFLGALA--GKTRVLATHQ--VHVVPRADYVVALGDGRVEFSG 863
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-244 |
1.34e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 32 TEGAVLSFHNICYRVKvksgflPGrkpvekEILSningimkpglnaILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGA 111
Cdd:TIGR02633 10 TFGGVKALDGIDLEVR------PG------ECVG------------LCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 112 ------LRPTNFKcnsGYVV--QDDVVMGTLTVRENLQFSAALRLPTTMTNH-EKNERINRVIQELGLDKVADSKVGTQF 182
Cdd:TIGR02633 66 plkasnIRDTERA---GIVIihQELTLVPELSVAENIFLGNEITLPGGRMAYnAMYLRAKNLLRELQLDADNVTRPVGDY 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 183 irgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:TIGR02633 143 ----GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
78-217 |
1.36e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.00 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING----ALRPTNFKCnsGYVVQDDVVMGTLTVRENLQFSAALRlp 149
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVA------GLeritSGEIWIGGrvvnELEPADRDI--AMVFQNYALYPHMSVRENMAYGLKIR-- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 150 tTMTNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11650 105 -GMPKAEIEERVAEAARILELEPLLDRKP-----RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
77-272 |
1.78e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKS----SLLDVLaarkdPSG---LSGDVLING-ALRPTNFKcnsGYVVQddvvmgtlTVRENLQfSA--AL 146
Cdd:PRK10418 33 ALVGGSGSGKSltcaAALGIL-----PAGvrqTAGRVLLDGkPVAPCALR---GRKIA--------TIMQNPR-SAfnPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 RlptTMTNHEK-----------NERINRVIQELGLDKVAdsKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK10418 96 H---TMHTHARetclalgkpadDATLTAALEAVGLENAA--RVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 216 LDSSTANAVLLLLKR-MSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK10418 171 LDVVAQARILDLLESiVQKRALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDVET 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
78-275 |
2.41e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.57 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPSG-----LSGDVLIN----GALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRL 148
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSgevnvRVGDEWVDmtkpGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 149 PTTMTNHekneRINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LL 227
Cdd:TIGR03269 395 PDELARM----KAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSI 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622936545 228 LKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:TIGR03269 471 LKAREEMEQTFIIVSHDMDF-VLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
64-263 |
2.49e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKdPSG-LSGDVLINGA-LRPTNFKCN--SGYVV--QDDVVMGTLTV 136
Cdd:PRK13549 21 LDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVY-PHGtYEGEIIFEGEeLQASNIRDTerAGIAIihQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 137 RENLqFSAALRLPTTMTNHEK-NERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK13549 100 LENI-FLGNEITPGGIMDYDAmYLRAQKLLAQLKLDINPATPVGN-----LGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622936545 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGR 263
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHGIACIYISHKLN-EVKAISDTICVIRDGR 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
44-245 |
3.02e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 44 YRV-KVKSGFLPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVL--AARKDPSGLSGDVLINgalrptnfKC 119
Cdd:COG2401 25 ERVaIVLEAFGVELRVVERYVLRDLNLEIEPGeIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDN--------QF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 120 NSGYVVQDDVVMgtltvreNLQFSAALrlpttmtnheknERINRViqelGL-DKVAdskvgtqFIRGV---SGGERKRTS 195
Cdd:COG2401 97 GREASLIDAIGR-------KGDFKDAV------------ELLNAV----GLsDAVL-------WLRRFkelSTGQKFRFR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 196 IGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP 245
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
160-243 |
3.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 160 RINRVIQELGLDkvADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKrmSKQGrTII 239
Cdd:PRK11147 138 RINEVLAQLGLD--PDAALSS-----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK--TFQG-SII 207
|
....
gi 1622936545 240 FSIH 243
Cdd:PRK11147 208 FISH 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
78-272 |
4.17e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKdPSGLSGDVLINGalRPTNFKcNSGYVVQDDVVM-----------GTLTVRENLQFSAAL 146
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGAY-PGKFEGNVFING--KPVDIR-NPAQAIRAGIAMvpedrkrhgivPILGVGKNITLSVLK 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 147 RLPTTMTNHEKNER--INRVIQELGLdkvadsKVGTQF--IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:TIGR02633 367 SFCFKMRIDAAAELqiIGSAIQRLKV------KTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 223 AVLLLLKRMSKQGRTIIFsIHQPRYSIFKLFDSLTLLASGRL----MFHGPAQE 272
Cdd:TIGR02633 441 EIYKLINQLAQEGVAIIV-VSSELAEVLGLSDRVLVIGEGKLkgdfVNHALTQE 493
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
187-240 |
4.34e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 49.68 E-value: 4.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 240
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLL 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
60-242 |
4.96e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 48.64 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLldvlaARkdpsglsgdvLINGALRPTNFkcNSGYVVQDDVVMGTLT--- 135
Cdd:PRK13640 19 KKPALNDISFSIPRGsWTALIGHNGSGKSTI-----SK----------LINGLLLPDDN--PNSKITVDGITLTAKTvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENL---------QF-------SAALRLPTTMTNHEKNERI-NRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGM 198
Cdd:PRK13640 82 IREKVgivfqnpdnQFvgatvgdDVAFGLENRAVPRPEMIKIvRDVLADVGMLDYIDSEPAN-----LSGGQKQRVAIAG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622936545 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 242
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-220 |
5.35e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 56 RKPVEkeILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA--LRPTNFK---CNSGYVVQDDV 129
Cdd:PTZ00265 395 RKDVE--IYKDLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPT--EGDIIINDShnLKDINLKwwrSKIGVVSQDPL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 130 VMGTlTVRENLQFSA-ALRLPTTMTNH----------EKNER----------INRVIQELGLDKVADSKVGTQFIRG--- 185
Cdd:PTZ00265 471 LFSN-SIKNNIKYSLySLKDLEALSNYynedgndsqeNKNKRnscrakcagdLNDMSNTTDSNELIEMRKNYQTIKDsev 549
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622936545 186 ------------------------------VSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:PTZ00265 550 vdvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
181-240 |
6.90e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 6.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 181 QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 240
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF 458
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
60-274 |
6.94e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.33 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalRPTN------FKCNSGYVVQDDVVMG 132
Cdd:PRK10790 353 DNLVLQNINlSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDG--RPLSslshsvLRQGVAMVQQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 TlTVRENLqfsaalrlptTMTNHEKNERINRVIQELGLDKVA-------DSKVGTQFiRGVSGGERKRTSIGMELITDPS 205
Cdd:PRK10790 429 D-TFLANV----------TLGRDISEEQVWQALETVQLAELArslpdglYTPLGEQG-NNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLkRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAH--RLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
60-217 |
7.70e-06 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 45.90 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGALRPtnfkcnsGYVVQddvvmgtltvre 138
Cdd:cd03221 12 GKLLLKDISLTINPGDRiGLVGRNGAGKSTLLKLIAGELEPD--EGIVTWGSTVKI-------GYFEQ------------ 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 139 nlqfsaalrlpttmtnheknerinrviqelgldkvadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-243 |
1.01e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.36 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 78 ILGPTGGGKSSLLDVLAARKDPS-GLSG------DVLingalrpTNFKcnsGYVVQD---DVVMGTLTVRENLQFSAalR 147
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNlGKFDdppdwdEIL-------DEFR---GSELQNyftKLLEGDVKVIVKPQYVD--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 LPTT--------MTNHEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:cd03236 99 IPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRN-----IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....
gi 1622936545 220 TANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
80-264 |
1.47e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 80 GPTGGGKSSLLDVLAArKDPSgLSGDVLINGA-LRPTN----FKCNSGYVVQ---DDVVMGTLTVRENLQFSAALRL--- 148
Cdd:PRK09700 296 GLVGSGRTELMNCLFG-VDKR-AGGEIRLNGKdISPRSpldaVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDggy 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 149 --PTTMTNHEKNERINRVIQELGLDKVADSKvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:PRK09700 374 kgAMGLFHEVDEQRTAENQRELLALKCHSVN---QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK 450
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622936545 227 LLKRMSKQGRTIIF-SIHQPRysIFKLFDSLTLLASGRL 264
Cdd:PRK09700 451 VMRQLADDGKVILMvSSELPE--IITVCDRIAVFCEGRL 487
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
60-239 |
1.58e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.53 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-----------ALRPtnfkcNSGYVVQD 127
Cdd:COG1126 13 DLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPD--SGTITVDGedltdskkdinKLRR-----KVGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 128 -----DvvmgtLTVRENLQFSaalrlPTTMTNHEKNERINRVIQEL---GLDKVADSKVGTqfirgVSGGERKRTSIGME 199
Cdd:COG1126 86 fnlfpH-----LTVLENVTLA-----PIKVKKMSKAEAEERAMELLervGLADKADAYPAQ-----LSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622936545 200 LITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMV 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
77-217 |
2.35e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.52 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSGlsGDVLING---ALRPTNFKCNSGYV--VQDDVVMGTLTVRENL---Q------- 141
Cdd:PRK11300 35 SLIGPNGAGKTTVFNCLTGFYKPTG--GTILLRGqhiEGLPGHQIARMGVVrtFQHVRLFREMTVIENLlvaQhqqlktg 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 142 -FSAALRLPT-TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11300 113 lFSGLLKTPAfRRAESEALDRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
73-246 |
2.87e-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: 45.68 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 73 PGLNAILGPTGGGKSSLLDVLAArkdpsGLSGDvlingaLRPTNfkcNSGYVVQDDVVMGTLTVRENLQFSaaLRLPTTM 152
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKY-----ALTGE------LPPNS---KGGAHDPKLIREGEVRAQVKLAFE--NANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 153 TNHEKNERINRVI---QElGLDKVADSKVGTqfirgVSGGERK------RTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:cd03240 86 TITRSLAILENVIfchQG-ESNWPLLDMRGR-----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|....*
gi 1622936545 224 VLL-LLKRMSKQG-RTIIFSIHQPR 246
Cdd:cd03240 160 SLAeIIEERKSQKnFQLIVITHDEE 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
124-285 |
3.63e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 124 VVQDDVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINRVIQELglDKVADSKVGTqFIRGVSGGERKRTSIGMELITD 203
Cdd:PTZ00265 1300 IVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVGP-YGKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 204 PSILFLDEPTTGLDSstaNAVLLLLKRM----SKQGRTIIFSIHqpRYSIFKLFDSLtllasgrLMFHGPAQEAlGYFES 279
Cdd:PTZ00265 1377 PKILLLDEATSSLDS---NSEKLIEKTIvdikDKADKTIITIAH--RIASIKRSDKI-------VVFNNPDRTG-SFVQA 1443
|
....*.
gi 1622936545 280 AGYHCE 285
Cdd:PTZ00265 1444 HGTHEE 1449
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
67-240 |
4.62e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 67 INGIMKPGLNA----------ILG---PTGGGKSSLLDVL--AARKDpsglSGDVLINGalRPTNFK-----CNSGYVV- 125
Cdd:PRK11288 260 LDGLKGPGLREpisfsvrageIVGlfgLVGAGRSELMKLLygATRRT----AGQVYLDG--KPIDIRsprdaIRAGIMLc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 -----QDDVVmGTLTVRENLQFSA-ALRLPTTMTNHEKNERIN--RVIQELgldkvadsKVGT----QFIRGVSGGERKR 193
Cdd:PRK11288 334 pedrkAEGII-PVHSVADNINISArRHHLRAGCLINNRWEAENadRFIRSL--------NIKTpsreQLIMNLSGGNQQK 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622936545 194 TSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 240
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-228 |
5.34e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 35 AVLSFHNICYRVKVKSGFLPGRKPVEKeilsnINGI---MKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLING 110
Cdd:PRK11308 4 PLLQAIDLKKHYPVKRGLFKPERLVKA-----LDGVsftLERGKTlAVVGESGCGKSTLARLLTMIETPT--GGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 alrpTNFKCNSGYVVQD---DVVM------GTLTVRENL--QFSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVG 179
Cdd:PRK11308 77 ----QDLLKADPEAQKLlrqKIQIvfqnpyGSLNPRKKVgqILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622936545 180 TQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:PRK11308 153 HMF----SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
186-243 |
7.05e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 7.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITH 227
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
187-246 |
7.54e-05 |
|
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: 43.85 E-value: 7.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 187 SGGERKRTSIGMELI--TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPR 246
Cdd:cd03238 89 SGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-239 |
7.66e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 45 RVKVKSGFLPGRKPV-----EKEILSnINGIMkpglnailgptGGGKSSLLDVL--AARKDpsglSGDVLINGalRPTNF 117
Cdd:PRK10762 257 RLKVDNLSGPGVNDVsftlrKGEILG-VSGLM-----------GAGRTELMKVLygALPRT----SGYVTLDG--HEVVT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 118 KC-----NSGYVV------QDDVVMGtLTVRENLQFSAALRLPTTM--TNH-EKNERINRVIQELgldkvadsKVGT--- 180
Cdd:PRK10762 319 RSpqdglANGIVYisedrkRDGLVLG-MSVKENMSLTALRYFSRAGgsLKHaDEQQAVSDFIRLF--------NIKTpsm 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 181 -QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:PRK10762 390 eQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
77-240 |
8.61e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.11 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---------ALRPtnFKCNSGYVVQDDvvMGTL----TVRENLqfS 143
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPT--SGEILFDGqditglsgrELRP--LRRRMQMVFQDP--YASLnprmTVGDII--A 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 144 AALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:COG4608 120 EPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEF----SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170
....*....|....*...
gi 1622936545 224 VLLLLKRMSKQ-GRTIIF 240
Cdd:COG4608 196 VLNLLEDLQDElGLTYLF 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
183-239 |
8.87e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 8.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 183 IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
63-244 |
9.95e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 63 ILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDpsgLSGDVLINGAlrptnfKCNSGYVVQDDVVMGTLTvRENLQ 141
Cdd:cd03289 19 VLENISFSISPGQRvGLLGRTGSGKSTLLSAFLRLLN---TEGDIQIDGV------SWNSVPLQKWRKAFGVIP-QKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 142 FSAALRLPTTMTNHEKNERINRVIQELGLDKVADS---KVGTQFIRG---VSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:cd03289 89 FSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQfpgQLDFVLVDGgcvLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180
....*....|....*....|....*....
gi 1622936545 216 LDSSTANAVLLLLKRmSKQGRTIIFSIHQ 244
Cdd:cd03289 169 LDPITYQVIRKTLKQ-AFADCTVILSEHR 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
158-239 |
1.63e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 158 NER--INRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQG 235
Cdd:COG1245 188 DERgkLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG 262
|
....
gi 1622936545 236 RTII 239
Cdd:COG1245 263 KYVL 266
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
178-239 |
2.04e-04 |
|
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: 44.62 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 178 VGTQFIR------GVSGGERKRTSIGMEL---ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:TIGR00630 816 VGLGYIRlgqpatTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-244 |
2.49e-04 |
|
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: 43.37 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 134 LTVRENLQFsaalrlpttMTNHEKNERINRVIQELGLDKVadsKVGtQFIRGVSGGERKRTSIGMELI---TDPSILFLD 210
Cdd:cd03271 131 MTVEEALEF---------FENIPKIARKLQTLCDVGLGYI---KLG-QPATTLSGGEAQRIKLAKELSkrsTGKTLYILD 197
|
90 100 110
....*....|....*....|....*....|....
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
286-589 |
2.86e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 43.53 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 286 AYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKR---DKPLIEKLAEIYVDSSFYKETKAELHQLSGgeKKKKIT 362
Cdd:pfam12698 25 AVNDPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYvdsEEEAKEALKNGKIDGLLVIPKGFSKDLLKG--ESATVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 363 VFKEISYTTS---FCHQLRWVSKRSFKNLLGNPQASIAQIIVtvilglvIGAIYFGLNNDSTGIQNraGVLFFLTTNQCF 439
Cdd:pfam12698 103 VYINSSNLLVsklILNALQSLLQQLNASALVLLLEALSTSAP-------IPVESTPLFNPQSGYAY--YLVGLILMIIIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 440 SSVSAVELFVVEKKL--FIHEYISGYYRVSSYFFGKLLSDLLpmrmLPSIIFTCIVYFMLGLKPTADAFFIMMFTLMMVA 517
Cdd:pfam12698 174 IGAAIIAVSIVEEKEsrIKERLLVSGVSPLQYWLGKILGDFL----VGLLQLLIILLLLFGIGIPFGNLGLLLLLFLLYG 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622936545 518 YSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQY---FSIPRYGFTALQHNEFLGQ 589
Cdd:pfam12698 250 LAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSiipFFSPIDGLLRLIYGDSLWE 324
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
181-242 |
3.82e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 3.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 181 QFIRgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 242
Cdd:cd03222 68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
158-217 |
3.84e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936545 158 NER--INRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13409 188 DERgkLDEVVERLGLENILDRD-----ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
187-290 |
4.72e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQprYSIFKLFDSLTLlasgrLM 265
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD--LAVVKHISDRVL-----VM 235
|
90 100
....*....|....*....|....*
gi 1622936545 266 FHGPAQEaLGYFEsagyhcEAYNNP 290
Cdd:PRK15079 236 YLGHAVE-LGTYD------EVYHNP 253
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-244 |
5.08e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.36 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 61 KEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARkdpSGLSGDVLING----ALRPTNFKCNSGyVVQDDVVMGTLT 135
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRvGLLGRTGSGKSTLLSALLRL---LSTEGEIQIDGvswnSVTLQTWRKAFG-VIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 136 VRENLQfsaalrlpttmtNHEK--NERINRVIQELGLDKVADS---KVGTQFIRG---VSGGERKRTSIGMELITDPSIL 207
Cdd:TIGR01271 1308 FRKNLD------------PYEQwsDEEIWKVAEEVGLKSVIEQfpdKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622936545 208 FLDEPTTGLDSSTanavLLLLKRMSKQGR---TIIFSIHQ 244
Cdd:TIGR01271 1376 LLDEPSAHLDPVT----LQIIRKTLKQSFsncTVILSEHR 1411
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
186-243 |
5.26e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 5.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 186 VSGGERKRTSIGMELIT---DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
54-274 |
7.95e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.70 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 54 PGRkpvEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLING----ALRPTNFKCNSGYVVQ-- 126
Cdd:PRK11176 352 PGK---EVPALRNINFKIPAGKTvALVGRSGSGKSTIANLLTRFYDID--EGEILLDGhdlrDYTLASLRNQVALVSQnv 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 127 ---DDVVMGTLTVRENLQFS-----AALRLPTTMtnheknERINRViqELGLDKVadskVGTQfirGV--SGGERKRTSI 196
Cdd:PRK11176 427 hlfNDTIANNIAYARTEQYSreqieEAARMAYAM------DFINKM--DNGLDTV----IGEN---GVllSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936545 197 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH--RLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
70-292 |
9.74e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 41.56 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 70 IMKPGLNAILGPTGGGKSSLLDVLAARKDpsgLSGDVLINGAL--------------------------RPTNFKCNsgy 123
Cdd:PRK14258 30 IYQSKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGRVeffnqniyerrvnlnrlrrqvsmvhpKPNLFPMS--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 124 vVQDDVVMGTLTV--RENLQFSAALRlpTTMTNHEKNERINRVIQELGLDkvadskvgtqfirgVSGGERKRTSIGMELI 201
Cdd:PRK14258 104 -VYDNVAYGVKIVgwRPKLEIDDIVE--SALKDADLWDEIKHKIHKSALD--------------LSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 202 TDPSILFLDEPTTGLDSSTANAVLLLLK--RMSKQGRTIIFSIHQPRYSIFKLFDSLtllasgrlmFHGpAQEALGYFES 279
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAF---------FKG-NENRIGQLVE 236
|
250
....*....|...
gi 1622936545 280 AGYHCEAYNNPAD 292
Cdd:PRK14258 237 FGLTKKIFNSPHD 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-243 |
1.11e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 36 VLSFHNICYRVKVKSGFLpGRKPVEKEILSNINGIMKPGLN-AILGPTGGGKS----SLLDVLAARKDPSGLSG---DVL 107
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLL-NRVTREVHAVEKVSFDLWPGETlSLVGESGSGKSttgrALLRLVESQGGEIIFNGqriDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 108 INGALRPtnFKCNSGYVVQDDvvMGTLTVRENLQFS--AALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQFirg 185
Cdd:PRK10261 392 SPGKLQA--LRRDIQFIFQDP--YASLDPRQTVGDSimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEF--- 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 186 vSGGERKRTSIGMELITDPSILFLDEPTTGLDSST-ANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK10261 465 -SGGQRQRICIARALALNPKVIIADEAVSALDVSIrGQIINLLLDLQRDFGIAYLFISH 522
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
141-240 |
1.15e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 141 QFSAALRLpttmtNHEKNER-INRVIQELgldkvadsKVGT----QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK13549 369 RFTGGSRI-----DDAAELKtILESIQRL--------KVKTaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
90 100
....*....|....*....|....*
gi 1622936545 216 LDSSTANAVLLLLKRMSKQGRTIIF 240
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
60-244 |
1.15e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.70 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGalrpTNFKCNSGYVVQDDVVMG------ 132
Cdd:PRK13540 13 DQPLLQQISfHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFER----QSIKKDLCTYQKQLCFVGhrsgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 133 -TLTVRENLQFSaalrLPTTMTNHEknerINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK13540 87 pYLTLRENCLYD----IHFSPGAVG----ITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 1622936545 212 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
155-239 |
1.22e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 155 HEKNERINRVIQELGLDKVADSKvgtqFIRgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 234
Cdd:PRK10938 110 VKDPARCEQLAQQFGITALLDRR----FKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
....*
gi 1622936545 235 GRTII 239
Cdd:PRK10938 185 GITLV 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
77-262 |
1.40e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSSLLDVLAA--RKDpsglSGDVLINGalRPTNFK-------CNSGYVVQDDVVMGTLTVRENLqFsaalr 147
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiyTRD----AGSILYLG--KEVTFNgpkssqeAGIGIIHQELNLIPQLTIAENI-F----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 148 LPTTMTNH-------EKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL-DSS 219
Cdd:PRK10762 102 LGREFVNRfgridwkKMYAEADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622936545 220 TAnAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASG 262
Cdd:PRK10762 177 TE-SLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVFRDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
189-274 |
2.08e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 189 GERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
....*.
gi 1622936545 269 PAQEAL 274
Cdd:PRK15093 242 PSKELV 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
77-217 |
2.13e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.49 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 77 AILGPTGGGKSS---LLD-VLAARkdpsglSGDVLING-ALRPTN---FKCNSGYVVQ--DDVVMGTlTVRENLQFSaal 146
Cdd:PRK13650 37 SIIGHNGSGKSTtvrLIDgLLEAE------SGQIIIDGdLLTEENvwdIRHKIGMVFQnpDNQFVGA-TVEDDVAFG--- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936545 147 rLPTTMTNHEknERINRVIQELGLDKVADSKvgTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13650 107 -LENKGIPHE--EMKERVNEALELVGMQDFK--EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
47-243 |
2.30e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 47 KVKSGFLPGRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAlrPTNFKCNSGyvv 125
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPN--KGTVDIKGS--AALIAISSG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 126 qddvVMGTLTVRENLQFSAalrLPTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:PRK13545 96 ----LNGQLTGIENIELKG---LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKT-----YSSGMKSRLGFAISVHINPD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISH 201
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
144-245 |
2.47e-03 |
|
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: 40.45 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 144 AALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITD---PSILFLDEPTTGLDSST 220
Cdd:pfam13304 195 ADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKL 274
|
90 100
....*....|....*....|....*
gi 1622936545 221 ANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:pfam13304 275 LRRLLELLKELSRNGAQLILTTHSP 299
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
186-274 |
2.81e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 186 VSGGERKRTSI----GMELITDPSILflDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ--------------PRY 247
Cdd:PRK00635 477 LSGGEQERTALakhlGAELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmisladriidigPGA 554
|
90 100
....*....|....*....|....*..
gi 1622936545 248 SIFklfdsltllaSGRLMFHGPAQEAL 274
Cdd:PRK00635 555 GIF----------GGEVLFNGSPREFL 571
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
70-273 |
3.21e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.77 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 70 IMKPGLNAILGPTGGGKSSLLDVLAARKD--PSG-LSGDVLINGA------LRPTNFKCNSGYVVQDDVVMGTlTVRENL 140
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrVEGKVTFHGKnlyapdVDPVEVRRRIGMVFQKPNPFPK-SIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 141 QFSAALrlpttmtNHEK---NERINRVIQELGL-----DKVADSKVGtqfirgVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK14243 112 AYGARI-------NGYKgdmDELVERSLRQAALwdevkDKLKQSGLS------LSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 213 TTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQ----PRYSIFKLFDSLTLLASG------------RLMFHGPAQEA 273
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ-YTIIIVTHNmqqaARVSDMTAFFNVELTEGGgrygylvefdrtEKIFNSPQQQA 254
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
34-222 |
3.75e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 34 GAVLSFHNICYRvkvksgFLPGRKPVekeiLSNINGIMKPGLN-AILGPTGGGKSSLldVLAARKDPSGLSGDVLING-- 110
Cdd:cd03288 17 GGEIKIHDLCVR------YENNLKPV----LKHVKAYIKPGQKvGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGid 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 111 --ALRPTNFKCNSGYVVQDDVVMGTlTVRENLQfsaALRLPTTMTNHEKNE--RINRVIQEL--GLDKVAdSKVGTQFir 184
Cdd:cd03288 85 isKLPLHTLRSRLSIILQDPILFSG-SIRFNLD---PECKCTDDRLWEALEiaQLKNMVKSLpgGLDAVV-TEGGENF-- 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622936545 185 gvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:cd03288 158 --SVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
186-243 |
4.34e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 4.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936545 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSS-TANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITH 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
187-243 |
4.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 4.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936545 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
59-243 |
4.40e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.69 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 59 VEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLING-----ALRPTNFKCNSGYVVQ--DDVV 130
Cdd:PRK13633 21 TEKLALDDVNLEVKKGeFLVILGRNGSGKSTIAKHMNALLIPSE--GKVYVDGldtsdEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936545 131 MGTLtVRENLQFSaalrlPTTMTNHEKNERiNRViqELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK13633 99 VATI-VEEDVAFG-----PENLGIPPEEIR-ERV--DESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190
....*....|....*....|....*....|....
gi 1622936545 211 EPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
187-245 |
5.91e-03 |
|
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: 38.78 E-value: 5.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936545 187 SGGERKR----TSIGMELItdpSILF-LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:cd03270 139 SGGEAQRirlaTQIGSGLT---GVLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| |
