|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
46-651 |
7.50e-141 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 424.46 E-value: 7.50e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 46 VKVKSGFLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARkDPKGL--SGDVLINGAPQPA-HFKCCSG 121
Cdd:TIGR00955 24 VSRLRGCFCRERPRKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFR-SPKGVkgSGSVLLNGMPIDAkEMRAISA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 122 YVVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQ-FIRGISGGERKRTSIGMELI 200
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 201 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHGPAQKALEYFASAG 280
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 281 YHCEPYNNPADFFLDVIngdssAVMLNREEQDNEankteepskgekpVIENLSEFYINSAIYGETKAE--LDQLPGAQEK 358
Cdd:TIGR00955 263 HPCPENYNPADFYVQVL-----AVIPGSENESRE-------------RIEKICDSFAVSDIGRDMLVNtnLWSGKAGGLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 359 KGTSAFKEPVYVTSFCHQLRWIARRSFKNLLGNPQASVAQLIVTVILGLIIGAIYFDLKYDAAGMQNRAGVLFFLTTNQC 438
Cdd:TIGR00955 325 KDSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 439 FSSV-SAVELFVVEKKLFIHEYISGYYRVSSYFFGKVMSDlLPMRFLPSVIFTCILYFMLGLKKTVDAFFIMMFTLIMVA 517
Cdd:TIGR00955 405 FQNVfPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAE-LPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 518 YTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFTALQYNEFLGQEFCPGFNV 597
Cdd:TIGR00955 484 NVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSA 563
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 598 TDNSTCVNSyaictGNEYLINQGIELSPwgLWKNHVALACMIIIFLTIAYLKLL 651
Cdd:TIGR00955 564 NTTGPCPSS-----GEVILETLSFRNAD--LYLDLIGLVILIFFFRLLAYFALR 610
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
36-267 |
1.03e-89 |
|
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: 277.12 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKSGflvrkTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGAPQPA 114
Cdd:cd03213 3 TLSFRNLTVTVKSSPS-----KSGKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 H-FKCCSGYVVQDDVVMGTLTVRENLQFSAALRlpttmknheknerintiikelglekvadskvgtqfirGISGGERKRT 193
Cdd:cd03213 78 RsFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 194 SIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
52-654 |
1.04e-88 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 302.03 E-value: 1.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 52 FLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKD--PKGLSGDVLINGAPQP---AHFKCCSGYVVQ 125
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASNTDgfHIGVEGVITYDGITPEeikKHYRGDVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 126 DDVVMGTLTVRENLQFSAALRLPTT-MKNHEKNERINTI----IKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELI 200
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCKTPQNrPDGVSREEYAKHIadvyMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 201 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF-SIHQPRYSIFKLFDSLTLLASGKLVFHGPAQKALEYFASA 279
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 280 GYHCEPYNNPADFFLDVINgdssavmlnreeqdneaNKTEEPSKG-EKPVIENLSEFY---INSAIYGETKAELDQ---- 351
Cdd:TIGR00956 306 GFKCPDRQTTADFLTSLTS-----------------PAERQIKPGyEKKVPRTPQEFEtywRNSPEYAQLMKEIDEyldr 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 352 ----------LPGAQEKKGTSAFKEPVYVTSFCHQLRWIARRSFKNLLGNPQASVAQLIVTVILGLIIGAIYFDLKYDAA 421
Cdd:TIGR00956 369 csesdtkeayRESHVAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTS 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 422 GMQNRAGVLFFLTTNQCFSSVSavELFVVEKKLFIHEYISGY--YRVSSYFFGKVMSDlLPMRFLPSVIFTCILYFMLGL 499
Cdd:TIGR00956 449 DFYSRGGALFFAILFNAFSSLL--EIASMYEARPIVEKHRKYalYHPSADAIASIISE-IPFKIIESVVFNIILYFMVNF 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 500 KKTVDAFFIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFT 579
Cdd:TIGR00956 526 RRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 580 ALQYNEFLGQEF-CP-----GFNVTDNSTcvnSYAICT------------GNEYLINQGIELSPWgLWKNHVALACMIII 641
Cdd:TIGR00956 606 SLMVNEFHGRRFeCSqyvpsGGGYDNLGV---TNKVCTvvgaepgqdyvdGDDYLKLSFQYYNSH-KWRNFGIIIGFTVF 681
|
650
....*....|...
gi 1720417991 642 FLTIAYLKLLFLK 654
Cdd:TIGR00956 682 FFFVYILLTEFNK 694
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-654 |
2.57e-87 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 286.39 E-value: 2.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRVKV------------------KSGFLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKD 97
Cdd:PLN03211 40 LKFMDVCYRVKFenmknkgsnikrilghkpKISDETRQIQERTILNGVTGMASPGeILAVLGPSGSGKSTLLNALAGRIQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 98 PKGLSGDVLINGAPQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKV 177
Cdd:PLN03211 120 GNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTII 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 178 GTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTL 257
Cdd:PLN03211 200 GNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 258 LASGKLVFHGPAQKALEYFASAGYHCEPYNNPADFFLDVINGdssavmlnreeqdneANKTEEPSKGEKPVIENLSEFYI 337
Cdd:PLN03211 280 LSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANG---------------VCQTDGVSEREKPNVKQSLVASY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 338 NSAIYGETKA--ELDQLPGAQEKK-GTSAFKE-----PVYVTSFCHQLRWIARRSFK-------NLLgnpqaSVAQLIVT 402
Cdd:PLN03211 345 NTLLAPKVKAaiEMSHFPQANARFvGSASTKEhrssdRISISTWFNQFSILLQRSLKerkhesfNTL-----RVFQVIAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 403 VILGliiGAIYFdlKYDAAGMQNRAGVLFFLTTN-QCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKVMSDlLPM 481
Cdd:PLN03211 420 ALLA---GLMWW--HSDFRDVQDRLGLLFFISIFwGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGD-LPM 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 482 RFLPSVIFTCILYFMLGLKKTVDAFFIMMftLIMVAYTASSMALAIATGQSVVSV--ATLLMTIAFVFMMLFSGLLVNlr 559
Cdd:PLN03211 494 ELILPTIFLTVTYWMAGLKPELGAFLLTL--LVLLGYVLVSQGLGLALGAAIMDAkkASTIVTVTMLAFVLTGGFYVH-- 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 560 TIGPWLSWLQYFSIPRYGFTAL---QYNEflgqefcpGFNVTDNSTCVNSYAICTGNEYLINQGI--ELSPWglwknhVA 634
Cdd:PLN03211 570 KLPSCMAWIKYISTTFYSYRLLinvQYGE--------GKRISSLLGCSLPHGSDRASCKFVEEDVagQISPA------TS 635
|
650 660
....*....|....*....|...
gi 1720417991 635 LACMIIIFL---TIAYLKLLFLK 654
Cdd:PLN03211 636 VSVLIFMFVgyrLLAYLALRRIK 658
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-642 |
4.44e-82 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 283.15 E-value: 4.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 33 EGDVLSFHHITYRVKVKSGflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDpKGL--SGDVLING 109
Cdd:TIGR00956 756 GEDIFHWRNLTYEVKIKKE-------KRVILNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVT-TGVitGGDRLVNG 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 110 APQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIrGISGGE 189
Cdd:TIGR00956 828 RPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQ 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 190 RKRTSIGMELITDP-SILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASG-KLVFHG 267
Cdd:TIGR00956 907 RKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFG 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 268 P----AQKALEYFASAGYH-CEPYNNPADFFLDVIngdsSAVMLNREEQDneankteepskgekpvienLSEFYINSAIY 342
Cdd:TIGR00956 987 DlgenSHTIINYFEKHGAPkCPEDANPAEWMLEVI----GAAPGAHANQD-------------------YHEVWRNSSEY 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 343 GETKAELDQ----LPGAQEKKGTSAFKEpvYVTSFCHQLRWIARRSFKNLLGNPQASVAQLIVTVILGLIIGAIYFDLKY 418
Cdd:TIGR00956 1044 QAVKNELDRleaeLSKAEDDNDPDALSK--YAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGT 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 419 DAAGMQNRAG-----VLFFLTTNQcfssvSAVELFVVEKKLF-IHEYISGYYRVSSYFFGKVMSDlLPMRFLPSVIFTCI 492
Cdd:TIGR00956 1122 SLQGLQNQMFavfmaTVLFNPLIQ-----QYLPPFVAQRDLYeVRERPSRTFSWLAFIAAQITVE-IPYNLVAGTIFFFI 1195
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 493 LYFMLGLKKTV-------DAFFIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLLVNLRTIGPWl 565
Cdd:TIGR00956 1196 WYYPVGFYWNAsktgqvhERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGF- 1274
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 566 sWLQYFSI-------------------------------PRYGFTALQYNE-FLgqEFCPGFNVTDNSTCVNSYAIC-TG 612
Cdd:TIGR00956 1275 -WIFMYRCspftylvqallstgladvpvtckvkelltfnPPSGQTCGEYMKpYL--ENAGGYLLNPNATDSCSFCQYsYT 1351
|
650 660 670
....*....|....*....|....*....|
gi 1720417991 613 NEYLINQGIELSpwGLWKNHVALACMIIIF 642
Cdd:TIGR00956 1352 NDFLEPISSKYS--GRWRNFGIFIAFIFFN 1379
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
46-267 |
1.32e-70 |
|
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: 228.31 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 46 VKVKSGFlVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKG-LSGDVLINGAP-QPAHFKCCSGY 122
Cdd:cd03234 7 WDVGLKA-KNWNKYARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPrKPDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 123 VVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTiikeLGLEKVADSKVGTQFIRGISGGERKRTSIGMELITD 202
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVED----VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 203 PSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-267 |
2.00e-62 |
|
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: 205.55 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 34 GDVLSFHHITYRVKVKSGflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGAPQ 112
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG-------KRQLLNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 113 PAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRlpttmknheknerintiikelglekvadskvgtqfirGISGGERKR 192
Cdd:cd03232 74 DKNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKR 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 193 TSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLAS-GKLVFHG 267
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2-594 |
1.51e-57 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 210.86 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 2 SSSNDHVLVPMSQRNNNGLPRMNSRAVRTLAEGD-------------VLSFHHITYRVKVKSGFLVRKTVEK--EILSDI 66
Cdd:PLN03140 820 ADGNNTREVAIQRMSNPEGLSKNRDSSLEAANGVapkrgmvlpftplAMSFDDVNYFVDMPAEMKEQGVTEDrlQLLREV 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 67 NGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGAPQPAH-FKCCSGYVVQDDVVMGTLTVRENLQFSAA 144
Cdd:PLN03140 900 TGAFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQEtFARISGYCEQNDIHSPQVTVRESLIYSAF 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 145 LRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 224
Cdd:PLN03140 980 LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 225 LLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLA-SGKLVFHGP----AQKALEYFASagYHCEP----YNNPADFFLD 295
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPlgrnSHKIIEYFEA--IPGVPkikeKYNPATWMLE 1137
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 296 VingdSSAVMLNREEQDneankteepskgekpvienLSEFYINSAIYGETKAELDQL----PGAQEKKGTSAFKEPVY-- 369
Cdd:PLN03140 1138 V----SSLAAEVKLGID-------------------FAEHYKSSSLYQRNKALVKELstppPGASDLYFATQYSQSTWgq 1194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 370 VTSFCHQLRWIARRSfknllgnPQASVAQLIVTVILGLIIGAIYFDL--KYDAAGMQNRA-----GVLFFLTTNQCfSSV 442
Cdd:PLN03140 1195 FKSCLWKQWWTYWRS-------PDYNLVRFFFTLAAALMVGTIFWKVgtKRSNANDLTMVigamyAAVLFVGINNC-STV 1266
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 443 SAVelFVVEKKLFIHEYISGYYRVSSYFFGKVMSDlLPMRFLPSVIFTCILYFMLGLKKTVDAF----FIMMFTLIMVAY 518
Cdd:PLN03140 1267 QPM--VAVERTVFYRERAAGMYSALPYAIAQVVCE-IPYVLIQTTYYTLIVYAMVAFEWTAAKFfwfyFISFFSFLYFTY 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 519 TAsSMALAIATGQsvvSVATLLMTIAFVFMMLFSGLLVNLRTIGPWlsWLQYFSI-----PRYGFTALQYNEFLGQEFCP 593
Cdd:PLN03140 1344 YG-MMTVSLTPNQ---QVAAIFAAAFYGLFNLFSGFFIPRPKIPKW--WVWYYWIcpvawTVYGLIVSQYGDVEDTIKVP 1417
|
.
gi 1720417991 594 G 594
Cdd:PLN03140 1418 G 1418
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
51-653 |
4.76e-48 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 182.35 E-value: 4.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 51 GFLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPK-GLSGDVLING------APQPAhfkccSGY 122
Cdd:PLN03140 169 GINLAKKTKLTILKDASGIIKPSrMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNGyrlnefVPRKT-----SAY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 123 VVQDDVVMGTLTVRENLQFSA---------------ALR------LP----------TTMKNHEKNERINTIIKELGLEK 171
Cdd:PLN03140 244 ISQNDVHVGVMTVKETLDFSArcqgvgtrydllselARRekdagiFPeaevdlfmkaTAMEGVKSSLITDYTLKILGLDI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 172 VADSKVGTQFIRGISGGERKRTSIGmELITDPS-ILFLDEPTTGLDSSTANAVLLLLKRMSKQGR-TIIFSIHQPRYSIF 249
Cdd:PLN03140 324 CKDTIVGDEMIRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETF 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 250 KLFDSLTLLASGKLVFHGPAQKALEYFASAGYHCEPYNNPADFFLDVIngdssavmlNREEQDNEANKTEEPSKgEKPV- 328
Cdd:PLN03140 403 DLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVT---------SKKDQEQYWADRNKPYR-YISVs 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 329 --IENLSEFYINSAIYGETKAELDQLPGAQEKKGTSAFKEP-VYVTSFCHQLRW--IARRSFknllgnpqASVAQLIVTV 403
Cdd:PLN03140 473 efAERFKSFHVGMQLENELSVPFDKSQSHKAALVFSKYSVPkMELLKACWDKEWllMKRNAF--------VYVFKTVQII 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 404 ILGLIIGAIYFDLKYDAAGMQNRA---GVLFFLTTNQCFSSVSAVELFVVEKKLFIHE-----YISGYYRVSSYFFGkvm 475
Cdd:PLN03140 545 IVAAIASTVFLRTEMHTRNEEDGAlyiGALLFSMIINMFNGFAELALMIQRLPVFYKQrdllfHPPWTFTLPTFLLG--- 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 476 sdlLPMRFLPSVIFTCILYFMLGLKKTVDAFFIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLL 555
Cdd:PLN03140 622 ---IPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFI 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 556 VNLRTIGPWLSWLQYFSIPRYGFTALQYNEFlgqeFCPGF---NVTDNSTCVnsyaictGNEYLINQGIELSPWGLWKNH 632
Cdd:PLN03140 699 LPKGEIPNWWEWAYWVSPLSYGFNALAVNEM----FAPRWmnkMASDNSTRL-------GTAVLNIFDVFTDKNWYWIGV 767
|
650 660
....*....|....*....|.
gi 1720417991 633 VALACMIIIFLTIAYLKLLFL 653
Cdd:PLN03140 768 GALLGFTILFNVLFTLALTYL 788
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
380-584 |
1.45e-44 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 157.82 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 380 IARRSFKNLLGNPQASVAQLIVTVILGLIIGAIYFDLKyDAAGMQNRAGVLFFLTTNQCFSSVSAVEL-FVVEKKLFIHE 458
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGISPvFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 459 YISGYYRVSSYFFGKVMSDLlPMRFLPSVIFTCILYFMLGLKKTVDAFFIMMFTLIMVAYTASSMALAIATGQSVVSVAT 538
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSEL-PLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720417991 539 LLMTIAFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFTALQYN 584
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
60-276 |
7.01e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.45 E-value: 7.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHFKCCSGYVVQDDVVMG 131
Cdd:COG1131 13 KTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLL------GLlrptSGEVRVLGEDvarDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:COG1131 87 DLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPAQKALEYF 276
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
55-267 |
3.93e-42 |
|
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: 151.26 E-value: 3.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 55 RKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKG-LSGDVLINGAP-QPAHFKCCSG--YVVQDDVV 129
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPyKEFAEKYPGEiiYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTLTVRENLQFSAALRlpttmknheknerintiikelglekvadskvGTQFIRGISGGERKRTSIGMELITDPSILFLD 209
Cdd:cd03233 95 FPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
59-270 |
3.90e-41 |
|
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: 150.01 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP---QPAHFKCCSGYVVQDDVVMGTLT 134
Cdd:COG4555 13 KVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGEDvrkEPREARRQIGVLPDERGLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFSAALRLpttMKNHEKNERINTIIKELGLEKVADSKVGtqfirGISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:COG4555 91 VRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 215 LDSSTANAVLLLLKRMSKQGRTIIFSIHQPrYSIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLD 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
76-271 |
7.52e-33 |
|
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: 126.08 E-value: 7.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALR-LPttm 151
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGysiRTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLKgLP--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 152 kNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMs 231
Cdd:cd03263 107 -KSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720417991 232 KQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQK 271
Cdd:cd03263 180 RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
60-267 |
7.60e-31 |
|
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: 119.99 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP---QPAHFKCCSGYVVQDDVVMGTLTVR 136
Cdd:cd03264 13 KRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPS--SGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:cd03264 91 EFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 217 SSTANAVLLLLKRMSKqGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03264 163 PEERIRFRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
59-273 |
9.18e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 9.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPqPAHFKCCSGYVVQD------- 126
Cdd:COG1121 18 GRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAIL------GLlpptSGTVRLFGKP-PRRARRRIGYVPQRaevdwdf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 -----DVVMGTLTVRENLqfsaaLRLPTtmknHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELIT 201
Cdd:COG1121 91 pitvrDVVLMGRYGRRGL-----FRRPS----RADREAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLAsGKLVFHGPAQKAL 273
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLN-RGLVAHGPPEEVL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
54-263 |
4.79e-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: 117.98 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKT-----VEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPqpahFKCCS------- 120
Cdd:cd03255 6 LSKTyggggEKVQALKGVSLSIEKGeFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVRVDGTD----ISKLSekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 121 -----GYVVQDDVVMGTLTVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSI 195
Cdd:cd03255 80 rrrhiGFVFQSFNLLPDLTALENVEL--PLLL-AGVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 196 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRysIFKLFDSLTLLASGKL 263
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE--LAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
38-262 |
7.48e-30 |
|
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: 117.18 E-value: 7.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 38 SFHHITYRvkvksgflvRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----Q 112
Cdd:cd03225 1 ELKNLSFS---------YPDGARPALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLLGPT--SGEVLVDGKDltklS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 113 PAHFKCCSGYVVQD-DVVMGTLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERK 191
Cdd:cd03225 70 LKELRRKVGLVFQNpDDQFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRD-----RSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 192 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGK 262
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
59-244 |
1.43e-29 |
|
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: 116.04 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHFKCCSGYVVQDDVVM 130
Cdd:COG4133 14 ERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILA------GLlppsAGEVLWNGEPirdAREDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENLQFSAALRlpttmKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDE 210
Cdd:COG4133 88 PELTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 244
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
36-264 |
1.62e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.68 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKSGflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGA 110
Cdd:COG1136 4 LLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILG------GLdrptSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 111 P-------QPAHFKCCS-GYVVQDDVVMGTLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfi 182
Cdd:COG1136 71 DisslserELARLRRRHiGFVFQFFNLLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPSQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 183 rgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRysIFKLFDSLTLLASG 261
Cdd:COG1136 145 --LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
...
gi 1720417991 262 KLV 264
Cdd:COG1136 221 RIV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
36-273 |
2.47e-29 |
|
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: 117.07 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKvksgflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPA 114
Cdd:COG1120 1 MLEAENLSVGYG-----------GRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPS--SGEVLLDGRDLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 HfkccS--------GYVVQDDVVMGTLTVREnlqfSAAL-RLPTT----MKNHEKNERINTIIKELGLEKVADSKVGTqf 181
Cdd:COG1120 68 L----SrrelarriAYVPQEPPAPFGLTVRE----LVALgRYPHLglfgRPSAEDREAVEEALERTGLEHLADRPVDE-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 182 irgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQP----RYSifklfDSLT 256
Cdd:COG1120 138 ---LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLnlaaRYA-----DRLV 209
|
250
....*....|....*..
gi 1720417991 257 LLASGKLVFHGPAQKAL 273
Cdd:COG1120 210 LLKDGRIVAQGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
63-213 |
8.12e-29 |
|
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: 111.97 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGapQPAHFKCCS------GYVVQDDVVMGTLTV 135
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSP--TEGTILLDG--QDLTDDERKslrkeiGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 136 RENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGtQFIRGISGGERKRTSIGMELITDPSILFLDEPTT 213
Cdd:pfam00005 77 RENLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVG-ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
60-267 |
9.13e-29 |
|
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: 114.17 E-value: 9.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHFkccsGYVVQDDVVMG 131
Cdd:cd03235 12 HPVLEDVSFEVKPGeFLAIVGPNGAGKSTLLKAIL------GLlkptSGSIRVFGKPlekERKRI----GYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 T--LTVRE-----NLQFSAALRLPTtmknHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPS 204
Cdd:cd03235 82 DfpISVRDvvlmgLYGHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 205 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLAsGKLVFHG 267
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
71-267 |
4.20e-28 |
|
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: 112.46 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 71 KPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALR 146
Cdd:cd03266 29 KPGeVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGfdvVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 147 lptTMKNHEKNERINTIIKELGLEKVADSKVGtqfirGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 226
Cdd:cd03266 107 ---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720417991 227 LKRMSKQGRTIIFSIHQpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03266 179 IRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
60-263 |
1.47e-27 |
|
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: 109.41 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHFKCCSGYVVQDDVVMG 131
Cdd:cd03230 13 KTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIIL------GLlkpdSGEIKVLGKDikkEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSaalrlpttmknheknerintiikelglekvadskvgtqfirgisGGERKRTSIGMELITDPSILFLDEP 211
Cdd:cd03230 87 NLTVRENLKLS--------------------------------------------GGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKL 263
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
59-270 |
2.91e-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: 110.28 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP----QPA---HFKCCSGYVVQDDVVM 130
Cdd:cd03261 12 GRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRP--DSGEVLIDGEDisglSEAelyRLRRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENLQFSaaLRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDE 210
Cdd:cd03261 90 DSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQpRYSIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
59-274 |
5.32e-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: 109.73 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP-QPAHFKCCS---GYVVQD-D- 127
Cdd:COG1122 13 GTPALDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLN------GLlkptSGEVLVDGKDiTKKNLRELRrkvGLVFQNpDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 128 -VVMGTltVRENLQFS-AALRLPTTmknhEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSI-GMeLITDPS 204
Cdd:COG1122 87 qLFAPT--VEEDVAFGpENLGLPRE----EIRERVEEALELVGLEHLADRPPHE-----LSGGQKQRVAIaGV-LAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 205 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
54-267 |
1.05e-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: 108.38 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV-EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHfKCCSGYVV 124
Cdd:cd03259 6 LSKTYgSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIA------GLerpdSGEILIDGRDvtgVPPE-RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 125 QDDVVMGTLTVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPS 204
Cdd:cd03259 79 QDYALFPHLTVAENIAF--GLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 205 ILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQE-EALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
37-242 |
1.07e-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: 108.33 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRVKVKSGflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP 111
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGeFVALVGPSGCGKSTLLRIIA------GLerptSGEVLVDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 -QPAHFKCcsGYVVQDDVVMGTLTVRENLQFSAALRLpttMKNHEKNERINTIIKELGLEKVADSkvgtqFIRGISGGER 190
Cdd:cd03293 68 vTGPGPDR--GYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENA-----YPHQLSGGMR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 191 KRTSIGMELITDPSILFLDEPTTGLDSSTANAV-LLLLKRMSKQGRTIIFSIH 242
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTH 190
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
76-270 |
5.72e-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: 108.63 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRlptTMK 152
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRMLTTLLRPT--SGTARVAGydvVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGRLY---GLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 153 NHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 232
Cdd:TIGR01188 98 KDEAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720417991 233 QGRTIIFSIHQpRYSIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:TIGR01188 173 EGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
59-270 |
2.25e-25 |
|
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: 105.06 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---------QPAHFKCcsGYVV 124
Cdd:COG1127 17 DRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLII------GLlrpdSGEILVDGQDitglsekelYELRRRI--GMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 125 QDDVVMGTLTVRENLQFsaALRLPTTMKNHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPS 204
Cdd:COG1127 89 QGGALFDSLTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAAD-----KMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 205 ILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLD-SAFAIADRVAVLADGKIIAEGTPE 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
59-267 |
2.26e-25 |
|
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: 103.28 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPqpahfkccsgyvvqddvvmgtl 133
Cdd:cd03214 11 GRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLA------GLlkpsSGEILLDGKD---------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 tvrenlqfsaalrlPTTMKNHEKNERI---NTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDE 210
Cdd:cd03214 63 --------------LASLSPKELARKIayvPQALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP----RYSifklfDSLTLLASGKLVFHG 267
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLnlaaRYA-----DRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
63-270 |
1.01e-24 |
|
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: 103.29 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP---QPAHFKCCSGyVV---QDDVVMGTLTV 135
Cdd:cd03219 16 LDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPT--SGSVLFDGEDitgLPPHEIARLG-IGrtfQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAALRLPTTM-------KNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFL 208
Cdd:cd03219 93 LENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD-VVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
59-262 |
1.75e-24 |
|
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: 100.01 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPqpahfkccsgyvvqddvvmgtltvre 137
Cdd:cd00267 11 GRTALDNVSlTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT--SGEILIDGKD-------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 nlqfsaalrlpttmknheknerINTIIKELGLEKVAdskvgtqFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDS 217
Cdd:cd00267 63 ----------------------IAKLPLEELRRRIG-------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720417991 218 STANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGK 262
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
53-242 |
4.17e-24 |
|
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: 100.91 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 53 LVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHFKCCSGYVVQDDV 128
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPT--SGRATVAGhdvVREPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 129 VMGTLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFL 208
Cdd:cd03265 84 VDDELTGWENLYIHARLY---GVPGAERRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIH 242
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTH 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
59-262 |
4.75e-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: 99.57 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQPAHFKCC------SGYVVQDD 127
Cdd:cd03229 12 QKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIA------GLeepdSGSILIDGEDLTDLEDELpplrrrIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 128 VVMGTLTVRENLQFsaalrlpttmknheknerintiikelglekvadskvgtqfirGISGGERKRTSIGMELITDPSILF 207
Cdd:cd03229 86 ALFPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGK 262
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
63-242 |
1.53e-23 |
|
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: 99.02 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP-------QPAHFKCCSGYVVQDDVVMGTLT 134
Cdd:cd03292 17 LDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPT--SGTIRVNGQDvsdlrgrAIPYLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:cd03292 95 VYENVAF--ALEV-TGVPPREIRKRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 1720417991 215 LDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
60-269 |
1.97e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP--------QPAH-FKCcsGYVVQD--- 126
Cdd:COG2884 15 REALSDVSLEIEKGeFVFLTGPSGAGKSTLLKLLYGEERPT--SGQVLVNGQDlsrlkrreIPYLrRRI--GVVFQDfrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 --DvvmgtLTVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPS 204
Cdd:COG2884 91 lpD-----RTVYENVAL--PLRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 205 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTL-LASGKLVFHGPA 269
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD--LELVDRMPKRVLeLEDGRLVRDEAR 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
76-274 |
2.18e-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: 99.33 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA------PQPAHFkccsGYVVQDDVVMGTLTVRENLQFsaALRLPT 149
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPD--SGKILLNGKditnlpPEKRDI----SYVPQNYALFPHMTVYKNIAY--GLKKRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 150 TMKNhEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKR 229
Cdd:cd03299 101 VDKK-EIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720417991 230 MSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
54-267 |
2.22e-23 |
|
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: 98.44 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV-EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQPAHFKCCS--GYVVQ 125
Cdd:cd03268 6 LTKTYgKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIIL------GLikpdSGEITFDGKSYQKNIEALRriGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 126 DDVVMGTLTVRENLQFSAALRLpttmknhEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSI 205
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLG-------IRKKRIDEVLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 206 LFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
32-239 |
3.16e-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: 99.39 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 32 AEGDVLSFHHITYRVKVKSGflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVL 106
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGeFVALVGPSGCGKSTLLRLIA------GLekptSGEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 107 ING----APQPAHfkccsGYVVQDDVVMGTLTVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfi 182
Cdd:COG1116 70 VDGkpvtGPGPDR-----GVVFQEPALLPWLTVLDNVAL--GLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQ--- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 183 rgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAnAVL--LLLKRMSKQGRTIIF 239
Cdd:COG1116 139 --LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTR-ERLqdELLRLWQETGKTVLF 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
60-264 |
4.83e-23 |
|
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: 97.33 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING--APQPAHFKCCsGYVVQD-DVVMGTLTV 135
Cdd:cd03226 13 TEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKES--SGSILLNGkpIKAKERRKSI-GYVMQDvDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAalrlpttMKNHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:cd03226 90 REELLLGL-------KELDAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720417991 216 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGKLV 264
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
37-238 |
6.41e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.19 E-value: 6.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRVKvksgflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP 111
Cdd:COG4619 1 LELEGLSFRVG-----------GKPILSPVSLTLEAGeCVAITGPSGSGKSTLLRALA------DLdpptSGEIYLDGKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 Q----PAHFKCCSGYVVQDdVVMGTLTVRENLQFSAALRlpttmKNHEKNERINTIIKELGL-EKVADSKVGTqfirgIS 186
Cdd:COG4619 64 LsampPPEWRRQVAYVPQE-PALWGGTVRDNLPFPFQLR-----ERKFDRERALELLERLGLpPDILDKPVER-----LS 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 187 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTII 238
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVL 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
73-267 |
6.54e-23 |
|
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: 97.37 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 73 GLNAILGPTGGGKSSLLDVLAARKDPKG----LSGDVL------INGAPQPAHFkccsGYVVQDDVVMGTLTVRENLQFS 142
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGgtivLNGTVLfdsrkkINLPPQQRKI----GLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 143 aalrlpttMKNHEKNE---RINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSST 219
Cdd:cd03297 100 --------LKRKRNREdriSVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720417991 220 ANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
59-274 |
1.74e-22 |
|
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: 102.60 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQ----PAHFKCCSGYVVQDDVV 129
Cdd:COG2274 487 SPPVLDNISLTIKPGeRVAIVGRSGSGKSTLLKLLL------GLyeptSGRILIDGIDLrqidPASLRRQIGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTlTVRENLQFSAALrlpTTMknheknERINTIIKELGLEKVA-------DSKVGTQFiRGISGGERKRTSIGMELITD 202
Cdd:COG2274 561 FSG-TIRENITLGDPD---ATD------EEIIEAARLAGLHDFIealpmgyDTVVGEGG-SNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 203 PSILFLDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAH--RLSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
63-244 |
1.75e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAPQPAhfkccsgYVVQDDVVMGTL--TVRENL 139
Cdd:NF040873 8 LHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRP--TSGTVRRAGGARVA-------YVPQRSEVPDSLplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 140 QFSA-ALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSS 218
Cdd:NF040873 79 AMGRwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*.
gi 1720417991 219 TANAVLLLLKRMSKQGRTIIFSIHQP 244
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
59-268 |
3.23e-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: 95.76 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTl 133
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKvAIVGPSGSGKSTILRLLFRFYDV--SSGSILIDGQDirevTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSaalRLPTT---MKNHEKNERINTIIkeLGLEKVADSKVGTqfiRG--ISGGERKRTSIGMELITDPSILFL 208
Cdd:cd03253 90 TIGYNIRYG---RPDATdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGE---RGlkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHGP 268
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK-GRTTIVIAH--RLSTIVNADKIIVLKDGRIVERGT 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
37-262 |
4.18e-22 |
|
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: 93.60 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRvkvksgflvRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP---- 111
Cdd:cd03228 1 IEFKNVSFS---------YPGRPKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPT--SGEILIDGVDlrdl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 QPAHFKCCSGYVVQDDVVMGTlTVRENLqfsaalrlpttmknheknerintiikelglekvadskvgtqfirgISGGERK 191
Cdd:cd03228 70 DLESLRKNIAYVPQDPFLFSG-TIRENI---------------------------------------------LSGGQRQ 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 192 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGK 262
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
59-274 |
7.92e-22 |
|
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: 99.83 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTl 133
Cdd:COG4988 349 GRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPY--SGSILINGVDlsdlDPASWRRQIAWVPQNPYLFAG- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSAAlrlpttmknHEKNERINTIIKELGLEKVA-------DSKVGTQFiRGISGGERKRTSIGMELITDPSIL 206
Cdd:COG4988 426 TIRENLRLGRP---------DASDEELEAALEAAGLDEFVaalpdglDTPLGEGG-RGLSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 207 FLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHQPrySIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL--ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
43-267 |
1.43e-21 |
|
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: 93.94 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 43 TYRVKVKSGFLV--------RKTVEKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING-APq 112
Cdd:cd03267 9 SYRVYSKEPGLIgslkslfkRKYREVEALKGISfTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT--SGEVRVAGlVP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 113 pahFKCCSGYVVQDDVVMGT-------LTVRENLQFSAAL-RLPTTmknhEKNERINTIIKELGLEKVADSKVgtqfiRG 184
Cdd:cd03267 86 ---WKRRKKFLRRIGVVFGQktqlwwdLPVIDSFYLLAAIyDLPPA----RFKKRLDELSELLDLEELLDTPV-----RQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKL 263
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMK-DIEALARRVLVIDKGRL 232
|
....
gi 1720417991 264 VFHG 267
Cdd:cd03267 233 LYDG 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
76-267 |
1.66e-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: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLING----APQPAHFKCCSgyVVQDDVVMGTLTVREN--LQFSAALRLpt 149
Cdd:cd03298 28 AIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGvdvtAAPPADRPVSM--LFQENNLFAHLTVEQNvgLGLSPGLKL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 150 tmkNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLK 228
Cdd:cd03298 102 ---TAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLdLVLD 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720417991 229 RMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03298 174 LHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
55-279 |
2.36e-21 |
|
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: 93.71 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 55 RKTVEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP----QPAHFKCCSGYVVQ 125
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESfGLVGESGSGKSTLLRALA------GLerpwSGEVTFDGRPvtrrRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 126 DdvVMGTL----TVRENLqfSAALRLpttMKNHEKNERINTIIKELGLekvaDSKVGTQFIRGISGGERKRTSIGMELIT 201
Cdd:COG1124 87 D--PYASLhprhTVDRIL--AEPLRI---HGLPDREERIAELLEQVGL----PPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPAQKALEYFASA 279
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAV-VAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
60-270 |
3.06e-21 |
|
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: 93.40 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCC-------SGYVVQDDVVMG 131
Cdd:cd03256 14 KKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPT--SGSVLIDGTDINKLKGKAlrqlrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSAALRLPT---TMKNHEKNERINTI--IKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSIL 206
Cdd:cd03256 92 RLSVLENVLSGRLGRRSTwrsLFGLFPKEEKQRALaaLERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 207 FLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKDGRIVFDGPPA 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
76-274 |
3.45e-21 |
|
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: 97.91 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP--------QPAHFkccsGYVVQDDVVMGTlTVRENL-------- 139
Cdd:COG4987 365 AIVGPSGSGKSTLLALLLRFLDP--QSGSITLGGVDlrdldeddLRRRI----AVVPQRPHLFDT-TLRENLrlarpdat 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 140 --QFSAALR----------LPttmknheknERINTIIKELGlekvadskvgtqfiRGISGGERKRTSIGMELITDPSILF 207
Cdd:COG4987 438 deELWAALErvglgdwlaaLP---------DGLDTWLGEGG--------------RRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHQPrySIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRL--AGLERMDRILVLEDGRIVEQGTHEELLA 558
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
59-267 |
3.73e-21 |
|
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: 92.27 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQ----PAHFKCCSGYVVQDdVVMGTL 133
Cdd:cd03245 16 EIPALDNVSLTIRAGEKvAIIGRVGSGKSTLLKLLAGLYKPT--SGSVLLDGTDIrqldPADLRRNIGYVPQD-VTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLqfsaALRLPttmknHEKNERINTIIKELGLEKVA-------DSKVGTQFiRGISGGERKRTSIGMELITDPSIL 206
Cdd:cd03245 93 TLRDNI----TLGAP-----LADDERILRAAELAGVTDFVnkhpnglDLQIGERG-RGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 207 FLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITH--RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
37-267 |
3.73e-21 |
|
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: 91.22 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRVKVKsgflvrktvEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLaaRKDPKGLSGDVLINGAPQPAH 115
Cdd:cd03247 1 LSINNVSFSYPEQ---------EQQVLKNLSLELKQGEKiALLGRSGSGKSTLLQLL--TGDLKPQQGEITLDGVPVSDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 116 FKCCSGYvvqddvvMGTLTVRENLqFSAALRlpttmknheknerintiikelglekvadSKVGTQFirgiSGGERKRTSI 195
Cdd:cd03247 70 EKALSSL-------ISVLNQRPYL-FDTTLR----------------------------NNLGRRF----SGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 196 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH--HLTGIEHMDKILFLENGKIIMQG 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
59-242 |
3.94e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP--QPAHFKccsGYVVQDDVVMGTLTV 135
Cdd:COG4525 19 PQPALQDVSLTIESGeFVVALGASGCGKTTLLNLIAGFLAP--SSGEITLDGVPvtGPGADR---GVVFQKDALLPWLNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:COG4525 94 LDNVAF--GLRL-RGVPKAERRARAEELLALVGLADFAR-----RRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGAL 165
|
170 180
....*....|....*....|....*...
gi 1720417991 216 DSSTANAV-LLLLKRMSKQGRTIIFSIH 242
Cdd:COG4525 166 DALTREQMqELLLDVWQRTGKGVFLITH 193
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
36-239 |
4.01e-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: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKSGflvrktvEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLING----A 110
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETlGLVGESGSGKSTLARAILGLLKPT--SGSIIFDGkdllK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 111 PQPAHFKCCS---GYVVQDdvVMGTL----TVREnlQFSAALRLPTTMKNHEKNERIntiiKELGLEKV-ADSKVGTQFI 182
Cdd:cd03257 72 LSRRLRKIRRkeiQMVFQD--PMSSLnprmTIGE--QIAEPLRIHGKLSKKEARKEA----VLLLLVGVgLPEEVLNRYP 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 183 RGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 239
Cdd:cd03257 144 HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLF 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
59-263 |
3.52e-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: 88.04 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTl 133
Cdd:cd03246 14 EPPVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRP--TSGRVRLDGADisqwDPNELGDHVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLqfsaalrlpttmknheknerintiikelglekvadskvgtqfirgISGGERKRTSIGMELITDPSILFLDEPTT 213
Cdd:cd03246 91 SIAENI---------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720417991 214 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPrySIFKLFDSLTLLASGKL 263
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
61-244 |
8.89e-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: 93.19 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAPQPAHFKC----CSGYVVQDDVVMGTlTV 135
Cdd:TIGR02868 349 PVLDGVSLDLPPGERvAILGPSGSGKSTLLATLAGLLDP--LQGEVTLDGVPVSSLDQDevrrRVSVCAQDAHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQF----------SAALRlpttmknhekNERINTIIKEL--GLekvaDSKVGTQFIRgISGGERKRTSIGMELITDP 203
Cdd:TIGR02868 426 RENLRLarpdatdeelWAALE----------RVGLADWLRALpdGL----DTVLGEGGAR-LSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720417991 204 SILFLDEPTTGLDSSTANAVL-LLLKRMSkqGRTIIFSIHQP 244
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLeDLLAALS--GRTVVLITHHL 530
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
76-273 |
1.22e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.27 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAH-------FkccsgyvvQDDVVMGTLTVREN--LQFSA 143
Cdd:COG3840 29 AILGPSGAGKSTLLNLIAGFLPPD--SGRILWNGqdlTALPPAerpvsmlF--------QENNLFPHLTVAQNigLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 144 ALRLpttmkNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:COG3840 99 GLKL-----TAEQRAQVEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 224 LLLLKRMSK-QGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:COG3840 169 LDLVDELCReRGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
76-274 |
1.91e-19 |
|
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: 87.49 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHFKCCSG--YVVQDDVVMGTLTVRENLQFSAALR 146
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIM------GLlpprSGSIRFDGRDitgLPPHERARAGigYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 147 lpttmknheKNERINTIIKEL-----GLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 221
Cdd:cd03224 104 ---------RRAKRKARLERVyelfpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 222 AVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNAR-FALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
59-274 |
2.27e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 91.89 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKG-LSGDVLING----APQPAHFKCCSGYVVQD-DVVMG 131
Cdd:COG1123 18 DVPAVDGVSLTIAPGeTVALVGESGSGKSTLALALMGLLPHGGrISGEVLLDGrdllELSEALRGRRIGMVFQDpMTQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:COG1123 98 PVTVGDQIAE--ALEN-LGLSRAEARARVLELLEAVGLERRLD-----RYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRErGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
59-274 |
2.33e-19 |
|
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: 87.28 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTl 133
Cdd:cd03254 15 KKPVLKDINFSIKPGeTVAIVGPTGAGKTTLINLLMRFYDPQ--KGQILIDGIDirdiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSaalrlpttmKNHEKNERINTIIKELG-------LEKVADSKVGTQFiRGISGGERKRTSIGMELITDPSIL 206
Cdd:cd03254 92 TIMENIRLG---------RPNATDEEVIEAAKEAGahdfimkLPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 207 FLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH--RLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
73-270 |
3.21e-19 |
|
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: 89.79 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 73 GLNAILGPTGGGKSSLLDVLAARKDPKG----LSGDVLINGAPQ---PAHfKCCSGYVVQDDVVMGTLTVRENLQFSAAL 145
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEgeivLNGRTLFDSRKGiflPPE-KRRIGYVFQEARLFPHLSVRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 146 RLPTtmknhEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 225
Cdd:TIGR02142 103 ARPS-----ERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720417991 226 LLKRMSKQGRT-IIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQ-EVLRLADRVVVLEDGRVAAAGPIA 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
62-273 |
3.27e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP-----QPAHFKCCSgyVVQDDVVMGTLTV 135
Cdd:PRK11160 355 VLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQ--QGEILLNGQPiadysEAALRQAIS--VVSQRVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAAlrlpttmknHEKNERINTIIKELGLEKVADSKVG-TQFI----RGISGGERKRTSIGMELITDPSILFLDE 210
Cdd:PRK11160 431 RDNLLLAAP---------NASDEALIEVLQQVGLEKLLEDDKGlNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHA-QNKTVLMITH--RLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
72-273 |
3.97e-19 |
|
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: 89.39 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 72 PGLNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP-Q--------PAHfKCCSGYVVQDDVVMGTLTVREN 138
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIA------GLerpdSGRIRLGGEVlQdsargiflPPH-RRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 139 LQFSAAlRLPTtmknHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSS 218
Cdd:COG4148 98 LLYGRK-RAPR----AERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 219 TANAVLLLLKRMSKQGRT-IIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:COG4148 168 RKAEILPYLERLRDELDIpILYVSHSLD-EVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
54-267 |
7.20e-19 |
|
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: 85.41 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV-EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCSGYVVQDDVVMG 131
Cdd:cd03269 6 VTKRFgRVTALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPD--SGEVLFDGKPLDIAARNRIGYLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:cd03269 84 KMKVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLYG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-274 |
7.59e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 90.35 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 20 LPRMNSRAVRTLAEGD-VLSFHHITYRvkvksgFLVRKTVEKEILSDINGIMKPG--LnAILGPTGGGKSSLLDVLAark 96
Cdd:COG1123 243 LGAARGRAAPAAAAAEpLLEVRNLSKR------YPVRGKGGVRAVDDVSLTLRRGetL-GLVGESGSGKSTLARLLL--- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 97 dpkGL----SGDVLINGAPqPAHFKCCS--------GYVVQDdvVMGTL----TVRENLQFsaALRLPTTMKNHEKNERI 160
Cdd:COG1123 313 ---GLlrptSGSILFDGKD-LTKLSRRSlrelrrrvQMVFQD--PYSSLnprmTVGDIIAE--PLRLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 161 NTIIKELGLekvaDSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 239
Cdd:COG1123 385 AELLERVGL----PPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLF 460
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720417991 240 SIHQ----PRYSifklfDSLTLLASGKLVFHGPAQKALE 274
Cdd:COG1123 461 ISHDlavvRYIA-----DRVAVMYDGRIVEDGPTEEVFA 494
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-245 |
8.57e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.99 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 31 LAEGDVLSFHHITYRVKvksgflvRKTVEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDpkGLSGDVLING 109
Cdd:PRK10584 1 MPAENIVEVHHLKKSVG-------QGEHELSILTGVELVVKRGETiALIGESGSGKSTLLAILAGLDD--GSSGEVSLVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 110 AP-------QPAHFKCCS-GYVVQDDVVMGTLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADsKVGTQf 181
Cdd:PRK10584 72 QPlhqmdeeARAKLRAKHvGFVFQSFMLIPTLNALENVELPALLR---GESSRQSRNGAKALLEQLGLGKRLD-HLPAQ- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 182 irgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPR 245
Cdd:PRK10584 147 ---LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQ 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
53-267 |
1.00e-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: 85.67 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 53 LVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGA---PQPAHFKCCSG--Y 122
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIV------GLvkpdSGKILLDGQditKLPMHKRARLGigY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 123 VVQDDVVMGTLTVRENLqfSAALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITD 202
Cdd:cd03218 80 LPQEASIFRKLTVEENI--LAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 203 PSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEG 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
59-244 |
1.14e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQ--PAHFKCCSgYVVQDDVVMG 131
Cdd:PRK13539 14 GRVLFSGLSFTLAAGeALVLTGPNGSGKTTLLRLIA------GLlppaAGTIKLDGGDIddPDVAEACH-YLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSAALRlpttmknHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:PRK13539 87 ALTVAENLEFWAAFL-------GGEELDIAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 244
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
55-264 |
1.28e-18 |
|
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: 85.10 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 55 RKTVEKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPA------------HFkccsG 121
Cdd:TIGR02211 13 EGKLDTRVLKGVSlSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT--SGEVLFNGQSLSKlssneraklrnkKL----G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 122 YVVQDDVVMGTLTVRENLQFSAalrLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELIT 201
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIFSIHQPRYSifKLFDSLTLLASGKLV 264
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFdLMLELNRELNTSFLVVTHDLELA--KKLDRVLEMKDGQLF 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
37-282 |
1.55e-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: 85.23 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRVKVKsgflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING----AP 111
Cdd:cd03252 1 ITFEHVRFRYKPD---------GPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPE--NGRVLVDGhdlaLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 QPAHFKCCSGYVVQDDVVMGTlTVRENLqfsAALRLPTTMKNHEKNERI---NTIIKEL--GLEKVadskVGTQFIrGIS 186
Cdd:cd03252 70 DPAWLRRQVGVVLQENVLFNR-SIRDNI---ALADPGMSMERVIEAAKLagaHDFISELpeGYDTI----VGEQGA-GLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 187 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFH 266
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQ 217
|
250
....*....|....*.
gi 1720417991 267 GPAQkalEYFASAGYH 282
Cdd:cd03252 218 GSHD---ELLAENGLY 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
54-242 |
1.69e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV-EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP----QPAHFKCcsGYV 123
Cdd:COG3839 9 VSKSYgGVEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIA------GLedptSGEILIGGRDvtdlPPKDRNI--AMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 124 VQDDVVMGTLTVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDP 203
Cdd:COG3839 81 FQSYALYPHMTVYENIAF--PLKL-RKVPKAEIDRRVREAAELLGLEDLLDRKPKQ-----LSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720417991 204 SILFLDEPTTGLDsstanAVL-----LLLKRMSKQ-GRTIIFSIH 242
Cdd:COG3839 153 KVFLLDEPLSNLD-----AKLrvemrAEIKRLHRRlGTTTIYVTH 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
59-243 |
1.85e-18 |
|
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: 84.50 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCS------GYVVQDDVVMG 131
Cdd:cd03262 12 DFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDGLKLTDDKKNINelrqkvGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFsaALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:cd03262 90 HLTVLENITL--APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
59-271 |
2.85e-18 |
|
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: 84.15 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLL-------DVLAARKDpkglSGDVLINGAPQpahfkccsgYVVQDDVV- 129
Cdd:cd03260 12 DKHALKDISLDIPKGeITALIGPSGCGKSTLLrllnrlnDLIPGAPD----EGEVLLDGKDI---------YDLDVDVLe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 ----MGTL---------TVRENLqfSAALRLPTTMKNHEKNERINTIIKELGL-EKVADSKVGtqfiRGISGGERKRTSI 195
Cdd:cd03260 79 lrrrVGMVfqkpnpfpgSIYDNV--AYGLRLHGIKLKEELDERVEEALRKAALwDEVKDRLHA----LGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 196 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQK 271
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ-QAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
36-245 |
4.26e-18 |
|
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: 84.02 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKSGFLVrktvekeILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGA 110
Cdd:COG4181 8 IIELRGLTKTVGTGAGELT-------ILKGISLEVEAGeSVAIVGASGSGKSTLLGLLA------GLdrptSGTVRLAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 111 P------------QPAHFkccsGYVVQDDVVMGTLTVRENLQfsaalrLPTTMKNH-EKNERINTIIKELGLEKVADskv 177
Cdd:COG4181 75 DlfaldedararlRARHV----GFVFQSFQLLPTLTALENVM------LPLELAGRrDARARARALLERVGLGHRLD--- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 178 gtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPR 245
Cdd:COG4181 142 --HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
59-242 |
4.70e-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: 82.47 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCS------GYVVQ--DDVV 129
Cdd:TIGR01166 4 GPEVLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQ--SGAVLIDGEPLDYSRKGLLerrqrvGLVFQdpDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTlTVRENLQFSaalrlPTTMKNHEknERINTIIKElGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLD 209
Cdd:TIGR01166 82 FAA-DVDQDVAFG-----PLNLGLSE--AEVERRVRE-ALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
63-244 |
6.52e-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: 87.34 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGlsGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTlTVRE 137
Cdd:TIGR02857 338 LRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTE--GSIAVNGVPladaDADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 NLQFSAALRLPTTMKNHEKNERINTIIKELGLEkvADSKVGTQFiRGISGGERKRTSIGMELITDPSILFLDEPTTGLDS 217
Cdd:TIGR02857 415 NIRLARPDASDAEIREALERAGLDEFVAALPQG--LDTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180
....*....|....*....|....*..
gi 1720417991 218 STANAVLLLLKRMSkQGRTIIFSIHQP 244
Cdd:TIGR02857 492 ETEAEVLEALRALA-QGRTVLLVTHRL 517
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
36-273 |
7.07e-18 |
|
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: 83.60 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITyrvkvksgflVRKTvEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARkdpkglsgdvlingapqpa 114
Cdd:COG1119 3 LLELRNVT----------VRRG-GKTILDDISWTVKPGEHwAILGPNGAGKSTLLSLITGD------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 HFKCcSGYVVQddvVMGTLTVRENLQ--------FSAAL--RLPTTMK-------------------NHEKNERINTIIK 165
Cdd:COG1119 53 LPPT-YGNDVR---LFGERRGGEDVWelrkriglVSPALqlRFPRDETvldvvlsgffdsiglyrepTDEQRERARELLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 166 ELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQG-RTIIFSIHQP 244
Cdd:COG1119 129 LLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHV 203
|
250 260
....*....|....*....|....*....
gi 1720417991 245 RYsIFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:COG1119 204 EE-IPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
77-267 |
7.25e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCS---GYVVQDDVVMGTLTVRENLQ-FSAALRlpttMK 152
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPARARLARariGVVPQFDNLDLEFTVRENLLvFGRYFG----MS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 153 NHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 232
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA 220
|
170 180 190
....*....|....*....|....*....|....*
gi 1720417991 233 QGRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHG 267
Cdd:PRK13536 221 RGKTILLTTHFMEEAE-RLCDRLCVLEAGRKIAEG 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
60-216 |
8.53e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.53 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPK-GLSGDVLING---APQPAHFKCCsGYVVQDDVVMGTLT 134
Cdd:COG4136 14 RPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGrrlTALPAEQRRI-GILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFSaalrLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:COG4136 93 VGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 1720417991 215 LD 216
Cdd:COG4136 164 LD 165
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
54-242 |
1.14e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV-EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPA---HFKCCSGYVVQDDV 128
Cdd:PRK13537 13 VEKRYgDKLVVDGLSFHVQRGeCFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPVPSrarHARQRVGVVPQFDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 129 VMGTLTVRENLQ-FSAALRLPTtmknHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILF 207
Cdd:PRK13537 91 LDPDFTVRENLLvFGRYFGLSA----AAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
76-268 |
2.12e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 83.23 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSL----LDVLAArkDpkglSGDVLINGAP----QPAHFkccsGYvvqddvvM----G---TLTVRENLQ 140
Cdd:COG4152 31 GLLGPNGAGKTTTiriiLGILAP--D----SGEVLWDGEPldpeDRRRI----GY-------LpeerGlypKMKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 141 FSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTA 220
Cdd:COG4152 94 YLARLK---GLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720417991 221 NAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGP 268
Cdd:COG4152 166 ELLKDVIRELAAKGTTVIFSSHQME-LVEELCDRIVIINKGRKVLSGS 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
76-239 |
3.13e-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: 83.61 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLING---APQPAH---FkccsGYVVQDDVVMGTLTVRENLQFSaaL 145
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIA------GFetpdSGRILLDGrdvTGLPPEkrnV----GMVFQDYALFPHLTVAENVAFG--L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 146 RLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 225
Cdd:COG3842 103 RM-RGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMRE 176
|
170
....*....|....*
gi 1720417991 226 LLKRMSKQ-GRTIIF 239
Cdd:COG3842 177 ELRRLQRElGITFIY 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
59-242 |
3.27e-17 |
|
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: 80.76 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCcsGYVVQDDVVMGTL 133
Cdd:cd03301 12 NVTALDDLNLDIADGeFVVLLGPSGCGKTTTLRMIAGLEEPT--SGRIYIGGRDvtdlPPKDRDI--AMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTT 213
Cdd:cd03301 88 TVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190
....*....|....*....|....*....|
gi 1720417991 214 GLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 242
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
61-268 |
3.35e-17 |
|
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: 81.09 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING-------APQPAHFKCCSGYVVQDDVVMGT 132
Cdd:cd03258 19 TALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPT--SGSVLVDGtdltllsGKELRKARRRIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 LTVRENLQFsaALRLPTTMKNhEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDEPT 212
Cdd:cd03258 97 RTVFENVAL--PLEIAGVPKA-EIEERVLELLELVGLEDKADA-----YPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 213 TGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQpRYSIFKLFDSLTLLASGKLVFHGP 268
Cdd:cd03258 169 SALDPETTQSILALLRDINRElGLTIVLITHE-MEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
77-244 |
3.81e-17 |
|
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: 80.23 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGapQPAHFKCCSG-----YVVQDDVVMGTLTVRENLQFSAALrlpttm 151
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPP--LAGRVLLNG--GPLDFQRDSIargllYLGHAPGIKTTLSVLENLRFWHAD------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 152 knhEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMS 231
Cdd:cd03231 101 ---HSDEQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGVARFAEAMA 169
|
170
....*....|....*.
gi 1720417991 232 ---KQGRTIIFSIHQP 244
Cdd:cd03231 170 ghcARGGMVVLTTHQD 185
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
56-242 |
5.70e-17 |
|
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: 80.74 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 56 KTVEKE-----ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHfKCCSGYVVQD 126
Cdd:cd03300 4 ENVSKFyggfvALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAGFETPT--SGEILLDGkdiTNLPPH-KRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 DVVMGTLTVRENLQFsaALRLPTTMKNhEKNERINTIIKELGLEKVADSKvgtqfIRGISGGERKRTSIGMELITDPSIL 206
Cdd:cd03300 81 YALFPHLTVFENIAF--GLRLKKLPKA-EIKERVAEALDLVQLEGYANRK-----PSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720417991 207 FLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 242
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
61-267 |
6.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKC--CSGYVVQ--DDVVMG 131
Cdd:PRK13639 16 EALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPT--SGEVLIKGEPikydKKSLLEVrkTVGIVFQnpDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TlTVRENLQFSaalrlPTTMK--NHEKNERINTIIKELGLEKVaDSKVGTQFirgiSGGERKRTSIGMELITDPSILFLD 209
Cdd:PRK13639 94 P-TVEEDVAFG-----PLNLGlsKEEVEKRVKEALKAVGMEGF-ENKPPHHL----SGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFHG 267
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPVYA-----DKVYVMSDGKIIKEG 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
59-267 |
7.18e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTL 133
Cdd:PRK11231 14 TKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQ--SGTVFLGDKPismlSSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQF--SAALRLPTTMkNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:PRK11231 92 TVRELVAYgrSPWLSLWGRL-SAEDNARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFHG 267
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGKTVVTVLHDlnqaSRYC-----DHLVVLANGHVMAQG 220
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
63-238 |
7.27e-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: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA-------PQPAHFKCCSGYvvQDDVVMGTLT 134
Cdd:TIGR03411 18 LNDLSLYVDPGeLRVIIGPNGAGKTTMMDVITGKTRPD--EGSVLFGGTdltglpeHQIARAGIGRKF--QKPTVFENLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFSAAL--RLPTTM---KNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLD 209
Cdd:TIGR03411 94 VFENLELALPRdkSVFASLffrLSAEEKDRIEEVLETIGLADEADRLAGL-----LSHGQKQWLEIGMLLMQDPKLLLLD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 210 EPTTGLD----SSTANavllLLKRMSKqGRTII 238
Cdd:TIGR03411 169 EPVAGMTdeetEKTAE----LLKSLAG-KHSVV 196
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
59-270 |
1.29e-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: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAA--RKDpkglSGDVLINGAP---QPAHFKCCSG--YVVQDDVVM 130
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGeIVGLLGPNGAGKTTSFYMIVGlvRPD----AGKILIDGQDithLPMHERARLGigYLPQEASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENLQfsAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDE 210
Cdd:TIGR04406 89 RKLTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPA 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
61-267 |
1.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQP------AHFKCCSGYVVQD-DVVMGT 132
Cdd:PRK13636 20 HALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPS--SGRILFDGKPIDysrkglMKLRESVGMVFQDpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 LTVRENLQFSAA-LRLPttmkNHEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:PRK13636 98 ASVYQDVSFGAVnLKLP----EDEVRKRVDNALKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQprYSIFKLF-DSLTLLASGKLVFHG 267
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKElGLTIIIATHD--IDIVPLYcDNVFVMKEGRVILQG 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
73-268 |
9.94e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 73 GLNAILGPTGGGKSSLLDVLAARKDP-KG---LSGDVL------INGAPQPAHFkccsGYVVQDDVVMGTLTVRENLQFS 142
Cdd:PRK11144 25 GITAIFGRSGAGKTSLINAISGLTRPqKGrivLNGRVLfdaekgICLPPEKRRI----GYVFQDARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 143 aalrlpttMKnHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 222
Cdd:PRK11144 101 --------MA-KSMVAQFDKIVALLGIEPLLD-----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720417991 223 VLLLLKRMSKQGRT-IIFSIHqpryS---IFKLFDSLTLLASGKLVFHGP 268
Cdd:PRK11144 167 LLPYLERLAREINIpILYVSH----SldeILRLADRVVVLEQGKVKAFGP 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-274 |
1.28e-15 |
|
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: 80.15 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 32 AEGDVlSFHHITYRVKVKsgflvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA 110
Cdd:TIGR02203 327 ARGDV-EFRNVTFRYPGR---------DRPALDSISLVIEPGeTVALVGRSGSGKSTLVNLIPRFYEPD--SGQILLDGH 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 111 P-QPAHFKCCSGYV--VQDDVVMGTLTVRENLQFSAALRLPttmknhekNERINTIIKELGLEKVAD-SKVGTQFIRG-- 184
Cdd:TIGR02203 395 DlADYTLASLRRQValVSQDVVLFNDTIANNIAYGRTEQAD--------RAEIERALAAAYAQDFVDkLPLGLDTPIGen 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 185 ---ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHqpRYSIFKLFDSLTLLASG 261
Cdd:TIGR02203 467 gvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAH--RLSTIEKADRIVVMDDG 543
|
250
....*....|...
gi 1720417991 262 KLVFHGPAQKALE 274
Cdd:TIGR02203 544 RIVERGTHNELLA 556
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
121-216 |
1.34e-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: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 121 GYVVQDDVVMGTLTVRENLQfsAALRLpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELI 200
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNIL--AVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAYS-----LSGGERRRVEIARALA 152
|
90
....*....|....*.
gi 1720417991 201 TDPSILFLDEPTTGLD 216
Cdd:COG1137 153 TNPKFILLDEPFAGVD 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
60-261 |
1.51e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP--QPAHFKccsGYVVQDDVVMGTLTVR 136
Cdd:PRK11248 14 KPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPveGPGAER---GVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVadskvGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK11248 89 DNVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGA-----EKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720417991 217 SSTANAV-LLLLKRMSKQGRTIIFSIHQPRYSIFkLFDSLTLLASG 261
Cdd:PRK11248 161 AFTREQMqTLLLKLWQETGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
54-230 |
1.79e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV------EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHfKCCS--G 121
Cdd:COG1101 7 LSKTFnpgtvnEKRALDGLNLTIEEGdFVTVIGSNGAGKSTLLNAIAGSLPPD--SGSILIDGkdvTKLPEY-KRAKyiG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 122 YVVQDdVVMGT---LTVRENLQFSAA------LRLPTTMKNHEK-NERINTIikELGLEKVADSKVGTqfirgISGGERK 191
Cdd:COG1101 84 RVFQD-PMMGTapsMTIEENLALAYRrgkrrgLRRGLTKKRRELfRELLATL--GLGLENRLDTKVGL-----LSGGQRQ 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720417991 192 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 230
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
43-268 |
2.16e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 43 TYRVKVK--------SGFLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLING 109
Cdd:COG4586 10 TYRVYEKepglkgalKGLFRREYREVEAVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLT------GIlvptSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 110 -APqpahFKCCSGYVVQDDVVMGT-------LTVRENLQFSAAL-RLPTTmknhEKNERINTIIKELGLEKVADskvgtQ 180
Cdd:COG4586 84 yVP----FKRRKEFARRIGVVFGQrsqlwwdLPAIDSFRLLKAIyRIPDA----EYKKRLDELVELLDLGELLD-----T 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 181 FIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHqprYS--IFKLFDSLTL 257
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSH---DMddIEALCDRVIV 227
|
250
....*....|.
gi 1720417991 258 LASGKLVFHGP 268
Cdd:COG4586 228 IDHGRIIYDGS 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
76-243 |
2.39e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.77 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQ--DDVVMGTlTVRENLQFSaalrlPT 149
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPT--SGSVLIRGEPitkeNIREVRKFVGLVFQnpDDQIFSP-TVEQDIAFG-----PI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 150 TMKNHEKN--ERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 227
Cdd:PRK13652 106 NLGLDEETvaHRVSSALHMLGLEELRD-----RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFL 180
|
170
....*....|....*..
gi 1720417991 228 KRMSKQ-GRTIIFSIHQ 243
Cdd:PRK13652 181 NDLPETyGMTVIFSTHQ 197
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
59-267 |
2.48e-15 |
|
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: 75.73 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGApQPAHFKCCS-----GYVVQDdVVMGT 132
Cdd:cd03251 14 GPPVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVD--SGRILIDGH-DVRDYTLASlrrqiGLVSQD-VFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 LTVRENLQFSaalRLPTTMKNHEKNERI---NTIIKELglEKVADSKVGTqfiRGI--SGGERKRTSIGMELITDPSILF 207
Cdd:cd03251 90 DTVAENIAYG---RPGATREEVEEAARAanaHEFIMEL--PEGYDTVIGE---RGVklSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMK-NRTTFVIAH--RLSTIENADRIVVLEDGKIVERG 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
63-238 |
2.52e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.31 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA-------PQPAH------FkccsgyvvQDDV 128
Cdd:COG4674 26 LNDLSLYVDPGeLRVIIGPNGAGKTTLMDVITGKTRPD--SGSVLFGGTdltgldeHEIARlgigrkF--------QKPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 129 VMGTLTVRENLQFSAA-----LRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDP 203
Cdd:COG4674 96 VFEELTVFENLELALKgdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGL-----LSHGQKQWLEIGMLLAQDP 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720417991 204 SILFLDEPTTGL-DSSTANAVlLLLKRMSKQgRTII 238
Cdd:COG4674 171 KLLLLDEPVAGMtDAETERTA-ELLKSLAGK-HSVV 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
58-242 |
2.75e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.62 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 58 VEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPahfKCCS-----------GYVVQ 125
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPT--SGDVIFNGQPMS---KLSSaakaelrnqklGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 126 DDVVMGTLTVRENLqfsAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSI 205
Cdd:PRK11629 95 FHHLLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSE-----LSGGERQRVAIARALVNNPRL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720417991 206 LFLDEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 242
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTH 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
60-273 |
3.04e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.92 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAH-------------------Fkcc 119
Cdd:COG4559 14 RTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPS--SGEVRLNGRPLAAWspwelarrravlpqhsslaF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 120 sGYVVQDDVVMGtltvrenlqfsaalRLPTTMKNHEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMEL 199
Cdd:COG4559 89 -PFTVEEVVALG--------------RAPHGSSAAQDRQIVREALALVGLAHLAG-----RSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 200 I-------TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP----RYSifklfDSLTLLASGKLVFHGP 268
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLnlaaQYA-----DRILLLHQGRLVAQGT 223
|
....*
gi 1720417991 269 AQKAL 273
Cdd:COG4559 224 PEEVL 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
59-270 |
4.19e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDvLAARKDPKGlSGDVLING-----------APQPAHFKccsgyvvQD 126
Cdd:COG4604 13 GKVVLDDVSlTIPKGGITALIGPNGAGKSTLLS-MISRLLPPD-SGEVLVDGldvattpsrelAKRLAILR-------QE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 DVVMGTLTVRENLQFSaalRLP-----TTMKNHEKnerINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELIT 201
Cdd:COG4604 84 NHINSRLTVRELVAFG---RFPyskgrLTAEDREI---IDEAIAYLDLEDLAD-----RYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFHGPAQ 270
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDinfaSCYA-----DHIVAMKDGRVVAQGTPE 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
59-274 |
4.22e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGA-------------------PQPAHFKc 118
Cdd:COG0396 12 GKEILKGVNLTIKPGeVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEdilelspderaragiflafQYPVEIP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 119 csgyvvqddvvmGtLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELGL-EKVADSKVGTQFirgiSGGERKRTSIGM 197
Cdd:COG0396 91 ------------G-VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEGF----SGGEKKRNEILQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 198 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysifkLFDSLT-----LLASGKLVFHGPAQKA 272
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQR-----ILDYIKpdfvhVLVDGRIVKSGGKELA 228
|
..
gi 1720417991 273 LE 274
Cdd:COG0396 229 LE 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
76-269 |
5.50e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTLTVREnlqFSAALRLPTtm 151
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPleswSSKAFARKVAYLPQQLPAAEGMTVRE---LVAIGRYPW-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 152 knH--------EKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:PRK10575 114 --HgalgrfgaADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 224 LLLLKRMSKQ-GRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFHGPA 269
Cdd:PRK10575 187 LALVHRLSQErGLTVIAVLHDinmaARYC-----DYLVALRGGEMIAQGTP 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
76-267 |
5.77e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGApQPAHFKCCS-----GYVVQDDVVMGTLTVREnlqFSAALRLPT- 149
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDGE-HIQHYASKEvarriGLLAQNATTPGDITVQE---LVARGRYPHq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 150 ---TMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 226
Cdd:PRK10253 111 plfTRWRKEDEEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720417991 227 LKRMSK-QGRTIIFSIHQ----PRYSIfklfdSLTLLASGKLVFHG 267
Cdd:PRK10253 186 LSELNReKGYTLAAVLHDlnqaCRYAS-----HLIALREGKIVAQG 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
76-270 |
6.20e-15 |
|
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: 74.63 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP---QPAHFKCCSG--YVVQDDVVMGTLTVRENLQFSAALR 146
Cdd:COG0410 33 ALLGRNGAGKTTLLKAIS------GLlpprSGSIRFDGEDitgLPPHRIARLGigYVPEGRRIFPSLTVEENLLLGAYAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 147 lPTTMKNHEKNERINT---IIKELglekvADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:COG0410 107 -RDRAEVRADLERVYElfpRLKER-----RRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720417991 224 LLLLKRMSKQGRTIIFS---IHQprysIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:COG0410 176 FEIIRRLNREGVTILLVeqnARF----ALEIADRAYVLERGRIVLEGTAA 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
76-245 |
7.46e-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: 73.55 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP---QPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMK 152
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGLLRP--DSGEVRWNGTPlaeQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 153 NHEKNERIntiikelGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMS- 231
Cdd:TIGR01189 108 IEDALAAV-------GLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALD---KAGVALLAGLLRa 172
|
170
....*....|....*.
gi 1720417991 232 --KQGRTIIFSIHQPR 245
Cdd:TIGR01189 173 hlARGGIVLLTTHQDL 188
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
59-238 |
2.16e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQP--------AHFkccsGYVVQDdVV 129
Cdd:COG1132 352 DRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPT--SGRILIDGVDIRdltleslrRQI----GVVPQD-TF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTLTVRENLQFS----------AALRLPttmknhekneRINTIIKEL--GLekvaDSKVGTqfiRGI--SGGERKRTSI 195
Cdd:COG1132 425 LFSGTIRENIRYGrpdatdeeveEAAKAA----------QAHEFIEALpdGY----DTVVGE---RGVnlSGGQRQRIAI 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720417991 196 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTII 238
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTI 529
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
63-293 |
3.40e-14 |
|
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: 72.76 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING------APQPAHFkccsGYVVQDDVVMGTLTV 135
Cdd:cd03296 18 LDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGedatdvPVQERNV----GFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAALRLPTTMKNH-EKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:cd03296 92 FDNVAFGLRVKPRSERPPEaEIRAKVHELLKLVQLDWLADR-----YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 215 LDSSTANAVLLLLKRM-SKQGRTIIFSIHQPRYSIfKLFDSLTLLASGKlvfhgpaqkaLEYFASAGyhcEPYNNPADFF 293
Cdd:cd03296 167 LDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEAL-EVADRVVVMNKGR----------IEQVGTPD---EVYDHPASPF 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
76-242 |
4.72e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 74.03 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQPAHFKCCS---GYVVQDDVVMGTLTVRENLQFSAALRLP 148
Cdd:COG1118 32 ALLGPSGSGKTTLLRIIA------GLetpdSGRIVLNGRDLFTNLPPRErrvGFVFQHYALFPHMTVAENIAFGLRVRPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 149 TtmkNHEKNERINTIIKELGLEKVADSKVgTQfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLK 228
Cdd:COG1118 106 S---KAEIRARVEELLELVQLEGLADRYP-SQ----LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLR 177
|
170
....*....|....*
gi 1720417991 229 RM-SKQGRTIIFSIH 242
Cdd:COG1118 178 RLhDELGGTTVFVTH 192
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
63-264 |
6.59e-14 |
|
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: 71.95 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTLTVRE 137
Cdd:cd03295 17 VNNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEPT--SGEIFIDGEDireqDPVELRRKIGYVIQQIGLFPHMTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 NLqfsaALrLPTTMK--NHEKNERINTIIKELGLEkvaDSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:cd03295 95 NI----AL-VPKLLKwpKEKIRERADELLALVGLD---PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720417991 216 DSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSiFKLFDSLTLLASGKLV 264
Cdd:cd03295 167 DPITRDQLQEEFKRLQQElGKTIVFVTHDIDEA-FRLADRIAIMKNGEIV 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
61-243 |
7.00e-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: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA----PQPAHFKCCS------GYVVQDDVV 129
Cdd:COG4161 16 QALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPD--SGQLNIAGHqfdfSQKPSEKAIRllrqkvGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTLTVRENLqFSAALRLpTTMKNHEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLD 209
Cdd:COG4161 94 WPHLTVMENL-IEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADR-----FPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
59-267 |
8.24e-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: 71.42 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGTl 133
Cdd:cd03249 15 DVPILKGLSLTIPPGKTvALVGSSGCGKSTVVSLLERFYDP--TSGEILLDGVDirdlNLRWLRSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSaalRLPTTMKNHEKNER---INTIIKEL--GLEKVADSKvGTQfirgISGGERKRTSIGMELITDPSILFL 208
Cdd:cd03249 92 TIAENIRYG---KPDATDEEVEEAAKkanIHDFIMSLpdGYDTLVGER-GSQ----LSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK-GRTTIVIAH--RLSTIRNADLIAVLQNGQVVEQG 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
36-264 |
9.13e-14 |
|
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: 71.76 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKvkSGFLVRKTVEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP--- 111
Cdd:TIGR02769 2 LLEVRDVTHTYR--TGGLFGAKQRAPVLTNVSLSIEEGETvGLLGRSGCGKSTLARLLLGLEKPA--QGTVSFRGQDlyq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 ----QPAHFKCCSGYVVQD--DVVMGTLTVRENLqfSAALRLPTTMKNHEKNERINTIIKELGLekvaDSKVGTQFIRGI 185
Cdd:TIGR02769 78 ldrkQRRAFRRDVQLVFQDspSAVNPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGL----RSEDADKLPRQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKLV 264
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLR-LVQSFCQRVAVMDKGQIV 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
59-275 |
9.79e-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: 70.25 E-value: 9.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGapqpahfkccsgyvvqDDVVMGTLTVRE 137
Cdd:cd03217 12 GKEILKGVNLTIKKGeVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG----------------EDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 NLQFSAALRLPttmknheknERINTIikelgleKVADskvgtqFIR----GISGGERKRTSIGMELITDPSILFLDEPTT 213
Cdd:cd03217 76 RLGIFLAFQYP---------PEIPGV-------KNAD------FLRyvneGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 214 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysIFKLF--DSLTLLASGKLVFHGPAQKALEY 275
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHYQR--LLDYIkpDRVHVLYDGRIVKSGDKELALEI 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
61-268 |
1.06e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQ----PAHFKCCSGYVV-QDDVVMGTLT 134
Cdd:PRK15439 25 EVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCarltPAKAHQLGIYLVpQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFsaalRLPTTMKNHEKNERIntiIKELGLEKVADSKVGTQFIrgisgGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:PRK15439 103 VKENILF----GLPKRQASMQKMKQL---LAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 215 LDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGP 268
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGK 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
76-279 |
1.13e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQ----PAH------FkccsgyvvQDDVVMGTLTVREN--LQFSA 143
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGQDHtttpPSRrpvsmlF--------QENNLFSHLTVAQNigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 144 ALRLpttmkNHEKNERINTIIKELGLEKVADsKVGTQfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:PRK10771 99 GLKL-----NAAQREKLHAIARQMGIEDLLA-RLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 224 LLLLKRMSKQGR-TIIFSIHQ--------PRysifklfdSLtLLASGKLVFHGPAQKALEYFASA 279
Cdd:PRK10771 169 LTLVSQVCQERQlTLLMVSHSledaariaPR--------SL-VVADGRIAWDGPTDELLSGKASA 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
61-244 |
1.97e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLA------------ARKDPKGLSGDVLinGAPQPAHFkccsGYVVQDD 127
Cdd:PRK10535 22 EVLKGISLDIYAGeMVAIVGASGSGKSTLMNILGcldkptsgtyrvAGQDVATLDADAL--AQLRREHF----GFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 128 VVMGTLTVRENLQFSAALrlpTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILF 207
Cdd:PRK10535 96 HLLSHLTAAQNVEVPAVY---AGLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 244
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
47-267 |
2.04e-13 |
|
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: 69.87 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 47 KVKSGFLVRKTVEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQP-----AHFkccs 120
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERiGLIGRNGAGKSTLLRLLAGIYPPD--SGTVTVRGRVSSllglgGGF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 121 gyvvqddvvMGTLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELI 200
Cdd:cd03220 96 ---------NPELTGRENIYLNGRLL---GLSRKEIDEKIDEIIEFSELGDFIDLPVKT-----YSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 201 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS-SIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
63-330 |
2.36e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA--PQPAH---FKCCSGYVVQDDVVMGTLTVR 136
Cdd:PRK09700 21 LKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPT--KGTITINNInyNKLDHklaAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSaalRLPT-------TMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLD 209
Cdd:PRK09700 99 ENLYIG---RHLTkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQkaleyfasagyhcepynnp 289
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDGSSVCSGMVS------------------- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720417991 290 adfflDVINGDSSAVMLNREEQDN-EANKTEEPSKGEKPVIE 330
Cdd:PRK09700 231 -----DVSNDDIVRLMVGRELQNRfNAMKENVSNLAHETVFE 267
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
60-273 |
2.86e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA-----------------PQPAH----FK 117
Cdd:PRK13548 15 RTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGRpladwspaelarrravlPQHSSlsfpFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 118 ccsgyvVQDDVVMGtltvrenlqfsaalRLPTTMKNHEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGM 197
Cdd:PRK13548 93 ------VEEVVAMG--------------RAPHGLSRAEDDALVAAALAQVDLAHLAGR-----DYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 198 ELI------TDPSILFLDEPTTGLDSSTANAVLLLLKRM-SKQGRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFH 266
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDlnlaARYA-----DRIVLLHQGRLVAD 222
|
....*..
gi 1720417991 267 GPAQKAL 273
Cdd:PRK13548 223 GTPAEVL 229
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
59-274 |
4.06e-13 |
|
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: 69.60 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGapqpahfkccsgyvvQDdvvMGTLTVRE 137
Cdd:TIGR01978 12 DKEILKGVNLTVKKGeIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKG---------------QD---LLELEPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 N------LQFSAALRLP--------TTMKNHEKNERINTIIKELGLEKVADSKVGT-----QFIR-----GISGGERKRT 193
Cdd:TIGR01978 74 RaraglfLAFQYPEEIPgvsnleflRSALNARRSARGEEPLDLLDFEKLLKEKLALldmdeEFLNrsvneGFSGGEKKRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 194 SIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysIFKLF--DSLTLLASGKLVFHGPAQK 271
Cdd:TIGR01978 154 EILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR--LLNYIkpDYVHVLLDGRIVKSGDVEL 231
|
...
gi 1720417991 272 ALE 274
Cdd:TIGR01978 232 AKE 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
55-262 |
4.59e-13 |
|
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: 68.65 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 55 RKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGApqpahfkccSGYVVQDDVVMGTl 133
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGeLVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPGS---------IAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSAALRlpttmknhekNERINTIIK----ELGLEKVAD---SKVGtqfIRGI--SGGERKRTSIGMELITDPS 204
Cdd:cd03250 81 TIRENILFGKPFD----------EERYEKVIKacalEPDLEILPDgdlTEIG---EKGInlSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 205 ILFLDEPTTGLDSSTANAVL--LLLKRMsKQGRTIIFSIHQPRYsiFKLFDSLTLLASGK 262
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQLQL--LPHADQIVVLDNGR 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
53-273 |
6.55e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 53 LVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLS---GDVLINGA----PQPA---HFKCCSG 121
Cdd:PRK11264 9 LVKKFHGQTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvGDITIDTArslsQQKGlirQLRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 122 YVVQDDVVMGTLTVRENLqfsaaLRLPTTMKNHEKNERInTIIKELgLEKVADSKVGTQFIRGISGGERKRTSIGMELIT 201
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENI-----IEGPVIVKGEPKEEAT-ARAREL-LAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGKLVFHGPAqKAL 273
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA-RDVADRAIFMDQGRIVEQGPA-KAL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
79-242 |
6.59e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 79 GPTGGGKSSLLDVLAARKDPKglSGDVLI-----NGAPqPAhfKCCSGYVVQDDVVMGTLTVRENLQFsaALRLPTTMKN 153
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDIT--SGDLFIgekrmNDVP-PA--ERGVGMVFQSYALYPHLSVAENMSF--GLKLAGAKKE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 154 hEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 233
Cdd:PRK11000 109 -EINQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
|
170
....*....|
gi 1720417991 234 -GRTIIFSIH 242
Cdd:PRK11000 183 lGRTMIYVTH 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
48-270 |
1.21e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 48 VKSGFLVRKTVEKEILSDINGIMKPGLN-AILGPTGGGKSS----LLDVLAARkdpkglsGDVLINGapQPAH------- 115
Cdd:PRK15134 287 IRKGILKRTVDHNVVVKNISFTLRPGETlGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDG--QPLHnlnrrql 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 116 --FKCCSGYVVQDDvvMGTLTVRENLQ--FSAALRL-PTTMKNHEKNERINTIIKELGLEKVADSKVGTQFirgiSGGER 190
Cdd:PRK15134 358 lpVRHRIQVVFQDP--NSSLNPRLNVLqiIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 191 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR-TIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPA 269
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHV-VRALCHQVIVLRQGEVVEQGDC 510
|
.
gi 1720417991 270 Q 270
Cdd:PRK15134 511 E 511
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
76-239 |
1.54e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQ----PA------------HFKccsgyVVQddvvmgTLTV 135
Cdd:COG3845 35 ALLGENGAGKSTLMKILY------GLyqpdSGEILIDGKPVrirsPRdaialgigmvhqHFM-----LVP------NLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180
....*....|....*....|....
gi 1720417991 216 DSSTANAVLLLLKRMSKQGRTIIF 239
Cdd:COG3845 173 TPQEADELFEILRRLAAEGKSIIF 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-236 |
1.59e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 33 EGDVlSFHHITYRVKVKSgflvrktvekEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP 111
Cdd:PRK13657 332 KGAV-EFDDVSFSYDNSR----------QGVEDVSFEAKPGQTvAIVGPTGAGKSTLINLLQRVFDPQ--SGRILIDGTD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 ----QPAHFKCCSGYVVQDDVVMGTlTVRENLQFS----------AALRLPTTMKNHEKNE-RINTIIKELGlekvadsk 176
Cdd:PRK13657 399 irtvTRASLRRNIAVVFQDAGLFNR-SIEDNIRVGrpdatdeemrAAAERAQAHDFIERKPdGYDTVVGERG-------- 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 177 vgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRT 236
Cdd:PRK13657 470 ------RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRT 522
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
59-267 |
1.60e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.52 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGlsGDVLINGAPQPaHFKCCS-----GYVVQDDVVMGT 132
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTG--GQVLLDGVPLV-QYDHHYlhrqvALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 lTVRENLQFSAALRLPTTMKNHEKNERINTIIKEL--GLEKVADSKvGTQfirgISGGERKRTSIGMELITDPSILFLDE 210
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEK-GSQ----LSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 211 PTTGLDsstANAVLLLLKRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:TIGR00958 644 ATSALD---AECEQLLQESRSRASRTVLLIAH--RLSTVERADQILVLKKGSVVEMG 695
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
61-243 |
2.00e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPGLNAIL-GPTGGGKSSLLDVLAARKDPKglSGDVLING-------APQPAHFKCCS---GYVVQDDVV 129
Cdd:PRK11124 16 QALFDITLDCPQGETLVLlGPSGAGKSSLLRVLNLLEMPR--SGTLNIAGnhfdfskTPSDKAIRELRrnvGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTLTVRENLqFSAALRLPTTMKNhEKNERINTIIKELGLEKVADskvgtQFIRGISGGERKRTSIGMELITDPSILFLD 209
Cdd:PRK11124 94 WPHLTVQQNL-IEAPCRVLGLSKD-QALARAEKLLERLRLKPYAD-----RFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
63-261 |
2.14e-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: 67.11 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING----APQPAHFkccsgYVVQDDVVMGTLTVRE 137
Cdd:TIGR01184 1 LKGVNLTIQQGeFISLIGHSGCGKSTLLNLISGLAQPT--SGGVILEGkqitEPGPDRM-----VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 NLQFSAALRLPTtMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDS 217
Cdd:TIGR01184 74 NIALAVDRVLPD-LSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720417991 218 ST-ANAVLLLLKRMSKQGRTIIFSIHQPRYSIFkLFDSLTLLASG 261
Cdd:TIGR01184 148 LTrGNLQEELMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
74-267 |
2.30e-12 |
|
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: 70.81 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 74 LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCS---GYVVQDDVVMGTLTVRENLQFSAALRlptT 150
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPT--SGTVLVGGKDIETNLDAVRqslGMCPQHNILFHHLTVAEHILFYAQLK---G 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 151 MKNHEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLKR 229
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWdLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720417991 230 MSkqGRTIIFSIHQPRYSIFkLFDSLTLLASGKLVFHG 267
Cdd:TIGR01257 1108 RS--GRTIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
46-276 |
2.60e-12 |
|
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: 69.45 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 46 VKVKSgfLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLIN----------GAPQPA 114
Cdd:TIGR03269 1 IEVKN--LTKKFDGKEVLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcgyvERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 HFKC--CSGYVVQDDVVMGTL--TVRENLQFSAALRLPTTMKNHEKNERINTIIK---ELG-------------LEKVAD 174
Cdd:TIGR03269 79 GEPCpvCGGTLEPEEVDFWNLsdKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEaleEIGyegkeavgravdlIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 175 SKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIFSIHQPRYsIFKLFD 253
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEV-IEDLSD 237
|
250 260
....*....|....*....|...
gi 1720417991 254 SLTLLASGKLVFHGPAQKALEYF 276
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
56-233 |
3.12e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 56 KTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDDVVM 130
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGeFKLITGPSGCGKSTLLKIVASLISPT--SGTLLFEGEDistlKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTlTVRENLQFSAALRlpttmKNHEKNERINTIIKELGLekvaDSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDE 210
Cdd:PRK10247 94 GD-TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFAL----PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180
....*....|....*....|...
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQ 233
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVRE 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
70-242 |
3.32e-12 |
|
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: 70.04 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 70 MKPG-LNAILGPTGGGKSSLLDVLAArkDPKGLSGDVLINGAP---QPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAAL 145
Cdd:TIGR01257 1962 VRPGeCFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSiltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 146 R-LPTtmknhEKNERI-NTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:TIGR01257 2040 RgVPA-----EEIEKVaNWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170
....*....|....*....
gi 1720417991 224 LLLLKRMSKQGRTIIFSIH 242
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSH 2128
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
62-263 |
4.14e-12 |
|
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: 66.34 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGlsGDVLINGAPQPAHFKCCSGYVV----QDDVVMGTlTVR 136
Cdd:cd03248 29 VLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQG--GQVLLDGKPISQYEHKYLHSKVslvgQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFsaALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfiRG--ISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:cd03248 106 DNIAY--GLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGE---KGsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720417991 215 LDSSTANAVLLLLkRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGKL 263
Cdd:cd03248 181 LDAESEQQVQQAL-YDWPERRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
77-273 |
4.62e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAarkdpkGL---SGDVLING-------APQPAHFKCcsgYVVQDDVVMGTLTVRENLqfsaALR 146
Cdd:PRK03695 27 LVGPNGAGKSTLLARMA------GLlpgSGSIQFAGqpleawsAAELARHRA---YLSQQQTPPFAMPVFQYL----TLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 147 LPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSI-GMELITDPSI------LFLDEPTTGLDSST 219
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRLaAVVLQVWPDInpagqlLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 220 ANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHT-LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
54-242 |
6.08e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTVE-KEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING------APQPAHFKCcsgyVVQ 125
Cdd:PRK09452 20 ISKSFDgKEVISNLDLTINNGeFLTLLGPSGCGKTTVLRLIAGFETPD--SGRIMLDGqdithvPAENRHVNT----VFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 126 DDVVMGTLTVRENLQFsaALRLPTTmKNHEKNERINTIIKELGLEKVADSKvgtqfIRGISGGERKRTSIGMELITDPSI 205
Cdd:PRK09452 94 SYALFPHMTVFENVAF--GLRMQKT-PAAEITPRVMEALRMVQLEEFAQRK-----PHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720417991 206 LFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 242
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
76-270 |
7.21e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAA--RKDpkglSGDVLINGapQPAHFKccS---------GYVVQDDVVMGTLTVRENLqfsaA 144
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvyQPD----SGEILLDG--EPVRFR--SprdaqaagiAIIHQELNLVPNLSVAENI----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 145 L-RLPTTMK--NHEK-NERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTA 220
Cdd:COG1129 102 LgREPRRGGliDWRAmRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDEPTASLTEREV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 221 NAVLLLLKRMSKQGRTIIFsIhqpryS-----IFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:COG1129 177 ERLFRIIRRLKAQGVAIIY-I-----ShrldeVFEIADRVTVLRDGRLVGTGPVA 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
54-219 |
7.89e-12 |
|
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: 68.04 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTVE--KEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpkGLSGDVLINGAPQPAhFKCcsGYVVQDDVVM 130
Cdd:TIGR03719 10 VSKVVPpkKEILKDISLSFFPGAKiGVLGLNGAGKSTLLRIMA------GVDKDFNGEARPQPG-IKV--GYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENL---------------QFSAALRLPTTMKNH--EKNERINTIIKELG-------LEKVADS---KVGTQFIR 183
Cdd:TIGR03719 81 PTKTVRENVeegvaeikdaldrfnEISAKYAEPDADFDKlaAEQAELQEIIDAADawdldsqLEIAMDAlrcPPWDADVT 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720417991 184 GISGGERKRTSIGMELITDPSILFLDEPTTGLDSST 219
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
242-299 |
9.48e-12 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 67.24 E-value: 9.48e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 242 HQPRYSIFKLFDSLTLLASGKL-VFHGPAQKALEYFASAGYHCEPYNNPADFFLDVING 299
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLtVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
76-271 |
1.35e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLdvlaarkdpKGLSGdvLINGAPQP-AHF--------------------KCCSGYVVQDDVVMGTLT 134
Cdd:PRK09984 34 ALLGPSGSGKSTLL---------RHLSG--LITGDKSAgSHIellgrtvqregrlardirksRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFSAALRLP---TTMK--NHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLD 209
Cdd:PRK09984 103 VLENVLIGALGSTPfwrTCFSwfTREQKQRALQALTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHGPAQK 271
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQ 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
63-273 |
1.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING--APQPAHF---KCCSGYVVQD-DVVMGTLTV 135
Cdd:PRK13644 18 LENINlVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGidTGDFSKLqgiRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAA-LRLPTTmknhEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:PRK13644 96 EEDLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKT-----LSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 215 LDSSTANAVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHN--LEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
53-273 |
1.98e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 53 LVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDV---LAARKDPKGLSGDVLINGAPQPAHFKCCSGYVVQDDV 128
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMvvgIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 129 VMGTLTVRENLQfsAALRLPTTMKNHEKNERINTIIKELGLEKVADSkVGtqfiRGISGGERKRTSIGMELITDPSILFL 208
Cdd:PRK10895 89 IFRRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDS-MG----QSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
77-296 |
2.15e-11 |
|
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: 64.97 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAhfkcCS------------GYVVQDDVVMGTLTVRENLQFSAA 144
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPT--SGKVLIDGQDIAA----MSrkelrelrrkkiSMVFQSFALLPHRTVLENVAFGLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 145 LRlptTMKNHEKNERINTIIKELGLEKVADSKvgtqfIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSstanavL 224
Cdd:cd03294 129 VQ---GVPRAEREERAAEALELVGLEGWEHKY-----PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP------L 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 225 -------LLLKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHGPAQKALeyfasagyhcepyNNPAD-----F 292
Cdd:cd03294 195 irremqdELLRLQAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTPEEIL-------------TNPANdyvreF 260
|
....
gi 1720417991 293 FLDV 296
Cdd:cd03294 261 FRGV 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-264 |
2.31e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITyrvKVKSGflVRKtvekeiLSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGapQPAH 115
Cdd:PRK11288 5 LSFDGIG---KTFPG--VKA------LDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDG--QEMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 116 FKCC-----SGYVV--QDDVVMGTLTVRENLQFSaalRLPTTM---KNHEKNERINTIIKELGLEKVADSKVGTqfirgI 185
Cdd:PRK11288 70 FASTtaalaAGVAIiyQELHLVPEMTVAENLYLG---QLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKY-----L 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLV 264
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDGRYV 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
59-274 |
2.54e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLING-------APQPAHFKCCSGYvvQDDVVM 130
Cdd:CHL00131 19 ENEILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGesildlePEERAHLGIFLAF--QYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTvreNLQFsaaLRLPTTMKNHEKN----------ERINTIIKELGLEKVadskvgtqFI-----RGISGGERKRTSI 195
Cdd:CHL00131 97 PGVS---NADF---LRLAYNSKRKFQGlpeldpleflEIINEKLKLVGMDPS--------FLsrnvnEGFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 196 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAKE 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
76-242 |
2.93e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGapQPAHFKCCS------GYVVQD-DVVMGTLTVRENLQFSaalrlP 148
Cdd:PRK13647 35 ALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMG--REVNAENEKwvrskvGLVFQDpDDQVFSSTVWDDVAFG-----P 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 149 TTM--KNHEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 226
Cdd:PRK13647 106 VNMglDKDEVERRVEEALKAVRMWDFRDKPP-----YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEI 180
|
170
....*....|....*.
gi 1720417991 227 LKRMSKQGRTIIFSIH 242
Cdd:PRK13647 181 LDRLHNQGKTVIVATH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
59-216 |
3.02e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGlN--AILGPTGGGKSSLLDVLAARKDPkgLSGDVLIngapqPAHFKCcsGYVVQDDVVMGTLTVR 136
Cdd:COG0488 10 GRPLLDDVSLSINPG-DriGLVGRNGAGKSTLLKILAGELEP--DSGEVSI-----PKGLRI--GYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLqFSAALRLPTTMKNHEKNE------------------------------RINTIIKELGL-EKVADSKVGTqfirgI 185
Cdd:COG0488 80 DTV-LDGDAELRALEAELEELEaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFpEEDLDRPVSE-----L 153
|
170 180 190
....*....|....*....|....*....|.
gi 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-274 |
3.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDIN-GIMKPGLNAILGPTGGGKSSLLD----VLAARKDPKgLSGDVLINGAP------QPAHFKCCSGYVVQDDVV 129
Cdd:PRK14267 18 HVIKGVDlKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEAR-VEGEVRLFGRNiyspdvDPIEVRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTLTVRENLqfSAALRLPTTMKNH-EKNERINTIIKELGL-EKVADSKvgTQFIRGISGGERKRTSIGMELITDPSILF 207
Cdd:PRK14267 97 FPHLTIYDNV--AIGVKLNGLVKSKkELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAA-RVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
62-279 |
3.28e-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: 66.31 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAP----QPAHFKCCSGYVVQDdvVmgT 132
Cdd:COG4618 347 ILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLV------GVwpptAGSVRLDGADlsqwDREELGRHIGYLPQD--V--E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 L---TVRENL-QFS---------AA---------LRLPttmknheknERINTIIKELGlekvadskvgtqfiRGISGGER 190
Cdd:COG4618 417 LfdgTIAENIaRFGdadpekvvaAAklagvhemiLRLP---------DGYDTRIGEGG--------------ARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 191 KRtsIGME--LITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHGP 268
Cdd:COG4618 474 QR--IGLAraLYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH--RPSLLAAVDKLLVLRDGRVQAFGP 549
|
250
....*....|.
gi 1720417991 269 AQKALEYFASA 279
Cdd:COG4618 550 RDEVLARLARP 560
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
35-276 |
4.46e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 35 DVLSFHHIT--YRV------KVKSGFLVRK---TVEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpkGL- 101
Cdd:COG1134 3 SMIEVENVSksYRLyhepsrSLKELLLRRRrtrREEFWALKDVSFEVERGESvGIIGRNGAGKSTLLKLIA------GIl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 102 ---SGDVLINGAPQP-----AHFkccsgyvvqddvvMGTLTVRENLQFSAALRlptTMKNHEKNERINTIIKELGLEKVA 173
Cdd:COG1134 77 eptSGRVEVNGRVSAllelgAGF-------------HPELTGRENIYLNGRLL---GLSRKEIDEKFDEIVEFAELGDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 174 DSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPT-TGlDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLF 252
Cdd:COG1134 141 DQPVKT-----YSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMG-AVRRLC 213
|
250 260
....*....|....*....|....
gi 1720417991 253 DSLTLLASGKLVFHGPAQKALEYF 276
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
76-268 |
5.37e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 64.33 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLdvlaaRkdpkglsgdvLINGAPQPAhfkccSGYVVQDDVVMGTL---------------------- 133
Cdd:COG1135 35 GIIGYSGAGKSTLI-----R----------CINLLERPT-----SGSVLVDGVDLTALserelraarrkigmifqhfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 ---TVRENLQFsaALRLpTTMKNHEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDE 210
Cdd:COG1135 95 ssrTVAENVAL--PLEI-AGVPKAEIRKRVAELLELVGLSDKADA-----YPSQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP---RysifKLFDSLTLLASGKLVFHGP 268
Cdd:COG1135 167 ATSALDPETTRSILDLLKDINRElGLTIVLITHEMdvvR----RICDRVAVLENGRIVEQGP 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
62-268 |
5.78e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLA----ARKDPKG--LSGDVLINGAP----QPAHFKCCSGYVVQDDVVM 130
Cdd:PRK13547 16 ILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAgdltGGGAPRGarVTGDVTLNGEPlaaiDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENLQFSaalRLPTTMKNHEKNERINTIIKElGLEKVADSKVGTQFIRGISGGERKRTSIGMEL---------IT 201
Cdd:PRK13547 96 FAFSAREIVLLG---RYPHARRAGALTHRDGEIAWQ-ALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI-HQP----RYSifklfDSLTLLASGKLVFHGP 268
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPnlaaRHA-----DRIAMLADGAIVAHGA 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
77-238 |
8.08e-11 |
|
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: 65.19 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDP-KG-LSGDVLINGAPQpahfkccsgYVVQDdvvmGTLTVRENLQFSAALRLPTTMKNH 154
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPdEGeVDEDLKISYKPQ---------YISPD----YDGTVEEFLRSANTDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 155 EknerintIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS-KQ 233
Cdd:COG1245 438 E-------IIKPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNR 505
|
....*
gi 1720417991 234 GRTII 238
Cdd:COG1245 506 GKTAM 510
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
62-273 |
9.61e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCSGYVV----QDDVVMGTLTVR 136
Cdd:PRK09536 18 VLDGVDLSVREGsLVGLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAGDDVEALSARAASRRVasvpQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSaalRLPTTMKNHEKNERINTIIKElGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK09536 96 QVVEMG---RTPHRSRFDTWTETDRAAVER-AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 217 SSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFHGPAQKAL 273
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDldlaARYC-----DELVLLADGRVRAAGPPADVL 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
59-238 |
2.30e-10 |
|
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: 63.69 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCSGYVVQDdVVMGTL 133
Cdd:COG5265 370 ERPILKGVSFEVPAGKTvAIVGPSGAGKSTLARLLFRFYDVT--SGRILIDGQDirdvTQASLRAAIGIVPQD-TVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFS----------AALRLPttmknhekneRINTIIKelGLEKVADSKVGTqfiRG--ISGGERKRTSIGMELIT 201
Cdd:COG5265 447 TIAYNIAYGrpdaseeeveAAARAA----------QIHDFIE--SLPDGYDTRVGE---RGlkLSGGEKQRVAIARTLLK 511
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTII 238
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVA-RGRTTL 547
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
132-239 |
2.39e-10 |
|
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: 62.38 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVREnlQFSAALRLPTTMKNHEKNERINTIIKELGL---EKVADSKVGtQFirgiSGGERKRTSIGMELITDPSILFL 208
Cdd:COG0444 102 VMTVGD--QIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPH-EL----SGGMRQRVMIARALALEPKLLIA 174
|
90 100 110
....*....|....*....|....*....|..
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 239
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLQRElGLAILF 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
37-288 |
2.41e-10 |
|
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: 63.61 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYrvkvKSGFlvrktvEKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP---- 111
Cdd:TIGR01193 474 IVINDVSY----SYGY------GSNILSDISlTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR--SGEILLNGFSlkdi 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 QPAHFKCCSGYVVQDDVVMgTLTVRENLQFSAalRLPTTMKNHEKNERINTIIKE-----LGLEKVADSKVGTqfirgIS 186
Cdd:TIGR01193 542 DRHTLRQFINYLPQEPYIF-SGSILENLLLGA--KENVSQDEIWAACEIAEIKDDienmpLGYQTELSEEGSS-----IS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 187 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMskQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFH 266
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQ 689
|
250 260
....*....|....*....|..
gi 1720417991 267 GPAQKALEYfasAGYHCEPYNN 288
Cdd:TIGR01193 690 GSHDELLDR---NGFYASLIHN 708
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
59-268 |
3.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING------APQPAHFKCCSGYVVQ-DDVVM 130
Cdd:PRK13637 19 EKKALDNVNIEIEDGeFVGLIGHTGSGKSTLIQHLNGLLKPT--SGKIIIDGvditdkKVKLSDIRKKVGLVFQyPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENLQFSaalrlPTTM--KNHEKNERINTIIKELGLEKvADSKVGTQFirGISGGERKRTSIGMELITDPSILFL 208
Cdd:PRK13637 97 FEETIEKDIAFG-----PINLglSEEEIENRVKRAMNIVGLDY-EDYKDKSPF--ELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGP 268
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME-DVAKLADRIIVMNKGKCELQGT 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
59-274 |
3.99e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAhfkccsgyvVQDDVVMGTLTVRE 137
Cdd:PRK10789 327 DHPALENVNFTLKPGqMLGICGPTGSGKSTLLSLIQRHFDVS--EGDIRFHDIPLTK---------LQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 NLQF--------SAALRLPT-TMKNHEKNERINTIIKE-LGLEKVADSKVGTqfiRGI--SGGERKRTSIGMELITDPSI 205
Cdd:PRK10789 396 QTPFlfsdtvanNIALGRPDaTQQEIEHVARLASVHDDiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 206 LFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAH--RLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
61-243 |
4.23e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGlsGDVLING--APQPAHFKCC----SGYVVQDDVVMGTL 133
Cdd:PRK09493 15 QVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITS--GDLIVDGlkVNDPKVDERLirqeAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSaalrlPTTMKNHEKNErINTIIKELgLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTT 213
Cdd:PRK09493 93 TALENVMFG-----PLRVRGASKEE-AEKQAREL-LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190
....*....|....*....|....*....|
gi 1720417991 214 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
184-267 |
5.00e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 184 GISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKL 263
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKI 254
|
....
gi 1720417991 264 VFHG 267
Cdd:PRK13631 255 LKTG 258
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-271 |
5.40e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKD--PKG-LSGDVLINGAP----QPAHFKCCSGYVVQDDVVMGT 132
Cdd:PRK14247 17 EVLDGVNLEIPDNtITALMGPSGSGKSTLLRVFNRLIElyPEArVSGEVYLDGQDifkmDVIELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 LTVRENLqfSAALRLPTTMKNH-EKNERINTIIKELGLEKVADSKVGTQFIRgISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:PRK14247 97 LSIFENV--ALGLKLNRLVKSKkELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 212 TTGLD-SSTANAVLLLLKRmsKQGRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHGPAQK 271
Cdd:PRK14247 174 TANLDpENTAKIESLFLEL--KKDMTIVLVTHFPQQAA-RISDYVAFLYKGQIVEWGPTRE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
76-264 |
6.78e-10 |
|
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: 58.21 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGapQPAHFkccsgyvvqddvvmgtLTVREnlqfsaALRLpttm 151
Cdd:cd03216 30 ALLGENGAGKSTLMKILS------GLykpdSGEILVDG--KEVSF----------------ASPRD------ARRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 152 knhekneRINTIikelglekvadskvgTQfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS 231
Cdd:cd03216 76 -------GIAMV---------------YQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR 129
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 232 KQGRTIIFSIHQPRySIFKLFDSLTLLASGKLV 264
Cdd:cd03216 130 AQGVAVIFISHRLD-EVFEIADRVTVLRDGRVV 161
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
76-242 |
8.52e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAHFKCCSGYVVQDDVVMGtLTVRENLQFSAALRL-------- 147
Cdd:PRK13651 37 AIIGQTGSGKTTFIEHLNALLLPD--TGTIEWIFKDEKNKKKTKEKEKVLEKLVIQ-KTRFKKIKKIKEIRRrvgvvfqf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 -----------------PTTM--KNHEKNERINTIIKELGLEKVADSKvgTQFirGISGGERKRTSIGMELITDPSILFL 208
Cdd:PRK13651 114 aeyqlfeqtiekdiifgPVSMgvSKEEAKKRAAKYIELVGLDESYLQR--SPF--ELSGGQKRRVALAGILAMEPDFLVF 189
|
170 180 190
....*....|....*....|....*....|....
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK13651 190 DEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
77-271 |
1.02e-09 |
|
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: 59.34 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDPKGlsGDVLINGA-----PQpahfkccsgYVVQDDvvmgTLTVRENLqfSAALRLPTTm 151
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDE--GDIEIELDtvsykPQ---------YIKADY----EGTVRDLL--SSITKDFYT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 152 KNHEKNErintIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS 231
Cdd:cd03237 92 HPYFKTE----IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720417991 232 KQGRTIIFSIHQPRYSIfklfdslTLLASGKLVFHGPAQK 271
Cdd:cd03237 163 ENNEKTAFVVEHDIIMI-------DYLADRLIVFEGEPSV 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
37-274 |
1.07e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 37 LSFHHITYRVKvkSGFLVRKTVEKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKGlsGDVLINGAP---- 111
Cdd:PRK10419 4 LNVSGLSHHYA--HGGLSGKHQHQTVLNNVSLSLKSGETvALLGRSGCGKSTLARLLVGLESPSQ--GNVSWRGEPlakl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 ---QPAHFKCCSGYVVQDDV--VMGTLTVRENLqfSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQfirgIS 186
Cdd:PRK10419 80 nraQRKAFRRDIQMVFQDSIsaVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 187 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRT-IIFSIHQPRYsIFKLFDSLTLLASGKLV- 264
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRL-VERFCQRVMVMDNGQIVe 232
|
250
....*....|....*....
gi 1720417991 265 ---------FHGPAQKALE 274
Cdd:PRK10419 233 tqpvgdkltFSSPAGRVLQ 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
59-243 |
1.19e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING-----------------APQPAHFKCCS 120
Cdd:PRK10619 17 EHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPS--EGSIVVNGqtinlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 121 GYVVQDDVVMGTLTVRENLQFSAALRLptTMKNHEKNERINTIIKELGLEKVADSKVGTQfirgISGGERKRTSIGMELI 200
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQGKYPVH----LSGGQQQRVSIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720417991 201 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-279 |
1.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.65 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 39 FHHITYRVKVKSGFlvrktvEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDP-KGLS--GDVLINGAPQPA 114
Cdd:PRK13634 5 FQKVEHRYQYKTPF------ERRALYDVNVSIPSGsYVAIIGHTGSGKSTLLQHLNGLLQPtSGTVtiGERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 HFKCCS---GYVVQ-DDVVMGTLTVRENLQFSaalrlPTT--MKNHEKNERINTIIKELGLekvaDSKVGTQFIRGISGG 188
Cdd:PRK13634 79 KLKPLRkkvGIVFQfPEHQLFEETVEKDICFG-----PMNfgVSEEDAKQKAREMIELVGL----PEELLARSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 189 ERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQ----PRYSifklfDSLTLLASGKL 263
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSmedaARYA-----DQIVVMHKGTV 224
|
250
....*....|....*.
gi 1720417991 264 VFHGPAQkalEYFASA 279
Cdd:PRK13634 225 FLQGTPR---EIFADP 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
185-270 |
1.44e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGKL 263
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLS-IVRKLADRVAVMQNGRC 235
|
....*..
gi 1720417991 264 VFHGPAQ 270
Cdd:PRK15134 236 VEQNRAA 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
180-279 |
1.96e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.87 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 180 QFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLA 259
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLR 210
|
90 100
....*....|....*....|
gi 1720417991 260 SGKLVFHGpaqKALEYFASA 279
Cdd:PRK13638 211 QGQILTHG---APGEVFACT 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
76-267 |
2.25e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAarkdpkGL---SGDVLINGAP----QPAHFKCCSGYVVQDDVVM-GTLtvRENLqfsaalrl 147
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALL------GFlpyQGSLKINGIElrelDPESWRKHLSWVGQNPQLPhGTL--RDNV-------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 ptTMKNHEKN-ERINTIIK-----------ELGLekvaDSKVGTQFIrGISGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:PRK11174 444 --LLGNPDASdEQLQQALEnawvseflpllPQGL----DTPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 216 DSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:PRK11174 517 DAHSEQLVMQALNAAS-RRQTTLMVTH--QLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-271 |
4.03e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAAR---KDPK-GLSGDVLINGAP----QPAHFKCCSGYVVQDDVV 129
Cdd:PRK14246 22 DKAILKDITiKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKiKVDGKVLYFGKDifqiDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 130 MGTLTVRENLQFSaaLRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIRgISGGERKRTSIGMELITDPSILFLD 209
Cdd:PRK14246 102 FPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQK 271
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ-QVARVADYVAFLYNGELVEWGSSNE 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
76-216 |
6.29e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLA-ARKDPKG----LSGDVlingaPQPAHFKCCSG---YVVQddvvmG-------TLTVRENLQ 140
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAgARKIQQGrvevLGGDM-----ADARHRRAVCPriaYMPQ-----GlgknlypTLSVFENLD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 141 FSAAL----RlpttmknHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:NF033858 101 FFGRLfgqdA-------AERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
54-216 |
6.96e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 54 VRKTV--EKEILSDINGIMKPGlnA---ILGPTGGGKSSLLDVLAarkdpkGLsgDVLINGAPQPAH-FKCcsGYVVQDD 127
Cdd:PRK11819 12 VSKVVppKKQILKDISLSFFPG--AkigVLGLNGAGKSTLLRIMA------GV--DKEFEGEARPAPgIKV--GYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 128 VVMGTLTVRENLQ------FSAALRL-PTTMKNHEKNERINTIIKELG-----------------LEKVA--------DS 175
Cdd:PRK11819 80 QLDPEKTVRENVEegvaevKAALDRFnEIYAAYAEPDADFDALAAEQGelqeiidaadawdldsqLEIAMdalrcppwDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720417991 176 KVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK11819 160 KVTK-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-271 |
7.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 7.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKG---LSGDVLINGAP-----QPAHFKCCSGYVVQDDVVM 130
Cdd:PRK14271 34 KTVLDQVSmGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyrYSGDVLLGGRSifnyrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 gTLTVRENLQfsAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIRgISGGERKRTSIGMELITDPSILFLDE 210
Cdd:PRK14271 114 -PMSIMDNVL--AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSifKLFDSLTLLASGKLVFHGPAQK 271
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAA--RISDRAALFFDGRLVEEGPTEQ 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
186-238 |
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 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 238
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
36-239 |
1.13e-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: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKS-GFLVRKtveKEILsdingimkpglnAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGapQPA 114
Cdd:cd03215 4 VLEVRGLSVKGAVRDvSFEVRA---GEIV------------GIAGLVGNGQTELAEALFGLRPPA--SGEITLDG--KPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 HFKCCS-------GYVVQD---DVVMGTLTVRENLQFSAALrlpttmknheknerintiikelglekvadskvgtqfirg 184
Cdd:cd03215 65 TRRSPRdairagiAYVPEDrkrEGLVLDLSVAENIALSSLL--------------------------------------- 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 185 iSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 239
Cdd:cd03215 106 -SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL 159
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
49-302 |
1.15e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 49 KSGFLVRKTVEKE-----ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGApqpahfKCCSGY 122
Cdd:PRK11432 3 QKNFVVLKNITKRfgsntVIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPT--EGQIFIDGE------DVTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 123 VVQDDVVM--------GTLTVRENLQFsaALRlpttMKNHEKNERiNTIIKElGLEKVADSKVGTQFIRGISGGERKRTS 194
Cdd:PRK11432 75 IQQRDICMvfqsyalfPHMSLGENVGY--GLK----MLGVPKEER-KQRVKE-ALELVDLAGFEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 195 IGMELITDPSILFLDEPTTGLDsstANavllLLKRMSKQGRTIifsihQPRYSIFKLF------------DSLTLLASGK 262
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLD---AN----LRRSMREKIREL-----QQQFNITSLYvthdqseafavsDTVIVMNKGK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720417991 263 LVFHGPAQkaleyfasagyhcEPYNNPADFFLDVINGDSS 302
Cdd:PRK11432 215 IMQIGSPQ-------------ELYRQPASRFMASFMGDAN 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
63-246 |
1.18e-08 |
|
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: 55.80 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLdvLAARKDPKGLSGDVLINGAPQPAHFKCCS--------GYVVQDDVVMGTl 133
Cdd:cd03290 17 LSNINIRIPTGqLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNKNESEPSFEATrsrnrysvAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 TVRENLQFSAALrlpttmknheKNERINTIIKELGLEKVAD-------SKVGTQFIrGISGGERKRTSIGMELITDPSIL 206
Cdd:cd03290 94 TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGERGI-NLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720417991 207 FLDEPTTGLDSSTANAVLL--LLKRMSKQGRTIIFSIHQPRY 246
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-242 |
1.29e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.67 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKSGFLVRKtvekeiLSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLS---GDVLINGAP 111
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRA------LFDIDLEVKKGsYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvGDIVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 QPAHFKCCS---GYVVQ-DDVVMGTLTVRENLQFSaalrlPTTMK-NHEKNERINTIIKEL-GLEKVADSKVGTQfirgI 185
Cdd:PRK13643 75 KQKEIKPVRkkvGVVFQfPESQLFEETVLKDVAFG-----PQNFGiPKEKAEKIAAEKLEMvGLADEFWEKSPFE----L 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
60-242 |
1.42e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.65 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPGLNAIL-GPTGGGKSSLLDVLAARKDPKglSGDVLING-------APQPAHFKCCSGYVVQDDVVMG 131
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLtGHSGAGKSTLLKLICGIERPS--AGKIWFSGhditrlkNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLqfsaALRLPTTMKNHEK-NERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDE 210
Cdd:PRK10908 93 DRTVYDNV----AIPLIIAGASGDDiRRRVSAALDKVGLLDKAKN-----FPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|..
gi 1720417991 211 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
77-216 |
1.46e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDP-KG-LSGDVLINGAPQpahfkccsgYVvQDDVVMgtlTVRENLqFSAALRLPTTMKNH 154
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPdEGeVDPELKISYKPQ---------YI-KPDYDG---TVEDLL-RSITDDLGSSYYKS 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 155 EknerintIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK13409 436 E-------IIKPLQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
59-267 |
1.56e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLS---GDVLINGAPQPAHFKCCS---GYVVQ------ 125
Cdd:PRK13646 19 EHQAIHDVNTEFEQGkYYAIVGQTGSGKSTLIQNINALLKPTTGTvtvDDITITHKTKDKYIRPVRkriGMVFQfpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 126 -DDvvmgtlTVRENLQFSaalrlPTT--MKNHEKNERINTIIKELGLEKVADSKVGTQfirgISGGERKRTSIGMELITD 202
Cdd:PRK13646 99 fED------TVEREIIFG-----PKNfkMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQ----MSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 203 PSILFLDEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIHQ----PRYSifklfDSLTLLASGKLVFHG 267
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmnevARYA-----DEVIVMKEGSIVSQT 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
77-265 |
1.57e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAArkDPKGLSGDVLINGA-----PQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALrlPTTM 151
Cdd:PRK11614 36 LIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKditdwQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFF--AERD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 152 KNHEKNERINTIIKELGLEKVadSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS 231
Cdd:PRK11614 112 QFQERIKWVYELFPRLHERRI--QRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLR 184
|
170 180 190
....*....|....*....|....*....|....
gi 1720417991 232 KQGRTiIFSIHQPRYSIFKLFDSLTLLASGKLVF 265
Cdd:PRK11614 185 EQGMT-IFLVEQNANQALKLADRGYVLENGHVVL 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
169-267 |
2.86e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 169 LEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIhQPRYSI 248
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEA 207
|
90
....*....|....*....
gi 1720417991 249 FKLFDSLTLLASGKLVFHG 267
Cdd:NF000106 208 EQLAHELTVIDRGRVIADG 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
44-274 |
3.11e-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: 57.26 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 44 YRVKVKSGFLVRKTVEKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGA----PQPAHFKC 118
Cdd:TIGR00957 635 NSITVHNATFTWARDLPPTLNGITfSIPEGALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVHMKGSvayvPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 119 CSgyvvqddvvmgtltVRENLQFSAALRLPTTMKNHEKNerinTIIKELGLEKVAD-SKVGTQFIRgISGGERKRTSIGM 197
Cdd:TIGR00957 713 DS--------------LRENILFGKALNEKYYQQVLEAC----ALLPDLEILPSGDrTEIGEKGVN-LSGGQKQRVSLAR 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 198 ELITDPSILFLDEPTTGLDSSTANAVL--LLLKRMSKQGRTIIFSIHQPRYsiFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFehVIGPEGVLKNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
57-274 |
5.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 57 TVEKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAH-----FKCCSGYVVQ-D 126
Cdd:PRK13641 17 PMEKKGLDNISfELEEGSFVALVGHTGSGKSTLMQHFNALLKPS--SGTITIAGyhiTPETGNknlkkLRKKVSLVFQfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 DVVMGTLTVRENLQFSaalrlPTTMKNHEKNERINTI--IKELGLEKVADSKvgTQFirGISGGERKRTSIGMELITDPS 204
Cdd:PRK13641 95 EAQLFENTVLKDVEFG-----PKNFGFSEDEAKEKALkwLKKVGLSEDLISK--SPF--ELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 205 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
77-294 |
6.64e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFKCCS----GYVVQDDVVMGTLTVRENLQFSAALrlp 148
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPT--RGQVLIDGVDiakiSDAELREVRrkkiAMVFQSFALMPHMTVLDNTAFGMEL--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 149 TTMKNHEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLL 227
Cdd:PRK10070 134 AGINAEERREKALDALRQVGLENYAHS-----YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELV 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 228 KRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGKLVFHGPAQKALeyfasagyhcepyNNPADFFL 294
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL-------------NNPANDYV 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
77-239 |
1.12e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTG--G-GKSSLLDVL--AARKDpkglSGDVLINGapQPAHFKccS---------GYVVQD---DVVMGTLTVRENL 139
Cdd:COG1129 280 ILGIAGlvGaGRTELARALfgADPAD----SGEIRLDG--KPVRIR--SprdairagiAYVPEDrkgEGLVLDLSIRENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 140 QFSAALRLPTTMKNHEKNER--INTIIKELGLeKVADSKvgtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDS 217
Cdd:COG1129 352 TLASLDRLSRGGLLDRRRERalAEEYIKRLRI-KTPSPE---QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
170 180
....*....|....*....|..
gi 1720417991 218 STANAVLLLLKRMSKQGRTIIF 239
Cdd:COG1129 428 GAKAEIYRLIRELAAEGKAVIV 449
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
36-239 |
1.33e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 36 VLSFHHITYRVKVKSGFLVRKTVEKeiLSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGapQPA 114
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVEA--VKPLSFTLREGQTlAIIGENGSGKSTLAKMLAGMIEPT--SGELLIDD--HPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 115 HF------KCCSGYVVQDDVVmgTLTVRENLQ--FSAALRLPTTMKNHEKNERINTIIKELGLekVADSkvGTQFIRGIS 186
Cdd:PRK15112 78 HFgdysyrSQRIRMIFQDPST--SLNPRQRISqiLDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDH--ASYYPHMLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 187 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIF 239
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLInLMLELQEKQGISYIY 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
61-217 |
1.33e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.93 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGapqpahfKCCS---------GYVVQD 126
Cdd:PRK10851 16 QVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIA------GLehqtSGHIRFHG-------TDVSrlhardrkvGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 DVVMGTLTVRENLQFSAALrLPttmknheKNERINT-IIK----ELgLEKVADSKVGTQFIRGISGGERKRTSIGMELIT 201
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTV-LP-------RRERPNAaAIKakvtQL-LEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170
....*....|....*.
gi 1720417991 202 DPSILFLDEPTTGLDS 217
Cdd:PRK10851 154 EPQILLLDEPFGALDA 169
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
59-228 |
1.46e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKP-GLNAILGPTGGGKSSLLDVLAARKDpkgLSGDVLINGApqpAHFKCCSGYVVQDDVV-----MGT 132
Cdd:PRK14239 17 KKKALNSVSLDFYPnEITALIGPSGSGKSTLLRSINRMND---LNPEVTITGS---IVYNGHNIYSPRTDTVdlrkeIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 ---------LTVRENLQFsaALRLPTTMKNHEKNERINTIIKELGL-----EKVADSKVGtqfirgISGGERKRTSIGME 198
Cdd:PRK14239 91 vfqqpnpfpMSIYENVVY--GLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG------LSGGQQQRVCIARV 162
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 199 LITDPSILFLDEPTTGLDSSTANAV---LLLLK 228
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIeetLLGLK 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
59-242 |
1.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDvlaarkdpkglsgdvLINGAPQPAhfkccSGYVVQDDVVMgtltvre 137
Cdd:PRK13649 19 EGRALFDVNLTIEDGsYTAFIGHTGSGKSTIMQ---------------LLNGLHVPT-----QGSVRVDDTLI------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 138 nlqfsaalrlpttmKNHEKNERINTIIKELGL--------------------------------EKVADSK---VGTQ-- 180
Cdd:PRK13649 72 --------------TSTSKNKDIKQIRKKVGLvfqfpesqlfeetvlkdvafgpqnfgvsqeeaEALAREKlalVGISes 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 181 -FIRG---ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK13649 138 lFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
77-243 |
1.73e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.65 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLdvlaaRkdpkglsgdvLINGAPQPAhfkccSGYVVQDDVVMGTL----------------------- 133
Cdd:PRK11153 36 VIGASGAGKSTLI-----R----------CINLLERPT-----SGRVLVDGQDLTALsekelrkarrqigmifqhfnlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 134 --TVRENLQFsaALRLPTTMKNhEKNERINTIIKELGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDEP 211
Cdd:PRK11153 96 srTVFDNVAL--PLELAGTPKA-EIKARVTELLELVGLSDKADR-----YPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 212 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQ 243
Cdd:PRK11153 168 TSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
76-270 |
1.87e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKdpKGLSGDVLINGAP-QPAHFKCCSGYV-------------VQDDVVMGtltvreNLQF 141
Cdd:PRK15056 37 ALVGVNGSGKSTLFKALMGFV--RLASGKISILGQPtRQALQKNLVAYVpqseevdwsfpvlVEDVVMMG------RYGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 142 SAALRLPttmKNHEKNerintiIKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 221
Cdd:PRK15056 109 MGWLRRA---KKRDRQ------IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720417991 222 AVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHN--LGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
59-267 |
1.92e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLING------APQPahfKCCSGYVVQDDVVMG 131
Cdd:PRK09580 13 DKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGkdllelSPED---RAGEGIFMAFQYPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSAALRLPTTMKNHEKNERI---NTIIKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFL 208
Cdd:PRK09580 90 IPGVSNQFFLQTALNAVRSYRGQEPLDRFdfqDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
76-269 |
2.09e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKS----SLLDVLaarkdPKG---LSGDVLINGAPQ-PAHFKccsGYVVQddvvmgtlTVRENLQfSA--AL 145
Cdd:PRK10418 33 ALVGGSGSGKSltcaAALGIL-----PAGvrqTAGRVLLDGKPVaPCALR---GRKIA--------TIMQNPR-SAfnPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 146 RlptTMKNHEK-----------NERINTIIKELGLEKVAdsKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:PRK10418 96 H---TMHTHARetclalgkpadDATLTAALEAVGLENAA--RVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 215 LDSSTANAVLLLLKR-MSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPA 269
Cdd:PRK10418 171 LDVVAQARILDLLESiVQKRALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDV 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
69-216 |
2.45e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 69 IMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING---APQPAHFKCCSgYVVQDDVVMGTLTVRENLQFSAAL 145
Cdd:PRK11607 42 IYKGEIFALLGASGCGKSTLLRMLAGFEQPT--AGQIMLDGvdlSHVPPYQRPIN-MMFQSYALFPHMTVEQNIAFGLKQ 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 146 -RLPTTmknhEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK11607 119 dKLPKA----EIASRVNEMLGLVHMQEFAKRKP-----HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
71-255 |
2.52e-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: 50.82 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 71 KPGLNAILGPTGGGKSSLLD---VLAARKDPKGLSGDVLingapQPAHFKCCSgyvvqddvvmgtltvrenlqfSAALRL 147
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGV-----KAGCIVAAV---------------------SAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 pttmknheknerintiikelglekvadskvgtqFIRGISGGERKRTSIGMEL----ITDPSILFLDEPTTGLDSSTANAV 223
Cdd:cd03227 74 ---------------------------------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|..
gi 1720417991 224 LLLLKRMSKQGRTIIFSIHQPRysIFKLFDSL 255
Cdd:cd03227 121 AEAILEHLVKGAQVIVITHLPE--LAELADKL 150
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
77-242 |
2.58e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDP------KGLSGDVLINgapqpaHFKccsGYVVQD---DVVMGTLTVRENLQFSAalRL 147
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPnlgkfdDPPDWDEILD------EFR---GSELQNyftKLLEGDVKVIVKPQYVD--LI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 PTTMKNH--------EKNERINTIIKELGLEKVADSKvgtqfIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSST 219
Cdd:cd03236 100 PKAVKGKvgellkkkDERGKLDELVDQLELRHVLDRN-----IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|...
gi 1720417991 220 ANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
131-242 |
3.77e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 131 GTLTVRENLQFSAAL-RLPTTmknhEKNERINTIIKELGLEKVADSKVGtqfirGISGGERKRTSIGMELITDPSILFLD 209
Cdd:NF033858 352 GELTVRQNLELHARLfHLPAA----EIAARVAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110
....*....|....*....|....*....|....
gi 1720417991 210 EPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 242
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTH 456
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-261 |
4.65e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 46 VKVKSG-FLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGdVLINGApqpahfkccSGYV 123
Cdd:PLN03232 615 ISIKNGyFSWDSKTSKPTLSDINLEIPVGsLVAIVGGTGEGKTSLISAMLGELSHAETSS-VVIRGS---------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 124 VQDDVVMGTlTVRENLQFSAALrlpttmknheKNERINTIIKELGLEKVADSKVGTQFI----RG--ISGGERKRTSIGM 197
Cdd:PLN03232 685 PQVSWIFNA-TVRENILFGSDF----------ESERYWRAIDVTALQHDLDLLPGRDLTeigeRGvnISGGQKQRVSMAR 753
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 198 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsiFKLFDSLTLLASG 261
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEG 815
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
76-216 |
7.95e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKGlsGDVLINGAP---QPAHFKCCSGYV--VQDDVVMGTLTVRENL---Q------- 140
Cdd:PRK11300 35 SLIGPNGAGKTTVFNCLTGFYKPTG--GTILLRGQHiegLPGHQIARMGVVrtFQHVRLFREMTVIENLlvaQhqqlktg 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 141 -FSAALRLPTTMKNH-EKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK11300 113 lFSGLLKTPAFRRAEsEALDRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
63-241 |
9.73e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.91 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAPQPAH----FKCCSGYVVQ--DDVVMGTLtv 135
Cdd:PRK13648 25 LKDVSfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK--SGEIFYNNQAITDDnfekLRKHIGIVFQnpDNQFVGSI-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 renLQFSAALRLPTTMKNHEK-NERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:PRK13648 101 ---VKYDVAFGLENHAVPYDEmHRRVSEALKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180
....*....|....*....|....*..
gi 1720417991 215 LDSSTANAVLLLLKRMSKQGRTIIFSI 241
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISI 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
77-216 |
1.07e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGApqpahfkccsgyVVQD------DVVM--------GTLTVREN 138
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVA------GLeritSGEIWIGGR------------VVNElepadrDIAMvfqnyalyPHMSVREN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 139 LQFSAALRlptTMKNHEKNERINTIIKELGLEKVADSKVgtqfiRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK11650 97 MAYGLKIR---GMPKAEIEERVAEAARILELEPLLDRKP-----RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-223 |
1.13e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 46 VKVKSG-FLVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDV----LAARKDpkglsGDVLINGApqpahfkcc 119
Cdd:PLN03130 615 ISIKNGyFSWDSKAERPTLSNINLDVPVGsLVAIVGSTGEGKTSLISAmlgeLPPRSD-----ASVVIRGT--------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 120 SGYVVQDDVVMGTlTVRENLQFSAalrlPTTMKNHEKNERINTIIKELGLEKVAD-SKVGTqfiRG--ISGGERKRTSIG 196
Cdd:PLN03130 681 VAYVPQVSWIFNA-TVRDNILFGS----PFDPERYERAIDVTALQHDLDLLPGGDlTEIGE---RGvnISGGQKQRVSMA 752
|
170 180
....*....|....*....|....*..
gi 1720417991 197 MELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
63-271 |
1.39e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAA--RKDpkglSGDVLINGapQPAHFKCcSGYVVQDDVVM--------G 131
Cdd:PRK10982 14 LDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGiyQKD----SGSILFQG--KEIDFKS-SKEALENGISMvhqelnlvL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 TLTVRENLQFSaalRLPTT--MKNHEKNER-INTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFL 208
Cdd:PRK10982 87 QRSVMDNMWLG---RYPTKgmFVDQDKMYRdTKAIFDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 209 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQK 271
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITILRDGQWIATQPLAG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
185-267 |
1.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPRySIFKLFDSLTLLASGKL 263
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMD-QVLRIADEVIVMHEGKV 229
|
....
gi 1720417991 264 VFHG 267
Cdd:PRK13645 230 ISIG 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
59-228 |
1.65e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.22 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG--LnAILGPTGGGKSSLLDVLAARKDPkgLSGDVLINgapQPAHFkccsGYVVQD-DVVMGTLTV 135
Cdd:COG0488 327 DKTLLDDLSLRIDRGdrI-GLIGPNGAGKSTLLKLLAGELEP--DSGTVKLG---ETVKI----GYFDQHqEELDPDKTV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQfsaalRLPTTMKNHE----------KNERINTIIKELglekvadskvgtqfirgiSGGERKRTSIGMELITDPSI 205
Cdd:COG0488 397 LDELR-----DGAPGGTEQEvrgylgrflfSGDDAFKPVGVL------------------SGGEKARLALAKLLLSPPNV 453
|
170 180
....*....|....*....|...
gi 1720417991 206 LFLDEPTTGLDSSTANAVLLLLK 228
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALD 476
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
59-267 |
1.81e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.99 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLING----APQPAHFKCCSGYVVQ--DDVVMG 131
Cdd:PRK13632 21 ENNALKNVSFEINEGeYVAILGHNGSGKSTISKILTGLLKPQ--SGEIKIDGitisKENLKEIRKKIGIIFQnpDNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 132 tLTVRENLQFSaalrLPTTMKNHEKnerINTIIKEL----GLEKVADSKvgTQFIrgiSGGERKRTSIGMELITDPSILF 207
Cdd:PRK13632 99 -ATVEDDIAFG----LENKKVPPKK---MKDIIDDLakkvGMEDYLDKE--PQNL---SGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 208 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI-HQPRYSIfkLFDSLTLLASGKLVFHG 267
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAI--LADKVIVFSEGKLIAQG 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
59-264 |
1.82e-06 |
|
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: 49.41 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAPqpahfkcCSGYVVQD----------D 127
Cdd:cd03244 16 LPPVLKNISFSIKPGEKvGIVGRTGSGKSSLLLALFRLVEL--SSGSILIDGVD-------ISKIGLHDlrsrisiipqD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 128 VVMGTLTVRENL----QFS-----AALRLpTTMKNH--EKNERINTIIKELGLekvadskvgtqfirGISGGERKRTSIG 196
Cdd:cd03244 87 PVLFSGTIRSNLdpfgEYSdeelwQALER-VGLKEFveSLPGGLDTVVEEGGE--------------NLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 197 MELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGKLV 264
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAH--RLDTIIDSDRILVLDKGRVV 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
180-267 |
2.06e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 180 QFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFsihqprysIFKLFDSLTLLA 259
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF--------ISSDLEEIEQMA 470
|
....*...
gi 1720417991 260 SGKLVFHG 267
Cdd:PRK15439 471 DRVLVMHQ 478
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-241 |
2.72e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 49.63 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 33 EGDVLSFHHITYRVKvksgflvrkTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGAP 111
Cdd:PRK13635 2 KEEIIRVEHISFRYP---------DAATYALKDVSFSVYEGeWVAIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGMV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 112 ------------------QP-AHFkccSGYVVQDDVVMGTltvrENLQfsaalrlpttMKNHEKNERINTIIKELGLEKV 172
Cdd:PRK13635 71 lseetvwdvrrqvgmvfqNPdNQF---VGATVQDDVAFGL----ENIG----------VPREEMVERVDQALRQVGMEDF 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 173 ADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 241
Cdd:PRK13635 134 LNREPHR-----LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSI 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
76-230 |
3.08e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPK----------GLSGDVLINGAPQPAH-FKCCSGYVVQDDvvmgtltvRENL--QFS 142
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDagevhyrmrdGQLRDLYALSEAERRRlLRTEWGFVHQHP--------RDGLrmQVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 143 A----ALRLPTTMKNHEKNerintiIKELGLEKVADSKVGTQFI----RGISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:PRK11701 108 AggniGERLMAVGARHYGD------IRATAGDWLERVEIDAARIddlpTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
170
....*....|....*.
gi 1720417991 215 LDSSTANAVLLLLKRM 230
Cdd:PRK11701 182 LDVSVQARLLDLLRGL 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
58-325 |
3.21e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 58 VEKEILSDIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGApqpahfkccSGYVVQDDVVMGTlTVR 136
Cdd:PTZ00243 671 EPKVLLRDVSvSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS--EGRVWAERS---------IAYVPQQAWIMNA-TVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSaalrlpttmkNHEKNERINTIIKELGLEkvAD---------SKVGTQFIrGISGGERKRTSIGMELITDPSILF 207
Cdd:PTZ00243 739 GNILFF----------DEEDAARLADAVRVSQLE--ADlaqlgggleTEIGEKGV-NLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 208 LDEPTTGLDSSTANAVL--LLLKRMSkqGRTIIFSIHQprYSIFKLFDSLTLLASGKLVFHGP----AQKALEYFASAGY 281
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVeeCFLGALA--GKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSsadfMRTSLYATLAAEL 881
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720417991 282 HCEPYNNPADFFLDVINGDSS---AVMLNR-EEQDNEANKTEEPSKGE 325
Cdd:PTZ00243 882 KENKDSKEGDADAEVAEVDAApggAVDHEPpVAKQEGNAEGGDGAALD 929
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
77-274 |
3.25e-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: 50.19 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKDP-KG----LSGDVLIN----GAPQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRL 147
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPtSGevnvRVGDEWVDmtkpGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 PttmKNHEKNERINTIiKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LL 226
Cdd:TIGR03269 395 P---DELARMKAVITL-KMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSI 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720417991 227 LKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGKLVFHGPAQKALE 274
Cdd:TIGR03269 471 LKAREEMEQTFIIVSHDMDF-VLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
62-253 |
3.33e-06 |
|
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: 47.53 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPGLNA-ILGPTGGGKSSLLDVLAarkdpkGL----SGDVLIngapqpaHFKCCSGYVVQDDVvMGTLTVR 136
Cdd:cd03223 16 LLKDLSFEIKPGDRLlITGPSGTGKSSLFRALA------GLwpwgSGRIGM-------PEGEDLLFLPQRPY-LPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 EnlqfsaALRLPttmknheknerintiikelgLEKVadskvgtqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:cd03223 82 E------QLIYP--------------------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720417991 217 SSTANAVLLLLKRMSkqgrTIIFSI-HQPrySIFKLFD 253
Cdd:cd03223 124 EESEDRLYQLLKELG----ITVISVgHRP--SLWKFHD 155
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-284 |
3.36e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 123 VVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELglEKVADSKVGTqFIRGISGGERKRTSIGMELITD 202
Cdd:PTZ00265 1300 IVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVGP-YGKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 203 PSILFLDEPTTGLDSstaNAVLLLLKRM----SKQGRTIIFSIHqpRYSIFKLFDSLtllasgkLVFHGPAQKAlEYFAS 278
Cdd:PTZ00265 1377 PKILLLDEATSSLDS---NSEKLIEKTIvdikDKADKTIITIAH--RIASIKRSDKI-------VVFNNPDRTG-SFVQA 1443
|
....*.
gi 1720417991 279 AGYHCE 284
Cdd:PTZ00265 1444 HGTHEE 1449
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
186-239 |
4.36e-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: 4.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 239
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLL 212
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
428-583 |
5.94e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 47.50 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 428 GVLFFLTTNQCFSSVSAVelFVVEKKL-FIHEYISGYYRVSSYFFGKVMSDLLPMrFLPSVIFTCILYFMLGLKKTVDAF 506
Cdd:COG0842 8 GLLAMSLLFTALMLTALS--IAREREQgTLERLLVTPVSRLEILLGKVLAYLLRG-LLQALLVLLVALLFFGVPLRGLSL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 507 FIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFTALQY 583
Cdd:COG0842 85 LLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRA 161
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
59-238 |
8.92e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 47.30 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpkGL----SGDVLINGAPQPAHFKCC------SGYVVQD- 126
Cdd:COG1126 13 DLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCIN------LLeepdSGTITVDGEDLTDSKKDInklrrkVGMVFQQf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 127 ----DvvmgtLTVRENLQFSaalrlPTTMKNHEKNErINTIIKELgLEKV-----ADSKVGTqfirgISGGERKRTSIGM 197
Cdd:COG1126 87 nlfpH-----LTVLENVTLA-----PIKVKKMSKAE-AEERAMEL-LERVgladkADAYPAQ-----LSGGQQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720417991 198 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 238
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMV 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
35-241 |
9.94e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 35 DVLSFHHITYrvkvksgflVRKTVEKEILSDINGIMKPG-LNAILGPTGGGKSS---LLD-VLAARKDPKGL-------- 101
Cdd:PRK13640 4 NIVEFKHVSF---------TYPDSKKPALNDISFSIPRGsWTALIGHNGSGKSTiskLINgLLLPDDNPNSKitvdgitl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 102 -----------SGDVLINGAPQPAhfkccsGYVVQDDVVMGTltvrENLQFSaalrlpttmknHEKNERI-NTIIKELGL 169
Cdd:PRK13640 75 taktvwdirekVGIVFQNPDNQFV------GATVGDDVAFGL----ENRAVP-----------RPEMIKIvRDVLADVGM 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 170 EKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 241
Cdd:PRK13640 134 LDYIDSEPAN-----LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
59-216 |
1.03e-05 |
|
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: 45.52 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPkgLSGDVLINGAPQPAHFkccsgyvvqddvvmgtltvre 137
Cdd:cd03221 12 GKLLLKDISLTINPGDRiGLVGRNGAGKSTLLKLIAGELEP--DEGIVTWGSTVKIGYF--------------------- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 138 nlqfsaalrlpttmknheknerintiikelglekvadskvgTQFirgiSGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:cd03221 69 -----------------------------------------EQL----SGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
59-216 |
1.11e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 59 EKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLingapQPAHFKCcsGYVVQDDVVMGTLTvre 137
Cdd:PRK09544 16 QRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIK-----RNGKLRI--GYVPQKLYLDTTLP--- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 138 nLQFSAALRLPTTMKNHEknerintIIKelGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK09544 84 -LTVNRFLRLRPGTKKED-------ILP--ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
186-241 |
1.99e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 1.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417991 186 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 241
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-552 |
2.01e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 11 PMSQRNNNGLPRMNSRAVrtlaEGDVLSFHHITyrvkvksgflvRKTVEkeILSDINGIMKPGLN-AILGPTGGGKSSLL 89
Cdd:PTZ00265 366 PLVENNDDGKKLKDIKKI----QFKNVRFHYDT-----------RKDVE--IYKDLNFTLTEGKTyAFVGESGCGKSTIL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 90 DVLAARKDPKglSGDVLINGAPQPAH-----FKCCSGYVVQDDVVMGTlTVRENLQFS---------------------- 142
Cdd:PTZ00265 429 KLIERLYDPT--EGDIIINDSHNLKDinlkwWRSKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealsnyynedgndsq 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 143 ------------AALRLPTTMKNHEKNERINT-----IIKELGLEKVA----------------DSKVGTQFIRgISGGE 189
Cdd:PTZ00265 506 enknkrnscrakCAGDLNDMSNTTDSNELIEMrknyqTIKDSEVVDVSkkvlihdfvsalpdkyETLVGSNASK-LSGGQ 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 190 RKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIHqpRYSIFKLFDSLTLLASGK------ 262
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAH--RLSTIRYANTIFVLSNRErgstvd 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 263 --LVFHGPAQKALE--------------------------YFASAGYHCEPYNNPADFFLDVIN-----GDSSAVMLNRE 309
Cdd:PTZ00265 663 vdIIGEDPTKDNKEnnnknnkddnnnnnnnnnnkinnagsYIIEQGTHDALMKNKNGIYYTMINnqkvsSKKSSNNDNDK 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 310 EQDNEANKTEEPSKGEKPVIENLSEFYINSAIYGETKAEL-DQLPGAQEKKGTSAFKEPVY--VTSFCHQLRWIARRSFk 386
Cdd:PTZ00265 743 DSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMsDENASENNAGGKLPFLRNLFkrKPKAPNNLRIVYREIF- 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 387 nllgnpqaSVAQLIVTVILGLII-GAIY--FDLKYdaagmQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGY 463
Cdd:PTZ00265 822 --------SYKKDVTIIALSILVaGGLYpvFALLY-----AKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNY 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 464 YrvsSYFFGKVMSDLLPMRFLPSVIFTCILYF---------------------MLGLKKTVDAF--FIMMFTLIMVayta 520
Cdd:PTZ00265 889 Y---NNVIGEKVEKTMKRRLFENILYQEISFFdqdkhapgllsahinrdvhllKTGLVNNIVIFthFIVLFLVSMV---- 961
|
650 660 670
....*....|....*....|....*....|..
gi 1720417991 521 ssMALAIATgqsvvSVATLLMTIAFVFMMLFS 552
Cdd:PTZ00265 962 --MSFYFCP-----IVAAVLTGTYFIFMRVFA 986
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
155-233 |
2.10e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.37 E-value: 2.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 155 EKNERINTIIKELGLEKVADSKVGTQFirgiSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 233
Cdd:COG4172 400 ERRARVAEALEEVGLDPAARHRYPHEF----SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
62-288 |
2.15e-05 |
|
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: 47.98 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGApqpahfkccSGYVVQDDVVMGTlTVRENLQ 140
Cdd:TIGR01271 441 VLKNISFKLEKGqLLAVAGSTGSGKSSLLMMIMGELEPS--EGKIKHSGR---------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 141 FSAALrlpttmknheKNERINTIIKELGLEK---VADSKVGTQFIRG---ISGGERKRTSIGMELITDPSILFLDEPTTG 214
Cdd:TIGR01271 509 FGLSY----------DEYRYTSVIKACQLEEdiaLFPEKDKTVLGEGgitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 215 LDSSTANAVL--LLLKRMSKQGRTIIFSihqpRYSIFKLFDSLTLLASGKLVFHGP---AQKALEYFASAGYHCEPYNN 288
Cdd:TIGR01271 579 LDVVTEKEIFesCLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTfseLQAKRPDFSSLLLGLEAFDN 653
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
159-274 |
2.40e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 159 RINTIIKELGLEkvADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKrmSKQGrTII 238
Cdd:PRK11147 138 RINEVLAQLGLD--PDAALSS-----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK--TFQG-SII 207
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720417991 239 FsIHQPRYSIFKLFDSLTLLASGKLV-FHGPAQKALE 274
Cdd:PRK11147 208 F-ISHDRSFIRNMATRIVDLDRGKLVsYPGNYDQYLL 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
77-263 |
2.78e-05 |
|
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: 47.13 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 77 ILGPTGGGKSSLLDVLAARKdPKGLSGDVLINGapQPAHFKCCS-------GYVVQD---DVVMGTLTVRENLQFSAALR 146
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGAY-PGKFEGNVFING--KPVDIRNPAqairagiAMVPEDrkrHGIVPILGVGKNITLSVLKS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 147 LPTTMKNHEKNER--INTIIKELGLekvadsKVGTQF--IRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 222
Cdd:TIGR02633 368 FCFKMRIDAAAELqiIGSAIQRLKV------KTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYE 441
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720417991 223 VLLLLKRMSKQGRTIIFsIHQPRYSIFKLFDSLTLLASGKL 263
Cdd:TIGR02633 442 IYKLINQLAQEGVAIIV-VSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-245 |
2.95e-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: 45.01 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQFSAALRLPTTMKNHEKNERI-----NTIIKeLGLEKVA-DSKVGTqfirgISGGERKRTSIGMELI--TDPSIL 206
Cdd:cd03238 38 VNEGLYASGKARLISFLPKFSRNKLIfidqlQFLID-VGLGYLTlGQKLST-----LSGGELQRVKLASELFsePPGTLF 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720417991 207 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPR 245
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
63-270 |
3.38e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 63 LSDINGIMKPG-LNAILGPTGGGKSSLLDVLAARKdPKG-LSGDVLINGAPQPAHFKCCS---GYVV--QDDVVMGTLTV 135
Cdd:PRK13549 21 LDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVY-PHGtYEGEIIFEGEELQASNIRDTeraGIAIihQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN-----LGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 216 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLVFHGPAQ 270
Cdd:PRK13549 175 TESETAVLLDIIRDLKAHGIACIYISHKLN-EVKAISDTICVIRDGRHIGTRPAA 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
79-238 |
3.38e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 79 GPTGGGKSSLLDVLAArKDPKgLSGDVLING------APQPAhFKCCSGYVVQ---DDVVMGTLTVRENLQFSAALRL-- 147
Cdd:PRK09700 296 GLVGSGRTELMNCLFG-VDKR-AGGEIRLNGkdisprSPLDA-VKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDgg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 ---PTTMKNHEKNERINTIIKELGLEKVADSKvgtQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 224
Cdd:PRK09700 373 ykgAMGLFHEVDEQRTAENQRELLALKCHSVN---QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
|
170
....*....|....
gi 1720417991 225 LLLKRMSKQGRTII 238
Cdd:PRK09700 450 KVMRQLADDGKVIL 463
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
61-238 |
5.31e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSdINGIMkpglnailgptGGGKSSLLDVL--AARKDpkglSGDVLING------APQPAhFKCCSGYVVQD----DV 128
Cdd:PRK10762 279 EILG-VSGLM-----------GAGRTELMKVLygALPRT----SGYVTLDGhevvtrSPQDG-LANGIVYISEDrkrdGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 129 VMGtLTVRENLQFSAALRLPTTM---KNHEKNERINTIIKELglekvadsKVGT----QFIRGISGGERKRTSIGMELIT 201
Cdd:PRK10762 342 VLG-MSVKENMSLTALRYFSRAGgslKHADEQQAVSDFIRLF--------NIKTpsmeQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720417991 202 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 238
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
185-242 |
5.66e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 5.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 242
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITH 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
157-238 |
6.86e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 157 NER--INTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQG 234
Cdd:COG1245 188 DERgkLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG 262
|
....
gi 1720417991 235 RTII 238
Cdd:COG1245 263 KYVL 266
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
182-238 |
6.93e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 6.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417991 182 IRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 238
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
66-243 |
8.27e-05 |
|
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: 45.59 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 66 INGI---MKPG-LNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGAP-QPAHFKCC--SGYVV--QDDVVMGTLTVR 136
Cdd:TIGR02633 17 LDGIdleVRPGeCVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPlKASNIRDTerAGIVIihQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSAALRLP-TTMKNHEKNERINTIIKELGLEKVADSKVGTQFirgiSGGERKRTSIGMELITDPSILFLDEPTTGL 215
Cdd:TIGR02633 97 ENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180
....*....|....*....|....*...
gi 1720417991 216 DSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
43-244 |
9.93e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 43 TYRV-KVKSGFLV-RKTVEKEILSDINGIMKPG-LNAILGPTGGGKSSLLDVL--AARKDPKGLSGDVLINGAPQPAhfk 117
Cdd:COG2401 24 SERVaIVLEAFGVeLRVVERYVLRDLNLEIEPGeIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGREA--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 118 ccsgyVVQDDVVMgtltvreNLQFSAALRLPTTMKnheknerINTIIkeLGLEKVADskvgtqfirgISGGERKRTSIGM 197
Cdd:COG2401 101 -----SLIDAIGR-------KGDFKDAVELLNAVG-------LSDAV--LWLRRFKE----------LSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720417991 198 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP 244
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
61-239 |
1.54e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPGLNA----------ILG---PTGGGKSSLLDVL--AARKDpkglSGDVLINGAP----QPAHfKCCSG 121
Cdd:PRK11288 255 EVRLRLDGLKGPGLREpisfsvrageIVGlfgLVGAGRSELMKLLygATRRT----AGQVYLDGKPidirSPRD-AIRAG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 122 YVV------QDDVVmGTLTVRENLQFSA-ALRLPTTMKNHEKNERintiikELGLEKVADSKVGT----QFIRGISGGER 190
Cdd:PRK11288 330 IMLcpedrkAEGII-PVHSVADNINISArRHHLRAGCLINNRWEA------ENADRFIRSLNIKTpsreQLIMNLSGGNQ 402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720417991 191 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 239
Cdd:PRK11288 403 QKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
177-238 |
1.64e-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: 45.00 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 177 VGTQFIR------GISGGERKRTSIGMEL---ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 238
Cdd:TIGR00630 816 VGLGYIRlgqpatTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-242 |
1.97e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 30 TLAEGD-VLSFHHITYRVKVKSGFLVRKTVEKEILSDINGIMKPGLN-AILGPTGGGKS----SLLDVLAARKDPKGLSG 103
Cdd:PRK10261 306 TVVDGEpILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETlSLVGESGSGKSttgrALLRLVESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 104 ---DVLINGAPQPAHFKCcsGYVVQDDvvMGTLTVRENLQFS--AALRLPTTMKNHEKNERINTIIKELGLEKVADSKVG 178
Cdd:PRK10261 386 qriDTLSPGKLQALRRDI--QFIFQDP--YASLDPRQTVGDSimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYP 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 179 TQFirgiSGGERKRTSIGMELITDPSILFLDEPTTGLDSST-ANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK10261 462 HEF----SGGQRQRICIARALALNPKVIIADEAVSALDVSIrGQIINLLLDLQRDFGIAYLFISH 522
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
157-216 |
2.58e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 157 NER--INTIIKELGLEKVADSKvgtqfIRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK13409 188 DERgkLDEVVERLGLENILDRD-----ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
62-267 |
2.91e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. 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: 213258 [Multi-domain] Cd Length: 282 Bit Score: 43.31 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPG-LNAILGPTGGGKSSLLdvlaarkdpkglsgdVLINGAPQPAHFKC-CSG---YVVQDDVVMGTlTVR 136
Cdd:cd03291 52 VLKNINLKIEKGeMLAITGSTGSGKTSLL---------------MLILGELEPSEGKIkHSGrisFSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQFSAAL---RLPTTMKNHEKNERI-------NTIIKELGLEkvadskvgtqfirgISGGERKRTSIGMELITDPSIL 206
Cdd:cd03291 116 ENIIFGVSYdeyRYKSVVKACQLEEDItkfpekdNTVLGEGGIT--------------LSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417991 207 FLDEPTTGLDSSTANAVL--LLLKRMSKQGRTIIFSihqpRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFesCVCKLMANKTRILVTS----KMEHLKKADKILILHEGSSYFYG 240
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
180-241 |
3.30e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417991 180 QFIRgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 241
Cdd:cd03222 68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
185-242 |
3.99e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 185 ISGGERKRTSIGMELIT---DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
102-239 |
4.13e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 102 SGDVLINGapQPAHFKCCS-------GYVVQD---DVVMGTLTVRENL------QFSAALRLpttmkNHEKNER-INTII 164
Cdd:PRK13549 317 EGEIFIDG--KPVKIRNPQqaiaqgiAMVPEDrkrDGIVPVMGVGKNItlaaldRFTGGSRI-----DDAAELKtILESI 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 165 KELglekvadsKVGT----QFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 239
Cdd:PRK13549 390 QRL--------KVKTaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
76-227 |
4.73e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAARKDPKglSGDVLING----APQPAHFKccsgyVVQDDVVM------GTLTVRENL--QFSA 143
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPT--GGELYYQGqdllKADPEAQK-----LLRQKIQIvfqnpyGSLNPRKKVgqILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 144 ALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFirgiSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAV 223
Cdd:PRK11308 118 PLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMF----SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
|
....
gi 1720417991 224 LLLL 227
Cdd:PRK11308 194 LNLM 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
151-242 |
5.31e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 151 MKNHEKNERINTIIKELGLEKVADSKVGTQFirgiSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 230
Cdd:PRK15079 132 LSRQEVKDRVKAMMLKVGLLPNLINRYPHEF----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
90
....*....|...
gi 1720417991 231 SKQ-GRTIIFSIH 242
Cdd:PRK15079 208 QREmGLSLIFIAH 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
71-243 |
5.62e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 71 KPGLNAILGPTGGGKSSLLDVLAARKDPKglSGDVLINGA---PQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSaalrL 147
Cdd:PRK13540 26 AGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFERQsikKDLCTYQKQLCFVGHRSGINPYLTLRENCLYD----I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 148 PTTMKNHEknerINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 227
Cdd:PRK13540 100 HFSPGAVG----ITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*.
gi 1720417991 228 KRMSKQGRTIIFSIHQ 243
Cdd:PRK13540 171 QEHRAKGGAVLLTSHQ 186
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
61-267 |
7.23e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain] Cd Length: 207 Bit Score: 41.24 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 61 EILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglSGDVLINGapqpahfkccsgyvvQDDVVMGTLTVRENL 139
Cdd:cd03369 22 PVLKNVSFKVKAGEKiGIVGRTGAGKSTLILALFRFLEAE--EGKIEIDG---------------IDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 140 Q--------FSAALRLPTTMKNHEKNERINTI--IKELGLEkvadskvgtqfirgISGGERKRTSIGMELITDPSILFLD 209
Cdd:cd03369 85 TiipqdptlFSGTIRSNLDPFDEYSDEEIYGAlrVSEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417991 210 EPTTGLDSSTaNAVLLLLKRMSKQGRTIIFSIHQPRySIFKlFDSLTLLASGKLVFHG 267
Cdd:cd03369 151 EATASIDYAT-DALIQKTIREEFTNSTILTIAHRLR-TIID-YDKILVMDAGEVKEYD 205
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
188-286 |
1.10e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 188 GERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHG 267
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
90
....*....|....*....
gi 1720417991 268 PAQKALeyfaSAGYHcePY 286
Cdd:PRK15093 242 PSKELV----TTPHH--PY 254
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
465-589 |
1.41e-03 |
|
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: 41.22 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 465 RVSSYFFGKVMSDLLpmrfLPSVIFTCILYFMLGLKKTVDAFFIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIA 544
Cdd:pfam12698 201 SPLQYWLGKILGDFL----VGLLQLLIILLLLFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIV 276
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720417991 545 FVFMMLFSGLLVNLRTIGPWLSWLQY---FSIPRYGFTALQYNEFLGQ 589
Cdd:pfam12698 277 ILLLSGFFGGLFPLEDPPSFLQWIFSiipFFSPIDGLLRLIYGDSLWE 324
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
185-267 |
1.46e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.54 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHqpRYSIFKLFDSLTLLASGKLV 264
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH--RLSTIEKADEILVVEDGEIV 557
|
...
gi 1720417991 265 FHG 267
Cdd:PRK11176 558 ERG 560
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
186-243 |
1.50e-03 |
|
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: 41.06 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417991 186 SGGERKRTSIGMELI---TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 243
Cdd:cd03271 171 SGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
185-278 |
1.58e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQ----PRYSIFKLFDSLTLLAS 260
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNmqqaARVSDMTAFFNVELTEG 230
|
90 100 110
....*....|....*....|....*....|
gi 1720417991 261 GK------------LVFHGPAQKALEYFAS 278
Cdd:PRK14243 231 GGrygylvefdrteKIFNSPQQQATRDYVS 260
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
76-264 |
1.62e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 76 AILGPTGGGKSSLLDVLAA--RKDpkglSGDVLINGapQPAHFK-------CCSGYVVQDDVVMGTLTVRENLQFSaalR 146
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiyTRD----AGSILYLG--KEVTFNgpkssqeAGIGIIHQELNLIPQLTIAENIFLG---R 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 147 LPTT----MKNHEKNERINTIIKELGLEKVADSKVGTqfirgISGGERKRTSIGMELITDPSILFLDEPTTGL-DSSTAn 221
Cdd:PRK10762 105 EFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720417991 222 AVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGKLV 264
Cdd:PRK10762 179 SLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVFRDGQFI 220
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-273 |
1.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 157 NERINTIIkELGLEKVADSKVgtqfIRGISGGERKRTSI----GMELITDPSILflDEPTTGLDSSTANAVLLLLKRMSK 232
Cdd:PRK00635 454 KSRLSILI-DLGLPYLTPERA----LATLSGGEQERTALakhlGAELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRD 526
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 233 QGRTIIFSIHQ--------------PRYSIFklfdsltllaSGKLVFHGPAQKAL 273
Cdd:PRK00635 527 QGNTVLLVEHDeqmisladriidigPGAGIF----------GGEVLFNGSPREFL 571
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
79-216 |
1.66e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.22 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 79 GPTGGGKSSLLDVLAARKDPKglSGDVLINGAP----QPAHFkccSGYVVQDDVVMGTLTVRENLQFSAAL--RLPTTMK 152
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTatrgDRSRF---MAYLGHLPGLKADLSTLENLHFLCGLhgRRAKQMP 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417991 153 NHEKnerinTIIkelGLEKVADSkvgtqFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLD 216
Cdd:PRK13543 119 GSAL-----AIV---GLAGYEDT-----LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
154-273 |
1.68e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 154 HEKNERINTIIKELGLEKVADSKvgtqFIRgISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 233
Cdd:PRK10938 110 VKDPARCEQLAQQFGITALLDRR----FKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720417991 234 GRTIIFSIHqpRYS-IFKLFDSLTLLASGKLVFHGPAQKAL 273
Cdd:PRK10938 185 GITLVLVLN--RFDeIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
60-243 |
2.30e-03 |
|
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: 41.43 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKGlsgDVLINGAPQPA----HFKCCSGyVVQDDVVMGTLT 134
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRvGLLGRTGSGKSTLLSALLRLLSTEG---EIQIDGVSWNSvtlqTWRKAFG-VIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 135 VRENLQfsaalrlpttmkNHEK--NERINTIIKELGLEKVADS---KVGTQFIRG---ISGGERKRTSIGMELITDPSIL 206
Cdd:TIGR01271 1308 FRKNLD------------PYEQwsDEEIWKVAEEVGLKSVIEQfpdKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720417991 207 FLDEPTTGLDSSTanavLLLLKRMSKQGR---TIIFSIHQ 243
Cdd:TIGR01271 1376 LLDEPSAHLDPVT----LQIIRKTLKQSFsncTVILSEHR 1411
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
185-242 |
3.50e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 3.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSS-TANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITH 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
183-242 |
3.98e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 3.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 183 RGISGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMSKQGRTIIFSIH 242
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
185-244 |
4.44e-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: 39.16 E-value: 4.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417991 185 ISGGERKR----TSIGMELItdpSILF-LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 244
Cdd:cd03270 138 LSGGEAQRirlaTQIGSGLT---GVLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
185-242 |
4.74e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.30 E-value: 4.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417991 185 ISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 242
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
62-243 |
5.18e-03 |
|
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: 39.45 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 62 ILSDINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPKglsGDVLINGAPQPA----HFKCCSGyVVQDDVVMGTLTVR 136
Cdd:cd03289 19 VLENISFSISPGQRvGLLGRTGSGKSTLLSAFLRLLNTE---GDIQIDGVSWNSvplqKWRKAFG-VIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 137 ENLQfsaalrlPTtmkNHEKNERINTIIKELGLEKVADS---KVGTQFIRG---ISGGERKRTSIGMELITDPSILFLDE 210
Cdd:cd03289 95 KNLD-------PY---GKWSDEEIWKVAEEVGLKSVIEQfpgQLDFVLVDGgcvLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190
....*....|....*....|....*....|...
gi 1720417991 211 PTTGLDSSTANAVLLLLKRmSKQGRTIIFSIHQ 243
Cdd:cd03289 165 PSAHLDPITYQVIRKTLKQ-AFADCTVILSEHR 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
72-245 |
5.32e-03 |
|
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: 38.74 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 72 PGLNAILGPTGGGKSSLLDVLAArkdpkGLSGDvlinGAPQpahfkcCSGYVVQDDVVM-GTLTVRENLQFSAAlrlptt 150
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKY-----ALTGE----LPPN------SKGGAHDPKLIReGEVRAQVKLAFENA------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 151 mknhekNERINTIIKELG-LEKVA-----DSKVGTQFIRG-ISGGERK------RTSIGMELITDPSILFLDEPTTGLDS 217
Cdd:cd03240 81 ------NGKKYTITRSLAiLENVIfchqgESNWPLLDMRGrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190
....*....|....*....|....*....|
gi 1720417991 218 STANAVLL-LLKRMSKQG-RTIIFSIHQPR 245
Cdd:cd03240 155 ENIEESLAeIIEERKSQKnFQLIVITHDEE 184
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
60-221 |
5.43e-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: 39.12 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 60 KEILSDINGIMKPGLN-AILGPTGGGKSSLldVLAARKDPKGLSGDVLING---APQPAHFKCCSGYVVQDDVVMGTLTV 135
Cdd:cd03288 34 KPVLKHVKAYIKPGQKvGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGidiSKLPLHTLRSRLSIILQDPILFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 136 RENLQFSAALRLPTTMKNHEKNErINTIIKEL--GLEKVAdSKVGTQFirgiSGGERKRTSIGMELITDPSILFLDEPTT 213
Cdd:cd03288 112 RFNLDPECKCTDDRLWEALEIAQ-LKNMVKSLpgGLDAVV-TEGGENF----SVGQRQLFCLARAFVRKSSILIMDEATA 185
|
....*...
gi 1720417991 214 GLDSSTAN 221
Cdd:cd03288 186 SIDMATEN 193
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
133-239 |
7.31e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 38.94 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 133 LTVRENLqfSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFirgiSGGERKRTSIGMELITDPSILFLDEPT 212
Cdd:COG4608 112 MTVGDII--AEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEF----SGGQRQRIGIARALALNPKLIVCDEPV 185
|
90 100
....*....|....*....|....*...
gi 1720417991 213 TGLDSSTANAVLLLLKRMSKQ-GRTIIF 239
Cdd:COG4608 186 SALDVSIQAQVLNLLEDLQDElGLTYLF 213
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
143-244 |
9.14e-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: 38.52 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417991 143 AALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITD---PSILFLDEPTTGLDSST 219
Cdd:pfam13304 195 ADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKL 274
|
90 100
....*....|....*....|....*
gi 1720417991 220 ANAVLLLLKRMSKQGRTIIFSIHQP 244
Cdd:pfam13304 275 LRRLLELLKELSRNGAQLILTTHSP 299
|
|
| |
