|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
75-631 |
1.08e-125 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 384.40 E-value: 1.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvNHKALDPSSAVLMNNRKItDYNQLRRLCGFVPQDDDLLPLLTVK 154
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR-SPKGVKGSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 155 ETLMYSAKFSL-RDSTAKEREERVESLLSDLGLVLVQDSFVGEGDEEdRGVSGGERKRVSIAVEMIRDPPILLLDEPTSG 233
Cdd:TIGR00955 118 EHLMFQAHLRMpRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 234 LDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYRILDYISDYLILSRGSVIHLGSLEHLEDSIAKLGFQIPEQLNPIEFA 313
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 314 MEIVESLRTFKPNSVAVVE-------SSSMWPENNENDGIISKKEAFRVLDV-------------TEISYLCSRFCKIIY 373
Cdd:TIGR00955 276 VQVLAVIPGSENESRERIEkicdsfaVSDIGRDMLVNTNLWSGKAGGLVKDSenmegigynaswwTQFYALLKRSWLSVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 374 RTKQLFLARTMQAVVAGLGLGSVYTRLKRDEEGVAERLG-LFAFSLSFLLSSTVEALPIYLRERRVLMKESSRGSYRISS 452
Cdd:TIGR00955 356 RDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGaLFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSA 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 453 YMIANTIAFVPFLFVVSLLFSIPVYWIVGLNPSIQAFSFFVLCVWLIILMASSLVLFLSAVSPDFISGNSLICTVLGAFF 532
Cdd:TIGR00955 436 YFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 533 LFSGYFIPKEKIPKPWMFMYYVSLYRYPLESMVVNEYWSMRE-ECFSSGNMG-CLMTGEDVLKERGLDKDTRWINVGIML 610
Cdd:TIGR00955 516 LFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNiECTSANTTGpCPSSGEVILETLSFRNADLYLDLIGLV 595
|
570 580
....*....|....*....|.
gi 1063732797 611 AFFVFYRILCWGILLRKASKS 631
Cdd:TIGR00955 596 ILIFFFRLLAYFALRIRIRRK 616
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
62-626 |
4.05e-75 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 253.26 E-value: 4.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 62 TVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALdpSSAVLMNNRKITdyNQLRRLCGFV 141
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNF--TGTILANNRKPT--KQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 142 PQDDDLLPLLTVKETLMYSAKFSLRDSTAKEREERV-ESLLSDLGLVLVQDSFVGegDEEDRGVSGGERKRVSIAVEMIR 220
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVaESVISELGLTKCENTIIG--NSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 221 DPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYRILDYISDYLILSRGSVIHLGSLEHLEDSIAKLG 300
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 301 FQIPEQLNPIEFAME----------------------IVESLRTFKPNSVAVVESSSMWPENNENDGIISKKEAFRVLDV 358
Cdd:PLN03211 303 FSPSFPMNPADFLLDlangvcqtdgvserekpnvkqsLVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDR 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 359 TEISYLCSRFCKIIYRT------KQLFLARTMQAVVAGLGLGSVYtrLKRDEEGVAERLGLFAF-SLSFLLSSTVEALPI 431
Cdd:PLN03211 383 ISISTWFNQFSILLQRSlkerkhESFNTLRVFQVIAAALLAGLMW--WHSDFRDVQDRLGLLFFiSIFWGVFPSFNSVFV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 432 YLRERRVLMKESSRGSYRISSYMIANTIAFVPFLFVVSLLFSIPVYWIVGLNPSIQAFSFFVLCVWLIILMASSLVLFLS 511
Cdd:PLN03211 461 FPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALG 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 512 AVSPDFISGNSLICTVLGAFFLFSGYFIpkEKIPKPWMFMYYVSLYRYPLESMVVNEYWSMRE-----ECFS---SGNMG 583
Cdd:PLN03211 541 AAIMDAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRissllGCSLphgSDRAS 618
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1063732797 584 CLMTGEDVLKERGLdkdtrWINVGIMLAFFVFYRILCWGILLR 626
Cdd:PLN03211 619 CKFVEEDVAGQISP-----ATSVSVLIFMFVGYRLLAYLALRR 656
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
58-619 |
1.93e-63 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 228.07 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 58 RYSLTVTNLSYTI-----------NHTP---ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAVLM 123
Cdd:TIGR00956 45 DYQPTFPNALLKIltrgfrklkkfRDTKtfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 124 NNRKITDY-NQLRRLCGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAK--EREERVESL----LSDLGLVLVQDSFVGe 196
Cdd:TIGR00956 125 DGITPEEIkKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNRPDgvSREEYAKHIadvyMATYGLSHTRNTKVG- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 197 gDEEDRGVSGGERKRVSIAvEMIRDPP-ILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRILDYISDY 275
Cdd:TIGR00956 204 -NDFVRGVSGGERKRVSIA-EASLGGAkIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 276 LILSRGSVIHLGSLEHLEDSIAKLGFQIPEQLNPIEFAMEIVE-SLRTFKPNSVAVV-----ESSSMW---PENNE---- 342
Cdd:TIGR00956 282 IVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTSpAERQIKPGYEKKVprtpqEFETYWrnsPEYAQlmke 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 343 ------NDGIISKKEAFRVLDVTEIS------------------YLCSRFCKIIYRTKQLFLARTMQAVVAGLGLGSVYT 398
Cdd:TIGR00956 362 ideyldRCSESDTKEAYRESHVAKQSkrtrpsspytvsfsmqvkYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 399 RLKRDEEGVAERLGLFAFSL------SFL-LSSTVEALPIYLRERRVLMkessrgsYRISSYMIANTIAFVPFLFVVSLL 471
Cdd:TIGR00956 442 NLPKNTSDFYSRGGALFFAIlfnafsSLLeIASMYEARPIVEKHRKYAL-------YHPSADAIASIISEIPFKIIESVV 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 472 FSIPVYWIVGLNPSIQAFSFFVLCVWLIILMASSLVLFLSAVSPDFISGNSLICTVLGAFFLFSGYFIPKEKIPKPWMFM 551
Cdd:TIGR00956 515 FNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWI 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 552 YYVSLYRYPLESMVVNEYWSMREEC------------FSSGNMGCLMT----------GEDVLKERGLDKDT-RWINVGI 608
Cdd:TIGR00956 595 YYVNPLAYAFESLMVNEFHGRRFECsqyvpsgggydnLGVTNKVCTVVgaepgqdyvdGDDYLKLSFQYYNShKWRNFGI 674
|
650
....*....|.
gi 1063732797 609 MLAFFVFYRIL 619
Cdd:TIGR00956 675 IIGFTVFFFFV 685
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
75-287 |
7.12e-60 |
|
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: 199.42 E-value: 7.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRV-NHKALdpSSAVLMNNRKITDYnQLRRLCGFVPQDDDLLPLLTV 153
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeGGGTT--SGQILFNGQPRKPD-QFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 154 KETLMYSAKFSL-RDSTAKEREERVE-SLLSDLGLVLVQDSFVgegdeedRGVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVEdVLLRDLALTRIGGNLV-------KGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 232 SGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPSYRILDYISDYLILSRGSVIHLG 287
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRN-RIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
60-287 |
1.15e-58 |
|
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: 195.08 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINH------TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALdpSSAVLMNNRKITDyNQ 133
Cdd:cd03213 3 TLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV--SGEVLINGRPLDK-RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLCGFVPQDDDLLPLLTVKETLMYSAKFslrdstakereervesllsdlglvlvqdsfvgegdeedRGVSGGERKRVS 213
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRETLMFAAKL--------------------------------------RGLSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkQRTVLFSIHQPSYRILDYISDYLILSRGSVIHLG 287
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
65-576 |
5.35e-49 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 184.93 E-value: 5.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTI----NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDpSSAVLMNNRKITDYNQlrRLCGF 140
Cdd:TIGR00956 764 NLTYEVkikkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVIT-GGDRLVNGRPLDSSFQ--RSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLLTVKETLMYSAKFSLRDS-TAKEREERVESLLSDLGLVLVQDSFVGEGDEedrGVSGGERKRVSIAVEMI 219
Cdd:TIGR00956 841 VQQQDLHLPTSTVRESLRFSAYLRQPKSvSKSEKMEYVEEVIKLLEMESYADAVVGVPGE---GLNVEQRKRLTIGVELV 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 220 RDPPILL-LDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPSYRILDYISDYLILSRGS-VIHLGSL-------- 289
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIHQPSAILFEEFDRLLLLQKGGqTVYFGDLgenshtii 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 290 EHLEDSIAKlgfQIPEQLNPIEFAMEIV-------------ESLRT---FKPNSVAVVESSSMwPENNENDGIISKKEAF 353
Cdd:TIGR00956 997 NYFEKHGAP---KCPEDANPAEWMLEVIgaapgahanqdyhEVWRNsseYQAVKNELDRLEAE-LSKAEDDNDPDALSKY 1072
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 354 RVLDVTEISYLCSRFCKIIYRTKQLFLARTMQAVVAGLGLGSVYTRLKRDEEGVAERlgLFAFSLSFLLSSTV--EALPI 431
Cdd:TIGR00956 1073 AASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQ--MFAVFMATVLFNPLiqQYLPP 1150
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 432 YLRERRVL-MKESSRGSYRISSYMIANTIAFVPFLFVVSLLFSIPVYWIVGL----NPSIQAFSFFVLcVWLIILM---- 502
Cdd:TIGR00956 1151 FVAQRDLYeVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnaSKTGQVHERGVL-FWLLSTMffly 1229
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 503 ASSLVLFLSAVSPDFISGNSLICTVLGAFFLFSGYFIPKEKIPKPWMFMYYVSLYRYPLESMVVNEYWSMREEC 576
Cdd:TIGR00956 1230 FSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTC 1303
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
61-294 |
4.45e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKI-TDYNQLRRLC 138
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG-----LLRPTSgEVRVLGEDVaRDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEM 218
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFAR--LYGLPRKEARERIDELLELFGLTDAADRKVGT-------LSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLGSLE-----H 291
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEeaERLCDRV---AIIDKGRIVADGTPDelkarL 222
|
...
gi 1063732797 292 LED 294
Cdd:COG1131 223 LED 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
61-298 |
1.58e-47 |
|
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: 166.96 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDYN-QLRRLC 138
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-----LKPDSgSILIDGEDVRKEPrEARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEM 218
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAE--LYGLFDEELKKRIEELIELLGLEEFLDRRVGE-------LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLGSLEHLEDSI 296
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQevEALCDRV---VILHKGKVVAQGSLDELREEI 223
|
..
gi 1063732797 297 AK 298
Cdd:COG4555 224 GE 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
61-304 |
6.57e-46 |
|
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: 162.91 E-value: 6.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN--QLRRL 137
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG-----LLKPSSgEVLLDGRDLASLSrrELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDDDLLPLLTVKETLMY--SAKFSLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRV 212
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgrYPHLGLFGRPSAEDREAVEEALERTGL----------EHLADRPVdelSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLGSLE 290
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNlaARYADRL---VLLKDGRIVAQGPPE 223
|
250
....*....|....*.
gi 1063732797 291 HL--EDSIAKLgFQIP 304
Cdd:COG1120 224 EVltPELLEEV-YGVE 238
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
364-567 |
7.89e-45 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 158.59 E-value: 7.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 364 LCSRFCKIIYRTKQLFLARTMQAVVAGLGLGSVYTRLKrDEEGVAERLGLFAFSLSFLLSSTV-EALPIYLRERRVLMKE 442
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALsGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 443 SSRGSYRISSYMIANTIAFVPFLFVVSLLFSIPVYWIVGLNPSIQAFSFFVLCVWLIILMASSLVLFLSAVSPDFISGNS 522
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063732797 523 LICTVLGAFFLFSGYFIPKEKIPKPWMFMYYVSLYRYPLESMVVN 567
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
75-619 |
8.57e-45 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 172.34 E-value: 8.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhKALDPSSAVLMNNRKITDYNQlRRLCGFVPQDDDLLPLLTVK 154
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLD-PSLKVSGEITYNGYRLNEFVP-RKTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 155 ETLMYSAKFS--------LRDSTAKERE------------------ERVES-LLSD-----LGLVLVQDSFVGegDEEDR 202
Cdd:PLN03140 258 ETLDFSARCQgvgtrydlLSELARREKDagifpeaevdlfmkatamEGVKSsLITDytlkiLGLDICKDTIVG--DEMIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 GVSGGERKRVSIAvEMIRDP-PILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRILDYISDYLILSRG 281
Cdd:PLN03140 336 GISGGQKKRVTTG-EMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 282 SVIHLGSLEHLEDSIAKLGFQIPEQLNPIEFAMEI----------VESLRTFKPNSVAVVESS------SMWPENNEN-- 343
Cdd:PLN03140 415 QIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVtskkdqeqywADRNKPYRYISVSEFAERfksfhvGMQLENELSvp 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 344 -DGIISKKEA--FRVLDVTEISYLCSRFCK---IIYRTKQLFLARTMQAVVAGLGLGSVYTRLK---RDEEGVAERLGLF 414
Cdd:PLN03140 495 fDKSQSHKAAlvFSKYSVPKMELLKACWDKewlLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEmhtRNEEDGALYIGAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 415 AFSL------SFL-LSSTVEALPIYLRERRVLMKESsrGSYRISSYMIAntiafVPFLFVVSLLFSIPVYWIVGLNPSIQ 487
Cdd:PLN03140 575 LFSMiinmfnGFAeLALMIQRLPVFYKQRDLLFHPP--WTFTLPTFLLG-----IPISIIESVVWVVITYYSIGFAPEAS 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 488 AFSFFVLCVWLIILMASSLVLFLSAVSPDFISGNSLICTVLGAFFLFSGYFIPKEKIPKPWMFMYYVSLYRYPLESMVVN 567
Cdd:PLN03140 648 RFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVN 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 568 EYWSMR-EECFSSGNMGCLmtGEDVLKERGL--DKDTRWINVGIMLAFFVFYRIL 619
Cdd:PLN03140 728 EMFAPRwMNKMASDNSTRL--GTAVLNIFDVftDKNWYWIGVGALLGFTILFNVL 780
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
61-274 |
1.08e-44 |
|
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: 158.42 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYT----INHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYN-- 132
Cdd:cd03255 1 IELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG------LDRPTSgeVRVDGTDISKLSek 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 ---QLRRL-CGFVPQDDDLLPLLTVKETLMYSAKFSLRDStaKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGE 208
Cdd:cd03255 75 elaAFRRRhIGFVFQSFNLLPDLTALENVELPLLLAGVPK--KERRERAEELLERVGLGDRLNHYPSE-------LSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSY-----RILdYISD 274
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELaeyadRII-ELRD 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
61-262 |
9.27e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.36 E-value: 9.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI----NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSS-AVLMNNRKITDYN-- 132
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG------LDrPTSgEVLIDGQDISSLSer 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 QLRRL----CGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGE 208
Cdd:COG1136 79 ELARLrrrhIGFVFQFFNLLPELTALENVALPLL--LAGVSRKERRERARELLERVGLGDRLDHRPSQ-------LSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
75-569 |
3.62e-42 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 164.25 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaldPSSAVLMNNRKITDYNQLR----RLCGFVPQDDDLLPL 150
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR-------KTGGYIEGDIRISGFPKKQetfaRISGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETLMYSAKFSLRDSTAKEREER-VESLLSDLGLVLVQDSFVGEGDEEdrGVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:PLN03140 968 VTVRESLIYSAFLRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGLPGVT--GLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 230 PTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPSYRILDYISDYLILSR-GSVIHLGSL--------EHLEdSIAKLG 300
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTG-RTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnshkiiEYFE-AIPGVP 1123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 301 fQIPEQLNPIEFAMEIveslrtfkpNSVAVVESSSM-WPENNENDGIISKKEAFrvldVTEIS---------YLCSRFCK 370
Cdd:PLN03140 1124 -KIKEKYNPATWMLEV---------SSLAAEVKLGIdFAEHYKSSSLYQRNKAL----VKELStpppgasdlYFATQYSQ 1189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 371 II---------------YRTKQLFLARTMQAVVAGLGLGSVYTRL--KRDEEG-VAERLGLFAFSLSFL---LSSTVEal 429
Cdd:PLN03140 1190 STwgqfksclwkqwwtyWRSPDYNLVRFFFTLAAALMVGTIFWKVgtKRSNANdLTMVIGAMYAAVLFVginNCSTVQ-- 1267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 430 PIYLRERRVLMKESSRGSYRISSYMIANTIAFVPFLFVVSLLFSIPVYWIVGLNPSIQAFSFFVLCVWLIILMASSLVLF 509
Cdd:PLN03140 1268 PMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMM 1347
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 510 LSAVSPDFISGNSLICTVLGAFFLFSGYFIPKEKIPKPWMFMYYVSLYRYPLESMVVNEY 569
Cdd:PLN03140 1348 TVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQY 1407
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
60-281 |
4.53e-41 |
|
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: 147.77 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTIN----HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkALDPSSAVLMNNRKITDYnqLR 135
Cdd:cd03232 3 VLTWKNLNYTVPvkggKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVITGEILINGRPLDKN--FQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLLTVKETLMYSAKFslrdstakereervesllsdlglvlvqdsfvgegdeedRGVSGGERKRVSIA 215
Cdd:cd03232 79 RSTGYVEQQDVHSPNLTVREALRFSALL--------------------------------------RGLSVEQRKRLTIG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPSYRILDYISDYLILSRG 281
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
61-258 |
1.27e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.49 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYN--QLRR 136
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD------LDPPTSgeIYLDGKPLSAMPppEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLlTVKETLMYSakFSLRDSTAKEreERVESLLSDLGLvlvQDSFVgegdeeDRGV---SGGERKRVS 213
Cdd:COG4619 75 QVAYVPQEPALWGG-TVRDNLPFP--FQLRERKFDR--ERALELLERLGL---PPDIL------DKPVerlSGGERQRLA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVL 258
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVL 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
62-287 |
3.32e-38 |
|
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: 139.49 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 62 TVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN--QLRRLC 138
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG-----LLKPSSgEILLDGKDLASLSpkELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQdddllplltvketlmysakfslrdstakereervesLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRVSIA 215
Cdd:cd03214 76 AYVPQ------------------------------------ALELLGL----------AHLADRPFnelSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLG 287
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNlaARYADRV---ILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
63-281 |
4.23e-38 |
|
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: 140.29 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINH--TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDYN--QLRRL 137
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSgEVLVDGKDLTKLSlkELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQD-DDLLPLLTVKETLMYSAKFSLRDstAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAV 216
Cdd:cd03225 77 VGLVFQNpDDQFFGPTVEEEVAFGLENLGLP--EEEIEERVEEALELVGLEGLRDRSPFT-------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPSYrILDYISDYLILSRG 281
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDL-LLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
61-288 |
6.33e-38 |
|
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: 140.16 E-value: 6.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI-NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN--QLRR 136
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-----LLKPTSgEVLVDGKDITKKNlrELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQD-DDLLPLLTVKETLMysakFSLRDS--TAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERK 210
Cdd:COG1122 76 KVGLVFQNpDDQLFAPTVEEDVA----FGPENLglPREEIRERVEEALELVGL----------EHLADRPPhelSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLGS 288
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGT 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
55-259 |
2.58e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 55 TPNRYSLTVTNLSYT----INHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKI 128
Cdd:COG1116 2 SAAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG------LEKPTSgeVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 TdynQLRRLCGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGE 208
Cdd:COG1116 76 T---GPGPDRGVVFQEPALLPWLTVLDNVALGLE--LRGVPKAERRERARELLELVGLAGFEDAYPHQ-------LSGGM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLDS--RNSLQvvELLATMAKSKQRTVLF 259
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDAltRERLQ--DELLRLWQETGKTVLF 194
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
61-262 |
3.88e-37 |
|
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: 137.60 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYT----INHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITdynQLR 135
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-----LERPTSgEVLVDGEPVT---GPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIA 215
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLE--LQGVPKAEARERAEELLELVGLSGFENAYPHQ-------LSGGMRQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDS--RNSLQvvELLATMAKSKQRTVLFSIH 262
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDAltREQLQ--EELLDIWRETGKTVLLVTH 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
61-292 |
1.29e-36 |
|
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: 136.48 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSS-AVLMNNRKI-TDYNQLRR 136
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-----PTSgTAYINGYSIrTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAV 216
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYAR--LKGLPKSEIKEEVELLLRVLGLTDKANKRART-------LSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHqpSYRILDYISDYL-ILSRGSVIHLGSLEHL 292
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTH--SMDEAEALCDRIaIMSDGKLRCIGSPQEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
61-292 |
3.28e-36 |
|
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: 142.35 E-value: 3.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYT-----INHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN-- 132
Cdd:COG1123 261 LEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-----LLRPTSgSILFDGKDLTKLSrr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 ---QLRRLCGFVPQDDD--LLPLLTVKETLMYSAKFsLRDSTAKEREERVESLLSDLGLvlvqdsfvgegDEEDRGV--- 204
Cdd:COG1123 336 slrELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRL-HGLLSRAERRERVAELLERVGL-----------PPDLADRyph 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 205 --SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHqpsyrilD-----YISDY-L 276
Cdd:COG1123 404 elSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH-------DlavvrYIADRvA 476
|
250
....*....|....*.
gi 1063732797 277 ILSRGSVIHLGSLEHL 292
Cdd:COG1123 477 VMYDGRIVEDGPTEEV 492
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
52-292 |
3.72e-36 |
|
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: 142.98 E-value: 3.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPTPNRYSLTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKI 128
Cdd:COG4987 325 PAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR-----FLDPQSgSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 TDYN--QLRRLCGFVPQDDDLLpLLTVKETLMysakfsLRDSTAKERE-----ERV--ESLLSDL--GLvlvqDSFVGEG 197
Cdd:COG4987 400 RDLDedDLRRRIAVVPQRPHLF-DTTLRENLR------LARPDATDEElwaalERVglGDWLAALpdGL----DTWLGEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 198 deeDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAksKQRTVLFSIHQPSyrILDYISDYLI 277
Cdd:COG4987 469 ---GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLA--GLERMDRILV 541
|
250
....*....|....*
gi 1063732797 278 LSRGSVIHLGSLEHL 292
Cdd:COG4987 542 LEDGRIVEQGTHEEL 556
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
76-232 |
7.55e-36 |
|
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: 131.62 E-value: 7.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDYN--QLRRLCGFVPQDDDLLPLLT 152
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL-----LSPTEgTILLDGQDLTDDErkSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 153 VKETLMYSAKFSLRDSTAKEReeRVESLLSDLGLVLVQDSFVGEGDeedRGVSGGERKRVSIAVEMIRDPPILLLDEPTS 232
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDA--RAEEALEKLGLGDLADRPVGERP---GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
63-295 |
3.70e-35 |
|
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: 132.63 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKIT-----DYNQLRR 136
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL-----LRPDSgEVLIDGEDISglseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMysakFSLRDSTA---KEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVS 213
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVA----FPLREHTRlseEEIREIVLEKLEAVGLRGAEDLYPAE-------LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQ--PSYRILDYIsdyLILSRGSVIHLGSLEH 291
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDldTAFAIADRI---AVLYDGKIVAEGTPEE 223
|
....
gi 1063732797 292 LEDS 295
Cdd:cd03261 224 LRAS 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
61-289 |
1.21e-34 |
|
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: 131.09 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI----NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQ-- 133
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-----LLKPTSgSIIFDGKDLLKLSRrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 ---LRRLCGFVPQDDD--LLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLVL-VQDSFVGEgdeedrgVSGG 207
Cdd:cd03257 77 rkiRRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHE-------LSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 208 ERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyrILDYISDYLIlsrgsVIHLG 287
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLG--VVAKIADRVA-----VMYAG 222
|
..
gi 1063732797 288 SL 289
Cdd:cd03257 223 KI 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
61-295 |
1.40e-34 |
|
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: 131.26 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKIT-----DYNQL 134
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL-----LRPDSgEILVDGQDITglsekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMysakFSLR---DSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKR 211
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVA----FPLRehtDLSEAEIRELVLEKLELVGLPGAADKMPSE-------LSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH--QPSYRILDYIsdyLILSRGSVIHLGSL 289
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHdlDSAFAIADRV---AVLADGKIIAEGTP 226
|
....*.
gi 1063732797 290 EHLEDS 295
Cdd:COG1127 227 EELLAS 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
61-287 |
2.20e-34 |
|
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: 130.01 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSkILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQ-LRRLC 138
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAT-----LTPPSSgTIRIDGQDVLKQPQkLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAkfSLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRVSIA 215
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIA--WLKGIPSKEVKARVDEVLELVNL----------GDRAKKKIgslSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIHQPSyRILDYISDYLILSRGSVIHLG 287
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
61-275 |
4.19e-34 |
|
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: 128.75 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITD-YNQLRRLC 138
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-----LLPPSAgEVLWNGEPIRDaREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKFSLRDSTakerEERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEM 218
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALYGLRAD----REAIDEALEAVGLAGLADLPVRQ-------LSAGQKRRVALARLL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQP----SYRILDyISDY 275
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQPlelaAARVLD-LGDF 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
61-291 |
7.20e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 7.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITdynQLRRLCG 139
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG-----LLPPTSgTVRLFGKPPR---RARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQD---DDLLPLlTVKETLM---YSAKFSLRDSTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVS 213
Cdd:COG1121 79 YVPQRaevDWDFPI-TVRDVVLmgrYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGE-------LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSyRILDYISDYLILSRGsVIHLGSLEH 291
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLG-AVREYFDRVLLLNRG-LVAHGPPEE 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
61-283 |
9.86e-34 |
|
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: 126.74 E-value: 9.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKI-TDYNQLRRLC 138
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG-----LLKPDSgEIKVLGKDIkKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYsakfslrdstakereervesllsdlglvlvqdsfvgegdeedrgvSGGERKRVSIAVEM 218
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL---------------------------------------------SGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHqpsyrILDYISDY----LILSRGSV 283
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSH-----ILEEAERLcdrvAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-292 |
1.26e-33 |
|
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: 135.66 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 10 MASCFHPSAMATSHREEdsiiLFSASNSPDEFSSASSSfsssPLPTPNRYSLTVTNLSYT-INHTPILNSVSLAAESSKI 88
Cdd:COG4988 294 LGSFYHARANGIAAAEK----IFALLDAPEPAAPAGTA----PLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 89 LAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDYN--QLRRLCGFVPQDDDLLPLlTVKETLMysakFSL 165
Cdd:COG4988 366 VALVGPSGAGKSTLLNLLLGF-----LPPYSgSILINGVDLSDLDpaSWRRQIAWVPQNPYLFAG-TIRENLR----LGR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 166 RDSTAKEREE-----RVESLLSDL--GLvlvqDSFVGEGDeedRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRN 238
Cdd:COG4988 436 PDASDEELEAaleaaGLDEFVAALpdGL----DTPLGEGG---RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 239 SLQVVELLATMAksKQRTVLFSIHQPSY-RILDYIsdyLILSRGSVIHLGSLEHL 292
Cdd:COG4988 509 EAEILQALRRLA--KGRTVILITHRLALlAQADRI---LVLDDGRIVEQGTHEEL 558
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
61-287 |
2.10e-33 |
|
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: 127.25 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYNQLRRLC 138
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG------LERPDSgeILIDGRDVTGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEM 218
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLK--LRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 219 IRDPPILLLDEPTSGLD--SRNSLQvvELLATMAKSKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLG 287
Cdd:cd03259 146 AREPSLLLLDEPLSALDakLREELR--EELKELQRELGITTIYVTHDQEeaLALADRI---AVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
61-278 |
2.41e-33 |
|
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: 125.76 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD--PSSAVLMNNRKITDYNQ----L 134
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG------LEepDSGSILIDGEDLTDLEDelppL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYsakfslrdstakereervesllsdlglvlvqdsfvgegdeedrGVSGGERKRVSI 214
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIAL-------------------------------------------GLSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYriLDYISDYLIL 278
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDE--AARLADRVVV 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
63-285 |
6.53e-33 |
|
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: 125.72 E-value: 6.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDynqLRRLCGFV 141
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG-----LLKPTSgSIRVFGKPLEK---ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 142 PQDDDLLPL--LTVKETLM---YSAKFSLRDSTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAV 216
Cdd:cd03235 74 PQRRSIDRDfpISVRDVVLmglYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIGE-------LSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIH 285
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLG-LVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
62-278 |
6.54e-32 |
|
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: 121.20 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 62 TVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHkaldPSSAVLMNNRKITDYN--QLRRLCG 139
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEILIDGKDIAKLPleELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQdddllplltvketlmysakfslrdstakereervesllsdlglvlvqdsfvgegdeedrgVSGGERKRVSIAVEMI 219
Cdd:cd00267 77 YVPQ------------------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYriLDYISDYLIL 278
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPEL--AELAADRVIV 152
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
61-292 |
8.46e-32 |
|
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: 123.76 E-value: 8.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI----NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKIT--DYN 132
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG------LERPWSgeVTFDGRPVTrrRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 QLRRLCGFVPQD--DDLLPLLTVKETLMYSAKFSLRDstakEREERVESLLSDLGLvlvqdsfvgegDEEDRG-----VS 205
Cdd:COG1124 76 AFRRRVQMVFQDpyASLHPRHTVDRILAEPLRIHGLP----DREERIAELLEQVGL-----------PPSFLDryphqLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 206 GGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPsyRILDYISDY-LILSRGSVI 284
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDL--AVVAHLCDRvAVMQNGRIV 218
|
....*...
gi 1063732797 285 HLGSLEHL 292
Cdd:COG1124 219 EELTVADL 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
67-287 |
2.05e-31 |
|
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: 121.22 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 67 SYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKaLDPSSAVLMNNRKITD-YNQLRRLCGFVPQDD 145
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-VSVEGDIHYNGIPYKEfAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 DLLPLLTVKETLmysaKFSLRdstakereervesllsdlglvlvqdsfvGEGDEEDRGVSGGERKRVSIAVEMIRDPPIL 225
Cdd:cd03233 93 VHFPTLTVRETL----DFALR----------------------------CKGNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 226 LLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRILDYISDYLILSRGSVIHLG 287
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
60-292 |
2.29e-31 |
|
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: 129.95 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN--QL 134
Cdd:COG2274 473 DIELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-----LYEPTSgRILIDGIDLRQIDpaSL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPlLTVKETLmysakfSLRDSTAkeREERVESLLSDLGL--VLVQ-----DSFVGEGdeeDRGVSGG 207
Cdd:COG2274 548 RRQIGVVLQDVFLFS-GTIRENI------TLGDPDA--TDEEIIEAARLAGLhdFIEAlpmgyDTVVGEG---GSNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 208 ERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAksKQRTVLFSIHQPSY-RILDYIsdyLILSRGSVIHL 286
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTiRLADRI---IVLDKGRIVED 690
|
....*.
gi 1063732797 287 GSLEHL 292
Cdd:COG2274 691 GTHEEL 696
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
72-292 |
2.52e-31 |
|
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: 121.95 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSS-AVLMNNRKITDYNQ--LRRLCGFVPQDddll 148
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-----FRFYDVSSgSILIDGQDIREVTLdsLRRAIGVVPQD---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 pllTV--KETLMYSAKFSLRDSTAKEREERVEslLSDLGLVLVQ-----DSFVGEgdeedRGV--SGGERKRVSIAVEMI 219
Cdd:cd03253 84 ---TVlfNDTIGYNIRYGRPDATDEEVIEAAK--AAQIHDKIMRfpdgyDTIVGE-----RGLklSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIHQPSyRILDyiSDYLI-LSRGSVIHLGSLEHL 292
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLS-TIVN--ADKIIvLKDGRIVERGTHEEL 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
71-262 |
2.92e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.31 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN-----QLRRLCGFVPQD 144
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG-----EERPTSgQVLVNGQDLSRLKrreipYLRRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 145 DDLLPLLTVKETLMysakFSLRDSTAKERE--ERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDP 222
Cdd:COG2884 88 FRLLPDRTVYENVA----LPLRVTGKSRKEirRRVREVLDLVGLSDKAKALPHE-------LSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063732797 223 PILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIH 262
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATH 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
73-290 |
1.00e-30 |
|
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: 120.57 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 73 TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvNHKALDPSSAVLMNNRKITDYNQLRRLCGFVPQD--DDLLPL 150
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD-LPPTYGNDVRLFGERRGGEDVWELRKRIGLVSPAlqLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETLMySAKFS----LRDSTAKEREeRVESLLSDLGLvlvqdsfvgeGDEEDR---GVSGGERKRVSIAVEMIRDPP 223
Cdd:COG1119 95 ETVLDVVL-SGFFDsiglYREPTDEQRE-RARELLELLGL----------AHLADRpfgTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLGSLE 290
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAGPKE 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
61-296 |
1.45e-30 |
|
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: 119.98 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH-TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVL------MNNRKITDYNQ 133
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG-----LVEPTSGSVlidgtdINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLCGFVPQDDDLLPLLTVKETLM-----YSAKF-SLRDSTAKEREERVESLLSDLGLVlvqDSFVGEGDEedrgVSGG 207
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLsgrlgRRSTWrSLFGLFPKEEKQRALAALERVGLL---DKAYQRADQ----LSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 208 ERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLG 287
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDL-AREYADRIVGLKDGRIVFDG 227
|
....*....
gi 1063732797 288 SLEHLEDSI 296
Cdd:cd03256 228 PPAELTDEV 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
60-291 |
1.50e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.12 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDP----SSAVLMNNRKITDYNQLR 135
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG-----TLSPafsaSGEVLLNGRRLTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLLTVKETLMysakFSLRDSTAK-EREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSI 214
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLA----FALPPTIGRaQRRARVEQALEEAGLAGFADRDPAT-------LSGGQRARVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyrilDyisdylILSRGSVIHLGSLEH 291
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE----D------APAAGRVLDLGNWQH 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
52-272 |
9.34e-30 |
|
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: 123.55 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPTPNRYSLTVTNLSYTI-NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkalDPSS-AVLMNNRKIT 129
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV-----DPTEgSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 DYNQ--LRRLCGFVPQdddlLPLL---TVKETLmysaKFSLRDSTAKEREERVE-----SLLSDLGLVLvqDSFVGEGDe 199
Cdd:TIGR02857 388 DADAdsWRDQIAWVPQ----HPFLfagTIAENI----RLARPDASDAEIREALEragldEFVAALPQGL--DTPIGEGG- 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 200 edRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIHQPSYRIL-DYI 272
Cdd:TIGR02857 457 --AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALaDRI 526
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
61-292 |
1.37e-29 |
|
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: 116.90 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSS-AVLMNNRKITDYNQ----LR 135
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgEVLLDGKDIYDLDVdvleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLlTVKETLMYSAKfsLRDS-TAKEREERVESLLSDLGLvlvqdsfvgeGDEEDR-----GVSGGER 209
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLR--LHGIkLKEELDERVEEALRKAAL----------WDEVKDrlhalGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 210 KRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAksKQRTVLFSIH--QPSYRILDYIsdyLILSRGSVIHLG 287
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHnmQQAARVADRT---AFLLNGRLVEFG 222
|
....*
gi 1063732797 288 SLEHL 292
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
76-303 |
1.50e-29 |
|
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: 117.05 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYNQLRRLCGFVPQDDDLLPLLTVK 154
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAG-----FIKPDSGkILLNGKDITNLPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 155 ETLMYSAKFSLRDStaKEREERVESLLSDLGL--VLvqdsfvgegDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTS 232
Cdd:cd03299 90 KNIAYGLKKRKVDK--KEIERKVLEIAEMLGIdhLL---------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 233 GLDSRNSLQVVELLATMAKSKQRTVLFSIH-QPSYRIL-DYIsdyLILSRGSVIHLGSLEHL-----EDSIAK-LGFQI 303
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHdFEEAWALaDKV---AIMLNGKLIQVGKPEEVfkkpkNEFVAEfLGFNN 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
61-299 |
1.65e-29 |
|
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: 122.70 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH--TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAlDPSSAVLMNNRKITDYN--QLRR 136
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG-RISGEVLLDGRDLLELSeaLRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQD-DDLLPLLTVKETLMysakFSLR--DSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVS 213
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIA----EALEnlGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLGSLEHLE 293
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEIL 231
|
....*.
gi 1063732797 294 DSIAKL 299
Cdd:COG1123 232 AAPQAL 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
62-251 |
2.42e-29 |
|
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: 115.43 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 62 TVTNLSYTINHTP-ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITdYNQLRRLCG 139
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-----LIKESSGsILLNGKPIK-AKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQD-DDLLPLLTVKETLMYSAKfslrdsTAKEREERVESLLSDLGLVlvqdsfvGEGDEEDRGVSGGERKRVSIAVEM 218
Cdd:cd03226 75 YVMQDvDYQLFTDSVREELLLGLK------ELDAGNEQAETVLKDLDLY-------ALKERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190
....*....|....*....|....*....|...
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAK 251
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAA 174
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
61-265 |
3.05e-29 |
|
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: 114.02 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHT--PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQ--LR 135
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR-----LYDPTSgEILIDGVDLRDLDLesLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDddllplltvkeTLMYSAkfSLRdstakereervESLLsdlglvlvqdsfvgegdeedrgvSGGERKRVSIA 215
Cdd:cd03228 76 KNIAYVPQD-----------PFLFSG--TIR-----------ENIL-----------------------SGGQRQRIAIA 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPS 265
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLS 156
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
67-292 |
7.74e-29 |
|
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: 115.02 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 67 SYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSS-AVLMNNRKITDY--NQLRRLCGFVPQ 143
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-----RFYDVDSgRILIDGHDVRDYtlASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 144 DddllPLL---TVKETLMYSAkfslRDSTAKERE---------ERVESLlsDLGLvlvqDSFVGEgdeedRGV--SGGER 209
Cdd:cd03251 84 D----VFLfndTVAENIAYGR----PGATREEVEeaaraanahEFIMEL--PEGY----DTVIGE-----RGVklSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 210 KRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIHQPS-YRILDYIsdyLILSRGSVIHLGS 288
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLStIENADRI---VVLEDGKIVERGT 219
|
....
gi 1063732797 289 LEHL 292
Cdd:cd03251 220 HEEL 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
54-262 |
2.20e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.93 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 54 PTPNRYSLTVTNLSYTI--NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSA-VLMNNRKITD 130
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-----RAWDPQQGeILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 131 YN--QLRRLCGFVPQDDDLLPLlTVKETLMYsAKFSLRDSTAKEREERV--ESLL-SDLGLvlvqDSFVGEGDeedRGVS 205
Cdd:PRK11160 407 YSeaALRQAISVVSQRVHLFSA-TLRDNLLL-AAPNASDEALIEVLQQVglEKLLeDDKGL----NAWLGEGG---RQLS 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 206 GGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqrTVLFSIH 262
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITH 532
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
60-245 |
2.70e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.35 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDynqL---R 135
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-----FETPDSgRILLDGRDVTG---LppeK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRV 212
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLR--MRGVPKAEIRARVAELLELVGL----------EGLADRYPhqlSGGQQQRV 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDS--RNSLQvVEL 245
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAklREEMR-EEL 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
69-292 |
4.14e-28 |
|
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: 112.67 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 69 TINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSS-AVLMNNRKITDYN-----QLRRLCGFV 141
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING------LErPTSgSVLVDGTDLTLLSgkelrKARRRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 142 PQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSdlglvlvqdsFVGEGDEEDR---GVSGGERKRVSIAVEM 218
Cdd:cd03258 88 FQHFNLLSSRTVFENVALPLE--IAGVPKAEIEERVLELLE----------LVGLEDKADAypaQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSY--RILDYIsdyLILSRGSVIHLGSLEHL 292
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVvkRICDRV---AVMEKGEVVEEGTVEEV 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
71-262 |
5.24e-28 |
|
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: 111.73 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkALDPSSAVLMNNRKITDYNQ-----LRRLCGFVPQDD 145
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE----ELPTSGTIRVNGQDVSDLRGraipyLRRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 DLLPLLTVKETLMysakFSLRDSTAKERE--ERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPP 223
Cdd:cd03292 88 RLLPDRNVYENVA----FALEVTGVPPREirKRVPAALELVGLSHKHRALPAE-------LSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELlatMAKSKQR--TVLFSIH 262
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNL---LKKINKAgtTVVVATH 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
60-288 |
1.35e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.09 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRV--NHKaldpssaVLMNNRKItd 130
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdSGRIvlNGR-------DLFTNLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 131 ynQLRRlCGFVPQDDDLLPLLTVKETLMysakFSLRD--STAKEREERVESLLSdlglvLVQ-DSFvgegdeEDR---GV 204
Cdd:COG1118 73 --RERR-VGFVFQHYALFPHMTVAENIA----FGLRVrpPSKAEIRARVEELLE-----LVQlEGL------ADRypsQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 205 SGGERKRVSIAVEMIRDPPILLLDEPTSGLDS--RNSL--QVVELLATMakskQRTVLFSIHQP--SYRILDYIsdyLIL 278
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDAkvRKELrrWLRRLHDEL----GGTTVFVTHDQeeALELADRV---VVM 207
|
250
....*....|
gi 1063732797 279 SRGSVIHLGS 288
Cdd:COG1118 208 NQGRIEQVGT 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
61-292 |
3.03e-27 |
|
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: 110.47 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH-TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSS-AVLMNNRKITDYN--QLRR 136
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN-----RLIEPTSgEIFIDGEDIREQDpvELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLmySAKFSLRDSTAKEREERVESLLSDLGLvlvqdsfvGEGDEEDR---GVSGGERKRVS 213
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENI--ALVPKLLKWPKEKIRERADELLALVGL--------DPAEFADRyphELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLD--SRNSLQvvELLATMAKSKQRTVLFSIH--QPSYRILDYISdylILSRGSVIHLGSL 289
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDpiTRDQLQ--EEFKRLQQELGKTIVFVTHdiDEAFRLADRIA---IMKNGEIVQVGTP 220
|
...
gi 1063732797 290 EHL 292
Cdd:cd03295 221 DEI 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
61-294 |
3.07e-27 |
|
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: 109.83 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITD---YNQLRR 136
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG-----LLPPRSgSIRFDGRDITGlppHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMYSAkFSLRDSTAKEREERVESLLSDLglvlvqdsfvgegdEEDRG-----VSGGERKR 211
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENLLLGA-YARRRAKRKARLERVYELFPRL--------------KERRKqlagtLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFsIHQPSYRILDyISDY-LILSRGSVIHLGSLE 290
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGV-TILL-VEQNARFALE-IADRaYVLERGRVVLEGTAA 217
|
....
gi 1063732797 291 HLED 294
Cdd:cd03224 218 ELLA 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
85-287 |
4.21e-27 |
|
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: 109.31 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 85 SSKILAVVGPSGTGKSTLLKIISG--RVNHKALDPSSAVLMNNRKITDYNQLRRLCGFVPQDDDLLPLLTVKETLMYSAK 162
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 163 FSLRdstaKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQV 242
Cdd:cd03297 102 RKRN----REDRISVDELLDLLGLDHLLNRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063732797 243 VELLATMAKSKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLG 287
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSeaEYLADRI---VVMEDGRLQYIG 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
61-263 |
5.93e-27 |
|
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: 108.77 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKaldpSSAVLMNNRKIT----DYNQLRR 136
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD----SGTIIIDGLKLTddkkNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMYsAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAV 216
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-------LSGGQQQRVAIAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQ 263
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGM-TMVVVTHE 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
54-292 |
7.83e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.26 E-value: 7.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 54 PTPNRYSLTVTNLSYT-INHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDY 131
Cdd:COG1132 333 LPPVRGEIEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-----YDPTSgRILIDGVDIRDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 NQ--LRRLCGFVPQDDDLLPlLTVKETLMYSAKfslrDSTAKEREE-----RVESLLSDL--GLvlvqDSFVGEgdeedR 202
Cdd:COG1132 408 TLesLRRQIGVVPQDTFLFS-GTIRENIRYGRP----DATDEEVEEaakaaQAHEFIEALpdGY----DTVVGE-----R 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 GV--SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPS-YRILDYIsdyLILS 279
Cdd:COG1132 474 GVnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLStIRNADRI---LVLD 548
|
250
....*....|...
gi 1063732797 280 RGSVIHLGSLEHL 292
Cdd:COG1132 549 DGRIVEQGTHEEL 561
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
60-288 |
1.42e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.95 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDP-SSAVLMNNRKITDY--NQLRR 136
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-----RLLTPqSGTVFLGDKPISMLssRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQdDDLLPL-LTVKETLMY--SAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVS 213
Cdd:PRK11231 77 RLALLPQ-HHLTPEgITVRELVAYgrSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTD-------LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSrnSLQvVELLATMAKSKQR-----TVLFSIHQPSyRILDYIsdyLILSRGSVIHLGS 288
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDI--NHQ-VELMRLMRELNTQgktvvTVLHDLNQAS-RYCDHL---VVLANGHVMAQGT 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
60-235 |
1.77e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.93 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaL-DPSS-AVLMNNRKITDYNQLRRL 137
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG------LeDPTSgEILIGGRDVTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDR---GVSGGERKRVSI 214
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLK--LRKVPKAEIDRRVREAAELLGL----------EDLLDRkpkQLSGGQRQRVAL 144
|
170 180
....*....|....*....|.
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLD 235
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLD 165
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
61-264 |
2.29e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPIlnSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQLRRLCG 139
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAG-----FLPPDSgRILWNGQDLTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLmysaKFSLRDS---TAKEREeRVESLLSDLGLvlvqdsfvgeGDEEDR---GVSGGERKRVS 213
Cdd:COG3840 75 MLFQENNLFPHLTVAQNI----GLGLRPGlklTAEQRA-QVEQALERVGL----------AGLLDRlpgQLSGGQRQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDS--RNSLqvVELLATMAKSKQRTVLFSIHQP 264
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPalRQEM--LDLVDELCRERGLTVLMVTHDP 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
61-235 |
2.55e-26 |
|
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: 107.63 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSS-AVLMNNRKITDYNQLRRL-- 137
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSgKILLDGQDITKLPMHKRArl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 -CGFVPQDDDLLPLLTVKETLMysAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGegdeedrGVSGGERKRVSIAV 216
Cdd:cd03218 76 gIGYLPQEASIFRKLTVEENIL--AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKAS-------SLSGGERRRVEIAR 146
|
170
....*....|....*....
gi 1063732797 217 EMIRDPPILLLDEPTSGLD 235
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
60-303 |
3.55e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKItDYNQLRRLc 138
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI-----LAPDSgEVLWDGEPL-DPEDRRRI- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRVSIA 215
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVYLAR--LKGLSKAEAKRRADEWLERLGL----------GDRANKKVeelSKGNQQKVQLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNslqvVELLATM---AKSKQRTVLFSIHQPSY--RILDYIsdyLILSRGSVIHLGSLE 290
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVN----VELLKDVireLAAKGTTVIFSSHQMELveELCDRI---VIINKGRKVLSGSVD 214
|
250
....*....|...
gi 1063732797 291 HLEDSIAKLGFQI 303
Cdd:COG4152 215 EIRRQFGRNTLRL 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
75-246 |
3.69e-26 |
|
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: 107.13 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSS-AVLMNNRKITDYNQ------LRRLCGFVPQDDD 146
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG------LDrPTSgTVRLAGQDLFALDEdararlRARHVGFVFQSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTVKETLMYSAKfsLRDstAKEREERVESLLSDLGLvlvqdsfvgeGDEED---RGVSGGERKRVSIAVEMIRDPP 223
Cdd:COG4181 101 LLPTLTALENVMLPLE--LAG--RRDARARARALLERVGL----------GHRLDhypAQLSGGEQQRVALARAFATEPA 166
|
170 180
....*....|....*....|...
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELL 246
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLL 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
61-287 |
9.39e-26 |
|
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: 105.53 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHTPI--LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS--AVLMNNRKITDYNQL 134
Cdd:cd03266 2 ITADALTkrFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG-----LLEPDAgfATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGegdeedrGVSGGERKRVSI 214
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAG--LYGLKGDELTARLEELADRLGMEELLDRRVG-------GFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLD---SRNSLQVVELLatmaKSKQRTVLFSIH--QPSYRILDYIsdyLILSRGSVIHLG 287
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDvmaTRALREFIRQL----RALGKCILFSTHimQEVERLCDRV---VVLHRGRVVYEG 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
61-265 |
1.05e-25 |
|
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: 103.84 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI--NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDY--NQLR 135
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG-----LLRPTSgRVRLDGADISQWdpNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPlltvketlmysakfslrDSTAkereervESLLsdlglvlvqdsfvgegdeedrgvSGGERKRVSIA 215
Cdd:cd03246 76 DHVGYLPQDDELFS-----------------GSIA-------ENIL-----------------------SGGQRQRLGLA 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLAtMAKSKQRTVLFSIHQPS 265
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIA-ALKAAGATRIVIAHRPE 157
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
61-265 |
1.09e-25 |
|
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: 105.27 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYtiNHTPIlnSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkALDPSSAVLMNNRKITDYNQLRRLCGF 140
Cdd:cd03298 3 LDKIRFSY--GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGF----ETPQSGRVLINGVDVTAAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLLTVKETLMYSAKFSLRdSTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIR 220
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLK-LTAEDRQ-AIEVALARVGLAGLEKRLPGE-------LSGGERQRVALARVLVR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063732797 221 DPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPS 265
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPE 190
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
71-298 |
1.57e-25 |
|
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: 107.09 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS--AVLMNNRKITDYNQLRRLCGFVPQDDDLL 148
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTT-----LLRPTSgtARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGegdeedrGVSGGERKRVSIAVEMIRDPPILLLD 228
Cdd:TIGR01188 79 EDLTGRENLEMMGR--LYGLPKDEAEERAEELLELFELGEAADRPVG-------TYSGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 229 EPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQpsYRILDYISDYL-ILSRGSVIHLGSLEHLEDSIAK 298
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEEGV-TILLTTHY--MEEADKLCDRIaIIDHGRIIAEGTPEELKRRLGK 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
63-292 |
3.25e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 103.99 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS--AVLMNNRKITDYNQLRRLCGF 140
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT-----LLKPTSgrATVAGHDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSdlglvlvqdsFVGEGDEEDRGV---SGGERKRVSIAVE 217
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHAR--LYGVPGAERRERIDELLD----------FVGLLEAADRLVktySGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH--QPSYRILDYISdylILSRGSVIHLGSLEHL 292
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHymEEAEQLCDRVA---IIDHGRIIAEGTPEEL 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
60-292 |
3.66e-25 |
|
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: 104.66 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkALDpSSAVLMNNRKITD---YNQLRR 136
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLV---RPD-AGKILIDGQDITHlpmHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMysAKFSLR-DSTAKEREERVESLLSDLGLVLVQDSFVGegdeedrGVSGGERKRVSIA 215
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIM--AVLEIRkDLDRAEREERLEALLEEFQISHLRDNKAM-------SLSGGERRRVEIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRnSLQVVELLATMAKSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIHLGSLEHL 292
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPI-AVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
61-262 |
3.90e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.94 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YT--INHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQLR 135
Cdd:COG4525 4 LTVRHVSvrYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAG-----FLAPSSgEITLDGVPVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 rlcGFVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIA 215
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLR--LRGVPKAERRARAEELLALVGLADFARRRIWQ-------LSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDS--RNSLQvvELLATMAKSKQRTVLFSIH 262
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDAltREQMQ--ELLLDVWQRTGKGVFLITH 193
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
61-251 |
5.07e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDY--NQLRRL 137
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG-----ELTPSSgEVRLNGRPLAAWspWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDDDL-LPLlTVKETLM---YSakfslRDSTAKEREERVESLLSDLGLV-LVQDSFvgegdeedRGVSGGERKRV 212
Cdd:COG4559 77 RAVLPQHSSLaFPF-TVEEVVAlgrAP-----HGSSAAQDRQIVREALALVGLAhLAGRSY--------QTLSGGEQQRV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 213 SIA-V-----EMIRDPP-ILLLDEPTSGLDSRNSLQVVELLATMAK 251
Cdd:COG4559 143 QLArVlaqlwEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLAR 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
60-258 |
6.64e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDYN--QLRR 136
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGE-----LSPDSgEVRLNGRPLADWSpaELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETL-MYSAKFSLRdstAKEREERVESLLSDLGLV-LVQDSFvgegdeedRGVSGGERKRVSI 214
Cdd:PRK13548 77 RRAVLPQHSSLSFPFTVEEVVaMGRAPHGLS---RAEDDALVAAALAQVDLAhLAGRDY--------PQLSGGEQQRVQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 215 AvemiR----------DPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVL 258
Cdd:PRK13548 146 A----RvlaqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVI 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
61-287 |
1.20e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.46 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAldpsSAVLMNNRKI--TDYNQLRRLC 138
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA----GTVLVAGDDVeaLSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETL-MYSAKFSLRDSTAKEREER-VESLLSDLGLvlvqDSFVgegDEEDRGVSGGERKRVSIAV 216
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVeMGRTPHRSRFDTWTETDRAaVERAMERTGV----AQFA---DRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQpsyriLD----YISDYLILSRGSVIHLG 287
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDG-KTAVAAIHD-----LDlaarYCDELVLLADGRVRAAG 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
74-258 |
1.48e-24 |
|
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: 108.37 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSS-AVLMNNRKITDYNQ--LRRLCGFVPQDddllpl 150
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF-----RFYDVTSgRILIDGQDIRDVTQasLRAAIGIVPQD------ 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 lTV--KETLMYSAKFSLRDSTAKEREERVESL-LSDLGLVLVQ--DSFVGEgdeedRGV--SGGERKRVSIAVEMIRDPP 223
Cdd:COG5265 441 -TVlfNDTIAYNIAYGRPDASEEEVEAAARAAqIHDFIESLPDgyDTRVGE-----RGLklSGGEKQRVAIARTLLKNPP 514
|
170 180 190
....*....|....*....|....*....|....*
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVL 258
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARG--RTTL 547
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
61-302 |
1.49e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.84 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSsaVLMNNRKITDYN-QLRRLCG 139
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGS--ILLDGEDILELSpDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 -FV----PQDddlLPLLTVKeTLMYSAKFSLRDS--TAKEREERVESLLSDLGLvlvqdsfvgegDEE--DRGV----SG 206
Cdd:COG0396 79 iFLafqyPVE---IPGVSVS-NFLRTALNARRGEelSAREFLKLLKEKMKELGL-----------DEDflDRYVnegfSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 207 GERKRVSIAVEMIRDPPILLLDEPTSGLDSrNSLQVV-ELLATMaKSKQRTVLFSIHQPsyRILDYIS-DY-LILSRGSV 283
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDI-DALRIVaEGVNKL-RSPDRGILIITHYQ--RILDYIKpDFvHVLVDGRI 219
|
250
....*....|....*....
gi 1063732797 284 IHLGSLEhLEDSIAKLGFQ 302
Cdd:COG0396 220 VKSGGKE-LALELEEEGYD 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
65-284 |
2.27e-24 |
|
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: 101.51 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNrkiTDYNQ-----LRRLC 138
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-----LYKPTSgSVLLDG---TDIRQldpadLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLpLLTVKETLMYSAKFSlrdstakeREERVESLLSDLGL-VLVQ------DSFVGEGDeedRGVSGGERKR 211
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAPLA--------DDERILRAAELAGVtDFVNkhpnglDLQIGERG---RGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqrTVLFSIHQPSyrILDYISDYLILSRGSVI 284
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPS--LLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
64-292 |
2.47e-24 |
|
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: 101.92 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 64 TNLSYtINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN--QLRRLCGF 140
Cdd:cd03254 8 VNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR-----FYDPQKgQILIDGIDIRDISrkSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLlTVKETLMYSakfslRDSTAKEREERVESL--LSDLGLVLVQ--DSFVGEGDEedrGVSGGERKRVSIAV 216
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRLG-----RPNATDEEVIEAAKEagAHDFIMKLPNgyDTVLGENGG---NLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPS-YRILDYIsdyLILSRGSVIHLGSLEHL 292
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLStIKNADKI---LVLDDGKIIEEGTHDEL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
74-264 |
2.75e-24 |
|
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: 107.06 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYNQ--LRRLCGFVPQDDDLLPL 150
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG-----LLDPLQGeVTLDGVPVSSLDQdeVRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 lTVKETLMYSAKfslrDSTAKE-----REERVESLLSDL--GLvlvqDSFVGEGDeedRGVSGGERKRVSIAVEMIRDPP 223
Cdd:TIGR02868 424 -TVRENLRLARP----DATDEElwaalERVGLADWLRALpdGL----DTVLGEGG---ARLSGGERQRLALARALLADAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLAtmAKSKQRTVLFSIHQP 264
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLL--AALSGRTVVLITHHL 530
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
76-291 |
5.59e-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: 100.97 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDY--NQLRRLcG----FvpQDDDLL 148
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG-----FLRPTSgSVLFDGEDITGLppHEIARL-GigrtF--QIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLLTVKETLMYSAKFSLRDSTA--------KEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIR 220
Cdd:cd03219 88 PELTVLENVMVAAQARTGSGLLlararreeREARERAEELLERVGLADLADRPAGE-------LSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 221 DPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLGSLEH 291
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDvvMSLADRV---TVLDQGRVIAEGTPDE 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
74-262 |
8.54e-24 |
|
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: 100.31 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSS-AVLMNNRKITDYN--QLRRLCGFVPQDddllPL 150
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-----ERFYDPTSgEILLDGVDIRDLNlrWLRSQIGLVSQE----PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 L---TVKETLMYSAkfslRDSTAKEREE-----RVESLLSDL--GLvlvqDSFVGEgdeedRGV--SGGERKRVSIAVEM 218
Cdd:cd03249 88 LfdgTIAENIRYGK----PDATDEEVEEaakkaNIHDFIMSLpdGY----DTLVGE-----RGSqlSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIH 262
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAH 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
61-262 |
1.24e-23 |
|
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: 98.15 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI--NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDY-NQLRR 136
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-----DLKPQQGeITLDGVPVSDLeKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQdddllplltvketlmysaKFSLRDSTakereervesLLSDLGlvlvqdsfvgegdeedRGVSGGERKRVSIAV 216
Cdd:cd03247 76 LISVLNQ------------------RPYLFDTT----------LRNNLG----------------RRFSGGERQRLALAR 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqrTVLFSIH 262
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITH 155
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
61-287 |
1.66e-23 |
|
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: 98.89 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDynQLRRLCG 139
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG-----IILPDSGeVLFDGKPLDI--AARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMYSAkfSLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRVSIAV 216
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLA--QLKGLKKEEARRRIDEWLERLEL----------SEYANKRVeelSKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQPSY--RILDyisDYLILSRGSVIHLG 287
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELveELCD---RVLLLNKGRAVLYG 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
52-287 |
2.06e-23 |
|
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: 104.44 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPTPnRYSLTVTNLSYTINHT--PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKI 128
Cdd:COG4618 323 PLPRP-KGRLSVENLTVVPPGSkrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG-----VWPPTAgSVRLDGADL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 TDYN--QLRRLCGFVPQDDDLLPlLTVKETLmysAKFSLRDStakerEERVESL----LSDLGLVLVQ--DSFVGEGdee 200
Cdd:COG4618 397 SQWDreELGRHIGYLPQDVELFD-GTIAENI---ARFGDADP-----EKVVAAAklagVHEMILRLPDgyDTRIGEG--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 201 DRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQPSyrILDYISDYLILSR 280
Cdd:COG4618 465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS--LLAAVDKLLVLRD 541
|
....*..
gi 1063732797 281 GSVIHLG 287
Cdd:COG4618 542 GRVQAFG 548
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
62-288 |
2.28e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.77 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 62 TVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgRVnhkaLDPSS-AVLMNNRKITDY--NQLRRLC 138
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-RL----LPPDSgEVLVDGLDVATTpsRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLM-----YSakfslRDSTAKEREERVESLLSDLGLVLVQDSFVgegDEedrgVSGGERKRVS 213
Cdd:COG4604 78 AILRQENHINSRLTVRELVAfgrfpYS-----KGRLTAEDREIIDEAIAYLDLEDLADRYL---DE----LSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHqpsyrilD------YiSDYLI-LSRGSVIHL 286
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH-------DinfascY-ADHIVaMKDGRVVAQ 217
|
..
gi 1063732797 287 GS 288
Cdd:COG4604 218 GT 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
61-235 |
4.58e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.56 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSS-AVLMNNRKITD---YNQLRR 136
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSgRIFLDGEDITHlpmHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMysAKFSLRDSTAKEREERVESLLSDLGLVLVQDSfvgegdeedRG--VSGGERKRVSI 214
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNIL--AVLELRKLSKKEREERLEELLEEFGITHLRKS---------KAysLSGGERRRVEI 147
|
170 180
....*....|....*....|.
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLD 235
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVD 168
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
73-292 |
6.46e-23 |
|
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: 98.87 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 73 TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkalDPSSA-VLMNNRKITDYN--QLRRL----CGFVPQDD 145
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI-----EPTSGkVLIDGQDIAAMSrkELRELrrkkISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 DLLPLLTVKETLMYSakFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPIL 225
Cdd:cd03294 112 ALLPHRTVLENVAFG--LEVQGVPRAEREERAAEALELVGLEGWEHKYPDE-------LSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 226 LLDEPTSGLDS--RNSLQvVELLATMAKSkQRTVLFSIHQP--SYRILDYISdylILSRGSVIHLGSLEHL 292
Cdd:cd03294 183 LMDEAFSALDPliRREMQ-DELLRLQAEL-QKTIVFITHDLdeALRLGDRIA---IMKDGRLVQVGTPEEI 248
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
76-259 |
7.98e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 98.19 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDY--NQLRRLcG----F-VPQdddL 147
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF-----YRPTSgRILFDGRDITGLppHRIARL-GiartFqNPR---L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 148 LPLLTVKETLM-----------YSAKFSLRDSTAKERE--ERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSI 214
Cdd:COG0411 91 FPELTVLENVLvaaharlgrglLAALLRLPRARREEREarERAEELLERVGLADRADEPAGN-------LSYGQQRRLEI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLF 259
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILL 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
61-249 |
9.77e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.37 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvNHkaLDP--SSAVLMNNRKIT----DYNQL 134
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI----NL--LEEpdSGTITVDGEDLTdskkDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAkEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSI 214
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKA-EAEERAMELLERVGLADKADAYPAQ-------LSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 215 AvemiR----DPPILLLDEPTSGLDSRNS---LQVVELLA----TM 249
Cdd:COG1126 148 A----RalamEPKVMLFDEPTSALDPELVgevLDVMRDLAkegmTM 189
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
61-247 |
9.79e-23 |
|
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: 97.12 E-value: 9.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHT-----PILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRV----NHKALDPSSAvl 122
Cdd:COG4778 5 LEVENLSktFTLHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSIlvrhDGGWVDLAQA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 123 mNNRKITDynqLRR-LCGFVPQDDDLLP----LLTVKETLmysakfsLRDSTAKER-EERVESLLSDLGLvlvqdsfvge 196
Cdd:COG4778 83 -SPREILA---LRRrTIGYVSQFLRVIPrvsaLDVVAEPL-------LERGVDREEaRARARELLARLNL---------- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 197 gDEEDRGV-----SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLA 247
Cdd:COG4778 142 -PERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIE 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
59-295 |
1.07e-22 |
|
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: 97.41 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 59 YSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYNQLRR 136
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG------LERPDSgtILFGGEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLmysaKFSLRDSTAKER------EERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERK 210
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNV----AFGLRVKPRSERppeaeiRAKVHELLKLVQLDWLADRYPAQ-------LSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIHLGSLE 290
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQE-EALEVADRVVVMNKGRIEQVGTPD 222
|
....*
gi 1063732797 291 HLEDS 295
Cdd:cd03296 223 EVYDH 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
71-262 |
1.15e-22 |
|
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: 95.95 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDYNQ-----LRRLCGFVPQD- 144
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNG-----LLRPQSGAVLIDGEPLDYSRkglleRRQRVGLVFQDp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 145 DDLLPLLTVKETLmysaKFSLRDSTAKERE--ERVESLLSDLGLVlvqdsfvGEGDEEDRGVSGGERKRVSIAVEMIRDP 222
Cdd:TIGR01166 78 DDQLFAADVDQDV----AFGPLNLGLSEAEveRRVREALTAVGAS-------GLRERPTHCLSGGEKKRVAIAGAVAMRP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063732797 223 PILLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIH 262
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTH 185
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
61-259 |
1.65e-22 |
|
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: 98.59 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHTPI--LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA-----VLMNNRKITDY 131
Cdd:COG0444 2 LEVRNLKvyFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILG------LLPPPGitsgeILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 N--QLRRLCG----FVPQD--DDLLPLLTVKETLMYSAKfSLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDRG 203
Cdd:COG0444 76 SekELRKIRGreiqMIFQDpmTSLNPVMTVGDQIAEPLR-IHGGLSKAEARERAIELLERVGL----------PDPERRL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 204 ------VSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLF 259
Cdd:COG0444 145 drypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILF 206
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
73-258 |
1.78e-22 |
|
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: 96.27 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 73 TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSSA-VLMNNRKI-----TDYNQLR-RLCGFVPQD 144
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGG------LDnPTSGeVLFNGQSLsklssNERAKLRnKKLGFIYQF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 145 DDLLPLLTVKETLMYSAKFSLRDstAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPI 224
Cdd:TIGR02211 92 HHLLPDFTALENVAMPLLIGKKS--VKEAKERAYEMLEKVGLEHRINHRPSE-------LSGGERQRVAIARALVNQPSL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1063732797 225 LLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVL 258
Cdd:TIGR02211 163 VLADEPTGNLDNNNAKIIFDLMLEL-NRELNTSF 195
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
74-264 |
2.02e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKitdynqlRRLcGFVPQ---DDDLLPL 150
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG-----VLRPTSGTVRRAGG-------ARV-AYVPQrseVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 lTVKETLM---YSAKFSLRDSTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLL 227
Cdd:NF040873 73 -TVRDLVAmgrWARRGLWRRLTRDDRA-AVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063732797 228 DEPTSGLDSRNSLQVVELLATMAkSKQRTVLFSIHQP 264
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDL 179
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
63-259 |
2.08e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLA-AESSKIlAVVGPSGTGKSTLLKIISGRvnhkaLDPSS--AVLMNNRKItdynqlrrlcG 139
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSiNPGDRI-GLVGRNGAGKSTLLKILAGE-----LEPDSgeVSIPKGLRI----------G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMY---------------SAKFSLRDSTAKEREE---------------RVESLLSDLGLvlv 189
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTVLDgdaelraleaeleelEAKLAEPDEDLERLAElqeefealggweaeaRAEEILSGLGF--- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 190 qdsfvgEGDEEDRGV---SGGERKRVSIAVEMIRDPPILLLDEPTSGLDsrnsLQVVELLATMAKSKQRTVLF 259
Cdd:COG0488 142 ------PEEDLDRPVselSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLV 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
52-288 |
2.52e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPTPNRYSLTVTNLS-----YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG--------------RVNH 112
Cdd:PRK13631 13 PNPLSDDIILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGlikskygtiqvgdiYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 113 KALDPSSAVLMNNRKITDYNQLRRLCGFVPQDDDL-LPLLTVKETLMYsAKFSLRDSTAKEREeRVESLLSDLGLvlvQD 191
Cdd:PRK13631 93 KKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEYqLFKDTIEKDIMF-GPVALGVKKSEAKK-LAKFYLNKMGL---DD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 192 SFVgegDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATmAKSKQRTVLFSIHQPSyRILDY 271
Cdd:PRK13631 168 SYL---ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTME-HVLEV 242
|
250
....*....|....*..
gi 1063732797 272 ISDYLILSRGSVIHLGS 288
Cdd:PRK13631 243 ADEVIVMDKGKILKTGT 259
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
61-294 |
8.80e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.46 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAVLMNN------RKITDYNQL 134
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRtvqregRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYSA-------KFSLRDSTAKEREERVESlLSDLGLVLVQDSFVGEgdeedrgVSGG 207
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQA-LTRVGMVHFAHQRVST-------LSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 208 ERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLG 287
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDY-ALRYCERIVALRQGHVFYDG 235
|
....*..
gi 1063732797 288 SLEHLED 294
Cdd:PRK09984 236 SSQQFDN 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
57-290 |
9.87e-22 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 94.71 E-value: 9.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 57 NRYSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALdpSSAVLMNNRKITDYN---- 132
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIL--EGDILFKGESILDLEpeer 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 -QLRRLCGF-----VP--QDDDLLplltvkeTLMYSAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEGDEEdrGV 204
Cdd:CHL00131 82 aHLGIFLAFqypieIPgvSNADFL-------RLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNE--GF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 205 SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQpsyRILDYIS-DYL-ILSRGS 282
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ---RLLDYIKpDYVhVMQNGK 229
|
....*...
gi 1063732797 283 VIHLGSLE 290
Cdd:CHL00131 230 IIKTGDAE 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
61-246 |
1.10e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHTPI--LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSS-AVLMNNRKITDYN-- 132
Cdd:COG1135 2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL------LErPTSgSVLVDGVDLTALSer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 ---QLRRLCGFVPQDDDLLPLLTVKETLMYS---AKFSlrdstAKEREERVESLLsdlglvlvqdSFVGEGDEEDR---G 203
Cdd:COG1135 76 elrAARRKIGMIFQHFNLLSSRTVAENVALPleiAGVP-----KAEIRKRVAELL----------ELVGLSDKADAypsQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063732797 204 VSGGERKRVSIAvemiR----DPPILLLDEPTSGLDSRNSLQVVELL 246
Cdd:COG1135 141 LSGGQKQRVGIA----RalanNPKVLLCDEATSALDPETTRSILDLL 183
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
61-266 |
1.39e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.43 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SG--RVNHKALDPSSAVLMNNRKItdy 131
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGtiRVGDITIDTARSLSQQKGLI--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 NQLRRLCGFVPQDDDLLPLLTVKETLMySAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFvgegdeeDRGVSGGERKR 211
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENII-EGPVIVKGEPKEEATARARELLAKVGLAGKETSY-------PRRLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGLDSRnslQVVELLAT---MAKSKqRTVLFSIHQPSY 266
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTirqLAQEK-RTMVIVTHEMSF 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
65-330 |
1.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHT-PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYN--QLRRLCGF 140
Cdd:PRK13652 8 DLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNG-----ILKPTSGsVLIRGEPITKENirEVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQD-DDLLPLLTVKETLMYS-AKFSLRDSTAkerEERVESLLSDLGLVLVQDSFvgegdeeDRGVSGGERKRVSIAVEM 218
Cdd:PRK13652 83 VFQNpDDQIFSPTVEQDIAFGpINLGLDEETV---AHRVSSALHMLGLEELRDRV-------PHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyrILDYISDYL-ILSRGSVIHLGSLEHLedsia 297
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLD--LVPEMADYIyVMDKGRIVAYGTVEEI----- 225
|
250 260 270
....*....|....*....|....*....|....
gi 1063732797 298 klgFQIPEQLNPIEFAMEIVESL-RTFKPNSVAV 330
Cdd:PRK13652 226 ---FLQPDLLARVHLDLPSLPKLiRSLQAQGIAI 256
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
61-295 |
2.82e-21 |
|
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: 93.12 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDY--NQLRRL 137
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG-----LLPPRSgSIRFDGEDITGLppHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 -CGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLSDLglvlvqdsfvgegdEEDRGV-----SGGERKR 211
Cdd:COG0410 79 gIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELFPRL--------------KERRRQragtlSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFsIHQPSYRILDyISDY-LILSRGSVIHLGSLE 290
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGV-TILL-VEQNARFALE-IADRaYVLERGRIVLEGTAA 221
|
....*
gi 1063732797 291 HLEDS 295
Cdd:COG0410 222 ELLAD 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
61-262 |
4.27e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.23 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAldpsSAVLMNNRKITDYNQLRrlcGF 140
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH----GSITLDGKPVEGPGAER---GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLLTVKETLMYSakFSLRDSTAKEREERVESLLSDLGLvlvqdsfvgEGDEEDR--GVSGGERKRVSIAVEM 218
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFG--LQLAGVEKMQRLEIAHQMLKKVGL---------EGAEKRYiwQLSGGQRQRVGIARAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
61-284 |
5.04e-21 |
|
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: 91.51 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITD-YNQLRRL 137
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG------LIKPDSgeITFDGKSYQKnIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 cGFVPQDDDLLPLLTVKETLMYSAKFSLRdstakeREERVESLLSDLGLvlvqdsfvgeGDEEDRGVSG---GERKRVSI 214
Cdd:cd03268 75 -GALIEAPGFYPNLTARENLRLLARLLGI------RKKRIDEVLDVVGL----------KDSAKKKVKGfslGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPSYriLDYISD-YLILSRGSVI 284
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSE--IQKVADrIGIINKGKLI 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
61-288 |
8.38e-21 |
|
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: 91.53 E-value: 8.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYNQLRRLCG 139
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-----FETPTSGeILLDGKDITNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLsdlglvlvqdSFVGEGDEEDRGV---SGGERKRVSIAV 216
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLR--LKKLPKAEIKERVAEAL----------DLVQLEGYANRKPsqlSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 217 EMIRDPPILLLDEPTSGLDS--RNSLQvVELlatmaKSKQR----TVLFSIHQPSYRILdyISDYL-ILSRGSVIHLGS 288
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLklRKDMQ-LEL-----KRLQKelgiTFVFVTHDQEEALT--MSDRIaVMNKGKIQQIGT 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
61-270 |
8.41e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgRVNHkaLDP----SSAVLMNNRKI----TDYN 132
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-RMND--LNPevtiTGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 QLRRLCGFVPQDDDLLPlLTVKETLMYsakfSLRDSTAKEREERVESllsdlglvlVQDSFVGEG--DE-EDR------G 203
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVY----GLRLKGIKDKQVLDEA---------VEKSLKGASiwDEvKDRlhdsalG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 204 VSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVE-LLATMAKSKQRTVLFSIHQPSyRILD 270
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEEtLLGLKDDYTMLLVTRSMQQAS-RISD 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
61-263 |
9.33e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPIlnSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLM-NNRKITDYNQLRRLCG 139
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAG-----FLTPASGSLTlNGQDHTTTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKEreERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMI 219
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQR--EKLHAIARQMGIEDLLARLPGQ-------LSGGQRQRVALARCLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQ 263
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHS 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
79-292 |
1.21e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 94.02 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLLKIISG--RVNHKALDPSSAVLMNNRKITDYNQLRRLCGFVPQDDDLLPLLTVKET 156
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGltRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 157 LMYSakfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDS 236
Cdd:TIGR02142 96 LRYG----MKRARPSERRISFERVIELLGIGHLLGRLPGR-------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 237 RNSLQVVELLATMAKSKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLGSLEHL 292
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQevLRLADRV---VVLEDGRVAAAGPIAEV 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
61-262 |
1.56e-20 |
|
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: 90.39 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYNQLRRLCG 139
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-----LEEPTSGrIYIGGRDVTDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVgegdeedRGVSGGERKRVSIAVEMI 219
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLK--LRKVPKDEIDERVREVAELLQIEHLLDRKP-------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-287 |
2.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVN-HKALDPSSAVLMNNRKI--TDYNQLRRL 137
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElYPEARVSGEVYLDGQDIfkMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLvlvQDSFVGEGDEEDRGVSGGERKRVSIAVE 217
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQL---WDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQP--SYRILDYISdylILSRGSVIHLG 287
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPqqAARISDYVA---FLYKGQIVEWG 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
79-292 |
3.17e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.47 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVnhkALDpsSAVLMNNRKITDynqL---RRLCGFVPQDDDLL 148
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdSGRI---RLG--GEVLQDSARGIF---LpphRRRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLLTVKETLMYSAKFSLRDSTAKEREERVEsLLsDLGLVLvqdsfvgegdeeDRGV---SGGERKRVSIAVEMIRDPPIL 225
Cdd:COG4148 90 PHLSVRGNLLYGRKRAPRAERRISFDEVVE-LL-GIGHLL------------DRRPatlSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 226 LLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPS--YRILDYIsdyLILSRGSVIHLGSLEHL 292
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDevARLADHV---VLLEQGRVVASGPLAEV 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
76-289 |
5.59e-20 |
|
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: 89.06 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkALDPSSAVLMNNRKITDYNQLRRLcgfVPQDDDLLPLLTVKE 155
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL----AQPTSGGVILEGKQITEPGPDRMV---VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 156 TLMYSAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-------LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 236 --SRNSLQvvELLATMAKSKQRTVLFSIHQPSYRILdyISDYLI-LSRGSVIHLGSL 289
Cdd:TIGR01184 147 alTRGNLQ--EELMQIWEEHRVTVLMVTHDVDEALL--LSDRVVmLTNGPAANIGQI 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
74-265 |
8.09e-20 |
|
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: 93.24 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSA-VLMNNRKITDY--NQLRRLCGFVPQD----DD 146
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIP-----RFYEPDSGqILLDGHDLADYtlASLRRQVALVSQDvvlfND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 llpllTVKETLMYSAkfslrdsTAKEREERVESLL-----------SDLGLvlvqDSFVGEgdeedRGV--SGGERKRVS 213
Cdd:TIGR02203 421 -----TIANNIAYGR-------TEQADRAEIERALaaayaqdfvdkLPLGL----DTPIGE-----NGVllSGGQRQRLA 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIHQPS 265
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQG--RTTLVIAHRLS 529
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
60-288 |
1.30e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAldpsSAVLMNNRKITD---YNQLRR 136
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----GNIIIDDEDISLlplHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMysAKFSLR-DSTAKEREERVESLLSDLGLVLVQDSFvgegdeeDRGVSGGERKRVSIA 215
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLM--AVLQIRdDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPSyRILDYISDYLILSRGSVIHLGS 288
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGL-GVLITDHNVR-ETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
74-262 |
1.65e-19 |
|
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: 88.16 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS--AVLMNNRKITDYNQLRRLCGFV-PQDDDLLPL 150
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG-----LLQPTSgeVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETL-MYSAKFSLRDSTAKEREERVESLLsDLGLVLvqdsfvgegDEEDRGVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:cd03267 110 LPVIDSFyLLAAIYDLPPARFKKRLDELSELL-DLEELL---------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190
....*....|....*....|....*....|...
gi 1063732797 230 PTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSH 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
65-249 |
3.11e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhkALDP--SSAVLMNNRKITDYN----QLRRLC 138
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN------KLEEitSGDLIVDGLKVNDPKvderLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKfSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEM 218
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPL-RVRGASKEEAEKQARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIARAL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063732797 219 IRDPPILLLDEPTSGLD---SRNSLQVVELLA----TM 249
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDpelRHEVLKVMQDLAeegmTM 189
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
60-246 |
6.28e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhkALD-PSSAVLMNNRKITDYNQ----- 133
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN------LLEtPDSGQLNIAGHQFDFSQkpsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 ----LRRLCGFVPQDDDLLPLLTVKETLMySAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFvgegdeeDRGVSGGER 209
Cdd:COG4161 76 airlLRQKVGMVFQQYNLWPHLTVMENLI-EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF-------PLHLSGGQQ 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063732797 210 KRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELL 246
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEII 184
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
61-324 |
7.82e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.06 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH-TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDYN-----QL 134
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNG-----ILKPTSGEVLIKGEPIKYDkksllEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQD-DDLLPLLTVKETLMY---SAKFSlrdstAKEREERVESLLSDLGLvlvqdsfvgEGDEED--RGVSGGE 208
Cdd:PRK13639 77 RKTVGIVFQNpDDQLFAPTVEEDVAFgplNLGLS-----KEEVEKRVKEALKAVGM---------EGFENKppHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYRILdYISDYLILSRGSVIHLGS 288
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPV-YADKVYVMSDGKIIKEGT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063732797 289 LEHL---EDSIAKLGFQIP------EQLN-----PIEFAMEIVESLRTFK 324
Cdd:PRK13639 221 PKEVfsdIETIRKANLRLPrvahliEILNkednlPIKMGYTIGEARRNIK 270
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
72-262 |
1.07e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSSA-VLMNNRKITDYN-----QLR-RLCGFVPQ 143
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG------LDtPTSGdVIFNGQPMSKLSsaakaELRnQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 144 DDDLLPLLTVKETLmySAKFSLRDSTAKEREERVESLLSDLGLvlvqdsfvgegdeEDRG------VSGGERKRVSIAVE 217
Cdd:PRK11629 95 FHHLLPDFTALENV--AMPLLIGKKKPAEINSRALEMLAAVGL-------------EHRAnhrpseLSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
69-259 |
1.32e-18 |
|
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: 89.36 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 69 TINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSS-AVLMNNRKITDYNQ-----LRRLCGFVP 142
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR------LIPSEgEIRFDGQDLDGLSRralrpLRRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 143 QD--DDLLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLvlvqdsfvgegDEEDRG-----VSGGERKRVSIA 215
Cdd:COG4172 369 QDpfGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGL-----------DPAARHrypheFSGGQRQRIAIA 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLF 259
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLF 481
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
60-321 |
1.63e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.25 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINH-TPI----LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITD--- 130
Cdd:PRK13637 2 SIKIENLTHIYMEgTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNG-----LLKPTSGkIIIDGVDITDkkv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 131 -YNQLRRLCGFVPQ--DDDLLplltvKETLMYSAKFSLRDSTAKERE--ERVESLLSDLGLvlvqdSFVGEGDEEDRGVS 205
Cdd:PRK13637 77 kLSDIRKKVGLVFQypEYQLF-----EETIEKDIAFGPINLGLSEEEieNRVKRAMNIVGL-----DYEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 206 GGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH--QPSYRILDYIsdyLILSRGSV 283
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmEDVAKLADRI---IVMNKGKC 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 284 IHLGS-------LEHLED-------------SIAKLGFQIPEQLNPIEFAM-EIVESLR 321
Cdd:PRK13637 224 ELQGTprevfkeVETLESiglavpqvtylvrKLRKKGFNIPDDIFTIEEAKeEILKYLR 282
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
74-263 |
1.66e-18 |
|
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: 90.46 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKI-TDYNQLRRLCGFVPQDDDLLPLL 151
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTG-----LLPPTSGtVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVlvqdsfvGEGDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:TIGR01257 1019 TVAEHILFYAQ--LKGRSWEEAQLEMEAMLEDTGLH-------HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190
....*....|....*....|....*....|..
gi 1063732797 232 SGLDSRNSLQVVELLatMAKSKQRTVLFSIHQ 263
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHH 1119
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
69-258 |
1.68e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 69 TINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQLRR--LCGFVPQDd 145
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG-----SLPPDSgSILIDGKDVTKLPEYKRakYIGRVFQD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 dllPL------LTVKETLMYSA----KFSLRDSTAKEREERVESLLSDLGLVLvqdsfvgegdeEDR-----G-VSGGER 209
Cdd:COG1101 89 ---PMmgtapsMTIEENLALAYrrgkRRGLRRGLTKKRRELFRELLATLGLGL-----------ENRldtkvGlLSGGQR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063732797 210 KRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVL 258
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTL 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
60-292 |
1.84e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsGRvnHKAldPSSA-VLMNNRKITDYNQ--LRR 136
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GR--HQP--PSEGeILLDAQPLESWSSkaFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDddlLPL---LTVKETLM---YSAKFSLRDSTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERK 210
Cdd:PRK10575 86 KVAYLPQQ---LPAaegMTVRELVAigrYPWHGALGRFGAADRE-KVEEAISLVGLKPLAHRLVDS-------LSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH--QPSYRILDYIsdyLILSRGSVIHLGS 288
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHdiNMAARYCDYL---VALRGGEMIAQGT 231
|
....
gi 1063732797 289 LEHL 292
Cdd:PRK10575 232 PAEL 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
54-271 |
2.06e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.47 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 54 PTPNRYSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgRVNhkALDPSSA----VLMNNRKI- 128
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLN-RMN--DLIPGARvegeILLDGEDIy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 ---TDYNQLRRLCGFVPQDDDLLPlLTVKETLMYSAK-FSLRDStaKEREERVESLLSDLGLvlvqdsfvgeGDE-EDR- 202
Cdd:COG1117 82 dpdVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRlHGIKSK--SELDEIVEESLRKAAL----------WDEvKDRl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 -----GVSGGERKRV----SIAVEmirdPPILLLDEPTSGLDSRNSLQVVELLATMAksKQRTVLF---SIHQPSyRILD 270
Cdd:COG1117 149 kksalGLSGGQQQRLciarALAVE----PEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIvthNMQQAA-RVSD 221
|
.
gi 1063732797 271 Y 271
Cdd:COG1117 222 Y 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
61-302 |
2.99e-18 |
|
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: 84.62 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAldPSSAVLMNNRKITDY--NQLRRLC 138
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEV--TSGTILFKGQDLLELepDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFV-PQDDDLLPLLTVKEtlmysakFsLRDSTAKEREERVESLLSDLGLV-LVQDSF-VGEGDEE--DRGV----SGGER 209
Cdd:TIGR01978 79 LFLaFQYPEEIPGVSNLE-------F-LRSALNARRSARGEEPLDLLDFEkLLKEKLaLLDMDEEflNRSVnegfSGGEK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 210 KRVSIAVEMIRDPPILLLDEPTSGLDSrNSLQVVELLATMAKSKQRTVLFSIHQPsyRILDYIS-DY-LILSRGSVIHLG 287
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDI-DALKIVAEGINRLREPDRSFLIITHYQ--RLLNYIKpDYvHVLLDGRIVKSG 227
|
250
....*....|....*
gi 1063732797 288 SLEhLEDSIAKLGFQ 302
Cdd:TIGR01978 228 DVE-LAKELEAKGYD 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
61-301 |
3.08e-18 |
|
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: 83.35 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSsaVLMNNRKITDYN-QLRRLCG 139
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGE--ILFKGEDITDLPpEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 -FV-PQDDDLLPLLTVKETLMYsakfslrdstakereervesllsdlglvlvqdsfVGEGdeedrgVSGGERKRVSIAVE 217
Cdd:cd03217 79 iFLaFQYPPEIPGVKNADFLRY----------------------------------VNEG------FSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQpsyRILDYI-SDYL-ILSRGSVIHLGSLEhLEDS 295
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ---RLLDYIkPDRVhVLYDGRIVKSGDKE-LALE 194
|
....*.
gi 1063732797 296 IAKLGF 301
Cdd:cd03217 195 IEKKGY 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
59-318 |
3.16e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 59 YSLTVTNLSYTI-NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDYN----- 132
Cdd:PRK13636 4 YILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNG-----ILKPSSGRILFDGKPIDYSrkglm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 QLRRLCGFVPQD-DDLLPLLTVKETLMYSA-KFSLRDstaKEREERVESLLSDLGLVLVQDsfvgegdEEDRGVSGGERK 210
Cdd:PRK13636 79 KLRESVGMVFQDpDNQLFSASVYQDVSFGAvNLKLPE---DEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRILdYISDYLILSRGSVIHLGSLE 290
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPL-YCDNVFVMKEGRVILQGNPK 227
|
250 260 270
....*....|....*....|....*....|.
gi 1063732797 291 HL---EDSIAKLGFQIPEqlnpIEFAMEIVE 318
Cdd:PRK13636 228 EVfaeKEMLRKVNLRLPR----IGHLMEILK 254
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
71-292 |
3.47e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.48 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSSAVL----MNNRKITdYNQLRRLCGFVPQDdd 146
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-----QRVFDPQSGRIlidgTDIRTVT-RASLRRNIAVVFQD-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 llPLL---TVKETLmysaKFSLRDSTAKEREERVES-------LLSDLGLvlvqDSFVGEgdeedRG--VSGGERKRVSI 214
Cdd:PRK13657 418 --AGLfnrSIEDNI----RVGRPDATDEEMRAAAERaqahdfiERKPDGY----DTVVGE-----RGrqLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPS-YRILDYIsdyLILSRGSVIHLGSLEHL 292
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLStVRNADRI---LVFDNGRVVESGSFDEL 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
75-264 |
5.48e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYN-----QLR-RLCGFVPQDDD 146
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG------LDDGSSgeVSLVGQPLHQMDeearaKLRaKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLvlvqdsfvGEG-DEEDRGVSGGERKRVSIAVEMIRDPPIL 225
Cdd:PRK10584 99 LIPTLNALENVELPAL--LRGESSRQSRNGAKALLEQLGL--------GKRlDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063732797 226 LLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQP 264
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-288 |
5.49e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG--RVNHKALDPSSAVLMNNRKI--TDYNQLRR 136
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRliEIYDSKIKVDGKVLYFGKDIfqIDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMYSAK-FSLRDStaKEREERVESLLSDLGL-VLVQDSFVGEGDEedrgVSGGERKRVSI 214
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYPLKsHGIKEK--REIKKIVEECLRKVGLwKEVYDRLNSPASQ----LSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSlQVVELLATMAKSKQRTVLFSiHQPSY--RILDYISdylILSRGSVIHLGS 288
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNS-QAIEKLITELKNEIAIVIVS-HNPQQvaRVADYVA---FLYNGELVEWGS 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
75-295 |
7.60e-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: 83.30 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVnhkaldpssAVLMNNRKITDYNQLRRLCGFVPQDDDL 147
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyvpeNGRV---------LVDGHDLALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 148 LplltvketlmysaKFSLRDSTAKERE----ERVESLLSDLG-------LVLVQDSFVGEgdeEDRGVSGGERKRVSIAV 216
Cdd:cd03252 88 F-------------NRSIRDNIALADPgmsmERVIEAAKLAGahdfiseLPEGYDTIVGE---QGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVEllaTMAK-SKQRTVLFSIHQPS-YRILDYIsdyLILSRGSVIHLGSLEHLED 294
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMR---NMHDiCAGRTVIIIAHRLStVKNADRI---IVMEKGRIVEQGSHDELLA 225
|
.
gi 1063732797 295 S 295
Cdd:cd03252 226 E 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
61-290 |
8.06e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvNHKALDPSSAVLMNNR------------KI 128
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI----NFLEKPSEGSIVVNGQtinlvrdkdgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 TDYNQLRRL---CGFVPQDDDLLPLLTVKETLMySAKFSLRDSTAKEREERVESLLSDLGLvlvqdsfvgegDEEDRG-- 203
Cdd:PRK10619 82 ADKNQLRLLrtrLTMVFQHFNLWSHMTVLENVM-EAPIQVLGLSKQEARERAVKYLAKVGI-----------DERAQGky 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 204 ---VSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYRilDYISDYLILsr 280
Cdd:PRK10619 150 pvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFA--RHVSSHVIF-- 224
|
250
....*....|
gi 1063732797 281 gsvIHLGSLE 290
Cdd:PRK10619 225 ---LHQGKIE 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
60-262 |
8.91e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.47 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD--PSSAVLMNNRKITDYNQLRRL 137
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG------LEdiTSGDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDDDLLPLLTVKETLmysaKFSLRDSTAK--EREERVE--SLLSDLGLVLvqdsfvgegDEEDRGVSGGERKRVS 213
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENM----SFGLKLAGAKkeEINQRVNqvAEVLQLAHLL---------DRKPKALSGGQRQRVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
60-237 |
1.23e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKaldpSSAVLMNNRKITDYNQLRRLCG 139
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT----SGHIRFHGTDVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLmysaKFSLRDSTAKER------EERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVS 213
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNI----AFGLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQ-------LSGGQKQRVA 146
|
170 180
....*....|....*....|....
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSR 237
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQ 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
60-246 |
1.52e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVN--HKALDPSSAVlmNNRKITd 130
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiaGNHFDFSKTP--SDKAIR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 131 ynQLRRLCGFVPQDDDLLPLLTVKETLMySAKFSLRDSTAKEREERVESLLSDLGLvlvqdsfvgeGDEEDR---GVSGG 207
Cdd:PRK11124 79 --ELRRNVGMVFQQYNLWPHLTVQQNLI-EAPCRVLGLSKDQALARAEKLLERLRL----------KPYADRfplHLSGG 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063732797 208 ERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELL 246
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
68-311 |
3.81e-17 |
|
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: 86.22 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 68 YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkALDPSSAVLMNNRKITDYNQLRRLCGFVPQDDDL 147
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDT---TVTSGDATVAGKSILTNISDVHQNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 148 LPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLL 227
Cdd:TIGR01257 2024 DDLLTGREHLYLYAR--LRGVPAEEIEKVANWSIQSLGLSLYADRLAGT-------YSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 228 DEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRILdyISDYLILSRGSVIHLGSLEHLEDS-----IAKLGFQ 302
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAL--CTRLAIMVKGAFQCLGTIQHLKSKfgdgyIVTMKIK 2172
|
250
....*....|....
gi 1063732797 303 IPE-----QLNPIE 311
Cdd:TIGR01257 2173 SPKddllpDLNPVE 2186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
61-262 |
4.63e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSA-VLMNNRKITDYN--QLRRL 137
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA-----SLISPTSGtLLFEGEDISTLKpeIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDddllPLL---TVKETLMYSakFSLRDSTAKEReerveSLLSDLGLVLVQDSFVGEGDEEdrgVSGGERKRVSi 214
Cdd:PRK10247 83 VSYCAQT----PTLfgdTVYDNLIFP--WQIRNQQPDPA-----IFLDDLERFALPDTILTKNIAE---LSGGEKQRIS- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 215 aveMIRD----PPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK10247 148 ---LIRNlqfmPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
72-263 |
5.46e-17 |
|
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: 80.59 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSSA-VLMNNRKITDYNQ--LRRLCGFVPQDddll 148
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-----ENFYQPQGGqVLLDGKPISQYEHkyLHSKVSLVGQE---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLL---TVKETLMYS-AKFSLRDSTAKEREERVESLLSDLglvlvQDSFVGEGDEEDRGVSGGERKRVSIAVEMIRDPPI 224
Cdd:cd03248 97 PVLfarSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISEL-----ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063732797 225 LLLDEPTSGLDSRNSLQVVELLATMAKSkqRTVLFSIHQ 263
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHR 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-273 |
5.64e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgRVNH--KALDPSSAVLMNNRKI----TDYNQ 133
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNEleSEVRVEGRVEFFNQNIyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLCGFVPQDDDLLPLlTVKETLMYSAKFsLRDSTAKEREERVESLLSDLGLvlvQDSFVGEGDEEDRGVSGGERKRVS 213
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPM-SVYDNVAYGVKI-VGWRPKLEIDDIVESALKDADL---WDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLF---SIHQPSyRILDYIS 273
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIvshNLHQVS-RLSDFTA 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
52-262 |
5.75e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPTPnrySLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkALDPSSAVLMNNRKITDY 131
Cdd:PRK13537 2 PMSVA---PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT---HPDAGSISLCGEPVPSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 NQLRRLCGFVPQDDDLLPLLTVKETLM-YSAKFSLrdsTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERK 210
Cdd:PRK13537 76 RHARQRVGVVPQFDNLDPDFTVRENLLvFGRYFGL---SAAAARALVPPLLEFAKLENKADAKVGE-------LSGGMKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLAT-MAKSKqrTVLFSIH 262
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGK--TILLTTH 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
61-264 |
6.64e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKItDYNQLRRLC 138
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG------LLPPAAgtIKLDGGDI-DDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDDDLLPLLTVKETLMYSAKFslrdstAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEM 218
Cdd:PRK13539 76 HYLGHRNAMKPALTVAENLEFWAAF------LGGEELDIAAALEAVGLAPLAHLPFGY-------LSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNslqvVELLATMAKSKQR---TVLFSIHQP 264
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAA----VALFAELIRAHLAqggIVIAATHIP 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
61-248 |
8.92e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS--AVLMNNRKItdynqlrrlc 138
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE-----LEPDSgtVKLGETVKI---------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQD-DDLLPLLTVKETlmysakfsLRDSTAKEREERVESLLSDLGLvlvqdsfvgEGDEEDRGV---SGGERKRVSI 214
Cdd:COG0488 381 GYFDQHqEELDPDKTVLDE--------LRDGAPGGTEQEVRGYLGRFLF---------SGDDAFKPVgvlSGGEKARLAL 443
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLD--SRNSLqvVELLAT 248
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDieTLEAL--EEALDD 477
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
60-262 |
9.52e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKA-----LD---PSSAVLMnnrkitdy 131
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgkitvLGvpvPARARLA-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 nqlRRLCGFVPQDDDLLPLLTVKETLM-YSAKFSLrdsTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERK 210
Cdd:PRK13536 113 ---RARIGVVPQFDNLDLEFTVRENLLvFGRYFGM---STREIEAVIPSLLEFARLESKADARVSD-------LSGGMKR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVE-LLATMAKSKqrTVLFSIH 262
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWErLRSLLARGK--TILLTTH 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
52-262 |
1.64e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPTPNRYSLTVTNLSY-----------TINHTPILNSVSLAAESSKILAVVGPSGTGKST----LLKIISGRvnhkald 116
Cdd:PRK15134 267 PLPEPASPLLDVEQLQVafpirkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 117 psSAVLMNNRKITDYNQ-----LRRLCGFVPQDDD--LLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLvlv 189
Cdd:PRK15134 340 --GEIWFDGQPLHNLNRrqllpVRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGL--- 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 190 qdsfvgegDEEDR-----GVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK15134 415 --------DPETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
65-288 |
2.45e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.05 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTI-NHTPI----LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRV---NHKALDPSSAVLMNNRKITDYNQLRR 136
Cdd:PRK13645 11 NVSYTYaKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiseTGQTIVGDYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQdddlLPLLTV-KETLMYSAKFSLRDsTAKEREERVESLLSDLGLVLVQDSFVGEGDEEdrgVSGGERKRVSIA 215
Cdd:PRK13645 91 EIGLVFQ----FPEYQLfQETIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPFE---LSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIHLGS 288
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
63-312 |
2.66e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNL--SYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYN--QLRRL 137
Cdd:PRK13632 10 VENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG-----LLKPQSGeIKIDGITISKENlkEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQD-DDLLPLLTVKETLmysaKFSLRDStaKEREERVESLLSDLGLVLVQDSFVgegDEEDRGVSGGERKRVSIAV 216
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDI----AFGLENK--KVPPKKMKDIIDDLAKKVGMEDYL---DKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRIL-DYIsdyLILSRGSVIHLGS-LEHLED 294
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILaDKV---IVFSEGKLIAQGKpKEILNN 232
|
250 260
....*....|....*....|....*.
gi 1063732797 295 ----SIAKLGF----QIPEQLNPIEF 312
Cdd:PRK13632 233 keilEKAKIDSpfiyKLSKKLKGIDP 258
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
61-246 |
3.40e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.65 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSS-AVLMNNRKITDYNQLRRLCG 139
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ-----PTAgQIMLDGVDLSHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMYSAKfslRDSTAK-EREERVESLlsdLGLVLVQDsFVGEGDEEdrgVSGGERKRVSIAVEM 218
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLK---QDKLPKaEIASRVNEM---LGLVHMQE-FAKRKPHQ---LSGGQRQRVALARSL 164
|
170 180 190
....*....|....*....|....*....|..
gi 1063732797 219 IRDPPILLLDEPTSGLDS----RNSLQVVELL 246
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKklrdRMQLEVVDIL 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
76-284 |
3.86e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDYN--QLRRLCGFVPQDDDLLPLLTV 153
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-----LLPGQGEILLNGRPLSDWSaaELARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 154 KETLMYSAKFSLRDSTAkerEERVESLLSDLGLvlvqdsfvgeGDEEDRGV---SGGERKRVSIAVEMIR-DPPI----- 224
Cdd:COG4138 87 FQYLALHQPAGASSEAV---EQLLAQLAEALGL----------EDKLSRPLtqlSGGEWQRVRLAAVLLQvWPTInpegq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 225 -LLLDEPTSGLDSRNSLQVVELLATMAkSKQRTVLFSIHQPSyRILDYISDYLILSRGSVI 284
Cdd:COG4138 154 lLLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLN-HTLRHADRVWLLKQGKLV 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
65-312 |
4.01e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.99 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSA-VLMNNRKITDY--NQLRRLCGFV 141
Cdd:PRK11176 348 TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT-----RFYDIDEGeILLDGHDLRDYtlASLRNQVALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 142 PQDDDLLPLlTVKETLMYSA--KFSlRDSTAKERE-----ERVESLlsDLGLvlvqDSFVGEGdeedrGV--SGGERKRV 212
Cdd:PRK11176 423 SQNVHLFND-TIANNIAYARteQYS-REQIEEAARmayamDFINKM--DNGL----DTVIGEN-----GVllSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPSyrILDYISDYLILSRGSVIHLGSLEHL 292
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS--TIEKADEILVVEDGEIVERGTHAEL 565
|
250 260
....*....|....*....|
gi 1063732797 293 edsIAKLGfqIPEQLNPIEF 312
Cdd:PRK11176 566 ---LAQNG--VYAQLHKMQF 580
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
75-270 |
4.25e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.15 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDY-NQLRRLCGFVPQDDDLLPLL 151
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG------LSPPLAgrVLLNGGPLDFQrDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAKFSLRDStakereerVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:cd03231 89 SVLENLRFWHADHSDEQ--------VEEALARVGLNGFEDRPVAQ-------LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063732797 232 SGLDSrnslQVVELLAT-MAKSKQR--TVLFSIHQP------SYRILD 270
Cdd:cd03231 154 TALDK----AGVARFAEaMAGHCARggMVVLTTHQDlglseaGARELD 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
75-264 |
4.90e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhkALD-PSSAVL-MNNRKITDYN-----QLRR-LCGFVPQDDD 146
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILG------CLDkPTSGTYrVAGQDVATLDadalaQLRReHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTVKETLMYSAKFSlrDSTAKEREERVESLLSDLGLvlvqdsfvgegdeEDR------GVSGGERKRVSIAVEMIR 220
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYA--GLERKQRLLRAQELLQRLGL-------------EDRveyqpsQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 221 DPPILLLDEPTSGLDSRNSlqvVELLATMAKSKQR--TVLFSIHQP 264
Cdd:PRK10535 162 GGQVILADEPTGALDSHSG---EEVMAILHQLRDRghTVIIVTHDP 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
76-320 |
5.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-------VLMNNRKITDYNQLRRLCGFVPQ--DDD 146
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNG-----LLQPTSGtvtigerVITAGKKNKKLKPLRKKVGIVFQfpEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTVKETLMYSAKFSLRDSTAKEReerVESLLSDLGL---VLVQDSFvgegdeedrGVSGGERKRVSIAVEMIRDPP 223
Cdd:PRK13634 98 LFEETVEKDICFGPMNFGVSEEDAKQK---AREMIELVGLpeeLLARSPF---------ELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIHLGSLEHL---EDSIAKLG 300
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSME-DAARYADQIVVMHKGTVFLQGTPREIfadPDELEAIG 244
|
250 260
....*....|....*....|
gi 1063732797 301 FQIPEQlnpIEFAMEIVESL 320
Cdd:PRK13634 245 LDLPET---VKFKRALEEKF 261
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
61-290 |
5.69e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTnlsYTINHTPiLNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnHKALDPSSAVLMNNRKITDYNqlrrLCGF 140
Cdd:PRK15056 12 VTVT---WRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-RLASGKISILGQPTRQALQKN----LVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDL---LPLLtVKETLM---YSAKFSLRDSTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSI 214
Cdd:PRK15056 83 VPQSEEVdwsFPVL-VEDVVMmgrYGHMGWLRRAKKRDRQ-IVTAALARVDMVEFRHRQIGE-------LSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQPSYriLDYISDYLILSRGSVIHLGSLE 290
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGS--VTEFCDYTVMVKGTVLASGPTE 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
61-261 |
8.35e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.13 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI--NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYN--QLR 135
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNG-----LLLPEAgTITVGGMVLSEETvwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDllpLLTVKETLMYSAKFSLRDSTAkEREERVESLLSDLGLVLVQDsFVgegDEEDRGVSGGERKRVSIA 215
Cdd:PRK13635 81 RQVGMVFQNPD---NQFVGATVQDDVAFGLENIGV-PREEMVERVDQALRQVGMED-FL---NREPHRLSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 216 VEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLfSI 261
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVL-SI 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
61-262 |
1.56e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.84 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnHKALDpSSAVLMNNRKITDYNQLRRLCGF 140
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG---FETPD-SGRIMLDGQDITHVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLLTVKETLMYSAKfsLRDSTAKEREERVESLLSdlglvLVQ-DSFvgeGDEEDRGVSGGERKRVSIAVEMI 219
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLR--MQKTPAAEITPRVMEALR-----MVQlEEF---AQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063732797 220 RDPPILLLDEPTSGLDS--RNSLQvVELlatmaKSKQR----TVLFSIH 262
Cdd:PRK09452 161 NKPKVLLLDESLSALDYklRKQMQ-NEL-----KALQRklgiTFVFVTH 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
65-288 |
1.57e-15 |
|
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: 75.99 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKST----LLKIISGRvnhkaldpSSAVLMNNRKITDY--NQLRRLC 138
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELS--------SGSILIDGVDISKIglHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDddllPLL---TVKETL----------MYSAkfsLRDSTAKEReerVESLLSDLGLVLvqdsfvgegDEEDRGVS 205
Cdd:cd03244 81 SIIPQD----PVLfsgTIRSNLdpfgeysdeeLWQA---LERVGLKEF---VESLPGGLDTVV---------EEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 206 GGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATmaKSKQRTVLFSIHQpsyriLDYISDY---LILSRGS 282
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHR-----LDTIIDSdriLVLDKGR 214
|
....*.
gi 1063732797 283 VIHLGS 288
Cdd:cd03244 215 VVEFDS 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
76-320 |
1.87e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.71 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKaldpSSAVLMNNRKITDYN--QLRRLCGFVPQDDDLLpllTV 153
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK----SGEIFYNNQAITDDNfeKLRKHIGIVFQNPDNQ---FV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 154 KETLMYSAKFSLRDSTA--KEREERVESLLSDLGLVlvqdsfvGEGDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:PRK13648 98 GSIVKYDVAFGLENHAVpyDEMHRRVSEALKQVDML-------ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 232 SGLDSRNSLQVVELLATMAKSKQRTVLfSIHQPSYRILDyiSDYLI-LSRGSVIHLGSLEHL---EDSIAKLGFQIPeql 307
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITII-SITHDLSEAME--ADHVIvMNKGTVYKEGTPTEIfdhAEELTRIGLDLP--- 244
|
250
....*....|...
gi 1063732797 308 npieFAMEIVESL 320
Cdd:PRK13648 245 ----FPIKINQML 253
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
52-292 |
2.29e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 52 PLPtPNRYSLTV--TNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSSA-VLMNNRKI 128
Cdd:PRK10789 306 PVP-EGRGELDVniRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI-----QRHFDVSEGdIRFHDIPL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 TD--YNQLRRLCGFVPQdddlLPLLtVKETLMYSAKFSLRDSTAKEREE--RVESLLSDLgLVLVQ--DSFVGEgdeedR 202
Cdd:PRK10789 380 TKlqLDSWRSRLAVVSQ----TPFL-FSDTVANNIALGRPDATQQEIEHvaRLASVHDDI-LRLPQgyDTEVGE-----R 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 GV--SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPSyrILDYISDYLILSR 280
Cdd:PRK10789 449 GVmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW--GEGRTVIISAHRLS--ALTEASEILVMQH 524
|
250
....*....|..
gi 1063732797 281 GSVIHLGSLEHL 292
Cdd:PRK10789 525 GHIAQRGNHDQL 536
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
65-287 |
2.55e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.03 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHtpILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaLDPSS----AVLMNNRKI----TDYNQLRR 136
Cdd:PRK14267 11 RVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLE---LNEEArvegEVRLFGRNIyspdVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLvlvQDSFVGEGDEEDRGVSGGERKRVSIAV 216
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAL---WDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPSY--RILDYISdylILSRGSVIHLG 287
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQaaRVSDYVA---FLYLGKLIEVG 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
76-290 |
2.64e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTL---LKII----SGRVNHKALDpssaVLMNNRkiTDYNQLRRLCGFVPQD--DD 146
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIetptGGELYYQGQD----LLKADP--EAQKLLRQKIQIVFQNpyGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTV----KETLMYSAKFSlrdstAKEREERVESLLSDLGLvlvqdsfvgEGDEEDR---GVSGGERKRVSIAVEMI 219
Cdd:PRK11308 105 LNPRKKVgqilEEPLLINTSLS-----AAERREKALAMMAKVGL---------RPEHYDRyphMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyrILDYISD-----YLilsrGSVIHLGSLE 290
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLS--VVEHIADevmvmYL----GRCVEKGTKE 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
76-298 |
3.95e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLmnnrkitdynqlrRLCGFVPQDDD--------- 146
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG-----ILVPTSGEV-------------RVLGYVPFKRRkefarrigv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 -------LLPLLTVKETL-MYSAKFSLRDSTAKEREERVESLLsDLGLVLvqDSFVgegdeedRGVSGGERKRVSIAVEM 218
Cdd:COG4586 100 vfgqrsqLWWDLPAIDSFrLLKAIYRIPDAEYKKRLDELVELL-DLGELL--DTPV-------RQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHqpsyrildYISD-------YLILSRGSVIHLGSLEH 291
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH--------DMDDiealcdrVIVIDHGRIIYDGSLEE 241
|
....*..
gi 1063732797 292 LEDSIAK 298
Cdd:COG4586 242 LKERFGP 248
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
74-294 |
6.13e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.23 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSSA-VLMNNRKITDYNQ--LRRLCGFVPQDddllPL 150
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ-----PTGGqVLLDGVPLVQYDHhyLHRQVALVGQE----PV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 L---TVKETLMYSAKFSLRDS-TAKEREERVESLLSdlGLVLVQDSFVGEGDEEdrgVSGGERKRVSIAVEMIRDPPILL 226
Cdd:TIGR00958 566 LfsgSVRENIAYGLTDTPDEEiMAAAKAANAHDFIM--EFPNGYDTEVGEKGSQ---LSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 227 LDEPTSGLDSrnslQVVELLATMAKSKQRTVLFSIHQ-PSYRILDYIsdyLILSRGSVIHLGSLEHLED 294
Cdd:TIGR00958 641 LDEATSALDA----ECEQLLQESRSRASRTVLLIAHRlSTVERADQI---LVLKKGSVVEMGTHKQLME 702
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
61-262 |
6.20e-15 |
|
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: 72.10 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhKALDPSSAVLMNNRKITDYNQLrrlcgf 140
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE---LEPDEGIVTWGSTVKIGYFEQL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 vpqdddllplltvketlmysakfslrdstakereervesllsdlglvlvqdsfvgegdeedrgvSGGERKRVSIAVEMIR 220
Cdd:cd03221 72 ----------------------------------------------------------------SGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063732797 221 DPPILLLDEPTSGLDsrnsLQVVELLATMAKSKQRTVLFSIH 262
Cdd:cd03221 88 NPNLLLLDEPTNHLD----LESIEALEEALKEYPGTVILVSH 125
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
61-288 |
8.66e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDYNQ-----LR 135
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSG-----LLRPQKGAVLWQGKPLDYSKrgllaLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLLTVKETlmySAKFSLRDSTAKERE--ERVESLLSdlgLVLVQdsfvGEGDEEDRGVSGGERKRVS 213
Cdd:PRK13638 77 QQVATVFQDPEQQIFYTDIDS---DIAFSLRNLGVPEAEitRRVDEALT---LVDAQ----HFRHQPIQCLSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLfSIHQPS--YRILDYIsdyLILSRGSVIHLGS 288
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDliYEISDAV---YVLRQGQILTHGA 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
76-259 |
1.37e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.60 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISG---------RVNHKALDPSSAVLMNNRKItdynqlrrlcGFVPQDDD 146
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvyqpdsgeiLLDGEPVRFRSPRDAQAAGI----------AIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTVKETLM---YSAKFSLRDStaKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPP 223
Cdd:COG1129 90 LVPNLSVAENIFlgrEPRRGGLIDW--RAMRRRARELLARLGLDIDPDTPVGD-------LSVAQQQLVEIARALSRDAR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063732797 224 ILLLDEPTSGLDSRnslQVVELLATMAKSKQR--TVLF 259
Cdd:COG1129 161 VLILDEPTASLTER---EVERLFRIIRRLKAQgvAIIY 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
60-288 |
1.70e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINH-TPI----LNSVSLAAESSKILAVVGPSGTGKSTL-------LKIISGRVNHKALDpssavLMNNRK 127
Cdd:PRK13646 2 TIRFDNVSYTYQKgTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLiqninalLKPTTGTVTVDDIT-----ITHKTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 128 ITDYNQLRRLCGFVPQ--DDDLLPLLTVKETLMYSAKFSLRDSTAKEREERvesLLSDLGL---VLVQDSFvgegdeedr 202
Cdd:PRK13646 77 DKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHR---LLMDLGFsrdVMSQSPF--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 GVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyRILDYISDYLILSRGS 282
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMN-EVARYADEVIVMKEGS 223
|
....*.
gi 1063732797 283 VIHLGS 288
Cdd:PRK13646 224 IVSQTS 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
61-304 |
1.79e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.07 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHT--PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAlDPSSAVLMNNRKITDYN--QLRR 136
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-NPNSKITVDGITLTAKTvwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLpllTVKETLMYSAKFSLrDSTAKEREER---VESLLSDLGLVLVQDSfvgegdeEDRGVSGGERKRVS 213
Cdd:PRK13640 85 KVGIVFQNPDNQ---FVGATVGDDVAFGL-ENRAVPRPEMikiVRDVLADVGMLDYIDS-------EPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVlFSIhqpSYRI--LDYISDYLILSRGSVIHLGSLEH 291
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTV-ISI---THDIdeANMADQVLVLDDGKLLAQGSPVE 229
|
250
....*....|....*.
gi 1063732797 292 L---EDSIAKLGFQIP 304
Cdd:PRK13640 230 IfskVEMLKEIGLDIP 245
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
79-276 |
1.97e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.77 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLlkiisGRVNHKALDPSS-AVLMNNRKITDYN-----QLRRLCGFVPQD--DDLLPL 150
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTL-----GRLLLRLEEPTSgEILFDGQDITGLSgrelrPLRRRMQMVFQDpyASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETLmySAKFSL-RDSTAKEREERVESLLSDLGLvlvqdsfvgegDEEDRG-----VSGGERKRVSIAVEMIRDPPI 224
Cdd:COG4608 112 MTVGDII--AEPLRIhGLASKAERRERVAELLELVGL-----------RPEHADrypheFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 225 LLLDEPTSGLDSrnSL--QVVELLATMAKSKQRTVLFSIHQPSyrILDYISD-----YL 276
Cdd:COG4608 179 IVCDEPVSALDV--SIqaQVLNLLEDLQDELGLTYLFISHDLS--VVRHISDrvavmYL 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
61-321 |
2.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.00 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH---TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYN--QL 134
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG-----LLEAESGqIIIDGDLLTEENvwDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLpllTVKETLMYSAKFSLRDS--TAKEREERVESLLSdlgLVLVQDsFvgeGDEEDRGVSGGERKRV 212
Cdd:PRK13650 80 RHKIGMVFQNPDNQ---FVGATVEDDVAFGLENKgiPHEEMKERVNEALE---LVGMQD-F---KEREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQpsyriLDYI--SD-YLILSRGSVIHLGSL 289
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD-----LDEValSDrVLVMKNGQVESTSTP 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1063732797 290 EHL---EDSIAKLGFQIPeqlnpieFAMEIVESLR 321
Cdd:PRK13650 225 RELfsrGNDLLQLGLDIP-------FTTSLVQSLR 252
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
60-292 |
2.18e-14 |
|
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: 76.70 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINH-TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYN--QLR 135
Cdd:TIGR01193 473 DIVINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG-----FFQARSGeILLNGFSLKDIDrhTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDddllPLL---TVKETLMYSAKfslRDSTAKEREERVESLLSDLGLVLVQDSFVGEGDEEDRGVSGGERKRV 212
Cdd:TIGR01193 548 QFINYLPQE----PYIfsgSILENLLLGAK---ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMaksKQRTVLFSIHQPSyrILDYISDYLILSRGSVIHLGSLEHL 292
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL---QDKTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
59-306 |
2.67e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.62 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 59 YSLTVTNLSYTI-NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrVNhkaLDPSSAVLMNNRKITDYNQ--LR 135
Cdd:PRK13647 3 NIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG-IY---LPQRGRVKVMGREVNAENEkwVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQD-DDLLPLLTVKETLMYSA-KFSLRdstAKEREERVESLLSdlglvlvqdsFVGEGDEEDRG---VSGGERK 210
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFGPvNMGLD---KDEVERRVEEALK----------AVRMWDFRDKPpyhLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLGSLE 290
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDL-AAEWADQVIVLKEGRVLAEGDKS 223
|
250 260
....*....|....*....|....*...
gi 1063732797 291 HLEDS------------IAKLGFQIPEQ 306
Cdd:PRK13647 224 LLTDEdiveqaglrlplVAQIFEDLPEL 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
76-288 |
2.99e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSA-VLMNN---RKITD--YNQLRRL-CGFVPQDDDLL 148
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-----RLIEPTRGqVLIDGvdiAKISDaeLREVRRKkIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLLTVKETLMYSakFSLRDSTAKEREERVESLLSDLGLvlvQDSFVGEGDEedrgVSGGERKRVSIAVEMIRDPPILLLD 228
Cdd:PRK10070 119 PHMTVLDNTAFG--MELAGINAEERREKALDALRQVGL---ENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 229 EPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH--QPSYRILDYISdylILSRGSVIHLGS 288
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHdlDEAMRIGDRIA---IMQNGEVVQVGT 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
76-284 |
3.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLmnnrKITDYN-----------QLRRLCGFVPQ- 143
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNA-----LLKPSSGTI----TIAGYHitpetgnknlkKLRKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 144 DDDLLPLLTVKETLMYSAK-FSLRDSTAKEREERvesLLSDLGLvlvQDSFVGEGDEEdrgVSGGERKRVSIAVEMIRDP 222
Cdd:PRK13641 94 PEAQLFENTVLKDVEFGPKnFGFSEDEAKEKALK---WLKKVGL---SEDLISKSPFE---LSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 223 PILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPSyRILDYISDYLILSRGSVI 284
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMD-DVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
76-288 |
4.15e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVN--HKALDPSSAVLMNNRKITDYNQLRRLCGFVPQ--DDDLLPLL 151
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAKFSLrdstAKEREERVESllSDLGLVLVQDSFVGEGDEEdrgVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:PRK13643 102 VLKDVAFGPQNFGI----PKEKAEKIAA--EKLEMVGLADEFWEKSPFE---LSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 232 SGLDSRNSLQVVELLATMAKSKQRTVLFSihqpsyRILDYISDY----LILSRGSVIHLGS 288
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVT------HLMDDVADYadyvYLLEKGHIISCGT 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
60-265 |
4.23e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLS-YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVNHkaldPSSAVLMnnrkitdy 131
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGRIAR----PAGARVL-------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 nqlrrlcgFVPQdDDLLPLLTVKETLMY---SAKFSlrdstakerEERVESLLSDLGLvlvqDSFVGEGDEE---DRGVS 205
Cdd:COG4178 430 --------FLPQ-RPYLPLGTLREALLYpatAEAFS---------DAELREALEAVGL----GHLAERLDEEadwDQVLS 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 206 GGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSkqrTVLFSI-HQPS 265
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG---TTVISVgHRST 545
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
73-282 |
5.77e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.96 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 73 TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKaldpSSAVLMNNRkitdynqlrrlCGFVPQdddlLPLL- 151
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL----SGSVSVPGS-----------IAYVSQ----EPWIq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 --TVKETLMYSAKFSlrdstaKEREERVE---SLLSDLGLVLVQD-SFVGEgdeedRGV--SGGERKRVSIAVEMIRDPP 223
Cdd:cd03250 79 ngTIRENILFGKPFD------EERYEKVIkacALEPDLEILPDGDlTEIGE-----KGInlSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSY-RILDYIsdyLILSRGS 282
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLlPHADQI---VVLDNGR 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
76-244 |
6.08e-14 |
|
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: 74.84 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA----------VLMNNRKITDYNQLRRLCGFVPQDD 145
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG-----VLEPTSGevnvrvgdewVDMTKPGPDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 DLLPLLTVKETLMYSAKFSLRDSTAKER-----------EERVESLLSDLGlvlvqdsfvgegDEedrgVSGGERKRVSI 214
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDELARMKavitlkmvgfdEEKAEEILDKYP------------DE----LSEGERHRVAL 438
|
170 180 190
....*....|....*....|....*....|
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVE 244
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTH 468
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
72-278 |
6.44e-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: 72.15 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVNHKA-----LDPSSAvlmnnrkitdyNQLRRLCG 139
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLlglekpaQGTVSFRGqdlyqLDRKQR-----------RAFRRDVQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQD--DDLLPLLTVKETLMYSAKfSLRDSTAKEREERVESLLSDLGLvlvQDSFVgegDEEDRGVSGGERKRVSIAVE 217
Cdd:TIGR02769 92 LVFQDspSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGL---RSEDA---DKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHqpSYRILDYISDYLIL 278
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITH--DLRLVQSFCQRVAV 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
61-284 |
9.72e-14 |
|
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: 69.38 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG---------RVNHKALDPSSAVLMNNRKItdy 131
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlykpdsgeiLVDGKEVSFASPRDARRAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 nqlrrlcGFVPQdddllplltvketlmysakfslrdstakereervesllsdlglvlvqdsfvgegdeedrgVSGGERKR 211
Cdd:cd03216 78 -------AMVYQ------------------------------------------------------------LSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGLDSRnslQVVELLATMAKSKQR--TVLFSIHQPS--YRILDYISdylILSRGSVI 284
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPA---EVERLFKVIRRLRAQgvAVIFISHRLDevFEIADRVT---VLRDGRVV 161
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
61-265 |
9.99e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG--RVNHKALDPSSAVLMNNRKITdynqlrRLC 138
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGleTPSAGELLAGTAPLAEAREDT------RLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 gFvpQDDDLLPLLTVKETLMYSAKFSLRDstakereeRVESLLSDLGLvlvqdsfvgegdeEDRG------VSGGERKRV 212
Cdd:PRK11247 87 -F--QDARLLPWKKVIDNVGLGLKGQWRD--------AALQALAAVGL-------------ADRAnewpaaLSGGQKQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPS 265
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVS 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
76-277 |
1.06e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKI-----LAVVGPSGTGKSTLLKIISGRvnhkaLDPSSAVLMNNRKITdynqlrrlcgFVPQ----DDD 146
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGV-----LKPDEGEVDPELKIS----------YKPQyikpDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LlpllTVKETLMySAKFSLRDSTAKEreerveSLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILL 226
Cdd:PRK13409 415 G----TVEDLLR-SITDDLGSSYYKS------EIIKPLQLERLLDKNVKD-------LSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 227 LDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHqpSYRILDYISDYLI 277
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH--DIYMIDYISDRLM 525
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
61-246 |
1.90e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkalDPSSAVLMNNRkitdynQLRrlCGF 140
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV-----APDEGVIKRNG------KLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQD---DDLLPlLTVKETLMysakfsLRDSTAKereervesllSDLGLVLVQDSFVGEGDEEDRGVSGGERKRVSIAVE 217
Cdd:PRK09544 72 VPQKlylDTTLP-LTVNRFLR------LRPGTKK----------EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARA 134
|
170 180
....*....|....*....|....*....
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRNSLQVVELL 246
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
84-276 |
2.75e-13 |
|
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: 70.09 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 84 ESSKILAVVGPSGTGKSTLLKIISGRV-----NHKALDPSSAVLMNNRKITDYNQLRRL------CGFVPQDDDLLPLL- 151
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLkpnlgKFDDPPDWDEILDEFRGSELQNYFTKLlegdvkVIVKPQYVDLIPKAv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 --TVKETLmysakfslrdsTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:cd03236 104 kgKVGELL-----------KKKDERGKLDELVDQLELRHVLDRNIDQ-------LSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063732797 230 PTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPSyrILDYISDYL 276
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDD-NYVLVVEHDLA--VLDYLSDYI 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
60-288 |
2.82e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.40 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHtpilnSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSA-VLMNNRKITDY--NQLRR 136
Cdd:PRK10253 12 QLTLGYGKYTVAE-----NLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-----RLMTPAHGhVWLDGEHIQHYasKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKEtLMYSAKFS---LRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVS 213
Cdd:PRK10253 82 RIGLLAQNATTPGDITVQE-LVARGRYPhqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDT-------LSGGQRQRAW 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIHLGS 288
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLN-QACRYASHLIALREGKIVAQGA 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
76-277 |
4.04e-13 |
|
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: 72.12 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKI-----LAVVGPSGTGKSTLLKIISGRvnhkaLDPSSAVLMNNRKITDYNQlrrlcgFVPQDDDLlpl 150
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGV-----LKPDEGEVDEDLKISYKPQ------YISPDYDG--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 lTVKETLMYSAKFSLRDSTAKEReervesLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEP 230
Cdd:COG1245 417 -TVEEFLRSANTDDFGSSYYKTE------IIKPLGLEKLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063732797 231 TSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyrILDYISDYLI 277
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIY--LIDYISDRLM 527
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
61-235 |
4.57e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSS-AVLMNNRKITDYN------- 132
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR-----LAPDAgEVHYRMRDGQLRDlyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 QLRRLC----GFVPQD--DDLLPLLT----VKETLM------YSAkfsLRDsTAKEREERVESLLSDLglvlvqdsfvge 196
Cdd:PRK11701 82 ERRRLLrtewGFVHQHprDGLRMQVSaggnIGERLMavgarhYGD---IRA-TAGDWLERVEIDAARI------------ 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063732797 197 gDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:PRK11701 146 -DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
76-307 |
4.74e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSS-AVLMNNRKITDYN-----QLRRLCGFVPQDDDLL 148
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL------LErPTSgRVLVDGQDLTALSekelrKARRQIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLLTVKEtlmySAKFSLR-DSTAK-EREERVESLLsDLglvlvqdsfVGEGDEEDR---GVSGGERKRVSIAVEMIRDPP 223
Cdd:PRK11153 95 SSRTVFD----NVALPLElAGTPKaEIKARVTELL-EL---------VGLSDKADRypaQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSY--RILDYISdylILSRGSVIHLGSLE----HLEDSIA 297
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVvkRICDRVA---VIDAGRLVEQGTVSevfsHPKHPLT 237
|
250
....*....|....*.
gi 1063732797 298 K------LGFQIPEQL 307
Cdd:PRK11153 238 RefiqstLHLDLPEDY 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
75-236 |
5.62e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSSA-VLMNNRKITDYN-QLRRLCgFVPQDDDLLPLLT 152
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEK-----PTEGqIFIDGEDVTHRSiQQRDIC-MVFQSYALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 153 VKETLMYSAKFSLRDSTakEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTS 232
Cdd:PRK11432 95 LGENVGYGLKMLGVPKE--ERKQRVKEALELVDLAGFEDRYVDQ-------ISGGQQQRVALARALILKPKVLLFDEPLS 165
|
....
gi 1063732797 233 GLDS 236
Cdd:PRK11432 166 NLDA 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
89-292 |
5.65e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 89 LAVVGPSGTGKSTLLKIISGRVNHKAldpssAVLMNNRKITDYN--QLRRLCGFVPQDDdLLPLLTVKETLmysakfSLR 166
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGFLPYQG-----SLKINGIELRELDpeSWRKHLSWVGQNP-QLPHGTLRDNV------LLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 167 DSTAkeREERVESLLSD-----------LGLvlvqDSFVGEGDeedRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:PRK11174 447 NPDA--SDEQLQQALENawvseflpllpQGL----DTPIGDQA---AGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 236 SRNSLQVVELLATMakSKQRTVLFSIHQpsyriLDYISDY---LILSRGSVIHLGSLEHL 292
Cdd:PRK11174 518 AHSEQLVMQALNAA--SRRQTTLMVTHQ-----LEDLAQWdqiWVMQDGQIVQQGDYAEL 570
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
71-237 |
7.19e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYNQLRRLCGFVPQDDDLL 148
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG------LERITSgeIWIGGRVVNELEPADRDIAMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 PLLTVKETLMYSAKfsLRDSTAKEREERVESLLSDLGLvlvqDSFVgegDEEDRGVSGGERKRVSIAVEMIRDPPILLLD 228
Cdd:PRK11650 89 PHMSVRENMAYGLK--IRGMPKAEIEERVAEAARILEL----EPLL---DRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
....*....
gi 1063732797 229 EPTSGLDSR 237
Cdd:PRK11650 160 EPLSNLDAK 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
74-235 |
9.89e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLA----AessKIlAVVGPSGTGKSTLLKIISGrvnhkaLDPSS---AVLMNNRKItdynqlrrlcGFVPQDDD 146
Cdd:PRK11819 21 QILKDISLSffpgA---KI-GVLGLNGAGKSTLLRIMAG------VDKEFegeARPAPGIKV----------GYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLLTVKETLM---------------YSAKFSLR----DSTAKER---EERVESL-LSDLglvlvqDSFVG-------- 195
Cdd:PRK11819 81 LDPEKTVRENVEegvaevkaaldrfneIYAAYAEPdadfDALAAEQgelQEIIDAAdAWDL------DSQLEiamdalrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063732797 196 -EGDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:PRK11819 155 pPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-295 |
1.02e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgRVNHK--ALDPSSAVLMNNRKITDYN---QL 134
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLN-RMNDKvsGYRYSGDVLLGGRSIFNYRdvlEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYSAKFSLrdSTAKEREERVESLLSDLGLvlvQDSFVGEGDEEDRGVSGGERKRVSI 214
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL--VPRKEFRGVAQARLTEVGL---WDAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAksKQRTVLFSIHQ--PSYRILDYISDYLilsRGSVIHLGSLEHL 292
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNlaQAARISDRAALFF---DGRLVEEGPTEQL 249
|
...
gi 1063732797 293 EDS 295
Cdd:PRK14271 250 FSS 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
76-259 |
1.53e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRK--ITDYNQLRRL-CGFVPQDDDLLPLL 151
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYG-----LYQPDSgEILIDGKPvrIRSPRDAIALgIGMVHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSA--KFSLRDSTAKEReERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:COG3845 96 TVAENIVLGLepTKGGRLDRKAAR-ARIRELSERYGLDVDPDAKVED-------LSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 1063732797 230 PTSGLdsrnSLQ-VVELLATMA--KSKQRTVLF 259
Cdd:COG3845 168 PTAVL----TPQeADELFEILRrlAAEGKSIIF 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
87-276 |
2.24e-12 |
|
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: 69.81 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 87 KILAVVGPSGTGKSTLLKIISGRV-----NHKAlDPS-SAVLMNNRKITDYNQLRRLC-GFV-----PQDDDLLPLL--- 151
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELkpnlgDYDE-EPSwDEVLKRFRGTELQDYFKKLAnGEIkvahkPQYVDLIPKVfkg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMysakfslrdsTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:COG1245 179 TVRELLE----------KVDERG-KLDELAEKLGLENILDRDISE-------LSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063732797 232 SGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPSyrILDYISDYL 276
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEG-KYVLVVEHDLA--ILDYLADYV 282
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
61-234 |
2.51e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG---------RVNHKALDPSSAVLMNNRKItdY 131
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGivppdsgtlEIGGNPCARLTPAKAHQLGI--Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 nqlrrlcgFVPQDDDLLPLLTVKETLMysakFSLRDStaKEREERVESLLSDLGLVLVQDSFVGEGDEEDRGVsggerkr 211
Cdd:PRK15439 90 --------LVPQEPLLFPNLSVKENIL----FGLPKR--QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQI------- 148
|
170 180
....*....|....*....|...
gi 1063732797 212 VSIAVEMIRDPPILLLDEPTSGL 234
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASL 171
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
76-281 |
3.01e-12 |
|
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: 67.05 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAES-----SKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAVlmnnRKITdynqlrrlcgFVPQDDDLLPL 150
Cdd:cd03237 10 LGEFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL----DTVS----------YKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETLMYSAKFSLRDSTAKEreerveSLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEP 230
Cdd:cd03237 76 GTVRDLLSSITKDFYTHPYFKT------EIAKPLQIEQILDREVPE-------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 231 TSGLDSRNSLQVVELLATMAKSKQRTVLFSIHqpSYRILDYISDYLILSRG 281
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEH--DIIMIDYLADRLIVFEG 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
61-287 |
4.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH-TPI----LNSVSLAAESSKILAVVGPSGTGKSTLLK---------------IISGRVNHKALDPSSA 120
Cdd:PRK13651 3 IKVKNIVKIFNKkLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalllpdtgtiewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 121 VLMNN-------RKITDYNQLRRLCGFVPQDDDL-LPLLTVKETLMYSA-KFSLRDSTAKEREERVesllsdLGLVLVQD 191
Cdd:PRK13651 83 VLEKLviqktrfKKIKKIKEIRRRVGVVFQFAEYqLFEQTIEKDIIFGPvSMGVSKEEAKKRAAKY------IELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 192 SFVgegDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqRTVLFSIHQPSyRILDY 271
Cdd:PRK13651 157 SYL---QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLD-NVLEW 231
|
250
....*....|....*.
gi 1063732797 272 ISDYLILSRGSVIHLG 287
Cdd:PRK13651 232 TKRTIFFKDGKIIKDG 247
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
75-287 |
4.78e-12 |
|
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: 66.02 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKIT---DYNqlrrlCGFVPQdddllplL 151
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG-----IYPPDSGTVTVRGRVSsllGLG-----GGFNPE-------L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAkfSLRDSTAKEREERVESLL--SDLGlvlvqDSFvgegDEEDRGVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:cd03220 100 TGRENIYLNG--RLLGLSRKEIDEKIDEIIefSELG-----DFI----DLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 230 PTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQPSYrILDYISDYLILSRGSVIHLG 287
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
87-276 |
5.28e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 87 KILAVVGPSGTGKSTLLKIISGRV-----NHKALDPSSAVLMNNRKITDYNQLRRLC-GFV-----PQDDDLLPLL---T 152
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILSGELipnlgDYEEEPSWDEVLKRFRGTELQNYFKKLYnGEIkvvhkPQYVDLIPKVfkgK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 153 VKETLMysakfslrdsTAKEREeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTS 232
Cdd:PRK13409 180 VRELLK----------KVDERG-KLDEVVERLGLENILDRDISE-------LSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063732797 233 GLDSRNSLQVVELLATMAKSKqrTVLFSIHQPSyrILDYISDYL 276
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAEGK--YVLVVEHDLA--VLDYLADNV 281
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
59-294 |
5.51e-12 |
|
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: 69.20 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 59 YSLTVTNLSYTINHT--PILNSVSLAAESSKILAVVGPSGTGKSTLLkiisgrvnhkaldpsSAVLMNNRKITDYNQLRR 136
Cdd:TIGR00957 635 NSITVHNATFTWARDlpPTLNGITFSIPEGALVAVVGQVGCGKSSLL---------------SALLAEMDKVEGHVHMKG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDdLLPLLTVKETLMYSAkfSLRDSTAKEREERVeSLLSDLGLVLVQDSfvGEGDEEDRGVSGGERKRVSIAV 216
Cdd:TIGR00957 700 SVAYVPQQA-WIQNDSLRENILFGK--ALNEKYYQQVLEAC-ALLPDLEILPSGDR--TEIGEKGVNLSGGQKQRVSLAR 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVE-LLATMAKSKQRTVLFSIHQPSYriLDYISDYLILSRGSVIHLGSLEHLED 294
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
74-235 |
5.65e-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: 68.42 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLA-AESSKIlAVVGPSGTGKSTLLKIISGrvnhkaLDPSS---AVLMNNRKItdynqlrrlcGFVPQDDDLLP 149
Cdd:TIGR03719 19 EILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAG------VDKDFngeARPQPGIKV----------GYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 150 LLTVKETLM---------------YSAKFSLRD----STAKEREERVESLLS------DLGLVLVQDSF-VGEGDEEDRG 203
Cdd:TIGR03719 82 TKTVRENVEegvaeikdaldrfneISAKYAEPDadfdKLAAEQAELQEIIDAadawdlDSQLEIAMDALrCPPWDADVTK 161
|
170 180 190
....*....|....*....|....*....|..
gi 1063732797 204 VSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
60-323 |
5.79e-12 |
|
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: 66.80 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINhtPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSSAVLMNNRKITdynqlrrlcg 139
Cdd:cd03291 39 NLFFSNLCLVGA--PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGE-----LEPSEGKIKHSGRIS---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPlLTVKETLMYSAKFSlrdstakerEERVES------LLSDLGLVLVQDSFV-GEGdeedrGV--SGGERK 210
Cdd:cd03291 102 FSSQFSWIMP-GTIKENIIFGVSYD---------EYRYKSvvkacqLEEDITKFPEKDNTVlGEG-----GItlSGGQRA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVE-LLATMAKSKQRtVLFSIHQPSYRILDYIsdyLILSRGSVIHLGSL 289
Cdd:cd03291 167 RISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTR-ILVTSKMEHLKKADKI---LILHEGSSYFYGTF 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063732797 290 EHLED-----SIAKLGFQIPEQLNPIEFAMEIVESLRTF 323
Cdd:cd03291 243 SELQSlrpdfSSKLMGYDTFDQFSAERRNSILTETLRRF 281
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
60-288 |
9.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.92 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINH-TPI----LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKIT---- 129
Cdd:PRK13649 2 GINLQNVSYTYQAgTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNG-----LHVPTQGsVRVDDTLITstsk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 --DYNQLRRLCGFVPQdddlLPLLTV-KETLMYSAKFSLRD-STAKEREERVEslLSDLGLVLVQDSFVGEGDEEdrgVS 205
Cdd:PRK13649 77 nkDIKQIRKKVGLVFQ----FPESQLfEETVLKDVAFGPQNfGVSQEEAEALA--REKLALVGISESLFEKNPFE---LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 206 GGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSihqpsyRILDYISDY----LILSRG 281
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVT------HLMDDVANYadfvYVLEKG 221
|
....*..
gi 1063732797 282 SVIHLGS 288
Cdd:PRK13649 222 KLVLSGK 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
60-354 |
9.97e-12 |
|
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: 68.40 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTInhTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSSAVLMNNRKITdynqlrrlcg 139
Cdd:TIGR01271 428 GLFFSNFSLYV--TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGE-----LEPSEGKIKHSGRIS---------- 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPlLTVKETLMYSAKFSLRDSTAKEREERVEsllSDLGLVLVQDSFV-GEGdeedrGV--SGGERKRVSIAV 216
Cdd:TIGR01271 491 FSPQTSWIMP-GTIKDNIIFGLSYDEYRYTSVIKACQLE---EDIALFPEKDKTVlGEG-----GItlSGGQRARISLAR 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 217 EMIRDPPILLLDEPTSGLDSRNSLQVVE-LLATMAKSKQRTVLFSihqpSYRILDYISDYLILSRGSVIHLGSLEHLED- 294
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVVTEKEIFEsCLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTFSELQAk 637
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 295 ----SIAKLGFQIPEQLNPIEFAMEIVESLRTFKPNSVAVVESssmWPEnnendgiiSKKEAFR 354
Cdd:TIGR01271 638 rpdfSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTVFS---GPE--------TIKQSFK 690
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
61-259 |
1.47e-11 |
|
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: 67.02 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI----NHTPILNSVSLAAESSKILAVVGPSGTGKS-TLLKIIsGRVNHKALDPSSAVLMNNRKITDYN--Q 133
Cdd:COG4172 7 LSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAHPSGSILFDGQDLLGLSerE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLCG----FVPQD--DDLLPLLTV----KETLMYSAKFSlrdstAKEREERVESLLSDLGLVlvqdsfvgegDEEDR- 202
Cdd:COG4172 86 LRRIRGnriaMIFQEpmTSLNPLHTIgkqiAEVLRLHRGLS-----GAAARARALELLERVGIP----------DPERRl 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 203 -----GVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLF 259
Cdd:COG4172 151 dayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLL 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
61-284 |
1.65e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkALDPSSAVLMNNRKIT----------- 129
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEV---LLDDGRIIYEQDLIVArlqqdpprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 -------------------DYNQLRRLCGFVPQDDDLLPLLTVKETLMYSAKFSLrdstakerEERVESLLSDLGLvlvq 190
Cdd:PRK11147 81 gtvydfvaegieeqaeylkRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQL--------ENRINEVLAQLGL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 191 dsfvgEGDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDsrnsLQVVELLATMAKSKQRTVLFSIHQPSY---- 266
Cdd:PRK11147 149 -----DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFirnm 219
|
250 260
....*....|....*....|
gi 1063732797 267 --RILDyisdyliLSRGSVI 284
Cdd:PRK11147 220 atRIVD-------LDRGKLV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
61-299 |
1.71e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.52 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkalDP---SSAVLMNNRKITDYNQ---L 134
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-------DPratSGRIVFDGKDITDWQTakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTaKEREERVESLLSDLGLVLVQDSFVgegdeedrgVSGGERKRVSI 214
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQF-QERIKWVYELFPRLHERRIQRAGT---------MSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 215 AVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIHQPSYRILDYISDYLILSRGSVIhlgslehLED 294
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL--REQGMTIFLVEQNANQALKLADRGYVLENGHVV-------LED 219
|
....*
gi 1063732797 295 SIAKL 299
Cdd:PRK11614 220 TGDAL 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-263 |
2.23e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII------------------SGRVNHKALDP---------------- 117
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehTNDMTNEQDYQgdeeqnvgmknvnefs 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 118 ---------SSAVLMNNRKI-------TDYN--QLRRLCGFVPQDddllPLLtVKETLMYSAKFSLRDSTAKER------ 173
Cdd:PTZ00265 1260 ltkeggsgeDSTVFKNSGKIlldgvdiCDYNlkDLRNLFSIVSQE----PML-FNMSIYENIKFGKEDATREDVkrackf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 174 ---EERVESLLSDLglvlvqDSFVGEgdeEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSrNSLQVVELLATMA 250
Cdd:PTZ00265 1335 aaiDEFIESLPNKY------DTNVGP---YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEKTIVDI 1404
|
250
....*....|....
gi 1063732797 251 KSK-QRTVLFSIHQ 263
Cdd:PTZ00265 1405 KDKaDKTIITIAHR 1418
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
63-258 |
2.23e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG--RVNHKALDpssaVL---MNNRKitdynQLRRL 137
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQQGRVE----VLggdMADAR-----HRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CG---FVPQ--DDDLLPLLTVKETLMYSAK-FSLRdstAKEREERVESLLSDLGLvlvqDSFVgegdeeDR--G-VSGGE 208
Cdd:NF033858 75 CPriaYMPQglGKNLYPTLSVFENLDFFGRlFGQD---AAERRRRIDELLRATGL----APFA------DRpaGkLSGGM 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLD--SRNslQVVELLATM-AKSKQRTVL 258
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDplSRR--QFWELIDRIrAERPGMSVL 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
61-293 |
2.46e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAV----LMNNRKIT--DYNQL 134
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVtgdvTLNGEPLAaiDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKEREERVeslLSDLGLVLV-QDSFVGegdeedRGV---SGGERK 210
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGE---IAWQALALAgATALVG------RDVttlSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAV---------EMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSY--RILDYI---SDYL 276
Cdd:PRK13547 153 RVQFARvlaqlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaaRHADRIamlADGA 232
|
250
....*....|....*..
gi 1063732797 277 ILSRGSVIHLGSLEHLE 293
Cdd:PRK13547 233 IVAHGAPADVLTPAHIA 249
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
61-263 |
2.63e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSSAVLMNNRKITDYNQL---RRL 137
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLN-----PEKGEILFERQSIKKDLCtyqKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CgFVPQDDDLLPLLTVKETLMYSAKFSlrdSTAKEREERVEslLSDLGLVLvqdsfvgegDEEDRGVSGGERKRVSIAVE 217
Cdd:PRK13540 77 C-FVGHRSGINPYLTLRENCLYDIHFS---PGAVGITELCR--LFSLEHLI---------DYPCGLLSSGQKRQVALLRL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 218 MIRDPPILLLDEPTSGLDSRnSLQVVELLATMAKSKQRTVLFSIHQ 263
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDEL-SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
76-269 |
2.96e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKITDYNQ-----LRRLCGFVPQDDDLLP 149
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-----IERPSAgKIWFSGHDITRLKNrevpfLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 150 LLTVKETLmySAKFSLRDSTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:PRK10908 93 DRTVYDNV--AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 230 PTSGLDSRNSLQVVELLATMAKSKQrTVLFSIH------QPSYRIL 269
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGV-TVLMATHdiglisRRSYRML 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
59-271 |
3.19e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.03 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 59 YSLTVTNLS-YTINHTPILNsVSLAAESSKILAVVGPSGTGKSTLLK--------IISGRVNHKaldpssaVLMNNRKI- 128
Cdd:PRK14243 9 TVLRTENLNvYYGSFLAVKN-VWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlIPGFRVEGK-------VTFHGKNLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 ---TDYNQLRRLCGFVPQDDDLLPLlTVKETLMYSAKFslrDSTAKEREERVESLLSDLGLV-LVQDSFVGEGdeedRGV 204
Cdd:PRK14243 81 apdVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARI---NGYKGDMDELVERSLRQAALWdEVKDKLKQSG----LSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 205 SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMakSKQRTVLFSIH--QPSYRILDY 271
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHnmQQAARVSDM 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
61-317 |
3.55e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKI---------ISGRV-NHKALDPSSAVLMNNRKItd 130
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrgmdqyepTSGRIiYHVALCEKCGYVERPSKV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 131 yNQLRRLCG--FVPQDDDLLPL-------LTVKETLMYSAKFSLRDStaKEREERVESLLSDLGLvlvqdsfvgEGDEE- 200
Cdd:TIGR03269 79 -GEPCPVCGgtLEPEEVDFWNLsdklrrrIRKRIAIMLQRTFALYGD--DTVLDNVLEALEEIGY---------EGKEAv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 201 -------------------DRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSI 261
Cdd:TIGR03269 147 gravdliemvqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 262 HQPsyRILDYISDYLI-LSRGSVIHLGSLEHLedsIAKL--GFQIPEQLNPIEFAMEIV 317
Cdd:TIGR03269 227 HWP--EVIEDLSDKAIwLENGEIKEEGTPDEV---VAVFmeGVSEVEKECEVEVGEPII 280
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
79-235 |
4.80e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS--AVL----MNNRKItdynQLRRLCGFVPQDDDLLPLLT 152
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTG-----LLPASEgeAWLfgqpVDAGDI----ATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 153 VKETLMYSAK-FSLrdsTAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:NF033858 356 VRQNLELHARlFHL---PAAEIAARVAEMLERFDLADVADALPDS-------LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 1063732797 232 SGLD 235
Cdd:NF033858 426 SGVD 429
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
75-279 |
5.33e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSSA-VLMN---NRKITDYNQLRRLCGFVPQDddllPL 150
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLI-----ERLYDPTEGdIIINdshNLKDINLKWWRSKIGVVSQD----PL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 L---TVKETLMYSAkFSLRDSTAKERE-------------------ERVESLLSDL-------GL--------------- 186
Cdd:PTZ00265 471 LfsnSIKNNIKYSL-YSLKDLEALSNYynedgndsqenknkrnscrAKCAGDLNDMsnttdsnELiemrknyqtikdsev 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 187 ------VLVQDSFVGEGDEEDRGV-------SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSK 253
Cdd:PTZ00265 550 vdvskkVLIHDFVSALPDKYETLVgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
|
250 260
....*....|....*....|....*.
gi 1063732797 254 QRTVLFSIHQPSyrILDYISDYLILS 279
Cdd:PTZ00265 630 NRITIIIAHRLS--TIRYANTIFVLS 653
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
55-292 |
9.18e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 55 TPNRYSLTVTNLSYTINH----TPILNSVSLAAESSKILAVVGPSGTGKS----TLLKII---SGRVNhkaldpSSAVLM 123
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQ------CDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 124 N--NRKITDYN-----QLRRLCG------FVPQDDDLLPLLTVKETLMYSakfsLRDSTAKEREERVESLLSDLGLVLVQ 190
Cdd:PRK10261 81 RrrSRQVIELSeqsaaQMRHVRGadmamiFQEPMTSLNPVFTVGEQIAES----IRLHQGASREEAMVEAKRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 191 DSFVGEGDEEDRgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYrILD 270
Cdd:PRK10261 157 EAQTILSRYPHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGV-VAE 234
|
250 260
....*....|....*....|..
gi 1063732797 271 YISDYLILSRGSVIHLGSLEHL 292
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQI 256
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
79-290 |
1.28e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSSA-VLMNNRKITDYNQ-------LRRLcGFVPQDDDLLPL 150
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTR-----PQKGrIVLNGRVLFDAEKgiclppeKRRI-GYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETLMYSAKfslrdstaKEREERVESLLSDLGLVLVQDSFvgegdeeDRGVSGGERKRVSIAVEMIRDPPILLLDEP 230
Cdd:PRK11144 91 YKVRGNLRYGMA--------KSMVAQFDKIVALLGIEPLLDRY-------PGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 231 TSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQpsyriLDYI---SDYLI-LSRGSVIHLGSLE 290
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIPILYVSHS-----LDEIlrlADRVVvLEQGKVKAFGPLE 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
77-292 |
2.77e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 77 NSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhKALDPSSAVLMNN-RKITD--YNQLRRLCGFVPQDD--DLLPLL 151
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV--KATDGEVAWLGKDlLGMKDdeWRAVRSDIQMIFQDPlaSLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLVlvqDSFVGEGDEEdrgVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:PRK15079 116 TIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLL---PNLINRYPHE---FSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 232 SGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSyrILDYISD-YLILSRGSVIHLGSLEHL 292
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLA--VVKHISDrVLVMYLGHAVELGTYDEV 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
76-288 |
3.28e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDY--NQLRRLCGFVPQDDDLLPLLTV 153
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-----LLPGSGSIQFAGQPLEAWsaAELARHRAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 154 KETLMYSakfslrdSTAKEREERVESLLSDLGlvlvqdSFVGEGDEEDRGV---SGGERKRVSIA-VEMIRDPPI----- 224
Cdd:PRK03695 87 FQYLTLH-------QPDKTRTEAVASALNEVA------EALGLDDKLGRSVnqlSGGEWQRVRLAaVVLQVWPDInpagq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 225 -LLLDEPTSGLDSRNSLQVVELLATMAkSKQRTVLFSIHQPSyRILDYISDYLILSRGSVIHLGS 288
Cdd:PRK03695 154 lLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGR 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
61-262 |
3.75e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI--NHTPI--LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAVLMNNRKITDYN--QL 134
Cdd:PRK11022 4 LNVDKLSVHFgdESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISekER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 135 RRLCG----FVPQD--DDLLPLLTVKETLMYSAKFSlRDSTAKEREERVESLLSdlglvlvqdsFVGEGDEEDR------ 202
Cdd:PRK11022 84 RNLVGaevaMIFQDpmTSLNPCYTVGFQIMEAIKVH-QGGNKKTRRQRAIDLLN----------QVGIPDPASRldvyph 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 GVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITH 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
56-288 |
5.71e-10 |
|
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: 59.35 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 56 PNRYSLTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIIsgrvnHKALDPSSA-VLMNNRKIT--D 130
Cdd:cd03369 2 PEHGEIEVENLSvrYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL-----FRFLEAEEGkIEIDGIDIStiP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 131 YNQLRRLCGFVPQDDDLLpLLTVKETLmysakfslrDSTAKEREERVESLLSdlglvlvqdsfVGEGDEEdrgVSGGERK 210
Cdd:cd03369 77 LEDLRSSLTIIPQDPTLF-SGTIRSNL---------DPFDEYSDEEIYGALR-----------VSEGGLN---LSQGQRQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 211 RVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELL-ATMAKSkqrTVLFSIHQpsyriLDYISDY---LILSRGSVIHL 286
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNS---TILTIAHR-----LRTIIDYdkiLVMDAGEVKEY 204
|
..
gi 1063732797 287 GS 288
Cdd:cd03369 205 DH 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
65-321 |
5.81e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTI-NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAldpsSAVLMNNRKITDYNQL---RRLCGF 140
Cdd:PRK13644 6 NVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK----GKVLVSGIDTGDFSKLqgiRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPL-LTVKETLMYSAKFSLRDSTakEREERVESLLSDLGLVLVQdsfvgegDEEDRGVSGGERKRVSIAVEMI 219
Cdd:PRK13644 82 VFQNPETQFVgRTVEEDLAFGPENLCLPPI--EIRKRVDRALAEIGLEKYR-------HRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQ-PSYRILDYIsdyLILSRGSVIHLGSLEHL--EDSI 296
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNlEELHDADRI---IVMDRGKIVLEGEPENVlsDVSL 228
|
250 260
....*....|....*....|....*
gi 1063732797 297 AKLGFQIPEqlnpiefAMEIVESLR 321
Cdd:PRK13644 229 QTLGLTPPS-------LIELAENLK 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
61-288 |
8.24e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.19 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI---------NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhkalDPSSA-VLMNNRKIT- 129
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMI-----EPTSGeLLIDDHPLHf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 -DYNQLRRLCGFVPQD--DDLLPLLTVKETLmysaKFSLR---DSTAKEREERVESLLSDLGLVLVQDSFVgegdeeDRG 203
Cdd:PRK15112 80 gDYSYRSQRIRMIFQDpsTSLNPRQRISQIL----DFPLRlntDLEPEQREKQIIETLRQVGLLPDHASYY------PHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 204 VSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQpSYRILDYISD-YLILSRGS 282
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQGISYIYVTQ-HLGMMKHISDqVLVMHQGE 227
|
....*.
gi 1063732797 283 VIHLGS 288
Cdd:PRK15112 228 VVERGS 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
76-262 |
2.09e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrVNHkaldPSSAVLMNNRKITDYNQLRRLCG----FVPQDDDLLPLL 151
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG-NYQ----PDAGSILIDGQEMRFASTTAALAagvaIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLM---YSAKFSLRDStaKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLD 228
Cdd:PRK11288 95 TVAENLYlgqLPHKGGIVNR--RLLNYEAREQLEHLGVDIDPDTPLKY-------LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190
....*....|....*....|....*....|....
gi 1063732797 229 EPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIH 262
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIREL-RAEGRVILYVSH 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
76-322 |
2.45e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.57 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkalDPSSAVLMNNRKITDYN--QLRRLCGFVPQD-DDLLPLLT 152
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE----EFEGKVKIDGELLTAENvwNLRRKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 153 VKETLMYSAkfslrDSTAKEREERVESLlsDLGLVLVqdSFVGEGDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTS 232
Cdd:PRK13642 99 VEDDVAFGM-----ENQGIPREEMIKRV--DEALLAV--NMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 233 GLDSRNSLQVVELLATMAKSKQRTVLFSIHQpsyriLDYISD---YLILSRGSVIHLGSLEHL---EDSIAKLGFQIPeq 306
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHD-----LDEAASsdrILVMKAGEIIKEAAPSELfatSEDMVEIGLDVP-- 242
|
250
....*....|....*.
gi 1063732797 307 lnpieFAMEIVESLRT 322
Cdd:PRK13642 243 -----FSSNLMKDLRK 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
76-234 |
2.99e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLmnNRKITDYNQL-RRLC-----GFVPQDDDLLP 149
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG-----IHEPTKGTI--TINNINYNKLdHKLAaqlgiGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 150 LLTVKETLmYSAKFSLRDSTA------KEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPP 223
Cdd:PRK09700 94 ELTVLENL-YIGRHLTKKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVAN-------LSISHKQMLEIAKTLMLDAK 165
|
170
....*....|.
gi 1063732797 224 ILLLDEPTSGL 234
Cdd:PRK09700 166 VIIMDEPTSSL 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
61-287 |
3.51e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSsaVLMNNRKITDYNQLRRLCGF 140
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGT--VEFKGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VpqdddLLPLLTVKETLMYSAKFSLRDSTAKEREERVESLLsdlglvlvqDSFVGEGDEEDR-----------------G 203
Cdd:PRK09580 80 I-----FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPL---------DRFDFQDLMEEKiallkmpedlltrsvnvG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 204 VSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSrNSLQVVELLATMAKSKQRTVLFSIHQPsyRILDYIS-DYL-ILSRG 281
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDI-DALKIVADGVNSLRDGKRSFIIVTHYQ--RILDYIKpDYVhVLYQG 222
|
....*.
gi 1063732797 282 SVIHLG 287
Cdd:PRK09580 223 RIVKSG 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
61-262 |
5.68e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHT----PILNSVSLAAESSKILAVVGPSGTGKS-TLLKIISGRVNHKALDPSSAVLMNNRKI--TDYNQ 133
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPSGDIRFHGESLlhASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLCG------FVPQDDDLLPLLTVKETLmySAKFSLRDSTAKErEERVEsLLSDLGLVLVQDSFVGEGDEEDRgVSGG 207
Cdd:PRK15134 86 LRGVRGnkiamiFQEPMVSLNPLHTLEKQL--YEVLSLHRGMRRE-AARGE-ILNCLDRVGIRQAAKRLTDYPHQ-LSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 208 ERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITH 215
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
89-246 |
6.09e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 89 LAVVGPSGTGKSTLLKIISGRvnhkaLDPSSAVLMNNRKItdynqlrRLCGFVPQDDDLLPLLTvkETLMYSAKfslrdS 168
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGE-----LQPSSGTVFRSAKV-------RMAVFSQHHVDGLDLSS--NPLLYMMR-----C 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 169 TAKEREERVESLLSDLGL---VLVQDSFVgegdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDsrnsLQVVEL 245
Cdd:PLN03073 599 FPGVPEQKLRAHLGSFGVtgnLALQPMYT---------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEA 665
|
.
gi 1063732797 246 L 246
Cdd:PLN03073 666 L 666
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
65-281 |
9.55e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnHKALDPSSAVLMNNRKItdynqlrrlcgfvPQD 144
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA--LKGTPVAGCVDVPDNQF-------------GRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 145 ----DDLLPLLTVKEtlmysakfslrdstAKEreervesLLSDLGLVLVQdSFVGEGDEedrgVSGGERKRVSIAVEMIR 220
Cdd:COG2401 100 asliDAIGRKGDFKD--------------AVE-------LLNAVGLSDAV-LWLRRFKE----LSTGQKFRFRLALLLAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 221 DPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQpsYRILDYISDYLILSRG 281
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH--YDVIDDLQPDLLIFVG 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
74-266 |
9.81e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.19 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLL-------KIISGRVNHKALDPSSAVLMNNRKITDYNqlrrlCGFVPQDDD 146
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemQTLEGKVHWSNKNESEPSFEATRSRNRYS-----VAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 147 LLPLlTVKETLMYSAKFSlrdstaKEREERVE---SLLSDLGLVLVQD-SFVGEgdeedRGV--SGGERKRVSIAVEMIR 220
Cdd:cd03290 90 LLNA-TVEENITFGSPFN------KQRYKAVTdacSLQPDIDLLPFGDqTEIGE-----RGInlSGGQRQRICVARALYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063732797 221 DPPILLLDEPTSGLDSRNSLQVV-ELLATMAKSKQRTVLFSIHQPSY 266
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
61-235 |
1.14e-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: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSytinHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYNQLRRL- 137
Cdd:cd03215 5 LEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG------LRPPASgeITLDGKPVTRRSPRDAIr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 --CGFVPQD---DDLLPLLTVKETLMysakfslrdstakereervesllsdLGLVLvqdsfvgegdeedrgvSGGERKRV 212
Cdd:cd03215 75 agIAYVPEDrkrEGLVLDLSVAENIA-------------------------LSSLL----------------SGGNQQKV 113
|
170 180
....*....|....*....|...
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLD 235
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVD 136
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
61-262 |
1.24e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHT---------PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLD-PSSA-VLMNNRKIT 129
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG------LEsPSQGnVSWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 DYNQ-----LRRLCGFVPQD--DDLLPLLTVKETLMYSAKFSLRDSTAkEREERVESLLSDLGLVLvqdsfvGEGDEEDR 202
Cdd:PRK10419 78 KLNRaqrkaFRRDIQMVFQDsiSAVNPRKTVREIIREPLRHLLSLDKA-ERLARASEMLRAVDLDD------SVLDKRPP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 203 GVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
86-281 |
1.27e-08 |
|
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: 54.89 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 86 SKILAVVGPSGTGKSTLLKIISGrvnhkALDPSsavlmnnrkitdynqlrrlcgfvpQDDDLLPLLTVKETLMYSAkfsl 165
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAG-----QLIPN------------------------GDNDEWDGITPVYKPQYID---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 166 rdstakereervesllsdlglvlvqdsfvgegdeedrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVEL 245
Cdd:cd03222 72 --------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063732797 246 LATMAKSKQRTVLFSIHqpSYRILDYISDYLILSRG 281
Cdd:cd03222 114 IRRLSEEGKKTALVVEH--DLAVLDYLSDRIHVFEG 147
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
61-235 |
2.00e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKITDYNQLRRLCGF 140
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAG-----LLHVESGQIQIDGKTATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 141 VPQDDDLLPLLTVKETLMYSAKFSLRdstakeREERVE-SLLSDLGLVLVQDSFVgegdeedRGVSGGERKRVSIAVEMI 219
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLCGLHGR------RAKQMPgSALAIVGLAGYEDTLV-------RQLSAGQKKRLALARLWL 153
|
170
....*....|....*.
gi 1063732797 220 RDPPILLLDEPTSGLD 235
Cdd:PRK13543 154 SPAPLWLLDEPYANLD 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
74-295 |
2.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHkaLDPSSAVLmnnrkitdynqlRRLCGFVPQdddlLPLL-- 151
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH--AETSSVVI------------RGSVAYVPQ----VSWIfn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 -TVKETLMYSAKFslrDSTAKEREERVESLLSDLGLVLVQD-SFVGEgdeedRGV--SGGERKRVSIAVEMIRDPPILLL 227
Cdd:PLN03232 693 aTVRENILFGSDF---ESERYWRAIDVTALQHDLDLLPGRDlTEIGE-----RGVniSGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 228 DEPTSGLDSRNSLQVVE-LLATMAKSKQRTVLFSihqpSYRILDYISDYLILSRGSVIHLGSLEHLEDS 295
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTN----QLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
61-265 |
3.34e-08 |
|
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: 53.31 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTI-NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVNHkaldPSSAVLMnnrkitdyn 132
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgSGRIGM----PEGEDLL--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 qlrrlcgFVPQdDDLLPLLTVKETLMYSakfslrdstakereervesllsdLGLVLvqdsfvgegdeedrgvSGGERKRV 212
Cdd:cd03223 68 -------FLPQ-RPYLPLGTLREQLIYP-----------------------WDDVL----------------SGGEQQRL 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLDsrnsLQVVELLATMAKSKQRTVLFSIHQPS 265
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALD----EESEDRLYQLLKELGITVISVGHRPS 149
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
80-264 |
5.24e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 80 SLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSS-AVLMNNRKIT----DYNQlrrlcgfvpqddDLL------ 148
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAG-----LARPDAgEVLWQGEPIRrqrdEYHQ------------DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 149 ---PLLTVKETLmysaKFSLRDStAKEREERVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPIL 225
Cdd:PRK13538 84 gikTELTALENL----RFYQRLH-GPGDDEALWEALAQVGLAGFEDVPVRQ-------LSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063732797 226 LLDEPTSGLDSrnslQVVELL-ATMAKSKQR--TVLFSIHQP 264
Cdd:PRK13538 152 ILDEPFTAIDK----QGVARLeALLAQHAEQggMVILTTHQD 189
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
58-235 |
5.27e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 58 RYSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLmnnrKITDYNQLrrl 137
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-----ELEPDSGTV----KWSENANI--- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 cGFVPQD--DDLLPLLTVKEtLMYSAKfslrdsTAKEREERVESLlsdLGLVLvqdsFvgEGDEEDRGV---SGGERKRV 212
Cdd:PRK15064 385 -GYYAQDhaYDFENDLTLFD-WMSQWR------QEGDDEQAVRGT---LGRLL----F--SQDDIKKSVkvlSGGEKGRM 447
|
170 180
....*....|....*....|...
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGLD 235
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
205-303 |
6.07e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 205 SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYRILDYisDYLILSRGSVI 284
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAH--ELTVIDRGRVI 223
|
90
....*....|....*....
gi 1063732797 285 HLGSLEHLEDSIAKLGFQI 303
Cdd:NF000106 224 ADGKVDELKTKVGGRTLQI 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
74-244 |
7.58e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 74 PILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVnhKALDPSSAVLmnnrkitdynqlRRLCGFVPQDDDLLPLlTV 153
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL--PPRSDASVVI------------RGTVAYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 154 KETLMYSAKFslrDSTAKEREERVESLLSDLGLVLVQD-SFVGEgdeedRGV--SGGERKRVSIAVEMIRDPPILLLDEP 230
Cdd:PLN03130 696 RDNILFGSPF---DPERYERAIDVTALQHDLDLLPGGDlTEIGE-----RGVniSGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170
....*....|....
gi 1063732797 231 TSGLDSRNSLQVVE 244
Cdd:PLN03130 768 LSALDAHVGRQVFD 781
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
61-235 |
9.58e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINH-TPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYN--QLR 135
Cdd:COG3845 258 LEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG------LRPPASgsIRLDGEDITGLSprERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RL-CGFVPQD---DDLLPLLTVKETLM--------YSAKFSLRDSTAKEREERvesllsdlglvLVQDSFVGEGDEED-- 201
Cdd:COG3845 332 RLgVAYIPEDrlgRGLVPDMSVAENLIlgryrrppFSRGGFLDRKAIRAFAEE-----------LIEEFDVRTPGPDTpa 400
|
170 180 190
....*....|....*....|....*....|....
gi 1063732797 202 RGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
57-262 |
1.17e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 57 NRYSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDY--NQ 133
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTG-----FYKPTGGtILLRGQHIEGLpgHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLcGFVP--QDDDLLPLLTVKETLM-----------YSAKFSLRDSTAKERE--ERVESLLSDLGLVLVQDSFVGEgd 198
Cdd:PRK11300 77 IARM-GVVRtfQHVRLFREMTVIENLLvaqhqqlktglFSGLLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGN-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 199 eedrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK11300 154 -----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
72-262 |
1.31e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKS----TLLKII-------SGRV--NHKALDPSS------AVLMNNRKiTDYN 132
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpagvrqtAGRVllDGKPVAPCAlrgrkiATIMQNPR-SAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 133 qlrrlcgfvpqdddllPLLT----VKETLMYSAKFSlRDSTAKEREERVEslLSDLGLVLvqDSFVGEgdeedrgVSGGE 208
Cdd:PRK10418 94 ----------------PLHTmhthARETCLALGKPA-DDATLTAALEAVG--LENAARVL--KLYPFE-------MSGGM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTH 199
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
61-235 |
2.85e-07 |
|
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: 52.55 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAVLMNnrKITdYNQLRRLC 138
Cdd:cd03289 3 MTVKDLTakYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWN--SVP-LQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQdddllplltvkETLMYSAKFSLR-DSTAKEREERVESLLSDLGLVLVQDSFVGEGD--EEDRG--VSGGERKRVS 213
Cdd:cd03289 80 GVIPQ-----------KVFIFSGTFRKNlDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDfvLVDGGcvLSHGHKQLMC 148
|
170 180
....*....|....*....|..
gi 1063732797 214 IAVEMIRDPPILLLDEPTSGLD 235
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLD 170
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
449-630 |
3.63e-07 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 50.97 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 449 RISSYMIANTIAFVPFLFVVSLLFSIPVYWIVGLNPSIQAFSFFVLCVWLIILMASSLVLFLSAVSPDFISGNSLICTVL 528
Cdd:COG0842 44 SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 529 GAFFLFSGYFIPKEKIPKPWM-------FMYYVSLYRYplesmvvneywsmreecfssgnmgcLMTGedvlkerGLDKDT 601
Cdd:COG0842 124 LPLTFLSGAFFPIESLPGWLQaiaylnpLTYFVEALRA-------------------------LFLG-------GAGLAD 171
|
170 180
....*....|....*....|....*....
gi 1063732797 602 RWINVGIMLAFFVFYRILCWGILLRKASK 630
Cdd:COG0842 172 VWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
61-234 |
4.76e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPS---SAVLMNNRKITDYNqlRRL 137
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEiywSGSPLKASNIRDTE--RAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 138 CGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKERE--ERVESLLSDLGLVLVQDS-FVGEgdeedrgVSGGERKRVSI 214
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTrPVGD-------YGGGQQQLVEI 152
|
170 180
....*....|....*....|
gi 1063732797 215 AVEMIRDPPILLLDEPTSGL 234
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSL 172
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
75-290 |
8.65e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSAVLMNNRKIT---DYNQlrrlcGFVPQdddllplL 151
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG-----ILEPTSGRVEVNGRVSallELGA-----GFHPE-------L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAK---FSLRDstAKEREERVESlLSDLGlvlvqDSFvgegdeeDRGV---SGGERKRVSIAVEMIRDPPIL 225
Cdd:COG1134 104 TGRENIYLNGRllgLSRKE--IDEKFDEIVE-FAELG-----DFI-------DQPVktySSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 226 LLDEPTSGLDSRNSLQVVELLATMaKSKQRTVLFSIHQpsyriLDYISDY----LILSRGSVIHLGSLE 290
Cdd:COG1134 169 LVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHS-----MGAVRRLcdraIWLEKGRLVMDGDPE 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
63-235 |
9.34e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRvnhkaLDPSSA-VLMNNRKI-----TDYNQLRR 136
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQ-----IAPDHGeILFDGENIpamsrSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 137 LCGFVPQDDDLLPLLTVKETLmysaKFSLRDSTAKEreervESLLSDlgLVLVQDSFVGEgdeedRG--------VSGGE 208
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNV----AYPLREHTQLP-----APLLHS--TVMMKLEAVGL-----RGaaklmpseLSGGM 148
|
170 180
....*....|....*....|....*..
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
63-244 |
1.43e-06 |
|
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: 51.09 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNhkaldPSSAVLmnnrKITDYNQLrrlcGFVP 142
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQ-----PDSGTI----EIGETVKL----AYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 143 QD-DDLLPLLTVKETL-----------------MYSAKFSLRDSTakereervesllsdlglvlvQDSFVGEgdeedrgV 204
Cdd:TIGR03719 392 QSrDALDPNKTVWEEIsggldiiklgkreipsrAYVGRFNFKGSD--------------------QQKKVGQ-------L 444
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063732797 205 SGGERKRVSIAVEMIRDPPILLLDEPTSGLDSrNSLQVVE 244
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV-ETLRALE 483
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
71-262 |
2.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 71 NHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITDYNQL---RRLCGFVPQD-D 145
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNA-----LLIPSEGkVYVDGLDTSDEENLwdiRNKAGMVFQNpD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 DLLPLLTVKETLMYSAKfSLrDSTAKEREERVESLLSDLGLVLVQDsfvgegdEEDRGVSGGERKRVSIAVEMIRDPPIL 225
Cdd:PRK13633 96 NQIVATIVEEDVAFGPE-NL-GIPPEEIRERVDESLKKVGMYEYRR-------HAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063732797 226 LLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
56-292 |
2.48e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 56 PNRYSLTVTN--LSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKaldpSSAVLMNNRKITDY-- 131
Cdd:PLN03232 1230 PSRGSIKFEDvhLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE----KGRIMIDDCDVAKFgl 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 NQLRRLCGFVPQDddllPLLTVKETLMYSAKFSLRDST----AKEREERVESL-LSDLGLvlvqDSFVGEGDEEdrgVSG 206
Cdd:PLN03232 1306 TDLRRVLSIIPQS----PVLFSGTVRFNIDPFSEHNDAdlweALERAHIKDVIdRNPFGL----DAEVSEGGEN---FSV 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 207 GERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKqrTVLFSIHQpsyriLDYISD---YLILSRGSV 283
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAHR-----LNTIIDcdkILVLSSGQV 1447
|
....*....
gi 1063732797 284 IHLGSLEHL 292
Cdd:PLN03232 1448 LEYDSPQEL 1456
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
61-265 |
2.67e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINHTPILNsVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkALDPSSA-VLMNNRKITdyNQLRRLCG 139
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAG-----IMQPSSGnIYYKNCNIN--NIAKPYCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 FVPQDDDLLPLLTVKETLMYSAKFSlrdstakereERVESLLSDLGLVLVQDSFvgegDEEDRGVSGGERKRVSIAVEMI 219
Cdd:PRK13541 74 YIGHNLGLKLEMTVFENLKFWSEIY----------NSAETLYAAIHYFKLHDLL----DEKCYSLSSGMQKIVAIARLIA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 220 RDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPS 265
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGG-IVLLSSHLES 184
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
54-263 |
3.24e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 54 PTPNRYSLTVTNLSYtiNHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvNHKALDPSSAVLMNNRK-----I 128
Cdd:PRK10938 256 ANEPRIVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGYSNDLTLFGRRRgsgetI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 129 TDynqLRRLCGFVpqdddllpllTVKETLMYSAKFSLR--------DS-----TAKEREER-VESLLSDLGLvlvqDSFV 194
Cdd:PRK10938 332 WD---IKKHIGYV----------SSSLHLDYRVSTSVRnvilsgffDSigiyqAVSDRQQKlAQQWLDILGI----DKRT 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063732797 195 GegDEEDRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQ 263
Cdd:PRK10938 395 A--DAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHH 461
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
89-287 |
5.46e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 89 LAVVGPSGTGKST----LLKIISGRvnhkaldpSSAVLMNNRKI-----TDYNQLRRLCGFVPQDD--DLLPLLTVKETL 157
Cdd:PRK10261 353 LSLVGESGSGKSTtgraLLRLVESQ--------GGEIIFNGQRIdtlspGKLQALRRDIQFIFQDPyaSLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 158 MYSAKF-SLRDSTAKEReeRVESLLSDLGLvlvQDSFVGEGDEEdrgVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDS 236
Cdd:PRK10261 425 MEPLRVhGLLPGKAAAA--RVAWLLERVGL---LPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063732797 237 RNSLQVVELLATMAKSKQRTVLFSIHQPSyrILDYISDYL-ILSRGSVIHLG 287
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMA--VVERISHRVaVMYLGQIVEIG 546
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
63-262 |
6.07e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 63 VTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVN------------HKA-LDPSSAVl 122
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMlgqlqadSGRIHcgtklevayfdqHRAeLDPEKTV- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 123 MNN-----RKITDYNQLRRLCGFVpQDddllplltvketLMYSAKfslRDSTAkereerVESLlsdlglvlvqdsfvgeg 197
Cdd:PRK11147 401 MDNlaegkQEVMVNGRPRHVLGYL-QD------------FLFHPK---RAMTP------VKAL----------------- 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 198 deedrgvSGGERKRVSIAVEMIRDPPILLLDEPTSGLDsrnsLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK11147 442 -------SGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
56-235 |
9.90e-06 |
|
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: 49.14 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 56 PNRYSLTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPSSAVLMNNRKItdyNQ 133
Cdd:TIGR01271 1213 PSGGQMDVQGLTakYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTL---QT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 134 LRRLCGFVPQdddllplltvkETLMYSAKFSLR-DSTAKEREERVESLLSDLGLVLVQDSFVGEGD--EEDRG--VSGGE 208
Cdd:TIGR01271 1290 WRKAFGVIPQ-----------KVFIFSGTFRKNlDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDfvLVDGGyvLSNGH 1358
|
170 180
....*....|....*....|....*..
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
72-290 |
1.08e-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: 48.28 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKAldpSSAVLMNNRKITDYN---QLRRLCGFVPQD---D 145
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF---EGNVFINGKPVDIRNpaqAIRAGIAMVPEDrkrH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 146 DLLPLLTVKETLMYSA--KFSLRDSTAKEREErvESLLSDLGLVLVQDSfvgEGDEEDRGVSGGERKRVSIAVEMIRDPP 223
Cdd:TIGR02633 349 GIVPILGVGKNITLSVlkSFCFKMRIDAAAEL--QIIGSAIQRLKVKTA---SPFLPIGRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 224 ILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPsyRILDyISDylilsRGSVIHLGSLE 290
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELA--EVLG-LSD-----RVLVIGEGKLK 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
59-234 |
1.88e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 59 YSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKalDPSSAVLMNNRKITDYN---QLR 135
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG--TYEGEIIFEGEELQASNirdTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 136 RLCGFVPQDDDLLPLLTVKETLMYSA---KFSLRDSTAKEReeRVESLLSDLGLVLVQDSFVGEgdeedrgVSGGERKRV 212
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNeitPGGIMDYDAMYL--RAQKLLAQLKLDINPATPVGN-------LGLGQQQLV 152
|
170 180
....*....|....*....|..
gi 1063732797 213 SIAVEMIRDPPILLLDEPTSGL 234
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASL 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
61-235 |
2.26e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.32 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSytinHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISG---------RVNHKALDPSSAVLMNNRKItdy 131
Cdd:COG1129 257 LEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGadpadsgeiRLDGKPVRIRSPRDAIRAGI--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 nqlrrlcGFVPQD---DDLLPLLTVKE--TLMYSAKFS---LRDStAKEREeRVESLLSDLGLVlvqdsfVGEGDEEDRG 203
Cdd:COG1129 330 -------AYVPEDrkgEGLVLDLSIREniTLASLDRLSrggLLDR-RRERA-LAEEYIKRLRIK------TPSPEQPVGN 394
|
170 180 190
....*....|....*....|....*....|..
gi 1063732797 204 VSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
413-552 |
3.44e-05 |
|
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: 46.23 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 413 LFAFSLSFLLSSTVEALPIYLRERRVLMkessrgSYRISSYMIANTIAfvpfLFVVSLLFSIPVYWIVgLNPSIQAFSFF 492
Cdd:pfam12698 171 IILIGAAIIAVSIVEEKESRIKERLLVS------GVSPLQYWLGKILG----DFLVGLLQLLIILLLL-FGIGIPFGNLG 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 493 VLCVWLII--LMASSLVLFLSAVSPDFISGNSLICTVLGAFFLFSGYFIPKEKIPKP--WMFMY 552
Cdd:pfam12698 240 LLLLLFLLygLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFlqWIFSI 303
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
76-241 |
3.70e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALDPS---SAVLMNNRKITDYNQLrrlcGFV--PQDDDLLPL 150
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEilfDGEVCRFKDIRDSEAL----GIViiHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 151 LTVKETLMYS---AKFSLRDstAKEREERVESLLSDLGLVLVQDSFVGegdeeDRGVsgGERKRVSIAVEMIRDPPILLL 227
Cdd:NF040905 93 LSIAENIFLGnerAKRGVID--WNETNRRARELLAKVGLDESPDTLVT-----DIGV--GKQQLVEIAKALSKDVKLLIL 163
|
170
....*....|....*..
gi 1063732797 228 DEPTSGL---DSRNSLQ 241
Cdd:NF040905 164 DEPTAALneeDSAALLD 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
66-237 |
5.69e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 66 LSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKII-------SGRVNHKALDPSSAVLMNnrkitdynqLRRLC 138
Cdd:PLN03130 1245 LRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALfriveleRGRILIDGCDISKFGLMD---------LRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 GFVPQDddllPLLtvketLMYSAKFSL------RDSTAKEREERVEslLSD------LGLvlvqDSFVGEGDEEdrgVSG 206
Cdd:PLN03130 1316 GIIPQA----PVL-----FSGTVRFNLdpfnehNDADLWESLERAH--LKDvirrnsLGL----DAEVSEAGEN---FSV 1377
|
170 180 190
....*....|....*....|....*....|.
gi 1063732797 207 GERKRVSIAVEMIRDPPILLLDEPTSGLDSR 237
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
72-264 |
6.22e-05 |
|
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: 43.89 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 72 HTPILNSVSLAAESskILAVVGPSGTGKSTLLKIISgrvnhkaldpsSAVLMNNRKITDYNQLRRLCgFVPQdddllpll 151
Cdd:cd03227 9 SYFVPNDVTFGEGS--LTIITGPNGSGKSTILDAIG-----------LALGGAQSATRRRSGVKAGC-IVAA-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 tvketlmysakfslrdstakereERVESLLSDLGLvlvqdsfvgegdeedrgvSGGERKRVSIAVEM----IRDPPILLL 227
Cdd:cd03227 67 -----------------------VSAELIFTRLQL------------------SGGEKELSALALILalasLKPRPLYIL 105
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063732797 228 DEPTSGLDSRNSLQVVELLATMAKsKQRTVLFSIHQP 264
Cdd:cd03227 106 DEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLP 141
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
58-129 |
6.53e-05 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 46.27 E-value: 6.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 58 RYSLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGRVNHKALD----PSSAVLMNNRKIT 129
Cdd:COG5192 41 RQAMRTADIEEKKLHVPMVDRTPKDLPPPFIVAVVGPPGTGKSTLIRSLVRRFTKQTIDeirgPITVVSGKTRRIT 116
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
61-246 |
1.37e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLSYTINhTP-----ILNSVSLAAESSKILAVVGPSGTGKS-TLLKII-----SGRVnhkaldpSSAVLMNNRKIT 129
Cdd:PRK09473 13 LDVKDLRVTFS-TPdgdvtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaaNGRI-------GGSATFNGREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 DY--NQLRRL----CGFVPQD--DDLLPLLTVKETLMYSAKFSLRDSTAKEREERVESLlsdlglvlvqDSfVGEGDEED 201
Cdd:PRK09473 85 NLpeKELNKLraeqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRML----------DA-VKMPEARK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063732797 202 R------GVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELL 246
Cdd:PRK09473 154 RmkmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
88-235 |
1.62e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 88 ILAVVGPSGTGKSTLLKIISGRVNhkaldPSSAVLmnnrKITDYNQLrrlcGFVPQD-DDLLPLLTVKE-------TLM- 158
Cdd:PRK11819 352 IVGIIGPNGAGKSTLFKMITGQEQ-----PDSGTI----KIGETVKL----AYVDQSrDALDPNKTVWEeisggldIIKv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 159 ---------YSAKFSLRDStakereervesllsDlglvlvQDSFVGEgdeedrgVSGGERKRVSIAVEMIRDPPILLLDE 229
Cdd:PRK11819 419 gnreipsraYVGRFNFKGG--------------D------QQKKVGV-------LSGGERNRLHLAKTLKQGGNVLLLDE 471
|
....*.
gi 1063732797 230 PTSGLD 235
Cdd:PRK11819 472 PTNDLD 477
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
204-283 |
2.12e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 204 VSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQPSYR-ILDYIsdyLILSRGS 282
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLgITDRI---LVMSNGL 468
|
.
gi 1063732797 283 V 283
Cdd:PRK10982 469 V 469
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
61-296 |
3.44e-04 |
|
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: 42.97 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 61 LTVTNLS--YTINHTPILNSVSLAAESSKILAVVGPSGTGKSTL-------LKIISGRVNHKALDPSSAVLmnnrkitdy 131
Cdd:cd03288 20 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPL--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 132 NQLRRLCGFVPQDddllPLLtvketLMYSAKFSLrDSTAKEREERV-ESL-LSDLGLVLVQ-----DSFVGEGDEEdrgV 204
Cdd:cd03288 91 HTLRSRLSIILQD----PIL-----FSGSIRFNL-DPECKCTDDRLwEALeIAQLKNMVKSlpgglDAVVTEGGEN---F 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 205 SGGERKRVSIAVEMIRDPPILLLDEPTSGLD--SRNSLQVVellaTMAKSKQRTVLFSIHQPSYrILDyISDYLILSRGS 282
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDmaTENILQKV----VMTAFADRTVVTIAHRVST-ILD-ADLVLVLSRGI 231
|
250
....*....|....*..
gi 1063732797 283 VIHLGSLEHL---EDSI 296
Cdd:cd03288 232 LVECDTPENLlaqEDGV 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
85-290 |
4.66e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 85 SSKILAVVGPSGTGKSTLLKIISGRVNhkalDPSSAVLMNNrkitdynqlrrlcgfvpqdddllplltvketlmysakfs 164
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG----PPGGGVIYID--------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 165 lrdstakereerveslLSDLGLVLVQDSFVGEGDEEDRGVSGGERKRvsIAVEMIR--DPPILLLDEPTSGLDSRNS--- 239
Cdd:smart00382 38 ----------------GEDILEEVLDQLLLIIVGGKKASGSGELRLR--LALALARklKPDVLILDEITSLLDAEQEall 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063732797 240 --LQVVELLATMAKSKQRTVLFSIHqpsyRILDYISDYLILSRGSVIHLGSLE 290
Cdd:smart00382 100 llLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
262-327 |
5.62e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 42.59 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063732797 262 HQPSYRILDYISDYLILSRGSVI-HLGSLEHLEDSIAKLGFQIPEQLNPIEFAMEIVESLrtFKPNS 327
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEGI--VKPST 65
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
79-262 |
5.63e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaldpssaVLMNNRKIT---------DYNQL-----RRLCG----- 139
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICG------------VTKDNWRVTadrmrfddiDLLRLsprerRKLVGhnvsm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 140 -FVPQDDDLLPLLTVKETLM-------YSAKFSLRdstAKEREERVESLLSDLGLVLVQD---SFVGEgdeedrgVSGGE 208
Cdd:PRK15093 94 iFQEPQSCLDPSERVGRQLMqnipgwtYKGRWWQR---FGWRKRRAIELLHRVGIKDHKDamrSFPYE-------LTEGE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063732797 209 RKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIH 262
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISH 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
205-277 |
7.48e-04 |
|
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: 40.77 E-value: 7.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063732797 205 SGGERKRVSIAVEMIRDPP--ILLLDEPTSGLDSRNSLQVVELLATMAKSKQrTVLFSIHQPsyRILDYiSDYLI 277
Cdd:cd03238 89 SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNL--DVLSS-ADWII 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
79-301 |
7.74e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 79 VSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaLDPSSA--VLMNNRKITDYNQLRRL-CGFV--PQDDDL------ 147
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYG------LRPARGgrIMLNGKEINALSTAQRLaRGLVylPEDRQSsglyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 148 LPLLTVKETLMYSAK-FSLRdsTAKEREeRVESLLSDLGLVLvqdsfvGEGDEEDRGVSGGERKRVSIAVEMIRDPPILL 226
Cdd:PRK15439 356 APLAWNVCALTHNRRgFWIK--PARENA-VLERYRRALNIKF------NHAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 227 LDEPTSGLD--SRNSL-QVVELLAtmaksKQRT-VLF------SIHQPSYRILdyisdylilsrgsVIHLGSLEHL---- 292
Cdd:PRK15439 427 VDEPTRGVDvsARNDIyQLIRSIA-----AQNVaVLFissdleEIEQMADRVL-------------VMHQGEISGAltga 488
|
250
....*....|..
gi 1063732797 293 ---EDSIAKLGF 301
Cdd:PRK15439 489 ainVDTIMRLAF 500
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
76-191 |
8.76e-04 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 40.71 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 76 LNSVSLAAESSKILAVVGPSGTGKSTLLKIISgrvnhKALDPSSAVLMN--NRKITDyNQLRRLCGFVPQDDDLLPLLTV 153
Cdd:pfam03215 35 LDAMFLENAKHRILLISGPSGCGKSTVIKELS-----KELGPKYREWSNptSFRSPP-NQVTDFRGDCIVNSRFLSQMES 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 1063732797 154 ketlmYSaKFSLRDSTAKEREERVESLLSDLGLVLVQD 191
Cdd:pfam03215 109 -----FS-EFELKGARYLVMQKRGKNAQGNKKLILIED 140
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
60-258 |
1.53e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 60 SLTVTNLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLKIISGrvnhkaldpsSAVLMNNRKITDYNQLRRLC- 138
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG----------ELPLLSGERQSQFSHITRLSf 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 139 -----------------GFVPQDDDLLplLTVKETLMYSAKfslrdstakeREERVESLLSDLGLV-LVQDSFvgegdee 200
Cdd:PRK10938 73 eqlqklvsdewqrnntdMLSPGEDDTG--RTTAEIIQDEVK----------DPARCEQLAQQFGITaLLDRRF------- 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063732797 201 dRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVL 258
Cdd:PRK10938 134 -KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
75-292 |
1.63e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.85 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 75 ILNSVSLAAESSKILAVVGPSGTGKSTLLKIISgRVNHKALDPSSAVLMNNRKITDYNqLRRLCGFVPQDddllPLL--- 151
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQD----PVLfsg 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 152 TVKETLMYSAKFSLRDSTAKEREERVESLLSDLGLVLvqDSFVGEGDEEdrgVSGGERKRVSIAVEMIRDPPILLLDEPT 231
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKL--DHECAEGGEN---LSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063732797 232 SGLDsrnsLQVVELLATMAKSKQR--TVLFSIHQpsyriLDYISDY---LILSRGSVIHLGSLEHL 292
Cdd:TIGR00957 1450 AAVD----LETDNLIQSTIRTQFEdcTVLTIAHR-----LNTIMDYtrvIVLDKGEVAEFGAPSNL 1506
|
|
| Cytidylate_kin |
pfam02224 |
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ... |
90-182 |
2.23e-03 |
|
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.
Pssm-ID: 280401 [Multi-domain] Cd Length: 211 Bit Score: 39.98 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 90 AVVGPSGTGKSTLLKIISGRVNHKALDpSSAVLmnnRKITdYNQLRRLCGfvPQDDDLLplltvkETLMYSAKFSLRDST 169
Cdd:pfam02224 2 AIDGPSGSGKSTVARILARKLGYKYLD-TGAMY---RALA-LAALRQKVD--LTDEDAL------AELASEVDISFGHTE 68
|
90
....*....|...
gi 1063732797 170 AKEREERVESLLS 182
Cdd:pfam02224 69 VFLNGEDVSSEIR 81
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
77-264 |
3.01e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.54 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 77 NSVSLAAESSKILAVVGPSGTGKSTLL-------KIISG--RVNHKALDPSSAVLMNNRKITDYNQLRRLCGFVPQdddl 147
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMnclfgvdKRAGGeiRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPN---- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 148 lplLTVKETLMYSAkfSLRDSTAK-------EREER--VESLLSDLGLvlvQDSFVGEGDEEdrgVSGGERKRVSIAVEM 218
Cdd:PRK09700 356 ---FSIAQNMAISR--SLKDGGYKgamglfhEVDEQrtAENQRELLAL---KCHSVNQNITE---LSGGNQQKVLISKWL 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063732797 219 IRDPPILLLDEPTSGLDSRNSLQVVELLATMAKSKQRTVLFSIHQP 264
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELP 470
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
65-235 |
4.77e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 65 NLSYTINHTPILNSVSLAAESSKILAVVGPSGTGKSTLLK-----IISG--------RVNHKALDPSSAVL--MNNRKIT 129
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGipkncqilHVEQEVVGDDTTALqcVLNTDIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063732797 130 DYNQLRRLCGFVPQDDDLLPLLTVKETLMYSAKFSLRDSTAKEREE---RVE-----SLLSDLGLVLVQDSFVGEGD-EE 200
Cdd:PLN03073 262 RTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEiykRLElidayTAEARAASILAGLSFTPEMQvKA 341
|
170 180 190
....*....|....*....|....*....|....*
gi 1063732797 201 DRGVSGGERKRVSIAVEMIRDPPILLLDEPTSGLD 235
Cdd:PLN03073 342 TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| |
