|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
97-689 |
6.61e-150 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 448.73 E-value: 6.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 97 LPAREPVDMEFKELSLTVKLGF--NRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGV--DGSILLNG 172
Cdd:TIGR00955 10 VFGRVAQDGSWKQLVSRLRGCFcrERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgSGSVLLNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 173 RRRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLT-----MR-LSG 246
Cdd:TIGR00955 90 MPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrVKgLSG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 247 GQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:TIGR00955 170 GERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 327 STQKLVPFLQSVDLPCPMYHNPADYIIELACGEYGYDK--VDTLKLATENgscltwFHNPSAVLRAEVLMRKYPIPKKTK 404
Cdd:TIGR00955 250 SPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENesRERIEKICDS------FAVSDIGRDMLVNTNLWSGKAGGL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 405 SRSLEDTSYSN-------QCSVLLRRGFIKAKRDTTMTHLRIGVNIAVAALFGAMYDHTGREGSRVLDNYNLLFAILMHH 477
Cdd:TIGR00955 324 VKDSENMEGIGynaswwtQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 478 SMTTMMLTVLTFPMDISILIKEHFNRWYSLKAYYTAMTLVDLPISIISCFFFTVIVYLWSYQPMEWIRFFMFFSISLLTV 557
Cdd:TIGR00955 404 TFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 558 FVGHSFGLMIGAWF-DVVNGTFLAPVLTIPMMMFAGFGVTLRDLPSYLRWGSHISYLRYGLEGFISAIYGLDR--GTLAC 634
Cdd:TIGR00955 484 NVATSFGYLISCAFsSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDniECTSA 563
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 635 EEAPYCHYRYPkKFLEEITMRGDQFWNDVIALGVMILVFRFVSYVVLKAKIKSIR 689
Cdd:TIGR00955 564 NTTGPCPSSGE-VILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
102-326 |
2.60e-79 |
|
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: 250.93 E-value: 2.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 102 PVDMEFKELSLTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTT-GVDGSILLNGRRRDLPSF 180
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 181 RRMSCYITQDDRLQPLLTVNENMHIAADLKlgqtvsyeekesriedillllglynhdqtltmRLSGGQKKRLSIAMELIN 260
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAKLR--------------------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 261 NPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
123-687 |
6.70e-74 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 251.34 E-value: 6.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 123 KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGVDGSILLNGRRRDLPSFRRMScYITQDDRLQPLLTVNE 201
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 202 NMHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLT----MR-LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDS 276
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIgnsfIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 277 SSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKLVPFLQSVDLPCPMYHNPADYIIELA 356
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 357 CGEYGYDKV----------------DTLkLATENGSCLTWFHNPSAvlrAEVLMRKYPIPKKTKSRSLEDTSYSNQCSVL 420
Cdd:PLN03211 320 NGVCQTDGVserekpnvkqslvasyNTL-LAPKVKAAIEMSHFPQA---NARFVGSASTKEHRSSDRISISTWFNQFSIL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 421 LRRGfIKAKRDTTMTHLRIGVNIAVAALFGAMYDHTgrEGSRVLDNYNLLFAILMHHSMTTMMLTVLTFPMDISILIKEH 500
Cdd:PLN03211 396 LQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWHS--DFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKER 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 501 FNRWYSLKAYYTAMTLVDLPISIISCFFFTVIVYLWSYQPMEWIRFFMFFSISLLTVFVGHSFGLMIGAwfDVVNGTFLA 580
Cdd:PLN03211 473 ASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGA--AIMDAKKAS 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 581 PVLTIPMMMF---AGFGVtlRDLPSYLRWGSHISYLRYGLEGFISAIYGLDR---GTLACeEAPYCHYRYPKKFLEEITM 654
Cdd:PLN03211 551 TIVTVTMLAFvltGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYGEGKrisSLLGC-SLPHGSDRASCKFVEEDVA 627
|
570 580 590
....*....|....*....|....*....|...
gi 442627138 655 RGDQFWNDVIALGVMILVFRFVSYVVLKaKIKS 687
Cdd:PLN03211 628 GQISPATSVSVLIFMFVGYRLLAYLALR-RIKH 659
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
105-326 |
2.91e-58 |
|
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: 195.15 E-value: 2.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKLgfNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTG-VDGSILLNGRRRDlPSFRRM 183
Cdd:cd03232 4 LTWKNLNYTVPV--KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 SCYITQDDRLQPLLTVNENMHIAADLKlgqtvsyeekesriedillllglynhdqtltmRLSGGQKKRLSIAMELINNPT 263
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLR--------------------------------GLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 264 VMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVL-SAGNCVYQG 326
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
114-326 |
2.07e-57 |
|
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: 194.03 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKE--ILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG----FKTTGvdGSILLNGRRRDLPSFRRMSCYI 187
Cdd:cd03234 9 VGLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvegGGTTS--GQILFNGQPRKPDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 188 TQDDRLQPLLTVNENMHIAADLKLGQTVSYEEKESRIEDILLL-LGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMF 266
Cdd:cd03234 87 RQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 267 LDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
106-679 |
1.11e-54 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 203.03 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVKLgfNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGV--DGSILLNGRRRDlPSFRRM 183
Cdd:TIGR00956 761 HWRNLTYEVKI--KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 SCYITQDDRLQPLLTVNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLT----MRLSGGQKKRLSIAMELI 259
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELV 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 260 NNPT-VMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLS-AGNCVYQG----STQKLVP 333
Cdd:TIGR00956 918 AKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQkGGQTVYFGdlgeNSHTIIN 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 334 FLQSVDLP-CPMYHNPADYIIELACGEYG-------YDKVDTLKLATENGSCLTWFHNPsavlraevlMRKYPIPKKTKS 405
Cdd:TIGR00956 998 YFEKHGAPkCPEDANPAEWMLEVIGAAPGahanqdyHEVWRNSSEYQAVKNELDRLEAE---------LSKAEDDNDPDA 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 406 RSLEDTSYSNQCSVLLRRGFIKAKRDTTMTHLRIGVNIAVAALFGAMYDHTGREgsrVLDNYNLLFAILmhhsmttmMLT 485
Cdd:TIGR00956 1069 LSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTS---LQGLQNQMFAVF--------MAT 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 486 VLTFPMDISIL-----------IKEHFNRWYSLKAYYTAMTLVDLPISIIscffFTVIVYLWSYQPM--EW--------- 543
Cdd:TIGR00956 1138 VLFNPLIQQYLppfvaqrdlyeVRERPSRTFSWLAFIAAQITVEIPYNLV----AGTIFFFIWYYPVgfYWnasktgqvh 1213
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 544 IRFFMFFSISLLTVFVGHSFGLMIGAWFDVV-NGTFLAPVLTIPMMMFAGFGVTLRDLPSY---LRWGSHISYLRYGL-- 617
Cdd:TIGR00956 1214 ERGVLFWLLSTMFFLYFSTLGQMVISFNPNAdNAAVLASLLFTMCLSFCGVLAPPSRMPGFwifMYRCSPFTYLVQALls 1293
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 618 ------------------------------EGFISAIYGLDRGTLACEEAPYCHYRYPKKFLEEITMRGDQFWNDviaLG 667
Cdd:TIGR00956 1294 tgladvpvtckvkelltfnppsgqtcgeymKPYLENAGGYLLNPNATDSCSFCQYSYTNDFLEPISSKYSGRWRN---FG 1370
|
650
....*....|..
gi 442627138 668 VMIlVFRFVSYV 679
Cdd:TIGR00956 1371 IFI-AFIFFNII 1381
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
102-626 |
2.20e-44 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 171.95 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 102 PVDMEFKELSLTVKL-------GFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTG-VDGSILLNGR 173
Cdd:PLN03140 865 PLAMSFDDVNYFVDMpaemkeqGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyIEGDIRISGF 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 174 RRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLT-----MRLSGGQ 248
Cdd:PLN03140 945 PKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQ 1024
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 249 KKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLS-AGNCVYQG- 326
Cdd:PLN03140 1025 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGp 1104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 327 ---STQKLVPFLQSV-DLP-CPMYHNPADYIIElacgeygydkVDTLKLATENGSCLTWFHNPSAVL-RAEVLMRKYPIP 400
Cdd:PLN03140 1105 lgrNSHKIIEYFEAIpGVPkIKEKYNPATWMLE----------VSSLAAEVKLGIDFAEHYKSSSLYqRNKALVKELSTP 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 401 KKTKSRSLEDTSYSN----QCSVLLRRGFIKAKRDTTMTHLRIGVNIAVAALFGAMYDHTG--REGSRVLDNY------N 468
Cdd:PLN03140 1175 PPGASDLYFATQYSQstwgQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGtkRSNANDLTMVigamyaA 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 469 LLFAILMHHSMTTMMLTVltfpmDISILIKEHFNRWYSLKAYYTAMTLVDLPISIISCFFFTVIVYlwSYQPMEW--IRF 546
Cdd:PLN03140 1255 VLFVGINNCSTVQPMVAV-----ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVY--AMVAFEWtaAKF 1327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 547 FMFFSISLLTVFVGHSFGLMIGAWF--DVVNGTFLAPVLTIpMMMFAGFGVTLRDLPSYLRWGSHISYLRYGLEGFISAI 624
Cdd:PLN03140 1328 FWFYFISFFSFLYFTYYGMMTVSLTpnQQVAAIFAAAFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQ 1406
|
..
gi 442627138 625 YG 626
Cdd:PLN03140 1407 YG 1408
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
420-623 |
3.23e-44 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 157.44 E-value: 3.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 420 LLRRGFIKAKRDTTMTHLRIGVNIAVAALFGAMYDHTGREGSrVLDNYNLLFAILMHHSMTTMMLTVLTFPMDISILIKE 499
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 500 HFNRWYSLKAYYTAMTLVDLPISIISCFFFTVIVYLWSYQPMEWIRFFMFFSISLLTVFVGHSFGLMIGAWF-DVVNGTF 578
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALApSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442627138 579 LAPVLTIPMMMFAGFGVTLRDLPSYLRWGSHISYLRYGLEGFISA 623
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
121-331 |
8.90e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.15 E-value: 8.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR--RRDLPSFRRMSCYITQDDRLQPLL 197
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlRPTS--GEVRVLGEdvARDPAEVRRRIGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENMHIAADLKlgqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSS 277
Cdd:COG1131 89 TVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 278 SCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1131 166 ARRELWELLRELAAEGKTVLLSTHY-LEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
106-320 |
2.08e-40 |
|
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: 147.23 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRR---RDLPSFRR 182
Cdd:cd03225 1 ELKNLSFS----YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MSCYITQDDRLQPL-LTVNEnmhiaaDLKLG---QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMEL 258
Cdd:cd03225 76 KVGLVFQNPDDQFFgPTVEE------EVAFGlenLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPtAKLFQIFDQVYVLSAG 320
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDG 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
87-623 |
2.31e-40 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 159.50 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 87 VHFDTDALNNLParepvDMEFKELSLTVKLGFNRG---SKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALS----GF 159
Cdd:TIGR00956 40 VAADSDYQPTFP-----NALLKILTRGFRKLKKFRdtkTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 160 KTtGVDGSILLNGRRRD--LPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKLGQT----VSYEEKESRIEDILL-LLG 232
Cdd:TIGR00956 115 HI-GVEGVITYDGITPEeiKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVYMaTYG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 233 LYNHDQT-----LTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSctkVLELLKKLTSQGR----TIICTIHQP 303
Cdd:TIGR00956 194 LSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT---ALEFIRALKTSANildtTPLVAIYQC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 304 TAKLFQIFDQVYVLSAGNCVYQGSTQKLVPFLQSVDLPCPMYHNPADYIIELACGEYGYDKVDTLKLATENGSCL-TWFH 382
Cdd:TIGR00956 271 SQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTSPAERQIKPGYEKKVPRTPQEFeTYWR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 383 NPS--AVLRAEV--------------LMRKYPI---PKKTKSRSLEDTSYSNQCSVLLRRGFIKAKRDTTMTHLRIGVNI 443
Cdd:TIGR00956 351 NSPeyAQLMKEIdeyldrcsesdtkeAYRESHVakqSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 444 AVAALFGAMYDHTGREGSrvlDNYN----LLFAIL--MHHSMTTMMLTVLTFPmdisiLIKEHfnRWYSL---KAYYTAM 514
Cdd:TIGR00956 431 IMALILSSVFYNLPKNTS---DFYSrggaLFFAILfnAFSSLLEIASMYEARP-----IVEKH--RKYALyhpSADAIAS 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 515 TLVDLPISII-SCFFFTVIVYLWSYQPmEWIRFFMFFSISLLTVFVGHSFGLMIGAWFDVVNGTF-LAPVLTIPMMMFAG 592
Cdd:TIGR00956 501 IISEIPFKIIeSVVFNIILYFMVNFRR-TAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMtPAAILLLALSIYTG 579
|
570 580 590
....*....|....*....|....*....|.
gi 442627138 593 FGVTLRDLPSYLRWGSHISYLRYGLEGFISA 623
Cdd:TIGR00956 580 FAIPRPSMLGWSKWIYYVNPLAYAFESLMVN 610
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
112-331 |
8.47e-39 |
|
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: 143.84 E-value: 8.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGR--RRDLPSFRRMSCYIT 188
Cdd:COG4555 2 IEVEnLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS-GSILIDGEdvRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDRLQPLLTVNENMHIAADLKLgqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
106-331 |
7.92e-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: 140.55 E-value: 7.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVklgfnRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtGVDGSILLNG---RRRDLPSFRR 182
Cdd:COG1122 2 ELENLSFSY-----PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-PTSGEVLVDGkdiTKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MSCYITQDDRLQpLL--TVNENmhIA-ADLKLGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELI 259
Cdd:COG1122 76 KVGLVFQNPDDQ-LFapTVEED--VAfGPENLG--LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 260 NNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
105-323 |
1.37e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.71 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKLGFNRgsKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKT-TGvdGSILLNGR------RRDL 177
Cdd:COG1136 5 LELRNLTKSYGTGEGE--VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRpTS--GEVLIDGQdisslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSFRRMSC-YITQDDRLQPLLTVNENMHIAADLklgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAM 256
Cdd:COG1136 81 ARLRRRHIgFVFQFFNLLPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 257 ELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQPtaKLFQIFDQVYVLSAGNCV 323
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDGRIV 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
126-272 |
3.07e-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: 133.16 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR---RRDLPSFRRMSCYITQDDRLQPLLTVNEN 202
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL-LSPTEGTILLDGQdltDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 203 MHIAADLklgQTVSYEEKESRIEDILLLLGLYN-HDQTLTMR---LSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:pfam00005 80 LRLGLLL---KGLSKREKDARAEEALEKLGLGDlADRPVGERpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
112-319 |
5.17e-36 |
|
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: 134.53 E-value: 5.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR--RRDLPSFRRMSCYIT 188
Cdd:COG4133 3 LEAEnLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGL-LPPSAGEVLWNGEpiRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDRLQPLLTVNENMHIAADLKlGQTVSyeekESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALY-GLRAD----REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPtakLFQIFDQVYVLSA 319
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
105-331 |
9.11e-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: 134.55 E-value: 9.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGR--RRDLPSFR 181
Cdd:cd03263 1 LQIRNLTKT----YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGeLRPTS--GTAYINGYsiRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 182 RMSCYITQDDRLQPLLTVNENMHIAADLKlGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINN 261
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLK-G--LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 262 PTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPT-AKLfqIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDeAEA--LCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
106-321 |
1.09e-35 |
|
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: 134.15 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVKLGFNRgsKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtgVD-GSILLNGR------RRDLP 178
Cdd:cd03255 2 ELKNLSKTYGGGGEK--VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTsGEVRVDGTdisklsEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 179 SFRR--MScYITQDDRLQPLLTVNENMHIAADLklgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAM 256
Cdd:cd03255 78 AFRRrhIG-FVFQSFNLLPDLTALENVELPLLL---AGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 257 ELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPtaKLFQIFDQVYVLSAGN 321
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
106-331 |
7.07e-35 |
|
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: 132.69 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVKlgfnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNG------RRRDLPS 179
Cdd:cd03256 2 EVENLSKTYP-----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGtdinklKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 180 FRRMSCYITQDDRLQPLLTVNENMHIAadlKLGQT---------VSYEEKESRIEdILLLLGLYNHDQTLTMRLSGGQKK 250
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSG---RLGRRstwrslfglFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 251 RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPT-AKLFqiFDQVYVLSAGNCVYQGST 328
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDGPP 229
|
...
gi 442627138 329 QKL 331
Cdd:cd03256 230 AEL 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
112-332 |
1.00e-34 |
|
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: 132.47 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR------RRDLPsfRRM 183
Cdd:COG1120 2 LEAEnLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLlKPSS--GEVLLDGRdlaslsRRELA--RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 ScYITQDDRLQPLLTVnenmhiaADL---------KLGQTVSYEEKEsRIEDILLLLGLYNH-DQTLTmRLSGGQKKRLS 253
Cdd:COG1120 78 A-YVPQEPPAPFGLTV-------RELvalgryphlGLFGRPSAEDRE-AVEEALERTGLEHLaDRPVD-ELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 254 IAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQPT-AklFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNlA--ARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 442627138 332 V 332
Cdd:COG1120 226 L 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
116-321 |
7.64e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRR---DLPSFRRMSCYITQddr 192
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-DPPTSGEIYLDGKPLsamPPPEWRRQVAYVPQ--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 lQPLL---TVNENMHIAADLKlgqtvSYEEKESRIEDILLLLGLynHDQTLTM---RLSGGQKKRLSIAMELINNPTVMF 266
Cdd:COG4619 82 -EPALwggTVRDNLPFPFQLR-----ERKFDRERALELLERLGL--PPDILDKpveRLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 267 LDEPTTGLDSSSCTKVLELLKKL-TSQGRTIICTIHQPtAKLFQIFDQVYVLSAGN 321
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
116-326 |
1.75e-32 |
|
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: 123.70 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRrrDLPSFRRmscyitqddrlqp 195
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGK--DLASLSP------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 lltvnenmhiaadLKLGQTVSYeekesrIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:cd03214 69 -------------KELARKIAY------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442627138 276 SSSCTKVLELLKKLT-SQGRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQG 326
Cdd:cd03214 130 IAHQIELLELLRRLArERGKTVVMVLHDLNLAA-RYADRVILLKDGRIVAQG 180
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
112-326 |
1.99e-32 |
|
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: 125.31 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF--KTTG---VDGSILLNGRRRDLPSFRRMSCY 186
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlkPTSGsiiFDGKDLLKLSRRLRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 187 ITQDDR--LQPLLTVNEnmHIAADLKLGQTVSYEEKESRIEdILLLLGLYNHDQTLTMR---LSGGQKKRLSIAMELINN 261
Cdd:cd03257 87 VFQDPMssLNPRMTIGE--QIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYpheLSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 262 PTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQ-PTAKlfQIFDQVYVLSAGNCVYQG 326
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDlGVVA--KIADRVAVMYAGKIVEEG 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
112-329 |
3.71e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 3.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLPSfRRMScYITQD 190
Cdd:COG1121 7 IELEnLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRAR-RRIG-YVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 ---DRLQPLlTVNE--NMHIAADLKLGQTVSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVM 265
Cdd:COG1121 84 aevDWDFPI-TVRDvvLMGRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAkLFQIFDQVYVLsAGNCVYQGSTQ 329
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLL-NRGLVAHGPPE 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
116-320 |
3.76e-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: 121.97 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR---RRDLPSFRRMSCYITQddr 192
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDGKdiaKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 lqplltvnenmhiaadlklgqtvsyeekesriedillllglynhdqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442627138 273 GLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFqIFDQVYVLSAG 320
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAEL-AADRVIVLKDG 156
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
120-301 |
3.91e-32 |
|
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: 123.52 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLPSFRRMSCYITQDDRLQpLLTV 199
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-SSGSILLNGKPIKAKERRKSIGYVMQDVDYQ-LFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NenmhIAADLKLGQTVSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:cd03226 88 S----VREELLLGLKELDAGNE-QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180
....*....|....*....|..
gi 442627138 280 TKVLELLKKLTSQGRTIICTIH 301
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
105-320 |
6.06e-32 |
|
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: 123.40 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTvklgfnRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtgVD-GSILLNGRR-RDLPSFRR 182
Cdd:cd03259 1 LELKGLSKT------YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER--PDsGEILIDGRDvTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MSCYITQDDRLQPLLTVNENMHIAadLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNP 262
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAENIAFG--LKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 263 TVMFLDEPTTGLDSSSCTKVLELLKKL-TSQGRTIICTIHQPtAKLFQIFDQVYVLSAG 320
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQ-EEALALADRIAVMNEG 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
79-332 |
7.65e-32 |
|
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: 130.65 E-value: 7.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 79 LEPVVEEEVHFDTDALNNLPAREPVDMEFKELSLTvklgfNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG 158
Cdd:COG4988 311 IFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFS-----YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 159 FkTTGVDGSILLNGRRR---DLPSFRRMSCYITQDDRLQPlLTVNENmhiaadLKLGQTVSYEEkesRIEDILLLLGLYN 235
Cdd:COG4988 386 F-LPPYSGSILINGVDLsdlDPASWRRQIAWVPQNPYLFA-GTIREN------LRLGRPDASDE---ELEAALEAAGLDE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 236 HDQTL-----TM------RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPt 304
Cdd:COG4988 455 FVAALpdgldTPlgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRL- 532
|
250 260
....*....|....*....|....*...
gi 442627138 305 aKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:COG4988 533 -ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
121-320 |
2.59e-31 |
|
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: 120.20 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR--RRDLPSFRRMSCYITQDDRLQPLL 197
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLlKPDS--GEIKVLGKdiKKEPEEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENMhiaadlklgqtvsyeekesriedillllglynhdqtltmRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSS 277
Cdd:cd03230 89 TVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627138 278 SCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAG 320
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHI-LEEAERLCDRVAILNNG 171
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
105-326 |
3.79e-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: 120.83 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF--KTTGVDGSILLNGRRRD--LPSF 180
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSVEGDIHYNGIPYKefAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 181 RRMSCYITQDDRLQPLLTVNENMHIAADLKLGQTVSyeekesriedillllglynhdqtltmRLSGGQKKRLSIAMELIN 260
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVR--------------------------GISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 261 NPTVMFLDEPTTGLDSSSctkVLELLKKL----TSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03233 136 RASVLCWDNSTRGLDSST---ALEILKCIrtmaDVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
137-327 |
4.09e-31 |
|
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: 121.78 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRR-RDLPSFRRMSCYIT---QDDRLQPLLTVNENMHIAADLKL 211
Cdd:cd03219 27 EIHGLIGPNGAGKTTLFNLISGFlRPTS--GSVLFDGEDiTGLPPHEIARLGIGrtfQIPRLFPELTVLENVMVAAQART 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 GQTV-------SYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLE 284
Cdd:cd03219 105 GSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627138 285 LLKKLTSQGRTIICTIHQPTAkLFQIFDQVYVLSAGNCVYQGS 327
Cdd:cd03219 185 LIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
116-331 |
5.16e-31 |
|
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: 121.13 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF----KTTGVDGSILLNGR-----RRDLPSFRRMSCY 186
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndliPGAPDEGEVLLDGKdiydlDVDVLELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 187 ITQddrlQPLL---TVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLYN--HDQTLTMRLSGGQKKRLSIAMELINN 261
Cdd:cd03260 86 VFQ----KPNPfpgSIYDN--VAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 262 PTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICT--IHQptAKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ--AA--RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
116-317 |
1.05e-30 |
|
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: 119.95 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRrrDLPSFRRMSCYITQD---D 191
Cdd:cd03235 5 LTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLlKPTS--GSIRVFGK--PLEKERKRIGYVPQRrsiD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLlTVNE--NMHIAADLKLGQTVSYEEKEsRIEDILLLLGLYNH-DQTLTMrLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:cd03235 81 RDFPI-SVRDvvLMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELaDRQIGE-LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAkLFQIFDQVYVL 317
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLL 205
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
105-331 |
1.24e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 120.48 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTvklgFNRGsKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG------RRRDLP 178
Cdd:TIGR02315 2 LEVENLSKV----YPNG-KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-SSGSILLEGtditklRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 179 SFRRMSCYITQDDRLQPLLTVNENMHIAadlKLG---------QTVSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQK 249
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHG---RLGykptwrsllGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 250 KRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQ-PTAKLFQifDQVYVLSAGNCVYQGS 327
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQvDLAKKYA--DRIVGLKAGEIVFDGA 229
|
....
gi 442627138 328 TQKL 331
Cdd:TIGR02315 230 PSEL 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
106-331 |
1.52e-30 |
|
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: 119.99 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKelSLTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR------RRDLPS 179
Cdd:cd03258 3 ELK--NVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT-SGSVLVDGTdltllsGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 180 FRRMSCYITQDDRLQPLLTVNENmhIAADLKLGQtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELI 259
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFEN--VALPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 260 NNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQ-PTAKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEmEVVK--RICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
121-331 |
1.88e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 120.16 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNG------RRRDLPSFRRMSCYITQDDRLQ 194
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGEILVDGqdvtalRGRALRRLRRRIGMIFQQFNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENMHIAAdlkLGQT---------VSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVM 265
Cdd:COG3638 93 PRLSVLTNVLAGR---LGRTstwrsllglFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKL-TSQGRTIICTIHQP-TAKLFqiFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG3638 169 LADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVdLARRY--ADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
105-319 |
2.63e-30 |
|
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: 118.73 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTvkLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRRRDLPSFRRM 183
Cdd:cd03293 1 LEVRNVSKT--YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTS--GEVLVDGEPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 scYITQDDRLQPLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPT 263
Cdd:cd03293 77 --YVFQQDALLPWLTVLDN--VALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 264 VMFLDEPTTGLDSSscTKVL---ELLKKLTSQGRTIICTIHQPTAKLFqIFDQVYVLSA 319
Cdd:cd03293 152 VLLLDEPFSALDAL--TREQlqeELLDIWRETGKTVLLVTHDIDEAVF-LADRVVVLSA 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
121-331 |
3.29e-30 |
|
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: 118.69 E-value: 3.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRR-RDLPSFRRMS---CYITQDDRLQPL 196
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 197 LTVNENMHIAAdlklgQTVSYEEKESRIEDILLLL-GLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:cd03224 90 LTVEENLLLGA-----YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 276 SSSCTKVLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
79-332 |
6.46e-30 |
|
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: 126.10 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 79 LEPVVEEEVHFDTDALNNLPAREPVDMEFKELSLtvklGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG 158
Cdd:COG2274 448 LDDILDLPPEREEGRSKLSLPRLKGDIELENVSF----RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 159 FkTTGVDGSILLNG---RRRDLPSFRRMSCYITQDDRLqplL--TVNENMHIAADlklgqTVSYEEkesrIEDILLLLGL 233
Cdd:COG2274 524 L-YEPTSGRILIDGidlRQIDPASLRRQIGVVLQDVFL---FsgTIRENITLGDP-----DATDEE----IIEAARLAGL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 234 ynHD--QTLTM-----------RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTI 300
Cdd:COG2274 591 --HDfiEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIA 667
|
250 260 270
....*....|....*....|....*....|..
gi 442627138 301 HQPTakLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:COG2274 668 HRLS--TIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
126-301 |
1.18e-29 |
|
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: 116.74 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFK--TTG---VDGSILLNGRRRDLPSFRRMSCYITQDDRLQPLLTVN 200
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElpTSGtirVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 201 ENMHIAadLKLGQtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCT 280
Cdd:cd03292 97 ENVAFA--LEVTG-VPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180
....*....|....*....|.
gi 442627138 281 KVLELLKKLTSQGRTIICTIH 301
Cdd:cd03292 174 EIMNLLKKINKAGTTVVVATH 194
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
106-301 |
1.23e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.08 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTvklgfNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTgvDGSILLNG------RRRDLP 178
Cdd:COG2884 3 RFENVSKR-----YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrlKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 179 SFRRMSCYITQDDRLQPLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMEL 258
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYEN--VALPLRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
120-320 |
1.77e-29 |
|
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: 114.98 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR-----RRDLPSFRRMSCYITQDDRLQ 194
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEdltdlEDELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENmhiaadlklgqtvsyeekesriedillllglynhdqtLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:cd03229 89 PHLTVLEN-------------------------------------IALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 275 DSSSCTKVLELLKKLTSQ-GRTIICTIHQPtAKLFQIFDQVYVLSAG 320
Cdd:cd03229 132 DPITRREVRALLKSLQAQlGITVVLVTHDL-DEAARLADRVVVLRDG 177
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
83-620 |
2.67e-29 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 124.96 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 83 VEEEVHFDTDALNNLP--ARepvDMEFKELSLtvkLGFNRGSKE---ILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALS 157
Cdd:PLN03140 139 VEADCYIGSRALPTLPnaAR---NIAESALGM---LGINLAKKTkltILKDASGIIKPSRMTLLLGPPSSGKTTLLLALA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 158 GF--KTTGVDGSILLNGRRRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAA---------------------------- 207
Cdd:PLN03140 213 GKldPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSArcqgvgtrydllselarrekdagifpea 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 208 --DLKLGQTVSYEEKESRIEDILL-LLGLYNHDQTLT----MR-LSGGQKKRLSIAmELINNPT-VMFLDEPTTGLDSSS 278
Cdd:PLN03140 293 evDLFMKATAMEGVKSSLITDYTLkILGLDICKDTIVgdemIRgISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSST 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 279 CTKVLELLKKLTSQGR-TIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKLVPFLQSVDLPCPMYHNPADYIIELAC 357
Cdd:PLN03140 372 TYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTS 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 358 G----EYGYDKVDTLKLAT--ENGSCLTWFH-------------NPSAVLRAEVLMRKYPIPKKTKSRSLEDTSYsnqcs 418
Cdd:PLN03140 452 KkdqeQYWADRNKPYRYISvsEFAERFKSFHvgmqlenelsvpfDKSQSHKAALVFSKYSVPKMELLKACWDKEW----- 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 419 VLLRR-GFIKAKRDTTMthlrIGVNIAVAALFGAMYDHTGREGSRVLDNYNLLFAIL--MHHSMTTMMLTVLTFPmdisI 495
Cdd:PLN03140 527 LLMKRnAFVYVFKTVQI----IIVAAIASTVFLRTEMHTRNEEDGALYIGALLFSMIinMFNGFAELALMIQRLP----V 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 496 LIKEHFNRWYSLKAYYTAMTLVDLPISIISCFFFTVIVYLW-SYQPmEWIRFFMffsiSLLTVFVGHSfglMIGAWFDVV 574
Cdd:PLN03140 599 FYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSiGFAP-EASRFFK----QLLLVFLIQQ---MAAGIFRLI 670
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 575 NGT----FLAP---VLTIPMM-MFAGFGVTLRDLPSYLRWGSHISYLRYGLEGF 620
Cdd:PLN03140 671 ASVcrtmIIANtggALVLLLVfLLGGFILPKGEIPNWWEWAYWVSPLSYGFNAL 724
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
116-337 |
3.88e-29 |
|
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: 116.06 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG-------RRRDLPSFRRMScYIT 188
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP-DSGEVLIDGedisglsEAELYRLRRRMG-MLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDRLQPLLTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:cd03261 84 QSGALFDSLTVFEN--VAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQ-PTAklFQIFDQVYVLSAGNCVYQGSTQKLV----PFLQS 337
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDlDTA--FAIADRIAVLYDGKIVAEGTPEELRasddPLVRQ 234
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
121-301 |
4.00e-29 |
|
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: 114.44 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGR-----RRDLPSFRRMSCYITQDDRLQ 194
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQS--GAVLIDGEpldysRKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLL-TVNENMHIAAdLKLGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:TIGR01166 81 LFAaDVDQDVAFGP-LNLG--LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180
....*....|....*....|....*...
gi 442627138 274 LDSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
97-332 |
5.46e-29 |
|
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: 122.18 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 97 LPAREPVDMEFKELSLtvklGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkttgVD---GSILLNG- 172
Cdd:COG4987 326 APAPGGPSLELEDVSF----RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF----LDpqsGSITLGGv 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 173 --RRRDLPSFRRMSCYITQDdrlqPLL---TVNENMHIAADlklgqTVSYEEkesrIEDILLLLGLYNHDQTL-----TM 242
Cdd:COG4987 398 dlRDLDEDDLRRRIAVVPQR----PHLfdtTLRENLRLARP-----DATDEE----LWAALERVGLGDWLAALpdgldTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 243 ------RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTsQGRTIICTIHQPTAklFQIFDQVYV 316
Cdd:COG4987 465 lgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAG--LERMDRILV 541
|
250
....*....|....*.
gi 442627138 317 LSAGNCVYQGSTQKLV 332
Cdd:COG4987 542 LEDGRIVEQGTHEELL 557
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
121-326 |
9.38e-29 |
|
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: 114.21 E-value: 9.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSqLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGR--RRDLPSFRRMSCYITQDDRLQPLLT 198
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP-SSGTIRIDGQdvLKQPQKLRRRIGYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 199 VNENMHIAADLKlgqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:cd03264 89 VREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442627138 279 CTKVLELLKKLtSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03264 166 RIRFRNLLSEL-GEDRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
106-331 |
1.29e-28 |
|
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: 120.39 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF--KTTGVDGSILLNGRR-RDLPSFRR 182
Cdd:COG1123 6 EVRDLSVR----YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRDlLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MS--CYITQD--DRLQPLlTVNEnmHIAADLKLGQtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMEL 258
Cdd:COG1123 82 GRriGMVFQDpmTQLNPV-TVGD--QIAEALENLG-LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
105-320 |
1.56e-28 |
|
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: 112.09 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLtvklGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG---RRRDLPSFR 181
Cdd:cd03228 1 IEFKNVSF----SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-TSGEILIDGvdlRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 182 RMSCYITQDdrlqPLL---TVNENMhiaadlklgqtvsyeekesriedillllglynhdqtltmrLSGGQKKRLSIAMEL 258
Cdd:cd03228 76 KNIAYVPQD----PFLfsgTIRENI----------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPTakLFQIFDQVYVLSAG 320
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
133-326 |
2.43e-28 |
|
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: 112.97 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRD-LPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKL 211
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINGVDVTaAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 GQTvsyEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS 291
Cdd:cd03298 100 KLT---AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 442627138 292 Q-GRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQG 326
Cdd:cd03298 177 EtKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
139-331 |
3.21e-28 |
|
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: 119.24 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR------RRDLPSFRRMSCYITQD--DRLQPLLTVNEnmHIAADL 209
Cdd:COG1123 294 LGLVGESGSGKSTLARLLLGLlRPTS--GSILFDGKdltklsRRSLRELRRRVQMVFQDpySSLNPRMTVGD--IIAEPL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 210 KLGQTVSYEEKESRIEDILLLLGL-------YNHDqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKV 282
Cdd:COG1123 370 RLHGLLSRAERRERVAELLERVGLppdladrYPHE------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 283 LELLKKLTSQ-GRTIictihqptakLF---------QIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1123 444 LNLLRDLQRElGLTY----------LFishdlavvrYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
132-331 |
3.47e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.31 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 132 KFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR-RRDLPSFRR---MscyITQDDRLQPLLTVNENMHIA- 206
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPD-SGRILWNGQdLTALPPAERpvsM---LFQENNLFPHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 207 -ADLKLGqtvsyEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLEL 285
Cdd:COG3840 97 rPGLKLT-----AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442627138 286 LKKL-TSQGRTIICTIHQPT-AKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG3840 172 VDELcRERGLTVLMVTHDPEdAA--RIADRVLLVADGRIAADGPTAAL 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
99-331 |
3.54e-28 |
|
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: 113.54 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 99 AREPVdMEFKELSltvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGRrrDL 177
Cdd:COG1127 1 MSEPM-IEVRNLT------KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPDS--GEILVDGQ--DI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSFRRmscyitqdDRLQPL----------------LTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLT 241
Cdd:COG1127 70 TGLSE--------KELYELrrrigmlfqggalfdsLTVFEN--VAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 242 MRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQpTAKLFQIFDQVYVLSAG 320
Cdd:COG1127 140 SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHD-LDSAFAIADRVAVLADG 218
|
250
....*....|.
gi 442627138 321 NCVYQGSTQKL 331
Cdd:COG1127 219 KIIAEGTPEEL 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
106-320 |
9.58e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 112.88 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTvkLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRRDLPSFRRMsc 185
Cdd:COG1116 9 ELRGVSKR--FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPVTGPGPDRG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 186 YITQDDRLQPLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVM 265
Cdd:COG1116 84 VVFQEPALLPWLTVLDN--VALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 266 FLDEPTTGLDSSscTKVL---ELLKKLTSQGRTIICTIHQPT-AklfqIF--DQVYVLSAG 320
Cdd:COG1116 161 LMDEPFGALDAL--TRERlqdELLRLWQETGKTVLFVTHDVDeA----VFlaDRVVVLSAR 215
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
137-328 |
3.48e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 109.57 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRR-DLPSFRRMSCYITQDDRLQPLLTVNENmhIAADLKLGQTV 215
Cdd:TIGR01277 25 EIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVRQN--IGLGLHPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 216 SYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GR 294
Cdd:TIGR01277 102 NAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSErQR 180
|
170 180 190
....*....|....*....|....*....|....
gi 442627138 295 TIICTIHQPTaKLFQIFDQVYVLSAGNCVYQGST 328
Cdd:TIGR01277 181 TLLMVTHHLS-DARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
112-331 |
7.07e-27 |
|
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: 109.00 E-value: 7.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVKLGFNRGSKEILHNVcgkfPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR--RRDLPSFRRMSCYIT 188
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRV----RRGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHdvVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDRLQPLLTVNENMHIAADLklgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIH-QPTAKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
124-327 |
1.17e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.17 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 124 EILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTgvDGSILLNGR-----RRDLPSFRRMSCYITQ--DDRL-Q 194
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT--SGEVLIKGEpikydKKSLLEVRKTVGIVFQnpDDQLfA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PllTVNENMHIAAdLKLGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:PRK13639 94 P--TVEEDVAFGP-LNLG--LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 275 DSSSCTKVLELLKKLTSQGRTIICTIHQptAKLFQIF-DQVYVLSAGNCVYQGS 327
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGT 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
114-332 |
3.78e-26 |
|
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: 107.32 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNG---RRRDLPSFRRMSCYITQD 190
Cdd:cd03253 6 VTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-SGSILIDGqdiREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 drlqpllTVNENMHIAADLKLGQ-TVSYEE-----KESRIEDILLLLglynHDQTLTM------RLSGGQKKRLSIAMEL 258
Cdd:cd03253 84 -------TVLFNDTIGYNIRYGRpDATDEEvieaaKAAQIHDKIMRF----PDGYDTIvgerglKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHqptaKLFQIF--DQVYVLSAGNCVYQGSTQKLV 332
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH----RLSTIVnaDKIIVLKDGRIVERGTHEELL 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
120-304 |
5.38e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.11 E-value: 5.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLPSFRRMSCYITQDDRLQPLLTV 199
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NENMHIAADLkLGQTvsyeekESRIEDILLLLGLYnHDQTLTMR-LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:PRK13539 91 AENLEFWAAF-LGGE------ELDIAAALEAVGLA-PLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*.
gi 442627138 279 CTKVLELLKKLTSQGRTIICTIHQPT 304
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHIPL 188
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
111-275 |
5.90e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.03 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 111 SLTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTG--VDGSILLNGRRRD-LPSFRRMSCY 186
Cdd:COG4136 1 MLSLEnLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRLTaLPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 187 ITQDDRLQPLLTVNENMHIAadlkLGQTVSYEEKESRIEDILL---LLGLYNHDqtlTMRLSGGQKKRLSIAMELINNPT 263
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFA----LPPTIGRAQRRARVEQALEeagLAGFADRD---PATLSGGQRARVALLRALLAEPR 153
|
170
....*....|..
gi 442627138 264 VMFLDEPTTGLD 275
Cdd:COG4136 154 ALLLDEPFSKLD 165
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
112-332 |
6.02e-26 |
|
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: 107.20 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR---RRDLPSFRRMSCYIT 188
Cdd:COG1124 7 LSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRpvtRRRRKAFRRRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDR--LQPLLTVNEnmHIAADLKL-GQTvsyeEKESRIEDILLLLGL-------YNHDqtltmrLSGGQKKRLSIAMEL 258
Cdd:COG1124 86 QDPYasLHPRHTVDR--ILAEPLRIhGLP----DREERIAELLEQVGLppsfldrYPHQ------LSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDL-AVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
121-331 |
6.75e-26 |
|
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: 106.60 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRR-RDLPSFRRMS---CYITQDDRLQPL 196
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL-LPPRSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 197 LTVNENMHIAADLKLGQtvsyEEKESRIEDILLL---LGlynhdqtlTMR------LSGGQKKRLSIAMELINNPTVMFL 267
Cdd:COG0410 93 LTVEENLLLGAYARRDR----AEVRADLERVYELfprLK--------ERRrqragtLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 268 DEPTTGLDSSSCTKVLELLKKLTSQGRTIICtIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
121-332 |
8.65e-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: 106.09 E-value: 8.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFktTGVD-GSILLNGRR-RDLPSFRRMS---CYITQDDRLQP 195
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL--VKPDsGKILLDGQDiTKLPMHKRARlgiGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:cd03218 89 KLTVEEN--ILAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 276 SSSCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:cd03218 166 PIAVQDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
136-326 |
1.03e-25 |
|
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: 105.45 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 136 SQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGR-------RRDLPSFRRMSCYITQDDRLQPLLTVNENmhIAAD 208
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDG-GTIVLNGTvlfdsrkKINLPPQQRKIGLVFQQYALFPHLNVREN--LAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 209 LKlgqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKK 288
Cdd:cd03297 100 LK---RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442627138 289 LTS--QGRTIICTiHQPTaKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03297 177 IKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
134-355 |
1.07e-25 |
|
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: 109.05 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR-------RRDLPSFRRMSCYITQDDRLQPLLTVNENmhia 206
Cdd:TIGR02142 21 PGQGVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGRtlfdsrkGIFLPPEKRRIGYVFQEARLFPHLSVRGN---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 207 adLKLGQT-VSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLEL 285
Cdd:TIGR02142 96 --LRYGMKrARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 286 LKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKLvpfLQSVDLPCpMYHNPADYIIEL 355
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV---WASPDLPW-LAREDQGSLIEG 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
121-302 |
2.22e-25 |
|
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: 104.53 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKT-TGvdGSILLNG-----RRRDLPSFRRMSCYITQDDRLQ 194
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpDS--GTIIIDGlkltdDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENMHIAadLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:cd03262 89 PHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180
....*....|....*....|....*...
gi 442627138 275 DSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:cd03262 167 DPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
137-320 |
2.53e-25 |
|
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: 105.51 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRR-RDLPSFRRMSCYIT---QDDRLQPLLTVNENMHIAADLKL 211
Cdd:COG0411 31 EIVGLIGPNGAGKTTLFNLITGFyRPTS--GRILFDGRDiTGLPPHRIARLGIArtfQNPRLFPELTVLENVLVAAHARL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 GQTVSY----------EEKESR--IEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:COG0411 109 GRGLLAallrlprarrEEREARerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEET 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442627138 280 TKVLELLKKLT-SQGRTIICTIHQPTAkLFQIFDQVYVLSAG 320
Cdd:COG0411 189 EELAELIRRLRdERGITILLIEHDMDL-VMGLADRIVVLDFG 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
132-331 |
4.38e-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: 105.94 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 132 KFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRR--RDLPSFRRMSCYITQDDRLQPLLTVNENMHIAAD 208
Cdd:TIGR01188 15 KVREGEVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGYDvvREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 209 LklgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKK 288
Cdd:TIGR01188 93 L---YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627138 289 LTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:TIGR01188 170 LKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
121-326 |
1.50e-24 |
|
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: 101.91 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR--RRDLPSFRRMSCYItqdDR--LQP 195
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLiKPDS--GEITFDGKsyQKNIEALRRIGALI---EApgFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMHIAADLKLGqtvsyeeKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:cd03268 86 NLTARENLRLLARLLGI-------RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442627138 276 SSSCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
121-349 |
1.90e-24 |
|
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: 102.32 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtgVD-GSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLT 198
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET--PTsGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 199 VNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:cd03300 89 VFEN--IAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 279 CTKVLELLKKL-TSQGRTIICTIH-QPTAklFQIFDQVYVLSAGNcvyqgstqklvpfLQSVDLPCPMYHNPA 349
Cdd:cd03300 166 RKDMQLELKRLqKELGITFVFVTHdQEEA--LTMSDRIAVMNKGK-------------IQQIGTPEEIYEEPA 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
140-301 |
5.15e-24 |
|
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: 101.26 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLTVNENmhIAADLKLgQTVSYE 218
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKP-DSGKILLNGKDiTNLPPEKRDISYVPQNYALFPHMTVYKN--IAYGLKK-RKVDKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 219 EKESRIEDILLLLG---LYNHDQTltmRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GR 294
Cdd:cd03299 105 EIERKVLEIAEMLGidhLLNRKPE---TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGV 181
|
....*..
gi 442627138 295 TIICTIH 301
Cdd:cd03299 182 TVLHVTH 188
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
121-275 |
5.83e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.02 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtgVD-GSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLT 198
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET--PDsGRILLDGRDvTGLPPEKRNVGMVFQDYALFPHLT 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 199 VNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:COG3842 94 VAEN--VAFGLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
140-341 |
1.01e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.85 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR------RRDLPSFRR---MscyITQDDRLQPLLTVNENmhIAADL 209
Cdd:COG1135 35 GIIGYSGAGKSTLIRCINLLeRPTS--GSVLVDGVdltalsERELRAARRkigM---IFQHFNLLSSRTVAEN--VALPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 210 KLgQTVSYEEKESRIEDILLLLGLYNH-----DQtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLE 284
Cdd:COG1135 108 EI-AGVPKAEIRKRVAELLELVGLSDKadaypSQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 285 LLKKLTSQ-GRTIICTIHQ-PTAKlfQIFDQVYVLSAGNCVYQGS------------TQKLVPFLQSVDLP 341
Cdd:COG1135 182 LLKDINRElGLTIVLITHEmDVVR--RICDRVAVLENGRIVEQGPvldvfanpqselTRRFLPTVLNDELP 250
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
114-331 |
1.14e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.76 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG----FKTTGVDGSILLNGR---RRDLPSFRRMSCY 186
Cdd:PRK14247 9 LKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQdifKMDVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 187 ITQDDRLQPLLTVNENmhIAADLKLGQTV-SYEEKESRIEDILLLLGLY----NHDQTLTMRLSGGQKKRLSIAMELINN 261
Cdd:PRK14247 87 VFQIPNPIPNLSIFEN--VALGLKLNRLVkSKKELQERVRWALEKAQLWdevkDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 262 PTVMFLDEPTTGLDSSSCTKVLELLKKLTSQgRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
111-289 |
1.63e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 111 SLTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPSFRRMSCYitQD 190
Cdd:COG4525 8 HVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-SGEITLDGVPVTGPGADRGVVF--QK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 DRLQPLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:COG4525 85 DALLPWLNVLDN--VAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170
....*....|....*....
gi 442627138 271 TTGLDSSSCTKVLELLKKL 289
Cdd:COG4525 162 FGALDALTREQMQELLLDV 180
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
134-332 |
3.50e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQlIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR--RRDLPSFRRMScYITQDDRLQPLLTVNENmhIAADLKL 211
Cdd:PRK10771 24 RGER-VAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGQdhTTTPPSRRPVS-MLFQENNLFSHLTVAQN--IGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 GQTVSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS 291
Cdd:PRK10771 99 GLKLNAAQRE-KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442627138 292 QGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
120-303 |
3.63e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 97.81 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG----RRRDLPSfrRMSCYITQDDRLQP 195
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGtplaEQRDEPH--ENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMHIAADLKLGQTVSyeekesrIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:TIGR01189 87 ELSALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*...
gi 442627138 276 SSSCTKVLELLKKLTSQGRTIICTIHQP 303
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
106-328 |
5.24e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTvklgFNRGSKEI--LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR------RRD 176
Cdd:PRK11153 3 ELKNISKV----FPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTS--GRVLVDGQdltalsEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 177 LPSFRRMSCYITQDDRLQPLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAM 256
Cdd:PRK11153 77 LRKARRQIGMIFQHFNLLSSRTVFDN--VALPLEL-AGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 257 ELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGST 328
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHE-MDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
133-329 |
8.59e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.99 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGsQLIAIMGPSGAGKSTLLDALSGFkTTGvDGSILLNGRR---RDLPSFRRMSCYITQDDRLQPLLTVNEnmHIAadL 209
Cdd:COG4138 20 NAG-ELIHLIGPNGAGKSTLLARMAGL-LPG-QGEILLNGRPlsdWSAAELARHRAYLSQQQSPPFAMPVFQ--YLA--L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 210 KLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELI-----NNPT--VMFLDEPTTGLDSSSCTKV 282
Cdd:COG4138 93 HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 283 LELLKKLTSQGRTIICTIHQPTAKLFQIfDQVYVLSAGNCVYQGSTQ 329
Cdd:COG4138 173 DRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGETA 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
114-332 |
1.42e-22 |
|
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: 96.92 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkttgVD---GSILLNG---RRRDLPSFRRMSCYI 187
Cdd:cd03251 6 VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF----YDvdsGRILIDGhdvRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 188 TQDdrlqPLL---TVNENMHIAADlklgqtvsyEEKESRIEDILLLLGLynHDQTLTM-------------RLSGGQKKR 251
Cdd:cd03251 82 SQD----VFLfndTVAENIAYGRP---------GATREEVEEAARAANA--HEFIMELpegydtvigergvKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 252 LSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHqptaKLFQI--FDQVYVLSAGNCVYQGSTQ 329
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAH----RLSTIenADRIVVLEDGKIVERGTHE 221
|
...
gi 442627138 330 KLV 332
Cdd:cd03251 222 ELL 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
87-331 |
1.93e-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: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 87 VHFDTDAlNNLPArepVDmefkELSLTVKlgfnRGskEILhnvcgkfpgsqliAIMGPSGAGKSTLLDALSGF--KTTGV 164
Cdd:COG0444 9 VYFPTRR-GVVKA---VD----GVSFDVR----RG--ETL-------------GLVGESGSGKSTLARAILGLlpPPGIT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 165 DGSILLNGR------RRDLPSFR--RMScYITQD--DRLQPLLTVNEnmHIAADLKLGQTVSYEEKESRIEDILLLLGLY 234
Cdd:COG0444 62 SGEILFDGEdllklsEKELRKIRgrEIQ-MIFQDpmTSLNPVMTVGD--QIAEPLRIHGGLSKAEARERAIELLERVGLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 235 NHDQTLTM---RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIIctihqptaklF-- 308
Cdd:COG0444 139 DPERRLDRyphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAIL----------Fit 208
|
250 260 270
....*....|....*....|....*....|
gi 442627138 309 -------QIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG0444 209 hdlgvvaEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
97-303 |
2.39e-22 |
|
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: 101.21 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 97 LPAREPVDMEFKELSLTVklgfnRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRrrD 176
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAY-----PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGV--P 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 177 LPSF-----RRMSCYITQddrlQPLLTvneNMHIAADLKLGQTvsyEEKESRIEDILLLLGLYNHDQTL-----TM---- 242
Cdd:TIGR02857 386 LADAdadswRDQIAWVPQ----HPFLF---AGTIAENIRLARP---DASDAEIREALERAGLDEFVAALpqgldTPigeg 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 243 --RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQP 303
Cdd:TIGR02857 456 gaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL 517
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
84-332 |
2.55e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.46 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 84 EEEVHFDTDALNNLPAREPVDMEFKELSLTVKLGfnrgsKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFktTG 163
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIEAEDLEILSPDG-----KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 164 VDGSILLNG---RRRDLPSFRRMSCYITQDDRLqPLLTVNENM----HIAADLKLGQTVsyeeKESRIEDIL--LLLGLy 234
Cdd:PRK11174 402 YQGSLKINGielRELDPESWRKHLSWVGQNPQL-PHGTLRDNVllgnPDASDEQLQQAL----ENAWVSEFLplLPQGL- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 235 NH---DQTLtmRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQptakLFQI- 310
Cdd:PRK11174 476 DTpigDQAA--GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQ----LEDLa 548
|
250 260
....*....|....*....|...
gi 442627138 311 -FDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK11174 549 qWDQIWVMQDGQIVQQGDYAELS 571
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
126-326 |
3.59e-22 |
|
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: 95.35 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNG---RRRDLPSFRRMSCYITQDDRLQpLLTVNEN 202
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-SGSVLLDGtdiRQLDPADLRRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 203 mhiaadLKLGQTVSYEEkesRIEDILLLLGLY----NHDQTLTMR-------LSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:cd03245 98 ------ITLGAPLADDE---RILRAAELAGVTdfvnKHPNGLDLQigergrgLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 272 TGLDSSSCTKVLELLKKLTSqGRTIICTIHQPTakLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLG-DKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
121-328 |
5.49e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 95.28 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRR-RDLPSFRRMS---CYITQDDRLQP 195
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLlPVKS--GSIRLDGEDiTKLPPHERARagiAYVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENmhiaadLKLGQTVSYEEKESRIEDILLL---LglynhdqtLTMR------LSGGQKKRLSIAMELINNPTVMF 266
Cdd:TIGR03410 89 RLTVEEN------LLTGLAALPRRSRKIPDEIYELfpvL--------KEMLgrrggdLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 267 LDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGST 328
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAG 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
106-345 |
5.67e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 96.37 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTvklgFNRGS---KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG--FKTTG---VDGSILLNGRRRDL 177
Cdd:TIGR04521 2 KLKNVSYI----YQPGTpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGllKPTSGtvtIDGRDITAKKKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSFRRMSCYITQddrlQP---L--LTVNENmhIAADLK-LGqtVSYEEKESRIEDILLLLGLynhDQTLTMR----LSGG 247
Cdd:TIGR04521 78 KDLRKKVGLVFQ----FPehqLfeETVYKD--IAFGPKnLG--LSEEEAEERVKEALELVGL---DEEYLERspfeLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 248 QKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL-TSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:TIGR04521 147 QMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHS-MEDVAEYADRVIVMHKGKIVLDG 225
|
250 260
....*....|....*....|..
gi 442627138 327 STQKL---VPFLQSVDLPCPMY 345
Cdd:TIGR04521 226 TPREVfsdVDELEKIGLDVPEI 247
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
113-327 |
8.40e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 95.84 E-value: 8.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 113 TVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR-----RRDLPSFRRMSCYI 187
Cdd:PRK13638 4 TSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-KGAVLWQGKpldysKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 188 TQDDRLQPLLTvNENMHIAADLK-LGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMF 266
Cdd:PRK13638 83 FQDPEQQIFYT-DIDSDIAFSLRnLG--VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 267 LDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGS 327
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
106-332 |
8.87e-22 |
|
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: 94.91 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVKlgfNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG---RRRDLPSFRR 182
Cdd:cd03249 2 EFKNVSFRYP---SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGvdiRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MSCYITQDdrlqPLLTvneNMHIAADLKLG---QTVSYEE---KESRIED-ILLLLGLYNhdqtlTM------RLSGGQK 249
Cdd:cd03249 78 QIGLVSQE----PVLF---DGTIAENIRYGkpdATDEEVEeaaKKANIHDfIMSLPDGYD-----TLvgergsQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 250 KRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPTAklFQIFDQVYVLSAGNCVYQGSTQ 329
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHD 222
|
...
gi 442627138 330 KLV 332
Cdd:cd03249 223 ELM 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
116-329 |
9.80e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 9.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRRDLPSFRRMSCY---ITQDDR 192
Cdd:COG4559 7 LSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGE-LTPSSGEVRLNGRPLAAWSPWELARRravLPQHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 LQPLLTVNEnmhIAAdlkLG---QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMEL--INNPT---- 263
Cdd:COG4559 86 LAFPFTVEE---VVA---LGrapHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggp 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 264 -VMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQP--TAklfQIFDQVYVLSAGNCVYQGSTQ 329
Cdd:COG4559 160 rWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLnlAA---QYADRILLLHQGRLVAQGTPE 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
113-303 |
1.52e-21 |
|
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: 92.94 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 113 TVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGR--RRDLPSFRRMSCYITQD 190
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGplDFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 DRLQPLLTVNENMHIAADLklgqtvsyeEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:cd03231 82 PGIKTTLSVLENLRFWHAD---------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|...
gi 442627138 271 TTGLDSSSCTKVLELLKKLTSQGRTIICTIHQP 303
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
104-331 |
2.25e-21 |
|
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: 93.44 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKElsltVKLGFNRGsKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR-RDLP--SF 180
Cdd:cd03254 2 EIEFEN----VNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQILIDGIDiRDISrkSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 181 RRMSCYITQDdrlqPLL---TVNENmhiaadLKLGQTVSYEE------KESRIEDILLLL--GLYNHDQTLTMRLSGGQK 249
Cdd:cd03254 76 RSMIGVVLQD----TFLfsgTIMEN------IRLGRPNATDEevieaaKEAGAHDFIMKLpnGYDTVLGENGGNLSQGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 250 KRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPTAKLFQifDQVYVLSAGNCVYQGSTQ 329
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHD 222
|
..
gi 442627138 330 KL 331
Cdd:cd03254 223 EL 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
120-328 |
2.40e-21 |
|
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: 94.00 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNV-----CGKFpgsqlIAIMGPSGAGKSTLLDALSG--FKTTGVDGSILlnGRRR---DLPSFRRMSCYITQ 189
Cdd:COG1119 13 RGGKTILDDIswtvkPGEH-----WAILGPNGAGKSTLLSLITGdlPPTYGNDVRLF--GERRggeDVWELRKRIGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 D--DRLQPLLTVnENMhIA----ADLKLGQTVSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPT 263
Cdd:COG1119 86 AlqLRFPRDETV-LDV-VLsgffDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 264 VMFLDEPTTGLDSSSCTKVLELLKKLTSQG-RTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGST 328
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHV-EEIPPGITHVLLLKDGRVVAAGPK 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
137-334 |
3.68e-21 |
|
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: 92.91 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLPSFRRMSCYitQDDRLQPLLTVNENMHIAADLKLgQTVS 216
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGLAQP-TSGGVILEGKQITEPGPDRMVVF--QNYSLLPWLTVRENIALAVDRVL-PDLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 217 YEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGR-T 295
Cdd:TIGR01184 88 KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRvT 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 442627138 296 IICTIHQPTAKLFqIFDQVYVLSAGNCVYQGSTQKlVPF 334
Cdd:TIGR01184 168 VLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE-VPF 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
73-332 |
3.75e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.28 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 73 PSKQPPlePVVEEEVHFDTDALNNLP-AREPVDMEFKELSLTVklgfnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKST 151
Cdd:PRK13536 11 PRRLEL--SPIERKHQGISEAKASIPgSMSTVAIDLAGVSKSY------GDKAVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 152 LLDALSGFKTTGVdGSILLNGRRrdLPSFRRMS----CYITQDDRLQPLLTVNENMhiaadLKLGQ--TVSYEEKESRIE 225
Cdd:PRK13536 83 IARMILGMTSPDA-GKITVLGVP--VPARARLArariGVVPQFDNLDLEFTVRENL-----LVFGRyfGMSTREIEAVIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 226 DILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIH-QPT 304
Cdd:PRK13536 155 SLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfMEE 234
|
250 260
....*....|....*....|....*...
gi 442627138 305 AKlfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK13536 235 AE--RLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
112-326 |
4.73e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.82 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG---FKTTGvdGSILLNGRrrDlpsfrrmscyI 187
Cdd:COG0396 1 LEIKnLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGE--D----------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 188 TQ---DDR--------LQ-----PLLTVNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLynhDQTLTMR-----LSG 246
Cdd:COG0396 67 LElspDERaragiflaFQypveiPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGL---DEDFLDRyvnegFSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 247 GQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPtaKLFQIF--DQVYVLSAGNCVY 324
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVK 221
|
..
gi 442627138 325 QG 326
Cdd:COG0396 222 SG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
121-338 |
5.31e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRrrDLPSF--RRMSCYITqddrLQP-LL 197
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-QSGTVFLGDK--PISMLssRQLARRLA----LLPqHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNEnmhiaaDLKLGQTVSY-------------EEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTV 264
Cdd:PRK11231 86 LTPE------GITVRELVAYgrspwlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 265 MFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQptakLFQI---FDQVYVLSAGNCVYQGS-----TQKLvpfLQ 336
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD----LNQAsryCDHLVVLANGHVMAQGTpeevmTPGL---LR 232
|
..
gi 442627138 337 SV 338
Cdd:PRK11231 233 TV 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
105-289 |
5.93e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTvklgFNRGS---KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfkTTGVD-GSILLNGRrrD---L 177
Cdd:COG1101 2 LELKNLSKT----FNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--SLPPDsGSILIDGK--DvtkL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSFRRmSCYI---TQDdrlqPL------LTVNENMHIAAD----LKLGQTVSYEEKESRIEDILLL-LGLYNHDQTLTMR 243
Cdd:COG1101 74 PEYKR-AKYIgrvFQD----PMmgtapsMTIEENLALAYRrgkrRGLRRGLTKKRRELFRELLATLgLGLENRLDTKVGL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442627138 244 LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL 289
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI 194
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
111-331 |
6.38e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 111 SLTVKLGFnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLL-------DALSGFKTTGvdgSILLNGRR----RDLPS 179
Cdd:PRK14271 24 AVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYRYSG---DVLLGGRSifnyRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 180 FRRMSCYITQDDRLQPLLTVNenmHIAADLKLGQTVSYEE----KESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIA 255
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMSIMD---NVLAGVRAHKLVPRKEfrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 256 MELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTihQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT--HNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
126-331 |
6.82e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.77 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKT--TGVDGSILLNGRR--------RDLPSFRRMSCYITQDDRLQP 195
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGSHIELLGRTvqregrlaRDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMHIAAdlkLGQT------VSY--EEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFL 267
Cdd:PRK09984 100 RLSVLENVLIGA---LGSTpfwrtcFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 268 DEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQF 240
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
140-297 |
7.69e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 92.49 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRrrDLpsfRRMSCY-IT--------QDDRLQPLLTVNENMHIAADLK 210
Cdd:COG4674 40 VIIGPNGAGKTTLMDVITG-KTRPDSGSVLFGGT--DL---TGLDEHeIArlgigrkfQKPTVFEELTVFENLELALKGD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 ------LGQTVSYEEKEsRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLE 284
Cdd:COG4674 114 rgvfasLFARLTAEERD-RIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAE 192
|
170
....*....|...
gi 442627138 285 LLKKLtSQGRTII 297
Cdd:COG4674 193 LLKSL-AGKHSVV 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
121-302 |
7.93e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLP---------SFRRMSCYITQDD 191
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETP-DSGQLNIAGHQFDFSqkpsekairLLRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENMhIAADLK-LGQtvSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:COG4161 92 NLWPHLTVMENL-IEAPCKvLGL--SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|..
gi 442627138 271 TTGLDSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:COG4161 169 TAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
104-297 |
7.97e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 92.41 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKELSLTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDAL-------SGFKttgVDGSILLNG--- 172
Cdd:COG1117 4 PASTLEPKIEVRnLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR---VEGEILLDGedi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 173 --RRRDLPSFRRMSCYITQddRLQPL-LTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLYNH--D--QTLTMRLS 245
Cdd:COG1117 81 ydPDVDVVELRRRVGMVFQ--KPNPFpKSIYDN--VAYGLRLHGIKSKSELDEIVEESLRKAALWDEvkDrlKKSALGLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442627138 246 GGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQgRTII 297
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIV 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
137-289 |
9.64e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 9.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPSFRRMSCYitQDDRLQPLLTVNENmhIAADLKLgQTVS 216
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAERGVVF--QNEGLLPWRNVQDN--VAFGLQL-AGVE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 217 YEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL 289
Cdd:PRK11248 102 KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
121-304 |
1.01e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDAL-------SG-FKTTGVDGSILLNGrrrDLPSFRRMSC-YITQDD 191
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDAD---ALAQLRREHFgFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENMHIAAdlkLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK10535 96 HLLSHLTAAQNVEVPA---VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190
....*....|....*....|....*....|...
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQGRTIICTIHQPT 304
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
121-320 |
1.26e-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: 90.78 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLTV 199
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGRDvTDLPPKDRDIAMVFQNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NENMhiAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:cd03301 90 YDNI--AFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442627138 280 TKVLELLKKLTSQ-GRTIICTIHQPTAKLfQIFDQVYVLSAG 320
Cdd:cd03301 167 VQMRAELKRLQQRlGTTTIYVTHDQVEAM-TMADRIAVMNDG 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
121-331 |
1.60e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.21 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtgVD-GSILLNG-----RRRDLPSFRRMSCYITQDDRLQ 194
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE--PDsGTITVDGedltdSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENMHIAadLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:COG1126 90 PHLTVLENVTLA--PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 275 DSSSCTKVLELLKKLTSQGRTIICTIHQPT-AKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1126 168 DPELVGEVLDVMRDLAKEGMTMVVVTHEMGfAR--EVADRVVFMDGGRIVEEGPPEEF 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
71-332 |
1.98e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 95.66 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 71 NEPSKQPPlepvveeEVHFDTdalNNLPAREPVDMEFKELSLTvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKS 150
Cdd:PRK11160 315 NEITEQKP-------EVTFPT---TSTAAADQVSLTLNNVSFT----YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 151 TLLDALsgfkTTGVD---GSILLNGRrrDLPSF-----RRMSCYITQddRLQpLL--TVNENMHIAADlklgqtvsyEEK 220
Cdd:PRK11160 381 TLLQLL----TRAWDpqqGEILLNGQ--PIADYseaalRQAISVVSQ--RVH-LFsaTLRDNLLLAAP---------NAS 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 221 ESRIEDILLLLGLYNH---DQTLTM-------RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLt 290
Cdd:PRK11160 443 DEALIEVLQQVGLEKLledDKGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH- 521
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 442627138 291 SQGRTIICTIHQPTAkLFQiFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK11160 522 AQNKTVLMITHRLTG-LEQ-FDRICVMDNGQIIEQGTHQELL 561
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
133-332 |
2.18e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGsQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRR--RDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLk 210
Cdd:PRK13537 31 QRG-ECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGEPvpSRARHARQRVGVVPQFDNLDPDFTVRENLLVFGRY- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 LGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT 290
Cdd:PRK13537 108 FG--LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627138 291 SQGRTIICTIH-QPTAKlfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK13537 186 ARGKTILLTTHfMEEAE--RLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
121-275 |
3.76e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.70 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVC-----GKFpgsqlIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR-RDLPSFRRMSCYITQDDRLQ 194
Cdd:PRK09452 25 DGKEVISNLDltinnGEF-----LTLLGPSGCGKTTVLRLIAGFETPD-SGRIMLDGQDiTHVPAENRHVNTVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:PRK09452 99 PHMTVFEN--VAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
.
gi 442627138 275 D 275
Cdd:PRK09452 176 D 176
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
123-331 |
3.84e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 123 KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-----KTTGVDGSILLNGR---RRDLPSFRRMSCYITQDDRLQ 194
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydSKIKVDGKVLYFGKdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLYN--HDQ--TLTMRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:PRK14246 103 PHLSIYDN--IAYPLKSHGIKEKREIKKIVEECLRKVGLWKevYDRlnSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 271 TTGLDSSSCTKVLELLKKLTSQgRTIICTIHQPTaKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ-QVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
113-331 |
4.02e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 113 TVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF----KTTGVDGSILLNGR-----RRDLPSFRRM 183
Cdd:PRK14267 7 TVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelnEEARVEGEVRLFGRniyspDVDPIEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 SCYITQDDRLQPLLTVNENmhIAADLKLGQTV-SYEEKESRIEDILLLLGLY----NHDQTLTMRLSGGQKKRLSIAMEL 258
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDN--VAIGVKLNGLVkSKKELDERVEWALKKAALWdevkDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQgRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSP-AQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
120-336 |
4.83e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR---RRDLPSFRRMSCYITQDDRLQPL 196
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI-LKPTSGSVLIRGEpitKENIREVRKFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 197 LTVNENmhiaaDLKLGQT---VSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:PRK13652 93 SPTVEQ-----DIAFGPInlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 274 LDSSSCTKVLELLKKLTSQ-GRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKLvpFLQ 336
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETyGMTVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEEI--FLQ 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
121-327 |
5.88e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkttgVD---GSILLNG---RRRDLPSFRRMSCYITQDdrlq 194
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----YDptsGRILIDGvdiRDLTLESLRRQIGVVPQD---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLL---TVNENmhiaadLKLGQ-TVSYEE-----KESRIEDILLLL--GLynhDQTLT---MRLSGGQKKRLSIAMELIN 260
Cdd:COG1132 423 TFLfsgTIREN------IRYGRpDATDEEveeaaKAAQAHEFIEALpdGY---DTVVGergVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 261 NPTVMFLDEPTTGLDSSSCTKVLELLKKLTsQGRTIIcTI-HQP-TAKLfqiFDQVYVLSAGNCVYQGS 327
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLM-KGRTTI-VIaHRLsTIRN---ADRILVLDDGRIVEQGT 557
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
122-301 |
7.69e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 122 SKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRrrdlpSFRRMSC------------YITQ 189
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP-TSGDVIFNGQ-----PMSKLSSaakaelrnqklgFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 DDRLQPLLTVNENmhIAADLKLGQtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDE 269
Cdd:PRK11629 95 FHHLLPDFTALEN--VAMPLLIGK-KKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|...
gi 442627138 270 PTTGLDSSSCTKVLELLKKLT-SQGRTIICTIH 301
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNrLQGTAFLVVTH 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
121-321 |
1.05e-19 |
|
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: 86.89 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG---RRRDLPSFRRMSCYITQDDRLQPLl 197
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP-TSGRVRLDGadiSQWDPNELGDHVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENMhiaadlklgqtvsyeekesriedillllglynhdqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSS 277
Cdd:cd03246 91 SIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627138 278 SCTKVLELLKKLTSQGRTIICTIHQPTakLFQIFDQVYVLSAGN 321
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
123-331 |
1.37e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.65 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 123 KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDAL-------SGFKTTG---VDGSILLNGRRRDLPSFRRMSCYITQDDR 192
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGditIDTARSLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 LQPLLTVNENMhIAADLKLGQTVSyEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:PRK11264 96 LFPHRTVLENI-IEGPVIVKGEPK-EEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 273 GLDSSSCTKVLELLKKLTSQGRTIICTIHQPT-AKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQGPAKAL 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
104-337 |
2.99e-19 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 92.24 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKELSLTvklgFNRGSKEILHNVcgKF---PGSQlIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG---RRRDl 177
Cdd:TIGR03375 463 EIEFRNVSFA----YPGQETPALDNV--SLtirPGEK-VAIIGRIGSGKSTLLKLLLGLYQP-TEGSVLLDGvdiRQID- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSF-RRMSCYITQDDRLQpLLTVNENMHIAAdlklgQTVSyeekESRIEDILLLLGLYN----HDQTLTMR-------LS 245
Cdd:TIGR03375 534 PADlRRNIGYVPQDPRLF-YGTLRDNIALGA-----PYAD----DEEILRAAELAGVTEfvrrHPDGLDMQigergrsLS 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 246 GGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPTakLFQIFDQVYVLSAGNCVYQ 325
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVAD 680
|
250
....*....|..
gi 442627138 326 GSTQKLVPFLQS 337
Cdd:TIGR03375 681 GPKDQVLEALRK 692
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
121-303 |
3.53e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGRRRdlpsfrrmSCYITQ----DDRLqP 195
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvLRPTS--GTVRRAGGAR--------VAYVPQrsevPDSL-P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LlTVNENMHIAADLKLGQTVSYE-EKESRIEDILLLLGLynhdQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:NF040873 72 L-TVRDLVAMGRWARRGLWRRLTrDDRAAVDDALERVGL----ADLAGRqlgeLSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|...
gi 442627138 271 TTGLDSSSCTKVLELLKKLTSQGRTIICTIHQP 303
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
121-302 |
4.26e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKT-TG----VDGsILLNGRRRDLPSFRRMSCYITQDDRLQP 195
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEiTSgdliVDG-LKVNDPKVDERLIRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMHIAADLKLGQtvSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:PRK09493 91 HLTALENVMFGPLRVRGA--SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180
....*....|....*....|....*..
gi 442627138 276 SSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
134-326 |
5.91e-19 |
|
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: 85.88 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGsQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR--RDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLkl 211
Cdd:cd03266 30 PG-EVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFDvvKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 gQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS 291
Cdd:cd03266 106 -YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 442627138 292 QGRTIICTIH--QPTAKLfqiFDQVYVLSAGNCVYQG 326
Cdd:cd03266 185 LGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
122-332 |
6.68e-19 |
|
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: 86.39 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 122 SKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRR---DLPSFRRMSCYITQDDRLQpllt 198
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP-ENGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 199 vneNMHIAADLKLGQTVSYEEkesRIEDILLLLGLynHDQTLTMR-------------LSGGQKKRLSIAMELINNPTVM 265
Cdd:cd03252 89 ---NRSIRDNIALADPGMSME---RVIEAAKLAGA--HDFISELPegydtivgeqgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPTAklFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
133-355 |
7.39e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 88.62 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNG-------RRRDLPSFRRMSCYITQDDRLQPLLTVNENmhi 205
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGevlqdsaRGIFLPPHRRRIGYVFQEARLFPHLSVRGN--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 aadLKLGQT-VSYEEKESRIEDILLLLGLynhdQTL----TMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCT 280
Cdd:COG4148 98 ---LLYGRKrAPRAERRISFDEVVELLGI----GHLldrrPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 281 KVLELLKKLTSQGRT-IICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKLvpfLQSVDLPCPMYHNPADYIIEL 355
Cdd:COG4148 171 EILPYLERLRDELDIpILYVSHSL-DEVARLADHVVLLEQGRVVASGPLAEV---LSRPDLLPLAGGEEAGSVLEA 242
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
134-343 |
7.81e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.21 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR-----RRDLPSFRRMSCYITQDDRLQPL-LTVNENMHIAA 207
Cdd:PRK13636 30 KKGEVTAILGGNGAGKSTLFQNLNGI-LKPSSGRILFDGKpidysRKGLMKLRESVGMVFQDPDNQLFsASVYQDVSFGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 208 -DLKLGQtvsyEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELL 286
Cdd:PRK13636 109 vNLKLPE----DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 287 KKLTSQ-GRTIICTIHQ-PTAKLFqiFDQVYVLSAGNCVYQGSTQKLVP---FLQSVDLPCP 343
Cdd:PRK13636 185 VEMQKElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQGNPKEVFAekeMLRKVNLRLP 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
114-332 |
1.72e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKeilhnvcgkfpgsqlIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR---RRDLPSFRRMSCYITQD 190
Cdd:PRK13647 24 LSLSIPEGSK---------------TALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGRevnAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 DRLQPLltvneNMHIAADLKLG---QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFL 267
Cdd:PRK13647 88 PDDQVF-----SSTVWDDVAFGpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 268 DEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
121-326 |
1.84e-18 |
|
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: 84.25 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTgvDGSILLNGRRRDLPSFRRMScYITQDDRLQPLLTV 199
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPD--SGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NENMHIAADLKlgqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:cd03269 88 IDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 280 TKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
110-302 |
2.44e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.07 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 110 LSLTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDAL-------SG----------FKTTGVDGSILLn 171
Cdd:PRK11124 1 MSIQLNgINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGtlniagnhfdFSKTPSDKAIRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 172 grrrdlpsFRRMSCYITQDDRLQPLLTVNENMhIAADLK-LGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKK 250
Cdd:PRK11124 80 --------LRRNVGMVFQQYNLWPHLTVQQNL-IEAPCRvLG--LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442627138 251 RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
116-275 |
3.61e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILlngRRRDLpsfrRMScYITQDDRLQP 195
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVS---IPKGL----RIG-YLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMhIAADLKLGQTVS-------------------------YEEK-----ESRIEDILLLLGLYNHDQTLTMR-L 244
Cdd:COG0488 75 DLTVLDTV-LDGDAELRALEAeleeleaklaepdedlerlaelqeeFEALggweaEARAEEILSGLGFPEEDLDRPVSeL 153
|
170 180 190
....*....|....*....|....*....|.
gi 442627138 245 SGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
112-327 |
4.75e-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: 82.96 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGVDGSILLNGRRrdlpsfrrmscyITQ 189
Cdd:cd03217 1 LEIKdLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYEVTEGEILFKGED------------ITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 ddrlqplLTVNENMhiaadlKLGQTVSYEEKEsRIEDILLLLGLYNhdqtLTMRLSGGQKKRLSIAMELINNPTVMFLDE 269
Cdd:cd03217 69 -------LPPEERA------RLGIFLAFQYPP-EIPGVKNADFLRY----VNEGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 270 PTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGS 327
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
105-302 |
5.92e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTvKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSgFKTTGVDGSILLNGR----------- 173
Cdd:PRK10619 1 MSENKLNVI-DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-FLEKPSEGSIVVNGQtinlvrdkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 174 -----RRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKLGqtVSYEEKESRIEDILLLLGLYNHDQ-TLTMRLSGG 247
Cdd:PRK10619 79 lkvadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKVGIDERAQgKYPVHLSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 248 QKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
141-339 |
6.33e-18 |
|
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: 84.23 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 141 IMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGR------RRDLPSFRR--MScYITQDDRLQPLLTVNENmhIAADLKL 211
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLiEPTS--GKVLIDGQdiaamsRKELRELRRkkIS-MVFQSFALLPHRTVLEN--VAFGLEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 gQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL-T 290
Cdd:cd03294 130 -QGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 291 SQGRTIICTIHQPtAKLFQIFDQVYVLSAGNCVYQGSTQKLV--P-------FLQSVD 339
Cdd:cd03294 209 ELQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTPEEILtnPandyvreFFRGVD 265
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
113-326 |
6.92e-18 |
|
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: 83.54 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 113 TVKLGFNRGSKEI--LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG--FKTTG---VDGSILLNGRRRDLpsfRRMSC 185
Cdd:cd03267 22 SLKSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPTSGevrVAGLVPWKRRKKFL---RRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 186 YITQDDRLQPLLTVNENMHIAADLklgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVM 265
Cdd:cd03267 99 VFGQKTQLWWDLPVIDSFYLLAAI---YDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIH--QPTAKLfqiFDQVYVLSAGNCVYQG 326
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
126-331 |
7.09e-18 |
|
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: 83.54 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLTVNENmh 204
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGGEDaTDVPVQERNVGFVFQHYALFRHMTVFDN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 205 IAADLKL---GQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDssscTK 281
Cdd:cd03296 95 VAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD----AK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 282 VLELLKKLTSQ-----GRTIICTIH-QPTAklFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03296 171 VRKELRRWLRRlhdelHVTTVFVTHdQEEA--LEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
114-303 |
7.34e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR--RRDLPSFRRMSCYITQDD 191
Cdd:PRK13538 5 RNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL-ARPDAGEVLWQGEpiRRQRDEYHQDLLYLGHQP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENMHIAAdlKLGQTVSyeekESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK13538 84 GIKTELTALENLRFYQ--RLHGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQGRTIICTIHQP 303
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
84-332 |
7.39e-18 |
|
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: 87.87 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 84 EEEVHFDTDALNNLPArepvDMEFKELSLtvKLGFNRgskEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTG 163
Cdd:TIGR01193 457 EFINKKKRTELNNLNG----DIVINDVSY--SYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 164 vDGSILLNG---RRRDLPSFRRMSCYITQDdrlqPLL---TVNENMHIAADLKLGQ-----TVSYEEKESRIEDilLLLG 232
Cdd:TIGR01193 528 -SGEILLNGfslKDIDRHTLRQFINYLPQE----PYIfsgSILENLLLGAKENVSQdeiwaACEIAEIKDDIEN--MPLG 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 233 LYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSqgRTIICTIHQPTakLFQIFD 312
Cdd:TIGR01193 601 YQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSD 676
|
250 260
....*....|....*....|
gi 442627138 313 QVYVLSAGNCVYQGSTQKLV 332
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELL 696
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
121-332 |
7.90e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRR-RDLPSFRR----MScYITQD---- 190
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLvKPDS--GRIFLDGEDiTHLPMHKRarlgIG-YLPQEasif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 -DrlqplLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDE 269
Cdd:COG1137 91 rK-----LTVEDN--ILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 270 PTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETL-GICDRAYIISEGKVLAEGTPEEIL 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
141-331 |
8.23e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 85.24 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 141 IMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLTVNENmhIAADLKLgQTVSYEE 219
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-SGSIMLDGEDvTNVPPHLRHINMVFQSYALFPHMTVEEN--VAFGLKM-RKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 220 KESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIIC 298
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVF 156
|
170 180 190
....*....|....*....|....*....|...
gi 442627138 299 TIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:TIGR01187 157 VTHDQEEAM-TMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
133-327 |
1.25e-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: 87.76 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR--RRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLK 210
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGL-LPPTSGTVLVGGKdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 lGQtvSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT 290
Cdd:TIGR01257 1032 -GR--SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190
....*....|....*....|....*....|....*...
gi 442627138 291 SqGRTII-CTIHQPTAKLFQifDQVYVLSAGNCVYQGS 327
Cdd:TIGR01257 1109 S-GRTIImSTHHMDEADLLG--DRIAIISQGRLYCSGT 1143
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
111-331 |
1.61e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.43 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 111 SLTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgvD-GSILLNGrrRDLPSF-----RRM 183
Cdd:COG1118 2 SIEVRnISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETP--DsGRIVLNG--RDLFTNlppreRRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 ScYITQDDRLQPLLTVNENmhIAADLKlGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPT 263
Cdd:COG1118 78 G-FVFQHYALFPHMTVAEN--IAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 264 VMFLDEPTTGLDssscTKV--------LELLKKLtsQGRTIICTiHQPT-AklFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG1118 154 VLLLDEPFGALD----AKVrkelrrwlRRLHDEL--GGTTVFVT-HDQEeA--LELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
121-301 |
3.12e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNG------RRRDLPSFRRMSCYITQDDRLQ 194
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS-AGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENMHIAADLKlgqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:PRK10908 92 MDRTVYDNVAIPLIIA---GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180
....*....|....*....|....*..
gi 442627138 275 DSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
140-317 |
3.28e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.07 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPSFR-------RMscyITQDDRLQPLLTVNENMHIAADLKLG 212
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPD-SGEILLDGEPVRFRSPRdaqaagiAI---IHQELNLVPNLSVAENIFLGREPRRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 213 QTVSYEEKESRIEDILLLLGLyNHD-QTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS 291
Cdd:COG1129 110 GLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA 188
|
170 180
....*....|....*....|....*....
gi 442627138 292 QGRTIICTIHqptaKL---FQIFDQVYVL 317
Cdd:COG1129 189 QGVAIIYISH----RLdevFEIADRVTVL 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
120-331 |
3.45e-17 |
|
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: 81.58 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNG---RRRDLPSFRRMSCYITQDDRLQPL 196
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL-IEPTSGEIFIDGediREQDPVELRRKIGYVIQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 197 LTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLynHDQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:cd03295 90 MTVEEN--IALVPKL-LKWPKEKIRERADELLALVGL--DPAEFADRypheLSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 273 GLDSSSCTKVLELLKKLTSQ-GRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQElGKTIVFVTHD-IDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
110-338 |
3.94e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 110 LSLTVKLGfnrgskEILHnvcgkfpgsqliaIMGPSGAGKSTLLDALSGfkTTGVDGSILLNGR---RRDLPSFRRMSCY 186
Cdd:PRK03695 15 LSAEVRAG------EILH-------------LVGPNGAGKSTLLARMAG--LLPGSGSIQFAGQpleAWSAAELARHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 187 ITQDDRLQPLLTVNENMhiaaDLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGG--QKKRLSIAMELI---NN 261
Cdd:PRK03695 74 LSQQQTPPFAMPVFQYL----TLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 262 P--TVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIfDQVYVLSAGNCVYQGSTQKL--VPFLQS 337
Cdd:PRK03695 150 PagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGRRDEVltPENLAQ 228
|
.
gi 442627138 338 V 338
Cdd:PRK03695 229 V 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
134-331 |
3.96e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQLiAIMGPSGAGKST----LLDALSGFKTTGVDGSILLNGRRRDLPSFRRMSCYITQD--DRLQPLLTVNEnmHIAA 207
Cdd:PRK15134 311 PGETL-GLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSLNPRLNVLQ--IIEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 208 DLKLGQ-TVSYEEKESRIEDILLLLGLynhDQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKV 282
Cdd:PRK15134 388 GLRVHQpTLSAAQREQQVIAVMEEVGL---DPETRHRypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 283 LELLKKLTSQgrtiictiHQpTAKLFQIFD---------QVYVLSAGNCVYQGSTQKL 331
Cdd:PRK15134 465 LALLKSLQQK--------HQ-LAYLFISHDlhvvralchQVIVLRQGEVVEQGDCERV 513
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
104-331 |
6.64e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 84.38 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKELSLTvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkttgVD---GSILLNG---RRRDL 177
Cdd:TIGR02203 330 DVEFRNVTFR----YPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF----YEpdsGQILLDGhdlADYTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSFRRMSCYITQDDRLQplltvneNMHIAADLKLGQTVSYEEkeSRIEDIL-----------LLLGLYNHDQTLTMRLSG 246
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLF-------NDTIANNIAYGRTEQADR--AEIERALaaayaqdfvdkLPLGLDTPIGENGVLLSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 247 GQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTsQGRTIICTIHQPTAklFQIFDQVYVLSAGNCVYQG 326
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLST--IEKADRIVVMDDGRIVERG 549
|
....*
gi 442627138 327 STQKL 331
Cdd:TIGR02203 550 THNEL 554
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
121-350 |
7.28e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.43 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVC-----GKFpgsqlIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRRR-DL-PSFRRMScYITQDDR 192
Cdd:COG3839 14 GGVEALKDIDldiedGEF-----LVLLGPSGCGKSTLLRMIAGLeDPTS--GEILIGGRDVtDLpPKDRNIA-MVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 LQPLLTVNENMhiAADLKLgQTVSYEEKESRIEDILLLLGLynhDQTLTMR---LSGGQKKRLSIAMELINNPTVMFLDE 269
Cdd:COG3839 86 LYPHMTVYENI--AFPLKL-RKVPKAEIDRRVREAAELLGL---EDLLDRKpkqLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 270 PTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPT-----AklfqifDQVYVLSAGNCVYQGSTQKLvpflqsvdlpcp 343
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVeamtlA------DRIAVMNDGRIQQVGTPEEL------------ 221
|
....*..
gi 442627138 344 mYHNPAD 350
Cdd:COG3839 222 -YDRPAN 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
116-327 |
7.61e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.97 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR------RRDLPSFRRMscyITQ 189
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPAELARRRAV---LPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 DDRLQPLLTVNENMHI-AADLKLGQTvsyeEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELI------NNP 262
Cdd:PRK13548 84 HSSLSFPFTVEEVVAMgRAPHGLSRA----EDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 263 TVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIH---QptAKLFQifDQVYVLSAGNCVYQGS 327
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHdlnL--AARYA--DRIVLLHQGRLVADGT 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
116-332 |
9.02e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALsGFKTTGVDGSILLNGR---RRDLPSFRRMSCYITQDDR 192
Cdd:PRK10575 17 VSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQpleSWSSKAFARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 LQPLLTVNENMHIA------ADLKLGQtvsyeEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMF 266
Cdd:PRK10575 96 AAEGMTVRELVAIGrypwhgALGRFGA-----ADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 267 LDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAA-RYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
103-320 |
1.15e-16 |
|
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: 78.24 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 103 VDMEFKELSLTVKLGfnrgskEILhnvcgkfpgsqliAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLPSFRR 182
Cdd:cd03215 12 VKGAVRDVSFEVRAG------EIV-------------GIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MS----CYITqDDRLQ----PLLTVNENMhiaadlklgqtvsyeekesriedillllglynhdqTLTMRLSGGQKKRLSI 254
Cdd:cd03215 72 AIragiAYVP-EDRKReglvLDLSVAENI-----------------------------------ALSSLLSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 255 AMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVLSAG 320
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVL-LISSELDELLGLCDRILVMYEG 180
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
134-303 |
1.41e-16 |
|
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: 83.18 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQlIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNG---RRRDLPSFRRMSCYITQDdrlqPLL---TVNENMHIAA 207
Cdd:TIGR02868 360 PGER-VAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGvpvSSLDQDEVRRRVSVCAQD----AHLfdtTVRENLRLAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 208 dlklgQTVSYEEkesrIEDILLLLGLYNHDQTLT-----------MRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDS 276
Cdd:TIGR02868 434 -----PDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*..
gi 442627138 277 SSCTKVLELLKKlTSQGRTIICTIHQP 303
Cdd:TIGR02868 505 ETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
104-327 |
1.50e-16 |
|
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: 79.07 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKELSLTvklgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALsgFKTT-GVDGSILLNGR------RRD 176
Cdd:cd03244 2 DIEFKNVSLR----YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRLVeLSSGSILIDGVdiskigLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 177 LPSfrRMSCyITQDdrlqPLL---TVNENMHIaadlkLGQtvsYEEKEsrIEDILLLLGLYNHDQTLTMRL--------- 244
Cdd:cd03244 76 LRS--RISI-IPQD----PVLfsgTIRSNLDP-----FGE---YSDEE--LWQALERVGLKEFVESLPGGLdtvveegge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 245 --SGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSqGRTIICTIHqptaKLFQI--FDQVYVLSAG 320
Cdd:cd03244 139 nlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAH----RLDTIidSDRILVLDKG 213
|
....*..
gi 442627138 321 NCVYQGS 327
Cdd:cd03244 214 RVVEFDS 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
120-341 |
1.60e-16 |
|
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: 80.23 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKT--------TGVDGSILLNGRRRdlpSFRRMSCYITQD- 190
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpaqgtvsfRGQDLYQLDRKQRR---AFRRDVQLVFQDs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 -DRLQPLLTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLY-NHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:TIGR02769 98 pSAVNPRMTVRQI--IGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKLVPF-------LQSVDLP 341
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFkhpagrnLQSAVLP 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
121-301 |
2.03e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.36 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSgfKTTGVD-GSILLNGRR------RDLPsfRRMScyI-TQDDR 192
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS--RLLPPDsGEVLVDGLDvattpsRELA--KRLA--IlRQENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 LQPLLTVnenmhiaADLklgqtVSY-----------EEKESRIEDILLLLGLynhdQTLTMR----LSGGQKKRLSIAME 257
Cdd:COG4604 86 INSRLTV-------REL-----VAFgrfpyskgrltAEDREIIDEAIAYLDL----EDLADRyldeLSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442627138 258 LINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIH 301
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLH 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
116-332 |
3.01e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRrdlpsfrrMSCYITQD-DRLQ 194
Cdd:PRK10253 15 LGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP-AHGHVWLDGEH--------IQHYASKEvARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTvnENMHIAADLKLGQTVSY-------------EEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINN 261
Cdd:PRK10253 84 GLLA--QNATTPGDITVQELVARgryphqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 262 PTVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHD-LNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
137-301 |
3.60e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLTVNENmhIAADLKLGQtV 215
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQP-TAGQIMLDGVDlSHVPPYQRPINMMFQSYALFPHMTVEQN--IAFGLKQDK-L 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 216 SYEEKESRIEDILLLLglynHDQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKV-LELLKKLT 290
Cdd:PRK11607 122 PKAEIASRVNEMLGLV----HMQEFAKRkphqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILE 197
|
170
....*....|.
gi 442627138 291 SQGRTIICTIH 301
Cdd:PRK11607 198 RVGVTCVMVTH 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
126-344 |
3.82e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.02 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPSFRRMSCYIT---QDDRLQPLLTVnen 202
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNQAITDDNFEKLRKHIGivfQNPDNQFVGSI--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 203 mhIAADLKLG---QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:PRK13648 101 --VKYDVAFGlenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 280 TKVLELLKKLTSQGR-TIICTIHQPTAKLFQifDQVYVLSAGNcVYQGSTQKLV----PFLQSV--DLPCPM 344
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHDLSEAMEA--DHVIVMNKGT-VYKEGTPTEIfdhaEELTRIglDLPFPI 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
114-326 |
4.13e-16 |
|
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: 76.58 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGrrrdlpsfrrmscyitqddrl 193
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-DLKPQQGEITLDG--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 194 QPLLTVNENMHiaadlklgQTVSYEEKESRIEDILLLlglynhdQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:cd03247 64 VPVSDLEKALS--------SLISVLNQRPYLFDTTLR-------NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442627138 274 LDSSSCTKVLELLKKLTsQGRTIICTIHQPTAklFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03247 129 LDPITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
140-343 |
4.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.02 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGF--KTTG---VDGSILLNG-RRRDLPSFRRMSCYITQDDRLQPLL-TVNEnmhiaaDLKLG 212
Cdd:PRK13649 37 AFIGHTGSGKSTIMQLLNGLhvPTQGsvrVDDTLITSTsKNKDIKQIRKKVGLVFQFPESQLFEeTVLK------DVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 213 QT---VSYEEKESRIEDILLLLGLynhDQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLEL 285
Cdd:PRK13649 111 PQnfgVSQEEAEALAREKLALVGI---SESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 286 LKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL---VPFLQSVDLPCP 343
Cdd:PRK13649 188 FKKLHQSGMTIVLVTHL-MDDVANYADFVYVLEKGKLVLSGKPKDIfqdVDFLEEKQLGVP 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
125-331 |
6.33e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 125 ILHNVCGKF-------------PGSQLIAIMGPSGAGKSTLLDALSGF-KTTgvDGSILLNG--------RRRDLpsfrr 182
Cdd:PRK11432 8 VLKNITKRFgsntvidnlnltiKQGTMVTLLGPSGCGKTTVLRLVAGLeKPT--EGQIFIDGedvthrsiQQRDI----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 msCYITQDDRLQPLLTVNENmhIAADLKLgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNP 262
Cdd:PRK11432 81 --CMVFQSYALFPHMSLGEN--VGYGLKM-LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 263 TVMFLDEPTTGLDS----SSCTKVLELLKKLtsqGRTIICTIHQPTaKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK11432 156 KVLLFDEPLSNLDAnlrrSMREKIRELQQQF---NITSLYVTHDQS-EAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
143-350 |
6.84e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 143 GPSGAGKSTLLDALSGFKTTgVDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLTVNENMhiAADLKLGQtVSYEEKE 221
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDI-TSGDLFIGEKRmNDVPPAERGVGMVFQSYALYPHLSVAENM--SFGLKLAG-AKKEEIN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 222 SRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSS----SCTKVLELLKKLtsqGRTII 297
Cdd:PRK11000 112 QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqMRIEISRLHKRL---GRTMI 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 298 CTIH-QPTAklFQIFDQVYVLSAGNcVYQgstqklvpflqsVDLPCPMYHNPAD 350
Cdd:PRK11000 189 YVTHdQVEA--MTLADKIVVLDAGR-VAQ------------VGKPLELYHYPAN 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
114-332 |
6.95e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.61 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNR-----GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRR-RDLPSFRRMS--- 184
Cdd:PRK11614 4 VMLSFDKvsahyGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATSGRIVFDGKDiTDWQTAKIMReav 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 185 CYITQDDRLQPLLTVNENMHIAADLKLGQtvSYEEKESRIEDILLLLGLYNHDQTLTMrlSGGQKKRLSIAMELINNPTV 264
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERD--QFQERIKWVYELFPRLHERRIQRAGTM--SGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 265 MFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
94-320 |
8.59e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.85 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 94 LNNLPAREPVdMEF----KELSL-TVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSI 168
Cdd:TIGR01842 298 LANYPSRDPA-MPLpepeGHLSVeNVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP-TSGSV 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 169 LLNG---RRRDLPSFRRMSCYITQDDRLQPLlTVNENmhIAadlKLGQTVSYEE--KESRIEDIL-LLLGLYN-HDQTLT 241
Cdd:TIGR01842 376 RLDGadlKQWDRETFGKHIGYLPQDVELFPG-TVAEN--IA---RFGENADPEKiiEAAKLAGVHeLILRLPDgYDTVIG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 242 MR---LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTakLFQIFDQVYVLS 318
Cdd:TIGR01842 450 PGgatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQ 527
|
..
gi 442627138 319 AG 320
Cdd:TIGR01842 528 DG 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
121-301 |
1.00e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTG----VDGSILLNGRRRDLpsfRRMscyiTQDDRLQPL 196
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagelLAGTAPLAEAREDT---RLM----FQDARLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 197 LTVNENmhiaadLKLGQTVSYEEkesRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDS 276
Cdd:PRK11247 96 KKVIDN------VGLGLKGQWRD---AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180
....*....|....*....|....*.
gi 442627138 277 SSCTKVLELLKKLTSQ-GRTIICTIH 301
Cdd:PRK11247 167 LTRIEMQDLIESLWQQhGFTVLLVTH 192
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
110-320 |
1.02e-15 |
|
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: 77.09 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 110 LSLTVKLGfnRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKT-TGvdGSILLNGR------RRDLPSFRR 182
Cdd:COG4181 14 LTKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRpTS--GTVRLAGQdlfaldEDARARLRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MSC-YITQDDRLQPLLTVNENMHIAADLKlgqtvSYEEKESRIEDILLLLGLynhDQTLTMR---LSGGQKKRLSIAMEL 258
Cdd:COG4181 90 RHVgFVFQSFQLLPTLTALENVMLPLELA-----GRRDARARARALLERVGL---GHRLDHYpaqLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS-QGRTIICTIHQPtaKLFQIFDQVYVLSAG 320
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDP--ALAARCDRVLRLRAG 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
123-331 |
1.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 123 KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF--KTTGV----DGSILLNGRRRDLPSFRRMSCYITQDDRLQPL 196
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALlkPTTGTvtvdDITITHKTKDKYIRPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 197 LTVNENMHIAADLKLGQTVsyEEKESRIEDILLLLGLYNHDQTLT-MRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNL--DEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 276 SSSCTKVLELLKKL-TSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK13646 178 PQSKRQVMRLLKSLqTDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
112-352 |
1.16e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFK----TTGVDGSILLNG-----RRRDLPSFR 181
Cdd:PRK14239 6 LQVSdLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpEVTITGSIVYNGhniysPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 182 RMSCYITQDDRLQPLlTVNENMHIAADLK-------LGQTVSYEEKESRI----EDILlllglynHDQTLTmrLSGGQKK 250
Cdd:PRK14239 86 KEIGMVFQQPNPFPM-SIYENVVYGLRLKgikdkqvLDEAVEKSLKGASIwdevKDRL-------HDSALG--LSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 251 RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKlfQIFDQVYVLSAGNCVYQGSTQK 330
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAS--RISDRTGFFLDGDLIEYNDTKQ 233
|
250 260
....*....|....*....|....*..
gi 442627138 331 lvpflqsvdlpcpMYHNPA-----DYI 352
Cdd:PRK14239 234 -------------MFMNPKhketeDYI 247
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
105-328 |
1.19e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.52 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKLG---FNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRRDLPSFR 181
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM-IEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 182 ------RMscyITQDdrlqPLLTVNENMHIA----ADLKLGQTVSYEEKESRIEDILLLLGLY-NHDQTLTMRLSGGQKK 250
Cdd:PRK15112 84 yrsqriRM---IFQD----PSTSLNPRQRISqildFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 251 RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtsQGRTIICTIH--QPTAKLFQIFDQVYVLSAGNCVYQGST 328
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL--QEKQGISYIYvtQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
123-332 |
1.27e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 123 KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGRRRDLPSF----RRMSCYITQDDRLQPLLT 198
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA-GNIIIDDEDISLLPLharaRRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 199 VNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:PRK10895 95 VYDN--LMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 279 CTKVLELLKKLTSQGRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
123-326 |
1.40e-15 |
|
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: 76.92 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 123 KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGV-DGSILLNGrrRDL----PSFR-RMSCYIT-QDDRLQP 195
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVtSGTILFKG--QDLlelePDERaRAGLFLAfQYPEEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMHIAADLKLGQTVSYEEKESRIEDIL-LLLGLYNHDQTLTMR-----LSGGQKKRLSIAMELINNPTVMFLDE 269
Cdd:TIGR01978 91 GVSNLEFLRSALNARRSARGEEPLDLLDFEKLLkEKLALLDMDEEFLNRsvnegFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 270 PTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPtaKLFQIF--DQVYVLSAGNCVYQG 326
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
139-331 |
1.68e-15 |
|
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: 79.73 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKSTLLDALSGFKTTGvdGSILLNGR------RRDLPSFRRmscyitqddRLQ-----------PLLTVN- 200
Cdd:COG4172 315 LGLVGESGSGKSTLGLALLRLIPSE--GEIRFDGQdldglsRRALRPLRR---------RMQvvfqdpfgslsPRMTVGq 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 201 ---ENMHIaadlkLGQTVSYEEKESRIEDILLLLGL-------YNHDqtltmrLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:COG4172 384 iiaEGLRV-----HGPGLSAAERRARVAEALEEVGLdpaarhrYPHE------FSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 271 TTGLDSSSCTKVLELLKKLtsQGRtiictiHQpTAKLF---------QIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG4172 453 TSALDVSVQAQILDLLRDL--QRE------HG-LAYLFishdlavvrALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
112-331 |
2.72e-15 |
|
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: 79.34 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVKLGFNRGSKEILHNVCgkF---PGsQLIAIMGPSGAGKStlLDALS-----GFKTTGVDGSILLNGRrrDLPSF--- 180
Cdd:COG4172 12 LSVAFGQGGGTVEAVKGVS--FdiaAG-ETLALVGESGSGKS--VTALSilrllPDPAAHPSGSILFDGQ--DLLGLser 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 181 -------RRMSCyITQD--DRLQPLLTVNEnmHIAADLKLGQTVSYEEKESRIEDILLLLGL---------YNHdqtltm 242
Cdd:COG4172 85 elrrirgNRIAM-IFQEpmTSLNPLHTIGK--QIAEVLRLHRGLSGAAARARALELLERVGIpdperrldaYPH------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 243 RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GrtiictihqpTAKLF---------QIFD 312
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElG----------MALLLithdlgvvrRFAD 225
|
250
....*....|....*....
gi 442627138 313 QVYVLSAGNCVYQGSTQKL 331
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAEL 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
139-331 |
2.74e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKS-TLLDALSGFKTTGVD---GSILLNGRRRDLPSFRRMSCYITQDDR--------------LQPLLTVN 200
Cdd:PRK10261 45 LAIVGESGSGKSvTALALMRLLEQAGGLvqcDKMLLRRRSRQVIELSEQSAAQMRHVRgadmamifqepmtsLNPVFTVG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 201 EnmHIAADLKLGQTVSYEE---------KESRIEDILLLLGLYNHdqtltmRLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK10261 125 E--QIAESIRLHQGASREEamveakrmlDQVRIPEAQTILSRYPH------QLSGGMRQRVMIAMALSCRPAVLIADEPT 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK10261 197 TALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
116-350 |
3.04e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSgfKTTGVDGSILLNG-----------RRRDLPSFRRMS 184
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGrveffnqniyeRRVNLNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 185 CYITQDDRLQPLlTVNENmhIAADLKLgqtVSYEEK-------ESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAME 257
Cdd:PRK14258 91 SMVHPKPNLFPM-SVYDN--VAYGVKI---VGWRPKleiddivESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 258 LINNPTVMFLDEPTTGLDSSSCTKVLELLK--KLTSQGRTIICTIHQPtaklfqifdQVYVLSAGNCVYQGSTQKLVPFL 335
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLH---------QVSRLSDFTAFFKGNENRIGQLV 235
|
250
....*....|....*
gi 442627138 336 QsVDLPCPMYHNPAD 350
Cdd:PRK14258 236 E-FGLTKKIFNSPHD 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
119-320 |
3.28e-15 |
|
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: 75.55 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 119 NRGSKEI--LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALsgFKTTGVD-GSILLN--GRRRDLPSF---------RRMS 184
Cdd:COG4778 18 LQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCI--YGNYLPDsGSILVRhdGGWVDLAQAspreilalrRRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 185 CYITQDDRLQPLLTVNEnmhIAADLKLGQTVSYEEKESRIEDILLLLGLynhDQTL------TmrLSGGQKKRLSIAMEL 258
Cdd:COG4778 96 GYVSQFLRVIPRVSALD---VVAEPLLERGVDREEARARARELLARLNL---PERLwdlppaT--FSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLfQIFDQVYVLSAG 320
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVRE-AVADRVVDVTPF 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
118-343 |
3.31e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.62 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 118 FNRGS---KEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTgvDGSILLNG-----RRRDLPSFRRMSCYIT 188
Cdd:PRK13637 12 YMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKPT--SGKIIIDGvditdKKVKLSDIRKKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QddrlQPLLTVNENMhIAADLKLGQT---VSYEEKESRIEDILLLLGL-YNH--DQTlTMRLSGGQKKRLSIAMELINNP 262
Cdd:PRK13637 90 Q----YPEYQLFEET-IEKDIAFGPInlgLSEEEIENRVKRAMNIVGLdYEDykDKS-PFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 263 TVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIH--QPTAKlfqIFDQVYVLSAGNCVYQGSTQ---KLVPFLQ 336
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHsmEDVAK---LADRIIVMNKGKCELQGTPRevfKEVETLE 240
|
....*..
gi 442627138 337 SVDLPCP 343
Cdd:PRK13637 241 SIGLAVP 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
136-303 |
4.32e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 136 SQLIAIMGPSGAGKSTLLDALSGFKTtGVDGSILLNGRrrdlpSFRRMS------------CYITQDDRLQPLLTVNENM 203
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDD-GSSGEVSLVGQ-----PLHQMDeearaklrakhvGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 204 HIAADLKlGQTvsyeEKESRIEDILLL--LGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTK 281
Cdd:PRK10584 110 ELPALLR-GES----SRQSRNGAKALLeqLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|...
gi 442627138 282 VLELLKKLT-SQGRTIICTIHQP 303
Cdd:PRK10584 185 IADLLFSLNrEHGTTLILVTHDL 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
140-329 |
6.30e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRD----LPSFRRMSCYITQDDRLQPLLTVNENMHIAADLK---LG 212
Cdd:PRK09700 35 ALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYNkldhKLAAQLGIGIIYQELSVIDELTVLENLYIGRHLTkkvCG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 213 -QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS 291
Cdd:PRK09700 114 vNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRK 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 442627138 292 QGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQ 329
Cdd:PRK09700 194 EGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
118-301 |
6.61e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.89 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 118 FNRGSK---EILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF--KTTGVDGSILLNGRRRDLPSFRR--MSCYITQD 190
Cdd:PRK13651 12 FNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllPDTGTIEWIFKDEKNKKKTKEKEkvLEKLVIQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 DRLQPLLTVNE-----------------NMHIAADLKLGQT---VSYEEKESRIEDILLLLGLynhDQTLTMR----LSG 246
Cdd:PRK13651 92 TRFKKIKKIKEirrrvgvvfqfaeyqlfEQTIEKDIIFGPVsmgVSKEEAKKRAAKYIELVGL---DESYLQRspfeLSG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 247 GQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
134-330 |
7.13e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGR-------RRDLPSFRRMSCYITQDDRLQPLLTVNENmhia 206
Cdd:PRK11144 22 PAQGITAIFGRSGAGKTSLINAISGL-TRPQKGRIVLNGRvlfdaekGICLPPEKRRIGYVFQDARLFPHYKVRGN---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 207 adLKLGQTvsyEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELL 286
Cdd:PRK11144 97 --LRYGMA---KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627138 287 KKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQK 330
Cdd:PRK11144 172 ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
137-326 |
1.09e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRR-RDLPSFR--RMSCYIT-QDDRLQPLLTVNENMHIAADLKL 211
Cdd:PRK11300 32 EIVSLIGPNGAGKTTVFNCLTGFyKPTG--GTILLRGQHiEGLPGHQiaRMGVVRTfQHVRLFREMTVIENLLVAQHQQL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 G--------QTVSYEEKES----RIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:PRK11300 110 KtglfsgllKTPAFRRAESealdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKET 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 280 TKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:PRK11300 190 KELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
134-299 |
1.32e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQLIaIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKlgq 213
Cdd:PRK13543 36 AGEALL-VQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLH--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 214 tvSYEEKESRiEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLK-KLTSQ 292
Cdd:PRK13543 111 --GRRAKQMP-GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGG 187
|
....*..
gi 442627138 293 GRTIICT 299
Cdd:PRK13543 188 GAALVTT 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
98-301 |
1.61e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.75 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 98 PAREPV---DMEFKELSLTVKLGFNRGSKEILHNVCGKFPGS---------------QLIAIMGPSGAGKSTLLDALSGf 159
Cdd:TIGR01257 1909 PAKEPIfdeDDDVAEERQRIISGGNKTDILRLNELTKVYSGTsspavdrlcvgvrpgECFGLLGVNGAGKTTTFKMLTG- 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 160 KTTGVDGSILLNGRR--RDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKlgqTVSYEEKESRIEDILLLLGLYNHD 237
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR---GVPAEEIEKVANWSIQSLGLSLYA 2064
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 238 QTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:TIGR01257 2065 DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
125-327 |
1.75e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 125 ILHNVCGKFPGSQLIAIMGPSGAGKSTLL-----------------DALSGFKTTGVDGSILLNGRR-RDLPSFRRMSCY 186
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnglikskygtiqvgDIYIGDKKNNHELITNPYSKKiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 187 ITQDDRLQPLLTVNENMHIAADLKLGQtvSYEEKESRIEDILLLLGL-YNHDQTLTMRLSGGQKKRLSIAMELINNPTVM 265
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVALGV--KKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGS 327
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGT 259
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
124-331 |
1.94e-14 |
|
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: 76.78 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 124 EILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkttgVD---GSILLNGRR-RDLP--SFRRMSCYITQDdrlqpll 197
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF----YDvtsGRILIDGQDiRDVTqaSLRAAIGIVPQD------- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENMHIAADLKLGQT-VSYEE-----KESRIEDilLLLGLYNHDQTLT----MRLSGGQKKRLSIAMELINNPTVMFL 267
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPdASEEEveaaaRAAQIHD--FIESLPDGYDTRVgergLKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 268 DEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHqptaKLFQIF--DQVYVLSAGNCVYQGSTQKL 331
Cdd:COG5265 519 DEATSALDSRTERAIQAALREV-ARGRTTLVIAH----RLSTIVdaDEILVLEAGRIVERGTHAEL 579
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
116-355 |
2.67e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLdALSGFKTTGVDGSILLNG-------RRRDLPSFRRMScYIT 188
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLL-RLIGGQIAPDHGEILFDGenipamsRSRLYTVRKRMS-MLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDRLQPLLTVNENmhiaadlklgqtVSYEEKE-SRIEDILL---------LLGLYNHDQTLTMRLSGGQKKRLSIAMEL 258
Cdd:PRK11831 91 QSGALFTDMNVFDN------------VAYPLREhTQLPAPLLhstvmmkleAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 259 INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKLVP---- 333
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQALQAnpdp 237
|
250 260
....*....|....*....|....*..
gi 442627138 334 ----FLQSV-DLPCPMYHNPADYIIEL 355
Cdd:PRK11831 238 rvrqFLDGIaDGPVPFRYPAGDYHADL 264
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
140-365 |
4.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGF--KTTGV----DGSILLNGRRRDLPSFRRMSCYITQDDRLQPLLTVnenmhIAADLKLGQ 213
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLlqPTEGKvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET-----VLKDVAFGP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 214 T---VSYEEKESRIEDILLLLGLYNHD-QTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL 289
Cdd:PRK13643 111 QnfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 290 TSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL---VPFLQSVDLPCPMYHNPADYIIElaCGEYGYDKV 365
Cdd:PRK13643 191 HQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVfqeVDFLKAHELGVPKATHFADQLQK--TGAVTFEKL 266
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
120-341 |
4.22e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGR------RRDLPSFRRMSCYITQD--D 191
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP-SQGNVSWRGEplaklnRAQRKAFRRDIQMVFQDsiS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGL-YNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:PRK10419 101 AVNPRKTVREI--IREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 271 TTGLDSSSCTKVLELLKKLTSQGRTIICTI-HQptAKLFQIFDQ-VYVLSAGNCVYQGSTQKLVPF-------LQSVDLP 341
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFItHD--LRLVERFCQrVMVMDNGQIVETQPVGDKLTFsspagrvLQNAVLP 256
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
105-320 |
4.39e-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: 71.35 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKLGFNRGSKeILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRRrdlpsfrrms 184
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF-TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG-ELEKLSGSVSVPGSI---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 185 CYITQddrlQPLL---TVNENMhiaadlklgqTVSYEEKESRIEDILLLLGLY-------NHDQTLT----MRLSGGQKK 250
Cdd:cd03250 69 AYVSQ----EPWIqngTIRENI----------LFGKPFDEERYEKVIKACALEpdleilpDGDLTEIgekgINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 251 RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLE-LLKKLTSQGRTIICTIHQPTakLFQIFDQVYVLSAG 320
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNG 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
140-323 |
4.48e-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: 70.54 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRRDLPSFRRMscyitqddrlqplltvnenmhiaadLKLG-QTVSye 218
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGL-YKPDSGEILVDGKEVSFASPRDA-------------------------RRAGiAMVY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 219 ekesriedillllglynhdQtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIIC 298
Cdd:cd03216 82 -------------------Q-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIF 137
|
170 180
....*....|....*....|....*...
gi 442627138 299 TIHqptaKL---FQIFDQVYVLSAGNCV 323
Cdd:cd03216 138 ISH----RLdevFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
114-327 |
5.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTgvDGSILLNG---RRRDLPSFRRMSCYITQ 189
Cdd:PRK13632 13 VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGitiSKENLKEIRKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 DDRLQPL-LTVNENmhIAADLKlGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:PRK13632 91 NPDNQFIgATVEDD--IAFGLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLTSQG-RTIICTIHQPTAKLFQifDQVYVLSAGNCVYQGS 327
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILA--DKVIVFSEGKLIAQGK 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
120-301 |
5.46e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGVDGSILLNGRRRDLPsfRRMSCYITQDDRLQ---P 195
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFvRLASGKISILGQPTRQALQ--KNLVAYVPQSEEVDwsfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLtVNENMHIAADLKLGQT-VSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:PRK15056 95 VL-VEDVVMMGRYGHMGWLrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180
....*....|....*....|....*..
gi 442627138 275 DSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
112-301 |
7.43e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.11 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGRRRDLPSFRRMScyitqd 190
Cdd:PRK09536 4 IDVSdLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA-GTVLVAGDDVEALSARAAS------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 drlQPLLTVNENMHIAADLKLGQTVSY-------------EEKESRIEDILLLLGLYNH-DQTLTmRLSGGQKKRLSIAM 256
Cdd:PRK09536 77 ---RRVASVPQDTSLSFEFDVRQVVEMgrtphrsrfdtwtETDRAAVERAMERTGVAQFaDRPVT-SLSGGERQRVLLAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442627138 257 ELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
141-348 |
9.12e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 141 IMGPSGAGKSTLLDALSGF-KTTgvDGSILLNGR---------RRDLPSFRRMscyITQDdrlqPLLTVNENMH----IA 206
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLvKAT--DGEVAWLGKdllgmkddeWRAVRSDIQM---IFQD----PLASLNPRMTigeiIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 207 ADLKLGQ-TVSYEEKESRIEDILLLLGL-------YNHDqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:PRK15079 123 EPLRTYHpKLSRQEVKDRVKAMMLKVGLlpnlinrYPHE------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 279 CTKVLELLKKLTSQ-GRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKLvpflqsvdlpcpmYHNP 348
Cdd:PRK15079 197 QAQVVNLLQQLQREmGLSLIFIAHD-LAVVKHISDRVLVMYLGHAVELGTYDEV-------------YHNP 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
72-320 |
1.29e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.07 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 72 EPSKQPPLEPVVEEEVHFDTDALNnLPAREPVdmeFKELSLTVKLGfnrgskeilhnvcgkfpgsQLIAIMGPSGAGKST 151
Cdd:COG4178 348 LPEAASRIETSEDGALALEDLTLR-TPDGRPL---LEDLSLSLKPG-------------------ERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 152 LLDALSGFKTTGvDGSIllngrrrDLPSFRRMsCYITQDDRLqPLLTvnenmhiaadlkLGQTVSY-----EEKESRIED 226
Cdd:COG4178 405 LLRAIAGLWPYG-SGRI-------ARPAGARV-LFLPQRPYL-PLGT------------LREALLYpataeAFSDAELRE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 227 ILLLLGL------YNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKlTSQGRTIICTI 300
Cdd:COG4178 463 ALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVG 541
|
250 260
....*....|....*....|
gi 442627138 301 HQPTakLFQIFDQVYVLSAG 320
Cdd:COG4178 542 HRST--LAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
137-356 |
1.85e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR----RDLPSFRRMSCYITQDDRLQPL-LTVNENMHIAAD-LK 210
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSGIDtgdfSKLQGIRKLVGIVFQNPETQFVgRTVEEDLAFGPEnLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 LGQTvsyeEKESRIEDILLLLGL--YNHDQTLTmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKK 288
Cdd:PRK13644 108 LPPI----EIRKRVDRALAEIGLekYRHRSPKT--LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 289 LTSQGRTIICTIHQptAKLFQIFDQVYVLSAGNCVYQGSTQKLV--PFLQSVDLPCPMyhnpadyIIELA 356
Cdd:PRK13644 182 LHEKGKTIVYITHN--LEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPS-------LIELA 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
104-331 |
2.13e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKELSLTVKLG--FNRGSkeiLHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF--KTTGV----DGSILLNGRRR 175
Cdd:PRK13634 2 DITFQKVEHRYQYKtpFERRA---LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlqPTSGTvtigERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 176 DLPSFRRMSCYITQDDRLQpLL--TVnenmhiAADLKLGQT---VSYEEKESRIEDILLLLGLynhDQTLTMR----LSG 246
Cdd:PRK13634 79 KLKPLRKKVGIVFQFPEHQ-LFeeTV------EKDICFGPMnfgVSEEDAKQKAREMIELVGL---PEELLARspfeLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 247 GQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL-TSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQ 325
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHS-MEDAARYADQIVVMHKGTVFLQ 227
|
....*.
gi 442627138 326 GSTQKL 331
Cdd:PRK13634 228 GTPREI 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
121-278 |
2.29e-13 |
|
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: 73.05 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKF-PGSQlIAIMGPSGAGKSTLLDALSGfkttgVDGSIllNGRRRDLPSFRRmsCYITQDDRLQPLLTV 199
Cdd:TIGR03719 16 PKKEILKDISLSFfPGAK-IGVLGLNGAGKSTLLRIMAG-----VDKDF--NGEARPQPGIKV--GYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NENM-----HIAADLKLGQTVSYE------------EKESRIEDILLLLGLYNHDQTLTM---------------RLSGG 247
Cdd:TIGR03719 86 RENVeegvaEIKDALDRFNEISAKyaepdadfdklaAEQAELQEIIDAADAWDLDSQLEIamdalrcppwdadvtKLSGG 165
|
170 180 190
....*....|....*....|....*....|.
gi 442627138 248 QKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
105-292 |
2.72e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.74 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGRR-RDLP--SFR 181
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS-GTLLFEGEDiSTLKpeIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 182 RMSCYITQddrlQPLL---TVNENMHIAADLKlGQTVsyeeKESRIEDILLLLGLYNHdqTLTMR---LSGGQKKRLSia 255
Cdd:PRK10247 81 QQVSYCAQ----TPTLfgdTVYDNLIFPWQIR-NQQP----DPAIFLDDLERFALPDT--ILTKNiaeLSGGEKQRIS-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442627138 256 meLINN----PTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ 292
Cdd:PRK10247 148 --LIRNlqfmPKVLLLDEITSALDESNKHNVNEIIHRYVRE 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
121-299 |
3.57e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLL-------DALSGFKttgVDGSILLNG-------------RRRDLPSF 180
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR---VEGKVTFHGknlyapdvdpvevRRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 181 RR-----MSCYitqdDRLQPLLTVNE---NMHIAADLKLGQTVSYEEkesrIEDILLLLGLynhdqtltmRLSGGQKKRL 252
Cdd:PRK14243 98 QKpnpfpKSIY----DNIAYGARINGykgDMDELVERSLRQAALWDE----VKDKLKQSGL---------SLSGGQQQRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 253 SIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICT 299
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
126-320 |
3.76e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPG-------------SQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGRRRDLPSFRRM----SCYIT 188
Cdd:PRK11288 7 FDGIGKTFPGvkalddisfdcraGQVHALMGENGAGKSTLLKILSGNYQPDA-GSILIDGQEMRFASTTAAlaagVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDDRLQPLLTVNENmhiaadLKLGQ------TVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNP 262
Cdd:PRK11288 86 QELHLVPEMTVAEN------LYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 263 TVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAG 320
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDG 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
106-331 |
4.85e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.45 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVKlgfNRGSKEILHNVCGKF-PGSqLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGrrRDLPSFRRm 183
Cdd:TIGR00958 480 EFQDVSFSYP---NRPDVPVLKGLTFTLhPGE-VVALVGPSGSGKSTVAALLQNLyQPTG--GQVLLDG--VPLVQYDH- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 184 sCYITQDDRL---QPLL---TVNENMHIAADLKLGQTVSYEEKESRIED-ILLLLGLYNHDQTLT-MRLSGGQKKRLSIA 255
Cdd:TIGR00958 551 -HYLHRQVALvgqEPVLfsgSVRENIAYGLTDTPDEEIMAAAKAANAHDfIMEFPNGYDTEVGEKgSQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 256 MELINNPTVMFLDEPTTGLDsSSCTKVLELLKKltSQGRTIICTIHQ-PTAklfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALD-AECEQLLQESRS--RASRTVLLIAHRlSTV---ERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
127-332 |
6.15e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 127 HNVCGKFPGS--------------QLIAIMGPSGAGKSTLLDALS-GFKTTGvdGSILLNG---RRRDLPSFRRMSCYIT 188
Cdd:PRK13657 338 DDVSFSYDNSrqgvedvsfeakpgQTVAIVGPTGAGKSTLINLLQrVFDPQS--GRILIDGtdiRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDdrlqPLLTvneNMHIAADLKLGQTVSYEEkESRI--------EDILLLLGLYNhdqtlTM------RLSGGQKKRLSI 254
Cdd:PRK13657 416 QD----AGLF---NRSIEDNIRVGRPDATDE-EMRAaaeraqahDFIERKPDGYD-----TVvgergrQLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 255 AMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHqptaKLFQI--FDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAH----RLSTVrnADRILVFDNGRVVESGSFDELV 557
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
139-301 |
8.16e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 69.06 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKSTLLDALSgFKTTGVDGSILLNGR----------------RRDLPSFRRMSCYITQDDRLQPLLTVNEN 202
Cdd:COG4598 37 ISIIGSSGSGKSTFLRCIN-LLETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGMVFQSFNLWSHMTVLEN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 203 MhIAADLK-LGqtVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTK 281
Cdd:COG4598 116 V-IEAPVHvLG--RPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGE 192
|
170 180
....*....|....*....|
gi 442627138 282 VLELLKKLTSQGRTIICTIH 301
Cdd:COG4598 193 VLKVMRDLAEEGRTMLVVTH 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
133-292 |
1.07e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGsQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRRRDLPSFRRMS------------CYITQD--DRL----- 193
Cdd:PRK11701 30 YPG-EVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprDGLrmqvs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 194 ------QPLLTVNENmH------IAADLkLGQTvsyEEKESRIEDillllglynhdqtLTMRLSGGQKKRLSIAMELINN 261
Cdd:PRK11701 108 aggnigERLMAVGAR-HygdiraTAGDW-LERV---EIDAARIDD-------------LPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190
....*....|....*....|....*....|.
gi 442627138 262 PTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ 292
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRE 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
140-317 |
1.24e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.59 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGFKTTGV-DGSILLNGRRRdlpSFRRMS-------CYITQDDRLQPLLTVNENMHIAADLKL 211
Cdd:NF040905 31 ALCGENGAGKSTLMKVLSGVYPHGSyEGEILFDGEVC---RFKDIRdsealgiVIIHQELALIPYLSIAENIFLGNERAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 GQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTS 291
Cdd:NF040905 108 RGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA 187
|
170 180
....*....|....*....|....*....
gi 442627138 292 QGRTIICTIHqptaKL---FQIFDQVYVL 317
Cdd:NF040905 188 QGITSIIISH----KLneiRRVADSITVL 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
102-321 |
2.06e-12 |
|
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: 66.67 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 102 PVDMEFKELSLTVKLGFNrgSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNG---RRRDLP 178
Cdd:cd03369 2 PEHGEIEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRF-LEAEEGKIEIDGidiSTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 179 SFRRMSCYITQDdrlqPLL---TVNENMHI---AADLKLGQTVSYEEkesriedillllGLYNhdqtltmrLSGGQKKRL 252
Cdd:cd03369 79 DLRSSLTIIPQD----PTLfsgTIRSNLDPfdeYSDEEIYGALRVSE------------GGLN--------LSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 253 SIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSqGRTIICTIHqptaKLFQI--FDQVYVLSAGN 321
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAH----RLRTIidYDKILVMDAGE 200
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
126-302 |
2.06e-12 |
|
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: 66.97 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRRRDLPSF-------RRMSCYITQddrlQPLL- 197
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQ----KPWLl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 --TVNENMHIAADLKLGQTVSYEEKESRIEDI-LLLLGlynhDQTLT----MRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:cd03290 92 naTVEENITFGSPFNKQRYKAVTDACSLQPDIdLLPFG----DQTEIgergINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....
gi 442627138 271 TTGLDSSSCTKVLE--LLKKLTSQGRTIICTIHQ 302
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
137-352 |
2.18e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.29 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGF--KTTG---VDGSILLNGRRRDLPSFRRMS-CYITQDDRLQPLLTVNENMHIAADLK 210
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLiePTRGqvlIDGVDIAKISDAELREVRRKKiAMVFQSFALMPHMTVLDNTAFGMELA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 lgqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT 290
Cdd:PRK10070 135 ---GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQ 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 291 SQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGStqklvpflqsvdlPCPMYHNPA-DYI 352
Cdd:PRK10070 212 AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT-------------PDEILNNPAnDYV 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
141-329 |
2.39e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 141 IMGPSGAGKSTLLDALSGF--KTTGVDGSILLNGRR------RDLPSFR--RMScYITQDdrlqPLLTVNENMHIAADL- 209
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGLlaANGRIGGSATFNGREilnlpeKELNKLRaeQIS-MIFQD----PMTSLNPYMRVGEQLm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 210 -------KLGQTVSYEEK----------ESRIEdilllLGLYNHDqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:PRK09473 122 evlmlhkGMSKAEAFEESvrmldavkmpEARKR-----MKMYPHE------FSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 273 GLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQ 329
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
106-320 |
2.96e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 66.73 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVKlgfNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGR---RRDLPSFRR 182
Cdd:cd03248 13 KFQNVTFAYP---TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-QGGQVLLDGKpisQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 183 MSCYITQddrlQPLL---TVNENmhIAADLklgQTVSYEE-----KESRIEDILLLL--GLYNHDQTLTMRLSGGQKKRL 252
Cdd:cd03248 89 KVSLVGQ----EPVLfarSLQDN--IAYGL---QSCSFECvkeaaQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 253 SIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKlTSQGRTIICTIHQptAKLFQIFDQVYVLSAG 320
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHR--LSTVERADQILVLDGG 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
122-332 |
3.41e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 122 SKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALS-GFKTTgvDGSILLNGR---RRDLPSFRRMSCYITQddrlQPLL 197
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVS--EGDIRFHDIpltKLQLDSWRSRLAVVSQ----TPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNEnmhIAADLKLGQ---TVSYEEKESRI----EDILLLLGLYnhdQTLT----MRLSGGQKKRLSIAMELINNPTVMF 266
Cdd:PRK10789 401 FSDT---VANNIALGRpdaTQQEIEHVARLasvhDDILRLPQGY---DTEVgergVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 267 LDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQPTAklFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSA--LTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
137-320 |
3.46e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGR----RRDLPSFRRMSCYITQDDR---LQPLLTVNENMHIAADL 209
Cdd:PRK09700 290 EILGFAGLVGSGRTELMNCLFGVDKR-AGGEIRLNGKdispRSPLDAVKKGMAYITESRRdngFFPNFSIAQNMAISRSL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 210 KLGQ-----TVSYEEKESRI-EDILLLLGLYNH--DQTLTmRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTK 281
Cdd:PRK09700 369 KDGGykgamGLFHEVDEQRTaENQRELLALKCHsvNQNIT-ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE 447
|
170 180 190
....*....|....*....|....*....|....*....
gi 442627138 282 VLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVLSAG 320
Cdd:PRK09700 448 IYKVMRQLADDGKVIL-MVSSELPEIITVCDRIAVFCEG 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
126-320 |
3.59e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGV-DGSILLNGRR------RDlpSFRRMSCYITQDDRLQPLLT 198
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyEGEIIFEGEElqasniRD--TERAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 199 VNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:PRK13549 99 VLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442627138 279 CTKVLELLKKLTSQGRTIICTIHqptaKL---FQIFDQVYVLSAG 320
Cdd:PRK13549 179 TAVLLDIIRDLKAHGIACIYISH----KLnevKAISDTICVIRDG 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
121-275 |
5.11e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSI-LLNGRRRDlPSFRRMSC----YITQD--DRL 193
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQ-QGRVeVLGGDMAD-ARHRRAVCpriaYMPQGlgKNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 194 QPLLTVNENMHIAADLkLGQtvSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:NF033858 90 YPTLSVFENLDFFGRL-FGQ--DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
..
gi 442627138 274 LD 275
Cdd:NF033858 167 VD 168
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
106-301 |
5.42e-12 |
|
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: 64.01 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 106 EFKELSLTVklgfnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRRRdlpsfrrmSC 185
Cdd:cd03221 2 ELENLSKTY------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 186 YITQddrlqplltvnenmhiaadlklgqtvsyeekesriedillllglynhdqtltmrLSGGQKKRLSIAMELINNPTVM 265
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*.
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLTsqgRTIICTIH 301
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYP---GTVILVSH 125
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
114-302 |
6.11e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 114 VKLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR--RRDLPSFRRMSCYITQDD 191
Cdd:PRK13540 5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILFERQsiKKDLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENMHIaaDLKLGQTvsyeekESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK13540 84 GINPYLTLRENCLY--DIHFSPG------AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
140-297 |
6.23e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.51 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNGRRRDLPSFRR-------MscyITQDDRLQPLLTVNENMHIAADLKL 211
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLyQPDS--GEILIDGKPVRIRSPRDaialgigM---VHQHFMLVPNLTVAENIVLGLEPTK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 212 GQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLdssscT-----KVLELL 286
Cdd:COG3845 110 GGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL-----TpqeadELFEIL 184
|
170
....*....|.
gi 442627138 287 KKLTSQGRTII 297
Cdd:COG3845 185 RRLAAEGKSII 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
139-331 |
6.27e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKS-TLLDALSGFKTTGV---DGSILLNGR---RRDLPSFR-----RMScYITQDD--RLQPLLTVNENMh 204
Cdd:PRK15134 38 LALVGESGSGKSvTALSILRLLPSPPVvypSGDIRFHGEsllHASEQTLRgvrgnKIA-MIFQEPmvSLNPLHTLEKQL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 205 iAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLT---MRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTK 281
Cdd:PRK15134 116 -YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQ 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442627138 282 VLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK15134 195 ILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
121-302 |
6.49e-12 |
|
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: 68.31 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGV-DGSILLNGRRRDLPSFRRMS----CYITQDDRLQP 195
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwDGEIYWSGSPLKASNIRDTEragiVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 196 LLTVNENMHIAADLKL-GQTVSYEEKESRIEDILLLLGLYNHDQTL-TMRLSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:TIGR02633 92 ELSVAENIFLGNEITLpGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180
....*....|....*....|....*....
gi 442627138 274 LDSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
137-331 |
8.19e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.88 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTGVD---GSILLNGRRRDLPSFR-RMSCYITQDDR--LQPLLTvnenMHIAAdLK 210
Cdd:PRK10418 30 RVLALVGGSGSGKSLTCAAALGILPAGVRqtaGRVLLDGKPVAPCALRgRKIATIMQNPRsaFNPLHT----MHTHA-RE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 LGQTVSYEEKESRIEDILLLLGLYNHDQTLTM---RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLK 287
Cdd:PRK10418 105 TCLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 288 KLT-SQGRTIICTIHQ--PTAKLfqiFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK10418 185 SIVqKRALGMLLVTHDmgVVARL---ADDVAVMSHGRIVEQGDVETL 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
140-289 |
1.00e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.68 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGR------RRDLPSFRRMSCYITQD--DRLQPLLTVNENmhIAADLK 210
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRlEEPTS--GEILFDGQditglsGRELRPLRRRMQMVFQDpyASLNPRMTVGDI--IAEPLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 LGQTVSYEEKESRIEDILLLLGL-------YNHDqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVL 283
Cdd:COG4608 124 IHGLASKAERRERVAELLELVGLrpehadrYPHE------FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVL 197
|
....*.
gi 442627138 284 ELLKKL 289
Cdd:COG4608 198 NLLEDL 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
125-320 |
1.49e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 67.47 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 125 ILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF-KTTGvdGSILLNG---RRRDLPSFRRMSCYITQDdrlqPLL--- 197
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwPPTA--GSVRLDGadlSQWDREELGRHIGYLPQD----VELfdg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENmhIAadlKLGQtVSYEE-----KESRIEDILLLL--GlYNhdqtlT------MRLSGGQKKRLSIAMELINNPTV 264
Cdd:COG4618 421 TIAEN--IA---RFGD-ADPEKvvaaaKLAGVHEMILRLpdG-YD-----TrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 265 MFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTakLFQIFDQVYVLSAG 320
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDG 542
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
120-331 |
1.96e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPSFR--RMSCYITQDDrlqPLL 197
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEIRLDGRPLSSLSHSvlRQGVAMVQQD---PVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNEnmhIAADLKLGQTVSYEEKESRIEDILLLL-------GLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEP 270
Cdd:PRK10790 427 LADT---FLANVTLGRDISEEQVWQALETVQLAElarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 271 TTGLDS---SSCTKVLELLKKLTsqgrTIICTIHqptaKLFQIF--DQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK10790 504 TANIDSgteQAIQQALAAVREHT----TLVVIAH----RLSTIVeaDTILVLHRGQAVEQGTHQQL 561
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
137-332 |
2.20e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKT-TGvdGSILLNGRR--RDLPSFRRMscyIT----QDDRLQPLLTVNENMHIAADL 209
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGILVpTS--GEVRVLGYVpfKRRKEFARR---IGvvfgQRSQLWWDLPAIDSFRLLKAI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 210 klgQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKL 289
Cdd:COG4586 124 ---YRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627138 290 -TSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:COG4586 201 nRERGTTILLTSHD-MDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
105-346 |
2.20e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVKlgfnRGSKEILHNVCGKFPGSQLIAIMGPSGAGKST---------LLDALSGFKTTgVDGSILLNGRRR 175
Cdd:PRK13640 6 VEFKHVSFTYP----DSKKPALNDISFSIPRGSWTALIGHNGSGKSTisklingllLPDDNPNSKIT-VDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 176 DLpsfrrmscyitqDDRLQPLLTVNENMHIAA----DLKLG---QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQ 248
Cdd:PRK13640 81 DI------------REKVGIVFQNPDNQFVGAtvgdDVAFGlenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 249 KKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ-GRTIICTIHQPTAKlfQIFDQVYVLSAGNCVYQGS 327
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGS 226
|
250 260
....*....|....*....|..
gi 442627138 328 TQKLVP---FLQSVDLPCPMYH 346
Cdd:PRK13640 227 PVEIFSkveMLKEIGLDIPFVY 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
134-318 |
2.82e-11 |
|
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: 62.56 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 134 PGSQLIaIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLpsfrrmscYITQddrlQPLLTvnenmhiaaDLKLGQ 213
Cdd:cd03223 26 PGDRLL-ITGPSGTGKSSLFRALAGLWPWG-SGRIGMPEGEDLL--------FLPQ----RPYLP---------LGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 214 TVSYeekesriedillllglynhdqTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLtsqG 293
Cdd:cd03223 83 QLIY---------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---G 138
|
170 180
....*....|....*....|....*
gi 442627138 294 RTIICTIHQPTakLFQIFDQVYVLS 318
Cdd:cd03223 139 ITVISVGHRPS--LWKFHDRVLDLD 161
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
70-332 |
3.21e-11 |
|
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: 66.39 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 70 GNEPSKQPPLEPVVEEEVHFDTDalnNLPAREPVDMEFKELSlTVKLGFNRGskEILhnvcgkfpgsqliAIMGPSGAGK 149
Cdd:TIGR02633 239 GREITSLYPHEPHEIGDVILEAR---NLTCWDVINPHRKRVD-DVSFSLRRG--EIL-------------GVAGLVGAGR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 150 STLLDALSGFKTTGVDGSILLNGR----RRDLPSFRRMSCYITQDDRLQ---PLLTVNENMHIAA-DLKLGQTVSYEEKE 221
Cdd:TIGR02633 300 TELVQALFGAYPGKFEGNVFINGKpvdiRNPAQAIRAGIAMVPEDRKRHgivPILGVGKNITLSVlKSFCFKMRIDAAAE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 222 SRI--EDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIIcT 299
Cdd:TIGR02633 380 LQIigSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII-V 458
|
250 260 270
....*....|....*....|....*....|....*..
gi 442627138 300 IHQPTAKLFQIFDQVYVLSAG----NCVYQGSTQKLV 332
Cdd:TIGR02633 459 VSSELAEVLGLSDRVLVIGEGklkgDFVNHALTQEQV 495
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
126-327 |
3.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGF------KTTGVDGSILLNGRR-RDLPSFRRMSCYITQDDRLQPLLT 198
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIVGDYAIPANLKKiKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 199 VnenmhIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEPTTGL 274
Cdd:PRK13645 107 T-----IEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 275 DSSSCTKVLELLKKLT-SQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGS 327
Cdd:PRK13645 182 DPKGEEDFINLFERLNkEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGS 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
139-331 |
4.28e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGR------RRDLPSFRRMSCYITQD--DRLQPLLTVN----ENMHIA 206
Cdd:PRK11308 44 LAVVGESGCGKSTLARLLTMIETP-TGGELYYQGQdllkadPEAQKLLRQKIQIVFQNpyGSLNPRKKVGqileEPLLIN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 207 ADLklgqtvSYEEKESRIEDILLLLGL-------YNHdqtltMrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:PRK11308 123 TSL------SAAERREKALAMMAKVGLrpehydrYPH-----M-FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442627138 280 TKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
118-326 |
4.76e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 118 FNRGSKEI--LHNVC-GKFPGSQLiAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRD------LPSFRRMSCYIT 188
Cdd:PRK10261 330 LNRVTREVhaVEKVSfDLWPGETL-SLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIDtlspgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QDD--RLQPLLTVNENmhIAADLKLGQTVSYEEKESRIEDILLLLGLY-NHDQTLTMRLSGGQKKRLSIAMELINNPTVM 265
Cdd:PRK10261 408 QDPyaSLDPRQTVGDS--IMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
126-331 |
6.30e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.69 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLL---DAL---SGFKTTGVDGSILLNGRRRDLPSFRRMSCYITQDDRLQplltV 199
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALlkpSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQ----L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NENMhIAADLKLG-QTVSYEEKESRIEDILLLLGLYNHDQTLT---MRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:PRK13641 99 FENT-VLKDVEFGpKNFGFSEDEAKEKALKWLKKVGLSEDLISkspFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 276 SSSCTKVLELLKKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
98-287 |
9.04e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 98 PAREPVDMEFKELS------LTVK-LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILL 170
Cdd:COG0488 296 RRDKTVEIRFPPPErlgkkvLELEgLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVKL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 171 N-----GrrrdlpsfrrmscYITQD-DRLQPLLTVNENMHIAADlklgqtvsyEEKESRIEDILLLLGLYNHDQ-TLTMR 243
Cdd:COG0488 375 GetvkiG-------------YFDQHqEELDPDKTVLDELRDGAP---------GGTEQEVRGYLGRFLFSGDDAfKPVGV 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627138 244 LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLK 287
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
126-304 |
1.08e-10 |
|
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: 60.80 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLdaLSGFKTTGVDGSIllngrrRDLPSFRRMScyITQDDRLQPLLTVNENMhi 205
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLI------SFLPKFSRNK--LIFIDQLQFLIDVGLGY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 aadLKLGQTVSyeekesriedillllglynhdqtltmRLSGGQKKRLSIAMELINNP--TVMFLDEPTTGLDSSSCTKVL 283
Cdd:cd03238 79 ---LTLGQKLS--------------------------TLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|.
gi 442627138 284 ELLKKLTSQGRTIICTIHQPT 304
Cdd:cd03238 130 EVIKGLIDLGNTVILIEHNLD 150
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
107-297 |
1.70e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 107 FKELSLTVKlgfnRGskEILhnvcgkfpgsqliAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRRDLPSFRRMS-- 184
Cdd:COG1129 268 VRDVSFSVR----AG--EIL-------------GIAGLVGAGRTELARALFGA-DPADSGEIRLDGKPVRIRSPRDAIra 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 185 --CYITQDDRLQ---PLLTVNENMHIAADLKLGQT--VSYEEKESRIEDILLLLGL-YNHDQTLTMRLSGG--QKkrLSI 254
Cdd:COG1129 328 giAYVPEDRKGEglvLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGnqQK--VVL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627138 255 AMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTII 297
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
122-343 |
1.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 122 SKEILHNVCGKFPGSQLIAIMGPSGAGKSTL---LDALsgfkTTGVDGSILLNG----RRRDLPSFRRMSCYITQDDRLQ 194
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL----LIPSEGKVYVDGldtsDEENLWDIRNKAGMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENmhiaaDLKLGQT---VSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK13633 98 IVATIVEE-----DVAFGPEnlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQ-GRTIICTIH--QPTAKLfqifDQVYVLSAGNCVYQGSTQKL---VPFLQSVDLPCP 343
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKyGITIILITHymEEAVEA----DRIIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
479-687 |
2.29e-10 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 60.60 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 479 MTTMMLTVLTFPMDIsilIKEHFNRWY--------SLKAYYTAMTLVDLPISIISCFFFTVIVYLWSYQPMEWIRFFMFF 550
Cdd:COG0842 12 MSLLFTALMLTALSI---AREREQGTLerllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 551 SISLLTVFVGHSFGLMIGAWF-DVVNGTFLAPVLTIPMMMFAGFGVTLRDLPSYLRWGSHISYLRYGLEGFISAIYGldr 629
Cdd:COG0842 89 LVLLLFALAFSGLGLLISTLArSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG--- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 630 gtlaceeapychyrypkkfleeiTMRGDQFWNDVIALGVMILVFRFVSYVVLKAKIKS 687
Cdd:COG0842 166 -----------------------GAGLADVWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
121-321 |
2.72e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGR------RRDlpsfRRMScYITQDDRLQ 194
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-SGHIRFHGTdvsrlhARD----RKVG-FVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PLLTVNENmhIAADLKL---GQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK10851 87 RHMTVFDN--IAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQGR--TIICTIHQPTAklFQIFDQVYVLSAGN 321
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKftSVFVTHDQEEA--MEVADRVVVMSQGN 214
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-315 |
3.30e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 59.30 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGSQLIAIMGPSGAGKSTLLDALsgfkttgvdgsillngrrrdlpsfrrmsCYItqddrlqpLLTVNENMHIAADLKLG 212
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAI----------------------------GLA--------LGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 213 QTVSYEEkesrIEDILLLlglynhdqtltMRLSGGQKKRLSIAMEL----INNPTVMFLDEPTTGLDSSSCTKVLELLKK 288
Cdd:cd03227 62 CIVAAVS----AELIFTR-----------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180
....*....|....*....|....*..
gi 442627138 289 LTSQGRTIICTIHQPtaKLFQIFDQVY 315
Cdd:cd03227 127 HLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
105-327 |
4.60e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 105 MEFKELSLTVklgfnrGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG---FKTTGvdGSILLNGRRrdlpsfr 181
Cdd:CHL00131 8 LEIKNLHASV------NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKILE--GDILFKGES------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 182 rmSCYITQDDRLQ-------------PLLTVNENMHIAADLKLgqtVSYEEKE----SRIEDILLLLGLYNHDQTLTMR- 243
Cdd:CHL00131 73 --ILDLEPEERAHlgiflafqypieiPGVSNADFLRLAYNSKR---KFQGLPEldplEFLEIINEKLKLVGMDPSFLSRn 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 244 ----LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSA 319
Cdd:CHL00131 148 vnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQN 227
|
....*...
gi 442627138 320 GNCVYQGS 327
Cdd:CHL00131 228 GKIIKTGD 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
126-340 |
4.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRR---RDLPSFRRMSCYITQDDRLQPL-LTVNE 201
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELltaENVWNLRRKIGMVFQNPDNQFVgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 202 NMHIAADlklGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTK 281
Cdd:PRK13642 102 DVAFGME---NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 282 VLELLKKLTSQGRTIICTIHQPTAKLFQiFDQVYVLSAGNCVYQGSTQKLvpFLQSVDL 340
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL--FATSEDM 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
121-275 |
4.93e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRR--------RDLPsfrrMscyITQDDR 192
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERI-TSGEIWIGGRVvnelepadRDIA----M---VFQNYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 193 LQPLLTVNENMhiAADLKLgQTVSYEEKESRIEDILLLLGLynhDQTLTMR---LSGGQKKRlsIAM--ELINNPTVMFL 267
Cdd:PRK11650 87 LYPHMSVRENM--AYGLKI-RGMPKAEIEERVAEAARILEL---EPLLDRKpreLSGGQRQR--VAMgrAIVREPAVFLF 158
|
....*...
gi 442627138 268 DEPTTGLD 275
Cdd:PRK11650 159 DEPLSNLD 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
111-332 |
5.37e-10 |
|
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: 63.04 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 111 SLTVKLG---FNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRRRDLPSfrrmSCYI 187
Cdd:TIGR00957 636 SITVHNAtftWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA-EMDKVEGHVHMKGSVAYVPQ----QAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 188 tQDDRLQplltvnENMHIAADLKLGQTVSYEEKESRIEDILLLLGlynHDQTLT----MRLSGGQKKRLSIAMELINNPT 263
Cdd:TIGR00957 711 -QNDSLR------ENILFGKALNEKYYQQVLEACALLPDLEILPS---GDRTEIgekgVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 264 VMFLDEPTTGLDSSSCTKVLE-------LLKkltsqGRTIICTIHQpTAKLFQIfDQVYVLSAGNCVYQGSTQKLV 332
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEhvigpegVLK-----NKTRILVTHG-ISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
104-332 |
6.82e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.96 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 104 DMEFKELSltvklgFNRGSKEI--LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTtgVD-GSILLNG---RRRDL 177
Cdd:PRK11176 341 DIEFRNVT------FTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD--IDeGEILLDGhdlRDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 178 PSFRRMSCYITQddrlqplltvneNMHIAADlKLGQTVSY--EEKESRiEDIL------LLLGLYNH-DQTL-TM----- 242
Cdd:PRK11176 413 ASLRNQVALVSQ------------NVHLFND-TIANNIAYarTEQYSR-EQIEeaarmaYAMDFINKmDNGLdTVigeng 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 243 -RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS---CTKVLELLKKltsqGRTIICTIHqptaKLFQI--FDQVYV 316
Cdd:PRK11176 479 vLLSGGQRQRIAIARALLRDSPILILDEATSALDTESeraIQAALDELQK----NRTSLVIAH----RLSTIekADEILV 550
|
250
....*....|....*.
gi 442627138 317 LSAGNCVYQGSTQKLV 332
Cdd:PRK11176 551 VEDGEIVERGTHAELL 566
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
118-326 |
1.13e-09 |
|
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: 59.08 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 118 FNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSgfkttGVD----GSILLNGrrrdlpsfrRMSCYITQDDRL 193
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GIYppdsGTVTVRG---------RVSSLLGLGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 194 QPLLTVNENMHIAADLkLGqtVSYEEKESRIEDILLLLGLYNHdQTLTMR-LSGGQKKRL--SIAMELinNPTVMFLDEP 270
Cdd:cd03220 96 NPELTGRENIYLNGRL-LG--LSRKEIDEKIDEIIEFSELGDF-IDLPVKtYSSGMKARLafAIATAL--EPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 271 TTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAkLFQIFDQVYVLSAGNCVYQG 326
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
133-320 |
1.30e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGsQLIAIMGPSGAGKSTLLDALSGFKTTGVdGSILLNGRRRDLPSFRRMS----CYITQDDRLQPLLTVNENMHIAAD 208
Cdd:PRK10762 28 YPG-RVMALVGENGAGKSTMMKVLTGIYTRDA-GSILYLGKEVTFNGPKSSQeagiGIIHQELNLIPQLTIAENIFLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 209 L--KLGqTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELL 286
Cdd:PRK10762 106 FvnRFG-RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVI 184
|
170 180 190
....*....|....*....|....*....|....
gi 442627138 287 KKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAG 320
Cdd:PRK10762 185 RELKSQGRGIVYISHR-LKEIFEICDDVTVFRDG 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
215-331 |
1.74e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 215 VSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGR 294
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|....*..
gi 442627138 295 TIICTIhQPTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:NF000106 196 TVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
139-301 |
1.79e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRRRDLPS---FRRMSCYITQDDRLQPLLTVNENmhiaaDLKLG--- 212
Cdd:PRK13635 36 VAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMVLSEETvwdVRRQVGMVFQNPDNQFVGATVQD-----DVAFGlen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 213 QTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQ 292
Cdd:PRK13635 110 IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQ 189
|
170
....*....|
gi 442627138 293 GR-TIICTIH 301
Cdd:PRK13635 190 KGiTVLSITH 199
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
138-301 |
1.86e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.00 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 138 LIAIMGPSGAGKSTLLDALSgFKTTGvDGSILLNGRRRDlPSFRRMSCYITQDDrLQPLLTVNENMHIAADLKLGQTVSY 217
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK-YALTG-ELPPNSKGGAHD-PKLIREGEVRAQVK-LAFENANGKKYTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 218 eekeSRIEDILLLLglynhdqtLTM--RLSGGQKK------RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVL-ELLKK 288
Cdd:cd03240 100 ----CHQGESNWPL--------LDMrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEE 167
|
170
....*....|....
gi 442627138 289 LTSQG-RTIICTIH 301
Cdd:cd03240 168 RKSQKnFQLIVITH 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
121-341 |
2.32e-09 |
|
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: 60.20 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVD-GSILLN-GR-----RRDLPSFRRMSC-------- 185
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTsGRIIYHvALcekcgYVERPSKVGEPCpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 186 -----YITQDDRLQPLL------------------TVNENMhiaadLKLGQTVSYEEKES--RIEDILLLLGLYNHDQTL 240
Cdd:TIGR03269 91 peevdFWNLSDKLRRRIrkriaimlqrtfalygddTVLDNV-----LEALEEIGYEGKEAvgRAVDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 241 TMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQPTAkLFQIFDQVYVLSA 319
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEV-IEDLSDKAIWLEN 244
|
250 260
....*....|....*....|...
gi 442627138 320 GNCVYQGSTQKLVP-FLQSVDLP 341
Cdd:TIGR03269 245 GEIKEEGTPDEVVAvFMEGVSEV 267
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
137-326 |
2.61e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSG---FKTTGVDGSILLNGRrrDL----PSFRRM-----SCYITQD--DRLQPLLTVNen 202
Cdd:PRK11022 34 EVVGIVGESGSGKSVSSLAIMGlidYPGRVMAEKLEFNGQ--DLqrisEKERRNlvgaeVAMIFQDpmTSLNPCYTVG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 203 MHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTM---RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSC 279
Cdd:PRK11022 110 FQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442627138 280 TKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVYQG 326
Cdd:PRK11022 190 AQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
137-331 |
3.73e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.58 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFktTGVD-GSILLNGRRRDLPSFRRMScYITQDDRLQPLLTVNENMHIAADLKlGqtV 215
Cdd:COG4152 28 EIFGLLGPNGAGKTTTIRIILGI--LAPDsGEVLWDGEPLDPEDRRRIG-YLPEERGLYPKMKVGEQLVYLARLK-G--L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 216 SYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRT 295
Cdd:COG4152 102 SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 442627138 296 IICTIHQ-PTAKlfQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:COG4152 182 VIFSSHQmELVE--ELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
126-297 |
3.86e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGR----RRDLPSFRRMSCYITQD---DRLQPLL 197
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGaLPRTS--GYVTLDGHevvtRSPQDGLANGIVYISEDrkrDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENMHIAADLKL----GQTVSYEEKESrIEDILLLLGLY--NHDQTLTMrLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:PRK10762 346 SVKENMSLTALRYFsragGSLKHADEQQA-VSDFIRLFNIKtpSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180
....*....|....*....|....*.
gi 442627138 272 TGLDSSSCTKVLELLKKLTSQGRTII 297
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
119-332 |
5.61e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 119 NRGSKeILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVDGSILLNGR----RRDLPSFRRMSCYITQD---D 191
Cdd:PRK13549 272 NPHIK-RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKpvkiRNPQQAIAQGIAMVPEDrkrD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENMHIAA--DLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTM-RLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:PRK13549 351 GIVPVMGVGKNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 269 EPTTGLDSSSCTKVLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVLS----AGNCVYQGSTQKLV 332
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQGVAII-VISSELPEVLGLSDRVLVMHegklKGDLINHNLTQEQV 497
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
116-303 |
5.63e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 116 LGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLL----DALSGFKTTGVDgSILLNGRRRDLPSFrrmscyitqdD 191
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLrllaGALKGTPVAGCV-DVPDNQFGREASLI----------D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 192 RLQPLLTVNENMHIAADLKLGqtvsyeekesrieDILLLLGLYNHdqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPT 271
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLS-------------DAVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 442627138 272 TGLDSSSCT----KVLELLKKLtsqGRTIICTIHQP 303
Cdd:COG2401 165 SHLDRQTAKrvarNLQKLARRA---GITLVVATHHY 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
121-278 |
6.18e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKF-PGSQlIAIMGPSGAGKSTLLDALSgfkttGVDGSIllNGRRRDLPSFRRmsCYITQDDRLQPLLTV 199
Cdd:PRK11819 18 PKKQILKDISLSFfPGAK-IGVLGLNGAGKSTLLRIMA-----GVDKEF--EGEARPAPGIKV--GYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 200 NENM-----HIAADLKLGQTVSYE------------EKESRIEDILLLLGLYNHDQTLTM---------------RLSGG 247
Cdd:PRK11819 88 RENVeegvaEVKAALDRFNEIYAAyaepdadfdalaAEQGELQEIIDAADAWDLDSQLEIamdalrcppwdakvtKLSGG 167
|
170 180 190
....*....|....*....|....*....|.
gi 442627138 248 QKKRLSIAMELINNPTVMFLDEPTTGLDSSS 278
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
125-347 |
9.04e-09 |
|
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: 59.15 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 125 ILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRrrdlPSFRRMSCYITQDdrlqpllTVNENMH 204
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-ELEPSEGKIKHSGR----ISFSPQTSWIMPG-------TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 205 IAadlklgqtVSYEE-------KESRIEDILLLLGlyNHDQTLTMR----LSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:TIGR01271 509 FG--------LSYDEyrytsviKACQLEEDIALFP--EKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 274 LDSSSCTKVLE--LLKKLTSQGRTIIctihqpTAKL--FQIFDQVYVLSAGNCVYQGS---TQKLVPFLQSVDLPCPMYH 346
Cdd:TIGR01271 579 LDVVTEKEIFEscLCKLMSNKTRILV------TSKLehLKKADKILLLHEGVCYFYGTfseLQAKRPDFSSLLLGLEAFD 652
|
.
gi 442627138 347 N 347
Cdd:TIGR01271 653 N 653
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-302 |
2.77e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.31 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLL----------------------DALSGF----KTTGVDGSILlnGRR-RDLP 178
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkkeqpgnhDRIEGLehidKVIVIDQSPI--GRTpRSNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 179 --------SFRRMSCYITQDDRLQP-LLTV---NENMHIAADLKLGQTVSYEEKESRIEDILLLL---GL-YNH-DQTLT 241
Cdd:cd03271 89 atytgvfdEIRELFCEVCKGKRYNReTLEVrykGKSIADVLDMTVEEALEFFENIPKIARKLQTLcdvGLgYIKlGQPAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 242 MrLSGGQKKRLSIAMELIN---NPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQ 302
Cdd:cd03271 169 T-LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
244-356 |
4.34e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 56.76 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 244 LSGGQKKRLSIAMELIN---NPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQptAKLFQIFDQVYVL--- 317
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN--MHVVKVADYVLELgpe 887
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627138 318 --SAGNCVYQGSTQK------------LVPFL-QSVDLP-----CPMYHNPADYIIELA 356
Cdd:PRK00635 888 ggNLGGYLLASCSPEelihlhtptakaLRPYLsSPQELPylpdpSPKPPVPADITIKNA 946
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
122-331 |
5.09e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 122 SKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVDGSILLNGRRRDLPSFRrmscYITQddrlqplLTVNE 201
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVS----WIFN-------ATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 202 NMHIAADLKLGQTVSYEEKESRIEDILLLLGlynHDQTLT----MRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSS 277
Cdd:PLN03232 698 NILFGSDFESERYWRAIDVTALQHDLDLLPG---RDLTEIgergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442627138 278 SCTKVLELLKKLTSQGRTIICTIHQptAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
115-275 |
5.10e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 115 KLGFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFkTTGVDGSILLNGRRRdlpsfrrmSCYITQDDRLQ 194
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL-VAPDEGVIKRNGKLR--------IGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 195 PL--LTVNENMHIAADLKLGqtvsyeekesrieDILLLLGLYN----HDQTLtMRLSGGQKKRLSIAMELINNPTVMFLD 268
Cdd:PRK09544 80 TTlpLTVNRFLRLRPGTKKE-------------DILPALKRVQaghlIDAPM-QKLSGGETQRVLLARALLNRPQLLVLD 145
|
....*..
gi 442627138 269 EPTTGLD 275
Cdd:PRK09544 146 EPTQGVD 152
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
139-301 |
5.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.74 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 139 IAIMGPSGAGKST-------LLDALSGfkTTGVDGSILLNGRRRDLpsfRRMSCYITQDDRLQPL-LTVNENmhIAADLK 210
Cdd:PRK13650 36 LSIIGHNGSGKSTtvrlidgLLEAESG--QIIIDGDLLTEENVWDI---RHKIGMVFQNPDNQFVgATVEDD--VAFGLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 lGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT 290
Cdd:PRK13650 109 -NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIR 187
|
170
....*....|..
gi 442627138 291 SQ-GRTIICTIH 301
Cdd:PRK13650 188 DDyQMTVISITH 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
133-331 |
1.29e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGsQLIAIMGPSGAGKSTLLDALSGFKTTGvDGSILLNGRR--RDLPSF-RRMSCY-ITQDDRLQPLLTVNENmhIAAD 208
Cdd:PRK15439 35 HAG-EVHALLGGNGAGKSTLMKIIAGIVPPD-SGTLEIGGNPcaRLTPAKaHQLGIYlVPQEPLLFPNLSVKEN--ILFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 209 LKLGQtvsyeEKESRIEDILLLLG--LYNHDQTLTMRLSGGQkkRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELL 286
Cdd:PRK15439 111 LPKRQ-----ASMQKMKQLLAALGcqLDLDSSAGSLEVADRQ--IVEILRGLMRDSRILILDEPTASLTPAETERLFSRI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442627138 287 KKLTSQGRTIICTIHQpTAKLFQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:PRK15439 184 RELLAQGVGIVFISHK-LPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-303 |
1.50e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 126 LHNVCGKFPGSQLIAIMGPSGAGKSTLldalsGFKTtgvdgsILLNGRRRDLPSFrrmSCYITQddrLQPLLTVNENMHI 205
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDT------IYAEGQRRYVESL---SAYARQ---FLGQMDKPDVDSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 AAdlkLGQTVSYEEKESR------------IEDILLLL----GLYNHDQTL-------------TMRLSGGQKKRLSIAM 256
Cdd:cd03270 74 EG---LSPAIAIDQKTTSrnprstvgtvteIYDYLRLLfarvGIRERLGFLvdvglgyltlsrsAPTLSGGEAQRIRLAT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442627138 257 ELINNPT-VMF-LDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQP 303
Cdd:cd03270 151 QIGSGLTgVLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
122-327 |
1.50e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 122 SKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDAL-SGFKTTgvDGSILLngrrrdlpsfRRMSCYITQddrlQPLL--- 197
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlSQFEIS--EGRVWA----------ERSIAYVPQ----QAWImna 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 198 TVNENMHI-----AADLKLGQTVSYEEKESRiediLLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:PTZ00243 736 TVRGNILFfdeedAARLADAVRVSQLEADLA----QLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 273 GLDSSSCTKVLE--LLKKLtsQGRTIICTIHQ----PTAklfqifDQVYVLSAGNCVYQGS 327
Cdd:PTZ00243 812 ALDAHVGERVVEecFLGAL--AGKTRVLATHQvhvvPRA------DYVVALGDGRVEFSGS 864
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
137-301 |
2.24e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTGVdgsillnGRRRDLPS-------FR--RMSCYITQ--DDRLQPLLTVNENMHI 205
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNL-------GKFDDPPDwdeildeFRgsELQNYFTKllEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 --AADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVL 283
Cdd:cd03236 100 pkAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170
....*....|....*...
gi 442627138 284 ELLKKLTSQGRTIICTIH 301
Cdd:cd03236 180 RLIRELAEDDNYVLVVEH 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
86-297 |
2.30e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 86 EVHFDTDALNNLPAREPVdmefkelSLTVKLGfnrgskEILhnvcGKFpgsqliaimGPSGAGKSTLLDALSGfKTTGVD 165
Cdd:PRK11288 255 EVRLRLDGLKGPGLREPI-------SFSVRAG------EIV----GLF---------GLVGAGRSELMKLLYG-ATRRTA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 166 GSILLNGRRRDLPSFRR------MSCyitQDDRLQ----PLLTVNENMHIAA---DLKLGQTVSyEEKESRIED--ILLL 230
Cdd:PRK11288 308 GQVYLDGKPIDIRSPRDairagiMLC---PEDRKAegiiPVHSVADNINISArrhHLRAGCLIN-NRWEAENADrfIRSL 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 231 LGLYNHDQTLTMRLSGG--QKKRLS--IAMELinnpTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTII 297
Cdd:PRK11288 384 NIKTPSREQLIMNLSGGnqQKAILGrwLSEDM----KVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVL 450
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
131-276 |
3.22e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.03 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 131 GKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGVDGSILLngrrrDLPSFRRMSCYITQDDRLQPLLtvnenMHIAADL 209
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGvLKPDEGDIEIEL-----DTVSYKPQYIKADYEGTVRDLL-----SSITKDF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 210 klgQTVSYEEKEsrIEDILLLLGLYnhDQTLTmRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDS 276
Cdd:cd03237 90 ---YTHPYFKTE--IAKPLQIEQIL--DREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-295 |
6.97e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 121 GSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTGVDGSILLNGRRR-------DLpsfRRMSCYIT----Q 189
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgsgetiwDI---KKHIGYVSsslhL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 DDRLQpllTVNENMHIAA---DLKLGQTVSyEEKESRIEDILLLLGLYNHDQTLTMR-LSGGQKKRLSIAMELINNPTVM 265
Cdd:PRK10938 348 DYRVS---TSVRNVILSGffdSIGIYQAVS-DRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190
....*....|....*....|....*....|
gi 442627138 266 FLDEPTTGLDSSSCTKVLELLKKLTSQGRT 295
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVDVLISEGET 453
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
110-289 |
7.08e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.39 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 110 LSLTVKlGFN--RGSKEIlhnvcgKFpGSQLIAIMGPSGAGKSTLLDAL--------------------SGFKTTGVDGS 167
Cdd:COG0419 3 LRLRLE-NFRsyRDTETI------DF-DDGLNLIVGPNGAGKSTILEAIryalygkarsrsklrsdlinVGSEEASVELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 168 ILLNGRR----RDLPSFRRMsCYITQDDR---LQPLL------TVNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLY 234
Cdd:COG0419 75 FEHGGKRyrieRRQGEFAEF-LEAKPSERkeaLKRLLgleiyeELKERLKELEEALESALEELAELQKLKQEILAQLSGL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 235 NHDQTltmrLSGGQKKRLSIAMELinnptVMFLDepTTGLDSSSCTKVLELLKKL 289
Cdd:COG0419 154 DPIET----LSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEEL 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
221-275 |
8.18e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 8.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442627138 221 ESRIEDILLLLGLyNHDQTLTmRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:PRK11147 136 ENRINEVLAQLGL-DPDAALS-SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
244-301 |
1.05e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 1.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 244 LSGGQKKRLSIAMEL---INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIH 301
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
468-626 |
1.20e-06 |
|
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: 51.24 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 468 NLLFAILMhhsMTTMMLTVLTFPMDIsilIKEHFNR--------WYSLKAYYTAMTLVDLPISIISCFFFTVIVYLWSYQ 539
Cdd:pfam12698 161 YYLVGLIL---MIIILIGAAIIAVSI---VEEKESRikerllvsGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 540 PMEWIRFFMFFsisLLTVFVGHSFGLMIGAWFDV-VNGTFLAPVLTIPMMMFAGFGVTLRDLPSYLRWGSHISYLRYGLE 618
Cdd:pfam12698 235 FGNLGLLLLLF---LLYGLAYIALGYLLGSLFKNsEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPID 311
|
....*...
gi 442627138 619 GFISAIYG 626
Cdd:pfam12698 312 GLLRLIYG 319
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
165-302 |
1.45e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 165 DGSILLNGRR---RDLPSFRRMSCYITQddrlQPLLTvneNMHIAADLKLGQTVSYEEKESRI-------EDILLLLGLY 234
Cdd:PTZ00265 1276 SGKILLDGVDicdYNLKDLRNLFSIVSQ----EPMLF---NMSIYENIKFGKEDATREDVKRAckfaaidEFIESLPNKY 1348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 235 NHD-QTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSScTKVLE--LLKKLTSQGRTIICTIHQ 302
Cdd:PTZ00265 1349 DTNvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEktIVDIKDKADKTIITIAHR 1418
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
120-327 |
1.94e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 120 RGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTG-------VDGSILLNGR---RRDLPSFRRMSCYITQ 189
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarVTGDVTLNGEplaAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 DDRLQPLLTVNENMHIA--ADLKLGQTVSYEEKEsrIEDILLLLG----LYNHDQTltmRLSGGQKKRLSIAMEL----- 258
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGryPHARRAGALTHRDGE--IAWQALALAgataLVGRDVT---TLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 259 ----INNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTI-HQPTAKLfQIFDQVYVLSAGNCVYQGS 327
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADGAIVAHGA 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
243-318 |
2.14e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 243 RLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT-SQGRTIICTIHQPTAKLFQifDQVYVLS 318
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYA--NTIFVLS 653
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
168-304 |
2.59e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 49.70 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 168 ILLNGRRRDLPSFRRMSCYITQDDRLQPLLTVNENMHIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTLTMR-LSG 246
Cdd:pfam13304 160 GLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFeLSD 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627138 247 GQKK---RLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPT 304
Cdd:pfam13304 240 GTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
107-320 |
4.04e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 107 FKELSLTVKLGfnrgskEILhnvcgkfpgsqliAIMGPSGAGKSTLLDALSGFKTTgVDGSILLNGRR-RDLPSFRRMS- 184
Cdd:PRK15439 279 FRNISLEVRAG------EIL-------------GLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGKEiNALSTAQRLAr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 185 --CYITQDDR-----LQPLLTVNENMHIAADLKLGQTVSYEEKesRIEDILLLLGL-YNHDQTLTMRLSGGQKKRLSIAM 256
Cdd:PRK15439 339 glVYLPEDRQssglyLDAPLAWNVCALTHNRRGFWIKPARENA--VLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 257 ELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVLSAG 320
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVL-FISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
83-275 |
5.30e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 83 VEEEVHFDTDALNNLParEPV-DMEfkelslTVKLGFnrGSKEILHNV-CGKFPGSQlIAIMGPSGAGKSTLLDALSGfK 160
Cdd:PRK10636 294 VDNPFHFSFRAPESLP--NPLlKME------KVSAGY--GDRIILDSIkLNLVPGSR-IGLLGRNGAGKSTLIKLLAG-E 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 161 TTGVDGSI-LLNGRRrdLPSFRRMSC-YITQDDrlQPLltvnenMHIAadlklgqTVSYEEKESRIEDILLLLGlYNHDQ 238
Cdd:PRK10636 362 LAPVSGEIgLAKGIK--LGYFAQHQLeFLRADE--SPL------QHLA-------RLAPQELEQKLRDYLGGFG-FQGDK 423
|
170 180 190
....*....|....*....|....*....|....*....
gi 442627138 239 T--LTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:PRK10636 424 VteETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
140-297 |
6.56e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 140 AIMGPSGAGKSTLLDALSGfkttgvdGSILLNGRRRDlpSFRRMScyITQDDRLQPLLTV-----NENMHIAADLKLGQT 214
Cdd:PRK10938 33 AFVGANGSGKSALARALAG-------ELPLLSGERQS--QFSHIT--RLSFEQLQKLVSDewqrnNTDMLSPGEDDTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 215 VS-----YEEKESRIEDILLLLGLynhDQTLTMR---LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELL 286
Cdd:PRK10938 102 TAeiiqdEVKDPARCEQLAQQFGI---TALLDRRfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
170
....*....|.
gi 442627138 287 KKLTSQGRTII 297
Cdd:PRK10938 179 ASLHQSGITLV 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
143-275 |
8.62e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 143 GPSGAGKST-------LLDALSGfkttgvdgSILLNGRR---RDLPSFRRMScYITQDDRLQPLLTVNENM-------HI 205
Cdd:NF033858 299 GSNGCGKSTtmkmltgLLPASEG--------EAWLFGQPvdaGDIATRRRVG-YMSQAFSLYGELTVRQNLelharlfHL 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 AAdlklgqtvsyEEKESRIEDILLLLGLYNHDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLD 275
Cdd:NF033858 370 PA----------AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
244-332 |
8.80e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.36 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 244 LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCV 323
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
....*....
gi 442627138 324 YQGSTQKLV 332
Cdd:COG4170 239 ESGPTEQIL 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
137-332 |
1.98e-05 |
|
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: 47.87 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGF--KTTGV------DGSILLNGRRRDLPSfrRMSCYIT---QDDRLQPLLTVNENMHI 205
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVlePTSGEvnvrvgDEWVDMTKPGPDGRG--RAKRYIGilhQEYDLYPHRTVLDNLTE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 AADLKLG------------QTVSYEEKESriEDILlllglynhdQTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTG 273
Cdd:TIGR03269 389 AIGLELPdelarmkavitlKMVGFDEEKA--EEIL---------DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 274 LDSSSCTKVLE-LLKKLTSQGRTIICTIHQPTAKLfQIFDQVYVLSAGNCVYQGSTQKLV 332
Cdd:TIGR03269 458 MDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVL-DVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
125-331 |
2.01e-05 |
|
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: 46.77 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 125 ILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGfKTTGVDGSILLNGRrrdlPSFRRMSCYITQDdrlqpllTVNENMH 204
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-ELEPSEGKIKHSGR----ISFSSQFSWIMPG-------TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 205 IAadlklgqtVSYEEKESRI--------EDILlllGLYNHDQTLT----MRLSGGQKKRLSIAMELINNPTVMFLDEPTT 272
Cdd:cd03291 120 FG--------VSYDEYRYKSvvkacqleEDIT---KFPEKDNTVLgeggITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627138 273 GLDSSSCTKVLE--LLKKLTSQGRTIIctihqpTAKL--FQIFDQVYVLSAGNCVYQGSTQKL 331
Cdd:cd03291 189 YLDVFTEKEIFEscVCKLMANKTRILV------TSKMehLKKADKILILHEGSSYFYGTFSEL 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
119-328 |
2.23e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 46.23 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 119 NRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSG-FKTTGvdGSILLNGRrrdLPS-------Frrmscyitqd 190
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTS--GRVEVNGR---VSAllelgagF---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 191 drlQPLLTVNENMHIAADLkLGqtVSYEEKESRIEDILLLLGLYNH-DQTLtMRLSGGQKKRL--SIAMELinNPTVMFL 267
Cdd:COG1134 100 ---HPELTGRENIYLNGRL-LG--LSRKEIDEKFDEIVEFAELGDFiDQPV-KTYSSGMRARLafAVATAV--DPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627138 268 DEPT-TGlDSSSCTKVLELLKKLTSQGRTIICTIHQPTAkLFQIFDQVYVLSAGNCVYQGST 328
Cdd:COG1134 171 DEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGDP 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
137-307 |
2.57e-05 |
|
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: 44.67 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALSGFKTTGVDGSILLNGrrrdlpsfrrmscyitqddrlqplltvnENMHIAADLKLGQTVS 216
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG----------------------------EDILEEVLDQLLLIIV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 217 YEEKESriedillllglynhdqtltmrLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSS------CTKVLELLKKLT 290
Cdd:smart00382 55 GGKKAS---------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 442627138 291 SQGRTIICTIHQPTAKL 307
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
244-346 |
4.07e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 244 LSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCV 323
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|...
gi 442627138 324 YQGSTQKLV-----PFLQSV-----DLPCPMYH 346
Cdd:PRK15093 239 ETAPSKELVttphhPYTQALiraipDFGSAMPH 271
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
238-320 |
4.88e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 238 QTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIIcTIHQPTAKLFQIFDQVYVL 317
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVM 464
|
...
gi 442627138 318 SAG 320
Cdd:PRK10982 465 SNG 467
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-326 |
1.26e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 133 FPGSQLIAIMGPSGAGKSTLLdaLSGFKTTG----------------VDGSILLNGRRRDL-------PSFRRMSCYITQ 189
Cdd:PRK00635 1513 APLHSLVAISGVSGSGKTSLL--LEGFYKQAcaliekgpsvfseiifLDSHPQISSQRSDIstyfdiaPSLRNFYASLTQ 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 190 DDRLQ---PLLTVNENMHIAAD-LKLG----------------------------QTVSYEEK------ESRIEDILLL- 230
Cdd:PRK00635 1591 AKALNisaSMFSTNTKQGQCSDcWGLGyqwidrafyalekrpcptcsgfriqplaQEVVYEGKhfgqllQTPIEEVAETf 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 231 -----------------LGLYNHDQTLTmRLSGGQKKRLSIAMELI---NNPTVMFLDEPTTGLDSSSCTKVLELLKKLT 290
Cdd:PRK00635 1671 pflkkiqkplqalidngLGYLPLGQNLS-SLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLV 1749
|
250 260 270
....*....|....*....|....*....|....*.
gi 442627138 291 SQGRTIICTIHQPtaKLFQIFDQVYVLSAGNCVYQG 326
Cdd:PRK00635 1750 SLGHSVIYIDHDP--ALLKQADYLIEMGPGSGKTGG 1783
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
112-332 |
1.88e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 112 LTVKlgFNRGSKEILHNVCGKFPGSQLIAIMGPSGAGKSTLLDALSGFKTTgvDGSILLNGRRRD---LPSFRRMSCYIT 188
Cdd:TIGR01271 1223 LTAK--YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST--EGEIQIDGVSWNsvtLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 189 QD---------DRLQPL--LTVNENMHIAADLKLGQTVsyEEKESRIeDILLLLGLYnhdqtltmRLSGGQKKRLSIAME 257
Cdd:TIGR01271 1299 QKvfifsgtfrKNLDPYeqWSDEEIWKVAEEVGLKSVI--EQFPDKL-DFVLVDGGY--------VLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 258 LINNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTIICTiHQPTAKLFQifdQVYVLSAGNCVYQ-GSTQKLV 332
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE-HRVEALLEC---QQFLVIEGSSVKQyDSIQKLL 1439
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
131-340 |
2.01e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 131 GKFPGSQLIAIMGPSGAGKSTLLDALSGfkttgvdgSILLNGRRRDLPsfrrmscyitqddrlqplltvnenmhiaadlk 210
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAG--------QLIPNGDNDEWD-------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 lGQTVSYEEKEsriedillllglynhdqtltMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLKKLT 290
Cdd:cd03222 60 -GITPVYKPQY--------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627138 291 SQGRTIICTIHQPTAKLFQIFDQVYVLSAGNCVY------QGSTQKLVPFLQSVDL 340
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYgiasqpKGTREGINRFLRGYLI 174
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
244-297 |
2.06e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 2.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 244 LSGGQKKRLSIAMELI---NNPTVMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTII 297
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVV 883
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
134-156 |
2.30e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.49 E-value: 2.30e-04
10 20
....*....|....*....|...
gi 442627138 134 PGSQLIAIMGPSGAGKSTLLDAL 156
Cdd:COG3709 3 GPGRLIYVVGPSGAGKDSLLAAA 25
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-320 |
2.56e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 141 IMGPSGAGKSTLldALSGF-KTTGVD--GSILLNGRRRDLPSFRRMS----CYITQDDRLQPLL---TVNENMHIAADLK 210
Cdd:NF040905 291 IAGLMGAGRTEL--AMSVFgRSYGRNisGTVFKDGKEVDVSTVSDAIdaglAYVTEDRKGYGLNlidDIKRNITLANLGK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 211 LGQ-TVSYEEKESRI-EDILLLLGLYNHD-QTLTMRLSGGQKKRLSIAMELINNPTVMFLDEPTTGLDSSSCTKVLELLK 287
Cdd:NF040905 369 VSRrGVIDENEEIKVaEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIIN 448
|
170 180 190
....*....|....*....|....*....|...
gi 442627138 288 KLTSQGRTIIcTIHQPTAKLFQIFDQVYVLSAG 320
Cdd:NF040905 449 ELAAEGKGVI-VISSELPELLGMCDRIYVMNEG 480
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
135-260 |
5.66e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.71 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 135 GSQLIAIMGPSGAGKSTLLDAL------------SGFKTTGVDGSILLNGRRRDLPSFRRMscYITQDDRLQPLLT---- 198
Cdd:pfam13476 17 SKGLTLITGPNGSGKTTILDAIklalygktsrlkRKSGGGFVKGDIRIGLEGKGKAYVEIT--FENNDGRYTYAIErsre 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627138 199 VNENMHIAADLKLGQTVSYEEKESRIEDILLLLG------LYNHDQTLTMRLSGGQKKRLSIAMELIN 260
Cdd:pfam13476 95 LSKKKGKTKKKEILEILEIDELQQFISELLKSDKiilpllVFLGQEREEEFERKEKKERLEELEKALE 162
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
122-164 |
9.10e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.23 E-value: 9.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 442627138 122 SKEILHNVCGkfpGSQLIAIMGPSGAGKSTLLDALSGF---KTTGV 164
Cdd:PRK01889 184 GLDVLAAWLS---GGKTVALLGSSGVGKSTLVNALLGEevqKTGAV 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
227-301 |
1.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 227 ILLLLGL--YNHDQTLTMrLSGGQKKRLSIA----MELINnptVMF-LDEPTTGLDSSSCTKVLELLKKLTSQGRTIICT 299
Cdd:PRK00635 459 ILIDLGLpyLTPERALAT-LSGGEQERTALAkhlgAELIG---ITYiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLV 534
|
..
gi 442627138 300 IH 301
Cdd:PRK00635 535 EH 536
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
244-303 |
1.06e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 41.42 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627138 244 LSGGQKKRLSIAMELI----NNPTVMFLDEPTTGLDSSSCTKVLELLKKLtSQGRTIICTIHQP 303
Cdd:cd03241 171 ASGGELSRLMLALKAIlarkDAVPTLIFDEIDTGISGEVAQAVGKKLKEL-SRSHQVLCITHLP 233
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
244-297 |
1.20e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627138 244 LSGGQKKRLSIAMELINNPT---VMFLDEPTTGLDSSSCTKVLELLKKLTSQGRTII 297
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVV 887
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
124-297 |
1.35e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 124 EILHNVCGKFPGSQLIAimGPSGAGKSTLLDALsgFKTTGVDGSILLNGRRRDLPSFRRMSCYITQDDRLQPLLTVNENM 203
Cdd:pfam13191 14 DALDRVRSGRPPSVLLT--GEAGTGKTTLLREL--LRALERDGGYFLRGKCDENLPYSPLLEALTREGLLRQLLDELESS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 204 -------HIAADLKLGQTVSYEEKESRIEDILLLLGLYNHDQTltmrlsggqkkrlsiamelinnPTVMFLDEpTTGLDS 276
Cdd:pfam13191 90 lleawraALLEALAPVPELPGDLAERLLDLLLRLLDLLARGER----------------------PLVLVLDD-LQWADE 146
|
170 180
....*....|....*....|.
gi 442627138 277 SScTKVLELLKKLTSQGRTII 297
Cdd:pfam13191 147 AS-LQLLAALLRLLESLPLLV 166
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
140-157 |
1.99e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 1.99e-03
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
137-158 |
5.48e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 5.48e-03
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
134-177 |
5.53e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 39.09 E-value: 5.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 442627138 134 PGSQLIAIMGPSGAGKSTLLDALS---GFKTTGVDGSILlngrrRDL 177
Cdd:cd03275 20 PFDRFTCIIGPNGSGKSNLMDAISfvlGEKSSHLRSKNL-----KDL 61
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
137-301 |
5.98e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 39.78 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 137 QLIAIMGPSGAGKSTLLDALsgfktTG----VDGSILLNGRR---RDLPSFRRMSCYITQD----DRLQPLLTVNENMHI 205
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLL-----TGlyrpESGEILLDGQPvtaDNREAYRQLFSAVFSDfhlfDRLLGLDGEADPARA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627138 206 AA---DLKLGQTVSYEEkesriedillllglynhDQTLTMRLSGGQKKRLSIAMELINNPTVMFLDE------PT----- 271
Cdd:COG4615 434 RElleRLELDHKVSVED-----------------GRFSTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPEfrrvf 496
|
170 180 190
....*....|....*....|....*....|.
gi 442627138 272 -TgldsssctkvlELLKKLTSQGRTIICTIH 301
Cdd:COG4615 497 yT-----------ELLPELKARGKTVIAISH 516
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
136-158 |
9.79e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 9.79e-03
|
| |
