|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-851 |
0e+00 |
|
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: 562.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselsKG-FGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALND 80
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM----KGsVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLP 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 81 DLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI--LGVLSHTTRLLCTHR 158
Cdd:TIGR00957 742 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHG 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 159 TEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPT-----AWAEKEQ---------VATSGQSP-------SVCDLERT 217
Cdd:TIGR00957 822 ISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEflrtyAPDEQQGhledswtalVSGEGKEAkliengmLVTDVVGK 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 218 TEEELEVEQST-----------------------CGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAILVSLLLMQATR 274
Cdd:TIGR00957 902 QLQRQLSASSSdsgdqsrhhgssaelqkaeakeeTWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSA 981
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 275 NGADWWLAHWlsqlkagrngsREDPAScspgstalfsprlllfspgnlytpllstplhkaasNGT-ADVHFYLIVYATIA 353
Cdd:TIGR00957 982 LASNYWLSLW-----------TDDPMV-----------------------------------NGTqNNTSLRLSVYGALG 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 354 GVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLG 433
Cdd:TIGR00957 1016 ILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIG 1095
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 434 LLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLE 513
Cdd:TIGR00957 1096 ALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVD 1175
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 514 LNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSV 593
Cdd:TIGR00957 1176 ENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHS--LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAV 1253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 594 ERLEEYSCDVPQEPHSQPLQSPHQqriSWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFL 673
Cdd:TIGR00957 1254 ERLKEYSETEKEAPWQIQETAPPS---GWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTL 1330
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 674 VLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GG 752
Cdd:TIGR00957 1331 GLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALpDK 1410
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 753 LDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVL 832
Cdd:TIGR00957 1411 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI 1490
|
890
....*....|....*....
gi 1039753393 833 VLQAGRVVELDSPSALRNQ 851
Cdd:TIGR00957 1491 VLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-848 |
5.28e-165 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 521.61 E-value: 5.28e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFglATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDD 81
Cdd:PLN03130 645 LVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAY--VPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHD 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 LSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEY 161
Cdd:PLN03130 723 LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHF 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 162 LERADVVLLMEAGQLVRTGPPSEIL---PLVQAV------------PTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQ 226
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELSnngPLFQKLmenagkmeeyveENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSK 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 227 STCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAILV-SLLLMQATRNGADWWLAHWLSQlkagrngsredpascspg 305
Cdd:PLN03130 883 EGKSVLIKQEERETGVVSWKVLERYKNALGGAWVVMILFlCYVLTEVFRVSSSTWLSEWTDQ------------------ 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 306 stalfsprlllfSPGNLYTPLlstplhkaasngtadvhFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHR 385
Cdd:PLN03130 945 ------------GTPKTHGPL-----------------FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGS 995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 386 LLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRA 465
Cdd:PLN03130 996 ILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQS 1075
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 466 SFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIA 545
Cdd:PLN03130 1076 TAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTA 1155
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 546 GIALVQH-----QQGLANpgLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYsCDVPQEphSQPLQSPHQQRI 620
Cdd:PLN03130 1156 SFAVMQNgraenQAAFAS--TMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTY-IDLPSE--APLVIENNRPPP 1230
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 621 SWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE 700
Cdd:PLN03130 1231 GWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD 1310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 701 LRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALL 779
Cdd:PLN03130 1311 LRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSlGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 780 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-848 |
2.34e-160 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 506.82 E-value: 2.34e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFglATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDD 81
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAY--VPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 LSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEY 161
Cdd:PLN03232 723 LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 162 LERADVVLLM------EAGQLVRTGPPSEILPLVQAVPTAWAEKEQVATSGQ-----SPSV-CDLERTTEEELEVEQSTC 229
Cdd:PLN03232 803 LPLMDRIILVsegmikEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDEnilklGPTVtIDVSERNLGSTKQGKRGR 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 230 GCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAIL-VSLLLMQATRNGADWWLAHWLSQlkagrngsrEDPASCSPGsta 308
Cdd:PLN03232 883 SVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILlVCYLTTEVLRVSSSTWLSIWTDQ---------STPKSYSPG--- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 309 lfsprlllfspgnlytpllstplhkaasngtadvhFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLM 388
Cdd:PLN03232 951 -----------------------------------FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILR 995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 389 APVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFR 468
Cdd:PLN03232 996 APMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSR 1075
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 469 ELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIA 548
Cdd:PLN03232 1076 EVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFA 1155
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 549 LVQH-----QQGLANpgLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYsCDVPQEphSQPLQSPHQQRISWL 623
Cdd:PLN03232 1156 VLRNgnaenQAGFAS--TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNY-IDLPSE--ATAIIENNRPVSGWP 1230
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 624 TQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS 703
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 704 QLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPfGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 783 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-848 |
4.30e-140 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 453.47 E-value: 4.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELhrlcgwvavsELSKG-------FGLATQEPWIQCATIRDNILFGKTFDAQLYREVLE 74
Cdd:PTZ00243 688 LTVVLGATGSGKSTLLQSLLSQF----------EISEGrvwaersIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVR 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 75 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLL 154
Cdd:PTZ00243 758 VSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 155 CTHRTEYLERADVVLLMEAGQLVRTGPPSEIL--PLVQAVPTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQS----- 227
Cdd:PTZ00243 838 ATHQVHVVPRADYVVALGDGRVEFSGSSADFMrtSLYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPvakqe 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 228 -------------TCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAILVSLLLMQATRNGADwwlAHWLSQLKAGRNG 294
Cdd:PTZ00243 918 gnaeggdgaaldaAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSS---GVWLSMWSTRSFK 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 295 SREDpascspgstalfspRLLLFSPGNLYTPLLSTPLHkaasngtadvhFYLIVYATIAGVNSL-CTLLRAVlfaagalq 373
Cdd:PTZ00243 995 LSAA--------------TYLYVYLGIVLLGTFSVPLR-----------FFLSYEAMRRGSRNMhRDLLRSV-------- 1041
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 374 aaaslhhrllhrlLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLP----FLLNILLANSVGLLGLLAVLGSGLPWLLLLL 449
Cdd:PTZ00243 1042 -------------SRGTMSFFDTTPLGRILNRFSRDIDILDNTLPmsylYLLQCLFSICSSILVTSASQPFVLVALVPCG 1108
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 450 pplsFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWL 529
Cdd:PTZ00243 1109 ----YLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWL 1184
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 530 DIRLQLMGAAVVSAIAGIALVQHQQGLA--NPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYSCDVPQE- 606
Cdd:PTZ00243 1185 GVRVEFLSNIVVTVIALIGVIGTMLRATsqEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEd 1264
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 607 ----------------------------PHSQPLQSPHQqriswLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKL 658
Cdd:PTZ00243 1265 mpeldeevdalerrtgmaadvtgtvviePASPTSAAPHP-----VQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKV 1339
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 659 GIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQAL 738
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAAL 1419
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 739 EQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT-DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVL 816
Cdd:PTZ00243 1420 ELVGLRErVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVI 1499
|
890 900 910
....*....|....*....|....*....|..
gi 1039753393 817 TIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:PTZ00243 1500 TIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
626-845 |
5.43e-119 |
|
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: 359.89 E-value: 5.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 784
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLpGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 785 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 845
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-851 |
6.50e-101 |
|
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: 343.82 E-value: 6.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVavsELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDD 81
Cdd:TIGR01271 454 LLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEED 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 LSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEY 161
Cdd:TIGR01271 531 IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEH 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 162 LERADVVLLMEAG---------------------------------------------------------------QLVR 178
Cdd:TIGR01271 611 LKKADKILLLHEGvcyfygtfselqakrpdfsslllgleafdnfsaerrnsiltetlrrvsidgdstvfsgpetikQSFK 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 179 TGPP--------SEIL---------PLVQAVPT-AWAEKEQVATSGQS-----------------PSVCDLERTTEEELE 223
Cdd:TIGR01271 691 QPPPefaekrkqSIILnpiasarkfSFVQMGPQkAQATTIEDAVREPSerkfslvpedeqgeeslPRGNQYHHGLQHQAQ 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 224 VEQSTCGcLVQEESKSEGAValHVYRAYWRAMGSGLAAAILVSLLLMQATRNGADwwlahwlSQLKAGRNGSREDPASC- 302
Cdd:TIGR01271 771 RRQSVLQ-LMTHSNRGENRR--EQLQTSFRKKSSITQQNELASELDIYSRRLSKD-------SVYEISEEINEEDLKECf 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 303 ------SPGSTA-------LFSPRLLLFS----------------------PGNLYTPLLSTPLHKAASNG--------T 339
Cdd:TIGR01271 841 aderenVFETTTwntylryITTNRNLVFVlifclviflaevaasllglwliTDNPSAPNYVDQQHANASSPdvqkpviiT 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 340 ADVHFYlIVYATIAGVNSLCTL--LRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSL 417
Cdd:TIGR01271 921 PTSAYY-IFYIYVGTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDML 999
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 418 PFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRA 497
Cdd:TIGR01271 1000 PLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRA 1079
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 498 AGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLVLSYALSLTGLLS 577
Cdd:TIGR01271 1080 FGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQ 1156
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 578 GLVSSFTQTEAMMVSVERLEEYsCDVPQEpHSQP--------------LQSPHQQRIsWLTQGSVEFQDVVLVYRPGLPN 643
Cdd:TIGR01271 1157 WAVNSSIDVDGLMRSVSRVFKF-IDLPQE-EPRPsggggkyqlstvlvIENPHAQKC-WPSGGQMDVQGLTAKYTEAGRA 1233
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNaGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL 723
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL 802
Cdd:TIGR01271 1313 DPYEQWSDEEIWKVAEEVGLKSVIEQFpDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*....
gi 1039753393 803 QQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:TIGR01271 1393 RKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
260-599 |
1.05e-94 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 299.44 E-value: 1.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 260 AAAILVSLLLMQATRNGADWWLAHWLSQLKagrngsredpascspgstalfsprlllfspgnlytpllstplHKAASNGT 339
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSN------------------------------------------NSFFNFIN 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 340 ADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPF 419
Cdd:cd18605 39 DSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 420 LLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAG 499
Cdd:cd18605 119 ILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 500 ATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGL-ANPGLVGLVLSYALSLTGLLSG 578
Cdd:cd18605 199 KQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsIDAGLIGLALSYALPITGLLSG 278
|
330 340
....*....|....*....|.
gi 1039753393 579 LVSSFTQTEAMMVSVERLEEY 599
Cdd:cd18605 279 LLNSFTETEKEMVSVERVRQY 299
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
390-851 |
9.49e-94 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 306.71 E-value: 9.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 390 PVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSG----LPWLLLLLPPLSFVYYSVQGYYRA 465
Cdd:COG1132 108 PLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIdwrlALIVLLVLPLLLLVLRLFGRRLRK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 466 SFRELR-RLGSLTwsplySHLADTLAGLPVLRAAGATY----RFEEENQRLLELNQRcqfaSYATMQWLDIRLQLMGAAV 540
Cdd:COG1132 188 LFRRVQeALAELN-----GRLQESLSGIRVVKAFGREEreleRFREANEELRRANLR----AARLSALFFPLMELLGNLG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 541 VSAIAGIALVQHQQGLANPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEY---SCDVPQEPHSQPLQSPhq 617
Cdd:COG1132 259 LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELldePPEIPDPPGAVPLPPV-- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 618 qriswltQGSVEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLE 697
Cdd:COG1132 337 -------RGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 698 LAELRSQLAVIPQEPFLFSGTIRENL---DPQglHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLC 773
Cdd:COG1132 409 LESLRRQIGVVPQDTFLFSGTIRENIrygRPD--ATDEEVEEAAKAAQAHEFIEALpDGYDTVVGERGVNLSGGQRQRIA 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 774 LARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-175 |
1.81e-92 |
|
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: 289.75 E-value: 1.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelsKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDD 81
Cdd:cd03250 33 LVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP---GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 LSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHT-TRLLCTHRTE 160
Cdd:cd03250 110 LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNkTRILVTHQLQ 189
|
170
....*....|....*
gi 1039753393 161 YLERADVVLLMEAGQ 175
Cdd:cd03250 190 LLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
622-845 |
8.38e-88 |
|
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: 277.76 E-value: 8.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 622 WLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAEL 701
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 702 RSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEqchlsevaVAMGGLdgelgergqNLSLGQRQLLCLARALLTD 781
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR--------VSEGGL---------NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 845
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
454-851 |
5.32e-82 |
|
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: 278.64 E-value: 5.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 454 FVYYSVQGYYRASFRELRRLGSLtwspLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRL 533
Cdd:COG2274 310 LLGLLFQPRLRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 534 QLMGAAVVSAI--AGIALVQHQQ-------------GLANPGLVGLVLSyalsltgllsglVSSFTQteaMMVSVERLEE 598
Cdd:COG2274 386 GLLQQLATVALlwLGAYLVIDGQltlgqliafnilsGRFLAPVAQLIGL------------LQRFQD---AKIALERLDD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 599 YScDVPQEPHSQPLQSPHQQriswlTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL 678
Cdd:COG2274 451 IL-DLPPEREEGRSKLSLPR-----LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 679 LEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQglHEDRALWQALEQCHLSEVAVAM-GGLD 754
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALpMGYD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 755 GELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVL 834
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
410
....*....|....*..
gi 1039753393 835 QAGRVVELDSPSALRNQ 851
Cdd:COG2274 683 DKGRIVEDGTHEELLAR 699
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
464-851 |
3.56e-73 |
|
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: 250.83 E-value: 3.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 464 RASFRELRRLGSltwsplysHLADTLAGLPVLRAAGATyrfEEENQRLLELNQRcqfasY--ATMQWLdiRLQLM----- 536
Cdd:COG4988 187 RRQWRALARLSG--------HFLDRLRGLTTLKLFGRA---KAEAERIAEASED-----FrkRTMKVL--RVAFLssavl 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 537 ------GAAVVSAIAGIALVQHQQGLAnPGLVGLVLS---YALSLTgllsglVSSFTQTEAM-MVSVERLEEyscdVPQE 606
Cdd:COG4988 249 effaslSIALVAVYIGFRLLGGSLTLF-AALFVLLLApefFLPLRD------LGSFYHARANgIAAAEKIFA----LLDA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 607 PHSQPLQSphQQRISWLTQGSVEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV 686
Cdd:COG4988 318 PEPAAPAG--TAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 687 LLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQ 762
Cdd:COG4988 395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFVAALpDGLDTPLGEGGR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 763 NLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVEL 842
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
....*....
gi 1039753393 843 DSPSALRNQ 851
Cdd:COG4988 553 GTHEELLAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
626-851 |
5.17e-73 |
|
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: 239.05 E-value: 5.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQ-ALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAK 783
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLpNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 784 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
626-851 |
7.08e-68 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 226.33 E-value: 7.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 784
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 785 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
628-838 |
2.57e-67 |
|
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: 221.49 E-value: 2.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSGTIRENLdpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCI 787
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 788 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGR 838
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
628-841 |
3.53e-63 |
|
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: 212.48 E-value: 3.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAK 783
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGATREE--VEEAARAANAHEFIMELpEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 784 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
628-848 |
3.38e-60 |
|
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: 204.39 E-value: 3.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAK 783
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDATDEE--VIEAAKAAQIHDKIMRFpDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 784 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
389-841 |
3.77e-60 |
|
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: 214.97 E-value: 3.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 389 APVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFR 468
Cdd:TIGR02203 100 LPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 469 ELRRLGSLTWSPLYSHLADTLAGLPVLRAAGA----TYRFEEENQRLLELNQRCQFASYAtmqwLDIRLQLMGAAVVSAI 544
Cdd:TIGR02203 180 RISKEIQNSMGQVTTVAEETLQGYRVVKLFGGqayeTRRFDAVSNRNRRLAMKMTSAGSI----SSPITQLIASLALAVV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 545 AGIALVQHQQGLANPG-LVGLVLSY-ALSLTGLLSGLVSSFTQTeaMMVSVERLEEYsCDVPQEPHSQPLqspHQQRIsw 622
Cdd:TIGR02203 256 LFIALFQAQAGSLTAGdFTAFITAMiALIRPLKSLTNVNAPMQR--GLAAAESLFTL-LDSPPEKDTGTR---AIERA-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 623 ltQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 702
Cdd:TIGR02203 328 --RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLR 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEPFLFSGTIRENL---DPQGLHEDRALwQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARAL 778
Cdd:TIGR02203 406 RQVALVSQDVVLFNDTIANNIaygRTEQADRAEIE-RALAAAYAQDFVDKLpLGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 779 LTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
628-848 |
1.36e-59 |
|
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: 202.77 E-value: 1.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVY--RPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENL-----DPQGLHEDRALWQALeqCHlSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT 780
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDATDEEVEEAAKKAN--IH-DFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 781 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
261-600 |
5.11e-59 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 203.50 E-value: 5.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 261 AAILVSLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfspgnlytpllstplhkAASNGTA 340
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD----------------------------------------------WSSSPNS 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 341 DVHFYLIVYATIAGVNS-LCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPF 419
Cdd:cd18580 36 SSGYYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 420 LLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAG 499
Cdd:cd18580 116 ALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 500 ATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLVLSYALSLTGLLSGL 579
Cdd:cd18580 196 WQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWL 273
|
330 340
....*....|....*....|.
gi 1039753393 580 VSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18580 274 VRQWTELETSMVSVERILEYT 294
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
626-840 |
1.58e-56 |
|
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: 193.57 E-value: 1.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENL---DPqgLHEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTD 781
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAP--LADDERILRAAELAGVTDfVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 840
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
602-841 |
3.27e-54 |
|
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: 198.89 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 602 DVPQE----PHSQPLQsphqqriswLTQGSVEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFR 677
Cdd:COG5265 337 DQPPEvadaPDAPPLV---------VGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 678 LLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSE-VAVAMGGL 753
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDASEEE--VEAAARAAQIHDfIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 754 DGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLV 833
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
....*...
gi 1039753393 834 LQAGRVVE 841
Cdd:COG5265 565 LEAGRIVE 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
628-841 |
1.37e-53 |
|
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: 186.15 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSGTIRENL---DPqGLHEDRALWQA-LEQCH--LSEVAVamgGLDGELGERGQNLSLGQRQLLCLARALLTD 781
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP-GMSMERVIEAAkLAGAHdfISELPE---GYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
393-852 |
7.90e-53 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 196.87 E-value: 7.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 393 FYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLA---VLGSGLPWLLLLLPPLSFVYYSVQG-YYRASFR 468
Cdd:TIGR00958 251 FFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGfmlWLSPRLTMVTLINLPLVFLAEKVFGkRYQLLSE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 469 ELRR-LGSLTWSPLyshlaDTLAGLPVLRAAGA----TYRFEEENQRLLELNQRCQFAsYATMQWLDiRLQLMGAAVVSA 543
Cdd:TIGR00958 331 ELQEaVAKANQVAE-----EALSGMRTVRSFAAeegeASRFKEALEETLQLNKRKALA-YAGYLWTT-SVLGMLIQVLVL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 544 IAGIALVQHQQgLANPGLVGLVLsYALSLTGLLSGLVSSFTQteaMMVSV---ERLEEYSCDVPQEPHSQPLQSPHqqri 620
Cdd:TIGR00958 404 YYGGQLVLTGK-VSSGNLVSFLL-YQEQLGEAVRVLSYVYSG---MMQAVgasEKVFEYLDRKPNIPLTGTLAPLN---- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 621 swlTQGSVEFQDVVLVY--RPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL 698
Cdd:TIGR00958 475 ---LEGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 699 AELRSQLAVIPQEPFLFSGTIRENLdPQGLH--EDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLA 775
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENI-AYGLTdtPDEEIMAAAKAANAHDFIMEFpNGYDTEVGEKGSQLSGGQKQRIAIA 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 776 RALLTDAKILCIDEATASVDQKTDQLLQQTicKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-174 |
1.13e-50 |
|
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: 177.52 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCG---WVAVSELSKGF-----------GLATQEPWIQCATIRDNILFGKTFDAQ 67
Cdd:cd03290 29 LTMIVGQVGCGKSSLLLAILGEMQTLEGkvhWSNKNESEPSFeatrsrnrysvAYAAQKPWLLNATVEENITFGSPFNKQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVL 147
Cdd:cd03290 109 RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFL 188
|
170 180
....*....|....*....|....*....
gi 1039753393 148 SHTTR--LLCTHRTEYLERADVVLLMEAG 174
Cdd:cd03290 189 QDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
336-600 |
1.84e-49 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 176.52 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 336 SNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDD 415
Cdd:cd18603 34 TQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 416 SLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVL 495
Cdd:cd18603 114 TLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 496 RAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlaNPGLVGLVLSYALSLTGL 575
Cdd:cd18603 194 RAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSL--SPGLVGLSISYALQITQT 271
|
250 260
....*....|....*....|....*
gi 1039753393 576 LSGLVSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18603 272 LNWLVRMTSELETNIVSVERIKEYS 296
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
479-841 |
3.57e-49 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 184.01 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 479 SPLYSHLADTLAGLPVLRaagaTY-RFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAA-----VVSAIAGIALvqH 552
Cdd:PRK13657 192 HDLFAHVSDAIGNVSVVQ----SYnRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAAstitmLAILVLGAAL--V 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 553 QQGLANPGLVGLVLSYALSLTGLLSGLVSSFTQTeamMVSVERLEEY------SCDVPQEPHSQPLQSphqqriswlTQG 626
Cdd:PRK13657 266 QKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQV---FMAAPKLEEFfevedaVPDVRDPPGAIDLGR---------VKG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLA 706
Cdd:PRK13657 334 AVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQEPFLFSGTIRENL---DPQGLHEDraLWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIrvgRPDATDEE--MRAAAERAQAHDfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 783 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
262-600 |
3.13e-47 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 170.35 E-value: 3.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 262 AILVSLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfspgnlyTPLLSTplhkaasngtad 341
Cdd:cd18606 3 LLLLLLILSQFAQVFTNLWLSFWTED------------------------------------FFGLSQ------------ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 342 vHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLL 421
Cdd:cd18606 35 -GFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 422 NILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGAT 501
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 502 YRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVqhQQGLANPGLVGLVLSYALSLTGLLSGLVS 581
Cdd:cd18606 194 DRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVT--RRFSISPSSTGLVLSYVLQITQVLSWLVR 271
|
330
....*....|....*....
gi 1039753393 582 SFTQTEAMMVSVERLEEYS 600
Cdd:cd18606 272 QFAEVENNMNSVERLLHYA 290
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
626-851 |
3.85e-46 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 166.57 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNaGRVLLDNVDTSQLELAELRSQL 705
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 784
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 785 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
260-600 |
1.20e-45 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 166.24 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 260 AAAILVSLLLMQATRNGADWWLAHWLSQ-LKAGRNGSREDPASCSPGSTALFSPRLLLFSPGNLYTPLLSTPLHKAAS-N 337
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEAnHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGlR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 338 GTADVHFylivyatiagvnslcTLLRAVLfaagalqaaaslhhrllhrllMAPVTFYDSTPSGRVLNRFSSDVACVDDSL 417
Cdd:cd18602 81 AARRLHD---------------RMLRNIV---------------------RAPMRFFDTTPIGRILNRFSSDTNVIDQKL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 418 PFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRA 497
Cdd:cd18602 125 PTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 498 AGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLVLSYALSLTGLLS 577
Cdd:cd18602 205 FRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLN 284
|
330 340
....*....|....*....|...
gi 1039753393 578 GLVSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18602 285 WVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
464-834 |
4.65e-45 |
|
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: 170.55 E-value: 4.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 464 RASFRELRRLGSltwsplysHLADTLAGLPVLRAAGATyrfEEENQRLLELNQrcQFASyATMQWLdiRLQLMGAAVVSA 543
Cdd:TIGR02857 173 RKQWAALSRLSG--------HFLDRLRGLPTLKLFGRA---KAQAAAIRRSSE--EYRE-RTMRVL--RIAFLSSAVLEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 544 IA--GIALVQHQQGLA--------NPGLVGLVLsyALSLTGLLSGLVSSFTQTEAMMVSVERLEEYscdvpQEPHSQPLQ 613
Cdd:TIGR02857 237 FAtlSVALVAVYIGFRllagdldlATGLFVLLL--APEFYLPLRQLGAQYHARADGVAAAEALFAV-----LDAAPRPLA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 614 SphQQRISWLTQGSVEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDT 693
Cdd:TIGR02857 310 G--KAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 694 SQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQR 769
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEfVAALPQGLDTPIGEGGAGLSGGQA 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 770 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVL 834
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
261-600 |
1.21e-44 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 163.02 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 261 AAILVSLLLMQATRNGADWWLAHWLSQlkagrngsredpascspgstalfsprlllfspgnlYTPLLSTPlhkaasngTA 340
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASA-----------------------------------YETSSALP--------PS 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 341 DVH--FYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLP 418
Cdd:cd18604 39 EVSvlYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 419 FLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSV-QGYYRASfRELRRLGSLTWSPLYSHLADTLAGLPVLRA 497
Cdd:cd18604 119 DSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIgRLYLRAS-RELKRLESVARSPILSHFGETLAGLVTIRA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 498 AGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQqglANPGLVGLVLSYALSLTGLLS 577
Cdd:cd18604 198 FGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPG---IDAGLAGFSLSFALGFSSAIL 274
|
330 340
....*....|....*....|...
gi 1039753393 578 GLVSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18604 275 WLVRSYNELELDMNSVERIQEYL 297
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
623-841 |
2.01e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 169.62 E-value: 2.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 623 LTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 702
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALL 779
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 780 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
625-839 |
9.42e-44 |
|
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: 158.02 E-value: 9.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 625 QGSVEFQDVVLVY--RPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 702
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEPFLFSGTIRENLdPQGLH--EDRALWQALEQCH----LSEVAVamgGLDGELGERGQNLSLGQRQLLCLAR 776
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI-AYGLQscSFECVKEAAQKAHahsfISELAS---GYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 777 ALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRV 839
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
256-600 |
1.31e-43 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 160.81 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 256 GSGLAAAILVSLLLMQATRNGADWWLAHWLSQlKAGRNGSREDPASCSPGSTalfsprlllfspgnlytpllstplhkaa 335
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQ-GSGNTTNNVDNSTVDSGNI---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 336 sNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDD 415
Cdd:cd18599 52 -SDNPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 416 SLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVL 495
Cdd:cd18599 131 RLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 496 RAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHqqGLANPGLVGLVLSYALSLTGL 575
Cdd:cd18599 211 HAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK--GSISPAFAGLALSYALQLSGL 288
|
330 340
....*....|....*....|....*
gi 1039753393 576 LSGLVSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18599 289 FQFTVRLASETEARFTSVERILEYI 313
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
625-841 |
3.94e-43 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 165.96 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 625 QGSVEFQDVVLVYrPGLPN-ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS 703
Cdd:PRK11176 339 KGDIEFRNVTFTY-PGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 704 QLAVIPQEPFLFSGTIRENLD--PQGLHEDRALWQALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLT 780
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMdNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 781 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
488-852 |
4.31e-42 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 164.36 E-value: 4.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 488 TLAGLPVLRAAGATYRFeeenqrllelnqrcqFAS----YATMQWLDIRLQLMGAAVVSAIAGIALVQhqqGLANPGLVG 563
Cdd:TIGR03797 320 LINGISKLRVAGAENRA---------------FARwaklFSRQRKLELSAQRIENLLTVFNAVLPVLT---SAALFAAAI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 564 LVLSYALSLTGLLSGLVSSFTQ-TEAMMVSVERLEEYSCDVPQEPHSQPL---------QSPHQQRISwltqGSVEFQDV 633
Cdd:TIGR03797 382 SLLGGAGLSLGSFLAFNTAFGSfSGAVTQLSNTLISILAVIPLWERAKPIlealpevdeAKTDPGKLS----GAIEVDRV 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 634 VLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPF 713
Cdd:TIGR03797 458 TFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGR 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 714 LFSGTIRENL-DPQGLHEDRAlWQALEQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEAT 791
Cdd:TIGR03797 538 LMSGSIFENIaGGAPLTLDEA-WEAARMAGLAEDIRAMPmGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 792 ASVDQKTDQLLQQTICKrfANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:TIGR03797 617 SALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-185 |
5.21e-42 |
|
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: 155.01 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVavsELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDD 81
Cdd:cd03291 65 MLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEED 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 LSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEY 161
Cdd:cd03291 142 ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEH 221
|
170 180
....*....|....*....|....
gi 1039753393 162 LERADVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03291 222 LKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
584-841 |
2.03e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 161.04 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 584 TQTEAMM----VSVERLEEYsCDVPQEPH---SQPLQSphqqriswltqGSVEFQDVVLVYRPGLPnALDGVTFRVEPGE 656
Cdd:PRK10790 302 TTQQSMLqqavVAGERVFEL-MDGPRQQYgndDRPLQS-----------GRIDIDNVSFAYRDDNL-VLQNINLSVPSRG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 657 KLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLD-PQGLHEDRaLW 735
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTlGRDISEEQ-VW 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 736 QALEQCHLSEVAVAM-GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKT 814
Cdd:PRK10790 448 QALETVQLAELARSLpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT 527
|
250 260
....*....|....*....|....*..
gi 1039753393 815 VLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:PRK10790 528 LVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
609-852 |
2.94e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 160.40 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 609 SQPLQSPHQQRISWLTQGSVEF--QDVVlVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRV 686
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIeaEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 687 LLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQ 762
Cdd:PRK11174 407 KINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEfLPLLPQGLDTPIGDQAA 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 763 NLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVEL 842
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
250
....*....|
gi 1039753393 843 DSPSALRNQP 852
Cdd:PRK11174 565 GDYAELSQAG 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
481-822 |
3.03e-41 |
|
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: 159.45 E-value: 3.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 481 LYSHLADTLAGLPVLRAAGATYRF----EEENQRLLELNQRcqfasyatmqwlDIRLQLMGAAVVSAIAGIA----LVQH 552
Cdd:TIGR02868 192 LAAQLTDALDGAAELVASGALPAAlaqvEEADRELTRAERR------------AAAATALGAALTLLAAGLAvlgaLWAG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 553 QQGLANPGLVGLVLSYALSLTGLLSGLVSSFT----QTEAMMVSVERLEEyscdVPQEPHSQPLQSPHQQRISWLTQGSV 628
Cdd:TIGR02868 260 GPAVADGRLAPVTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIVE----VLDAAGPVAEGSAPAAGAVGLGKPTL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 629 EFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 708
Cdd:TIGR02868 336 ELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 709 PQEPFLFSGTIRENL---DPQGlhEDRALWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKI 784
Cdd:TIGR02868 415 AQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADwLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039753393 785 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRL 822
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
629-839 |
8.69e-41 |
|
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: 147.75 E-value: 8.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 629 EFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 708
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 709 PQEPFLFSGTIRENLdpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCID 788
Cdd:cd03246 82 PQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 789 EATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 839
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
628-841 |
1.19e-40 |
|
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: 147.46 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAV 707
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSGTIRENLdpqglhedralwqaleqchlsevavamggldgelgerGQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 788 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
604-852 |
7.42e-39 |
|
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: 151.98 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 604 PQEPHSQPLQSPHQQRISWLTQGS---VEFQDVVLVYRPGLPN---ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFR 677
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 678 LLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPF--LFSG-TIRENL-DPQGLH--------EDRALwQALEQCh 742
Cdd:COG1123 314 LLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPYssLNPRmTVGDIIaEPLRLHgllsraerRERVA-ELLERV- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 743 lsevavamgGLDGELGER--GQnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLT 817
Cdd:COG1123 392 ---------GLPPDLADRypHE-LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVqAQILNllRDLQREL-GLTYLF 460
|
250 260 270
....*....|....*....|....*....|....*.
gi 1039753393 818 IAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:COG1123 461 ISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
626-851 |
1.08e-38 |
|
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: 154.13 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:TIGR01193 472 GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSGTIRENL---DPQGLHEDRaLWQALEQCHLSEVAVAMG-GLDGELGERGQNLSLGQRQLLCLARALLTD 781
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLllgAKENVSQDE-IWAACEIAEIKDDIENMPlGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 782 AKILCIDEATASVdqktDQLLQQTICKRFAN---KTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:TIGR01193 630 SKVLILDESTSNL----DTITEKKIVNNLLNlqdKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
258-600 |
4.12e-38 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 144.77 E-value: 4.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 258 GLAAAILVSLL--LMQATRNGADWWLAHWL-SQLKAGRNgsredpascspgstalfsprlllFSPGNLYTPLLSTPLHKa 334
Cdd:cd18601 1 GVFVFILLVLLniAAQVLYVLSDWWLSYWAnLEEKLNDT-----------------------TDRVQGENSTNVDIEDL- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 335 asngtaDVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVD 414
Cdd:cd18601 57 ------DRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 415 DSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPV 494
Cdd:cd18601 131 DLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 495 LRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVqhqqgLA---NPGLVGLVLSYALS 571
Cdd:cd18601 211 IRAYSAQERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLF-----LAeslDAGLVGLSLSYALT 285
|
330 340
....*....|....*....|....*....
gi 1039753393 572 LTGLLSGLVSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18601 286 LMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
594-840 |
4.44e-38 |
|
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: 150.67 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 594 ERLEEYSCDVPQEPHSQPLQSPhqqriswltQGSVEFQDVVLVYrPGLPNA-LDGVTFRVEPGEKLGIVGRTGSGKSSLF 672
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPRP---------KGRLSVENLTVVP-PGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 673 LVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIREN------LDPQ---------GLHEdraLWQA 737
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENiarfgdADPEkvvaaaklaGVHE---MILR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 738 LEQchlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVL 816
Cdd:COG4618 453 LPD-----------GYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVV 521
|
250 260
....*....|....*....|....
gi 1039753393 817 TIAHRLNTILNSDRVLVLQAGRVV 840
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
629-838 |
3.68e-37 |
|
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: 138.75 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 629 EFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 708
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 709 PQEPF--LFSGTIRE----NLDPQGLHED---RALWQALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLARALL 779
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafGLENLGLPEEeieERVEEALELV----------GLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 780 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGR 838
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
628-841 |
1.25e-36 |
|
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: 137.64 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRP--GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 702
Cdd:cd03257 2 LEVKNLSVSFPTggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEPFL---FSGTIRENL-DPQGLHE-DRALWQALEQCHLSEVAVamgGLDGELGER--GQnLSLGQRQLLCLA 775
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIaEPLRIHGkLSKKEARKEAVLLLLVGV---GLPEEVLNRypHE-LSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 776 RALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
645-792 |
1.73e-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: 134.70 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG-TIRENL 723
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 724 -------DPQGLHEDRALWQALEQchlsevaVAMGGLDGE-LGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-186 |
1.47e-35 |
|
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: 142.97 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS-----KGFGLATQEPWIQCATIRDNILFGKTF--DAQL 68
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLLGFLPpysgsiLING-VDLSDLDpaswrRQIAWVPQNPYLFAGTIRENLRLGRPDasDEEL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 yREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLS 148
Cdd:COG4988 444 -EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAK 521
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039753393 149 HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-186 |
1.62e-34 |
|
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: 139.90 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGK---TfDAQL 68
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLdpqsgsitlggVDLRDL-DEDDLRRRIAVVPQRPHLFDTTLRENLRLARpdaT-DEEL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 yREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLS 148
Cdd:COG4987 442 -WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALA 519
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039753393 149 HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG4987 520 GRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-186 |
3.19e-34 |
|
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: 140.35 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF--DAQLyR 70
Cdd:COG2274 504 VAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPDatDEEI-I 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHT 150
Cdd:COG2274 583 EAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGR 661
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039753393 151 TRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG2274 662 TVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
628-838 |
3.75e-34 |
|
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: 129.90 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPG---LPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlelaELRSQ 704
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 705 LAVIPQEPFLFSGTIRENL---DPqgLHEDRaLWQALEQCHLSE-VAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT 780
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKP--FDEER-YEKVIKACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 781 DAKILCIDEATASVDQKT-DQLLQQTICKRFA-NKTVLTIAHRLNTILNSDRVLVLQAGR 838
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
644-852 |
5.85e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 138.31 E-value: 5.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL 723
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 dpqGLHEDRALWQALEQ-CHLSEVAVAM----GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:PRK10789 410 ---ALGRPDATQQEIEHvARLASVHDDIlrlpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 799 DQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK10789 487 EHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
629-838 |
3.52e-33 |
|
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: 125.43 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 629 EFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVI 708
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 709 PQepflfsgtirenldpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCID 788
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 789 EATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGR 838
Cdd:cd00267 106 EPTSGLDPASRERLLELL-RELAeeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
628-852 |
1.22e-32 |
|
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: 133.49 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQLELAELRSQ 704
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 705 LAVIPQEPF--LFSGT----IRENLDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARAL 778
Cdd:COG1123 85 IGMVFQDPMtqLNPVTvgdqIAEALENLGLSRAEARARVLE-------LLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 779 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
628-848 |
1.94e-32 |
|
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: 125.76 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGlpNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE-----PNAGRVLLD--NVDTSQLELAE 700
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 701 LRSQLAVIPQEPFLFSGTIRENLD----PQGLHEDRALWQaleqchLSEVAVAMGGLDGELGER--GQNLSLGQRQLLCL 774
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELDE------RVEEALRKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 775 ARALLTDAKILCIDEATASVD----QKTDQLLQQtICKRFankTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDpistAKIEELIAE-LKKEY---TIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-180 |
2.37e-32 |
|
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: 125.01 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF-DAQLYRE 71
Cdd:cd03245 33 VAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpADLRRNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHTT 151
Cdd:cd03245 113 AAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGDKT 191
|
170 180
....*....|....*....|....*....
gi 1039753393 152 RLLCTHRTEYLERADVVLLMEAGQLVRTG 180
Cdd:cd03245 192 LIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
628-853 |
3.16e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 125.69 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQL 705
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFL-----FS--GTIRENLDPQGL-HEDRALWQALEQChlsevavamgGLDGELGER--GQnLSLGQRQLLCLA 775
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLpDREERIAELLEQV----------GLPPSFLDRypHQ-LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 776 RALLTDAKILCIDEATASVD---Q-KTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRN 850
Cdd:COG1124 151 RALILEPELLLLDEPTSALDvsvQaEILNLLKDL--REERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
...
gi 1039753393 851 QPH 853
Cdd:COG1124 229 GPK 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
628-852 |
8.14e-32 |
|
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: 124.23 E-value: 8.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVY--RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLfLVLFRLLE-PNAGRVLLDNVDTSQL---ELAEL 701
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 702 RSQLAVIPQEPFLFSG-TIREN----LDPQGLHEDRALWQALEQCHLSevavamgGLDGELGERGQNLSLGQRQLLCLAR 776
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVLELLELV-------GLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 777 ALLTDAKILCIDEATASVDQKTDQ----LLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQsilaLLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 1039753393 852 P 852
Cdd:cd03258 232 P 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
628-841 |
3.38e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 3.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 702
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQ-LAVIPQEPFLFSG-TIREN----LDPQGLHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQLLCLAR 776
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENvalpLLLAGVSRKERRERAREL--LERV-----GLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 777 ALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
628-839 |
1.18e-30 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 120.29 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 702
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 -SQLAVIPQE----PFLfsgTIRENL--------DPQGLHEDRALwQALEQChlsevavamgGLDGELGERGQNLSLGQR 769
Cdd:cd03255 81 rRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERV----------GLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 770 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 839
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
628-839 |
2.09e-30 |
|
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: 117.88 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAV 707
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSG-TIRENLDpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILC 786
Cdd:cd03230 78 LPEEPSLYENlTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 787 IDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:cd03230 119 LDEPTSGLDPESRREFWELL-RELKkeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
645-848 |
5.70e-30 |
|
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: 119.38 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFL-FSGTIRE-- 721
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRElv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 --------NLDPQGLHEDRAL-WQALEQCHLSEvavamggldgeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEAT 791
Cdd:COG1120 97 algryphlGLFGRPSAEDREAvEEALERTGLEH-----------LADRPvDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 792 ASVD---QKtdQLLQqtICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:COG1120 166 SHLDlahQL--EVLE--LLRRLArerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
644-853 |
2.25e-29 |
|
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: 117.15 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAEL---RS-QlavIPQepfLFS 716
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpphEIARLgigRTfQ---IPR---LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 G-TIRENLD-PQGLHEDRALWQALEQCHLSEV------AVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 788
Cdd:cd03219 89 ElTVLENVMvAAQARTGSGLLLARARREEREAreraeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 789 EATASV-DQKTDQLLqQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQPH 853
Cdd:cd03219 169 EPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-186 |
2.49e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.12 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAIT-------GELhRLCGwVAVSELS-----KGFGLATQEPWIQCATIRDNILFGK---TfDAQ 67
Cdd:COG1132 369 VALVGPSGSGKSTLVNLLLrfydptsGRI-LIDG-VDIRDLTleslrRQIGVVPQDTFLFSGTIRENIRYGRpdaT-DEE 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGVL 147
Cdd:COG1132 446 V-EEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE-ALIQEALERLM 523
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 148 SHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG1132 524 KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
628-853 |
2.85e-29 |
|
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: 117.02 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSG-TIREN--LDPQGLHEDRALWQ--ALEqchlsevAVAMGGLD-GELGER-GQNLSLGQRQLLCLARALLT 780
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKWPKEKIRerADE-------LLALVGLDpAEFADRyPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 781 DAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPSALRNQPH 853
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFkrLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
628-843 |
3.81e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.92 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ 704
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 705 LAVIPQE-PFLFSGTIREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALL 779
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENvalpLRVTGKSRKEIRRRVRE-------VLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 780 TDAKILCIDEATASVDQKT-DQLLQ--QTICKRfaNKTVLtIA-HRLNtILNS--DRVLVLQAGRVVELD 843
Cdd:COG2884 154 NRPELLLADEPTGNLDPETsWEIMEllEEINRR--GTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVRDE 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
628-841 |
7.74e-29 |
|
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: 114.88 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVdtsqlELAELRSQL 705
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFS-GTIREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLT 780
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalgLELQGVPKAEARERAEE-------LLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 781 DAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLN-TILNSDRVLVLQA--GRVVE 841
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
623-846 |
8.62e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.63 E-value: 8.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 623 LTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELR 702
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEP-FLFSGTIRENLDPQGLhEDRALWQALEQCHLSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTD 781
Cdd:PRK13632 83 KKIGIIFQNPdNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKV-GMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPS 846
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
635-840 |
1.35e-28 |
|
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: 112.91 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 635 LVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQepfl 714
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 fsgtirenldpqglhedralwqALEQCHLSEvavamggldgeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:cd03214 81 ----------------------ALELLGLAH-----------LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 794 VD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:cd03214 128 LDiahqIELLELLRRL--ARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
623-834 |
2.39e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 123.22 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 623 LTQGSVEFQDVVLVY--RPGLPNALDgVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE-------------------- 680
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 681 ----------------------------------PNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLdpQ 726
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI--K 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 727 GLHEDRALWQALEQCHLSEVAVAMGGL----DGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL 802
Cdd:PTZ00265 1318 FGKEDATREDVKRACKFAAIDEFIESLpnkyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270
....*....|....*....|....*....|....
gi 1039753393 803 QQTIC--KRFANKTVLTIAHRLNTILNSDRVLVL 834
Cdd:PTZ00265 1398 EKTIVdiKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
645-853 |
1.38e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.82 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFLFSG-TIR 720
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLD-PqgLHEDRALWQAlEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD 799
Cdd:cd03261 96 ENVAfP--LREHTRLSEE-EIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 800 QLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQPH 853
Cdd:cd03261 173 GVIDDLIrsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
628-853 |
1.90e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.72 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRpGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDtsqleLAELRSQLAV 707
Cdd:COG1121 7 IELENLTVSYG-GRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQepflfsgtiRENLDPQ-----------GL-----------HEDRAL-WQALEQCHLSEVAvamgglDGELGErgqnL 764
Cdd:COG1121 80 VPQ---------RAEVDWDfpitvrdvvlmGRygrrglfrrpsRADREAvDEALERVGLEDLA------DRPIGE----L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 765 SLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTIL-NSDRVLVLqAGRVVEL 842
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAH 219
|
250
....*....|.
gi 1039753393 843 DSPSALRNQPH 853
Cdd:COG1121 220 GPPEEVLTPEN 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
644-841 |
2.15e-27 |
|
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: 113.61 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQL---ELAELR-SQLAVIPQEPF--- 713
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLsekELRKIRgREIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 714 --LFsgTIRENL-DPQGLH--------EDRALwQALEQCHLSEVAvamggldgelgERGQN----LSLGQRQLLCLARAL 778
Cdd:COG0444 100 npVM--TVGDQIaEPLRIHgglskaeaRERAI-ELLERVGLPDPE-----------RRLDRypheLSGGMRQRVMIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 779 LTDAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:COG0444 166 ALEPKLLIADEPTTALDvtiQA--QILNllKDLQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-171 |
1.03e-26 |
|
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: 115.46 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF-DAQLYR 70
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadaDSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHT 150
Cdd:TIGR02857 430 EALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQGR 508
|
170 180
....*....|....*....|.
gi 1039753393 151 TRLLCTHRTEYLERADVVLLM 171
Cdd:TIGR02857 509 TVLLVTHRLALAALADRIVVL 529
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
629-847 |
1.29e-26 |
|
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: 109.19 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 629 EFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAEL---RSQL 705
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFL----------------FSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAmggldgelgeRGQNLSLGQR 769
Cdd:cd03256 81 GMIFQQFNLierlsvlenvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQ----------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 770 QLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTIL-NSDRVLVLQAGRVVeLDS 844
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKR-INREE-GITVIVSLHQVDLAReYADRIVGLKDGRIV-FDG 227
|
...
gi 1039753393 845 PSA 847
Cdd:cd03256 228 PPA 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-180 |
1.30e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 115.71 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITG-------------ELHRL--------CGWVAvselskgfglatQEPWIQCATIRDNILFG 61
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGflpyqgslkingiELRELdpeswrkhLSWVG------------QNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 KTF--DAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 139
Cdd:PRK11174 447 NPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 140 hRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 180
Cdd:PRK11174 526 -QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
628-841 |
4.34e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.17 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPN--ALDGVTFRVEPGEKLGIVGRTGSGKSSLfLVLFRLLE-PNAGRVLLDNVDTSQL---ELAEL 701
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTL-IRCINLLErPTSGSVLVDGVDLTALserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 702 RSQLAVIPQEPFLFSG-TIRENLdpqglhedrALwqALEQCHLSEVAVA--------MGGLDGELGERGQNLSLGQRQLL 772
Cdd:COG1135 81 RRKIGMIFQHFNLLSSrTVAENV---------AL--PLEIAGVPKAEIRkrvaelleLVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRsildLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-175 |
1.58e-25 |
|
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: 104.00 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILfgktfdaqlyre 71
Cdd:cd03228 31 VAIVGPSGSGKSTLLKLLLRLYdptsgeilidgVDLRDL-DLESLRKNIAYVPQDPFLFSGTIRENIL------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 vleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTT 151
Cdd:cd03228 98 -----------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEALRALAKGKT 147
|
170 180
....*....|....*....|....
gi 1039753393 152 RLLCTHRTEYLERADVVLLMEAGQ 175
Cdd:cd03228 148 VIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
592-837 |
1.60e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.21 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 592 SVERLEEYScDVPQEPHSQPLQSPHQQRIswlTQGSVEFQDVVLVyrpgLPNA---LDGVTFRVEPGEKLGIVGRTGSGK 668
Cdd:COG4178 331 TVDRLAGFE-EALEAADALPEAASRIETS---EDGALALEDLTLR----TPDGrplLEDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 669 SSLFLVLFRLLEPNAGRVLLDNVDtsqlelaelrsQLAVIPQEPFLFSGTIRENL---DPQGLHEDRALWQALEQCHLSE 745
Cdd:COG4178 403 STLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 746 VAvamGGLDGELgERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTI 825
Cdd:COG4178 472 LA---ERLDEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLA 547
|
250
....*....|..
gi 1039753393 826 LNSDRVLVLQAG 837
Cdd:COG4178 548 AFHDRVLELTGD 559
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
629-840 |
2.82e-25 |
|
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: 104.54 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 629 EFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqLELAELRSQLAVI 708
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 709 PQepflfsgtiRENLDPQ-----------GLHEDRALWQAL--EQCHLSEVAVAMGGLdGELGER--GQnLSLGQRQLLC 773
Cdd:cd03235 74 PQ---------RRSIDRDfpisvrdvvlmGLYGHKGLFRRLskADKAKVDEALERVGL-SELADRqiGE-LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 774 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNS-DRVLVLqAGRVV 840
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLL-NRTVV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
628-841 |
3.29e-25 |
|
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: 104.52 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSqLAV 707
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRN-IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSG-TIREN----LDPQGLHEDralwQALEQCHLsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:cd03259 77 VFQDYALFPHlTVAENiafgLKLRGVPKA----EIRARVRE---LLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 783 KILCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-186 |
7.22e-25 |
|
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: 104.16 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI-------TGEL----HRLCGwVAVSELSKGFGLATQEPWIQCATIRDNILFGKtFDAQLyRE 71
Cdd:cd03249 32 VALVGSSGCGKSTVVSLLerfydptSGEIlldgVDIRD-LNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK-PDATD-EE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD---VANHLLHRCILG 145
Cdd:cd03249 109 VEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQEALDRAMKG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 146 vlshTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03249 189 ----RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
644-850 |
7.69e-25 |
|
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: 103.67 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQEPFLFSG-TIRE 721
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NLdpqglhedRALWQALEQCHLSEVAVAMGGLDGELGER----GQNLSLGQRQLLCLARALLTDAKILCIDEATAS---- 793
Cdd:cd03224 95 NL--------LLGAYARRRAKRKARLERVYELFPRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGlapk 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 794 -VDQKTDQLlqQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRN 850
Cdd:cd03224 167 iVEEIFEAI--RELRDE--GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-186 |
1.75e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 102.69 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 1 MLVGIVGKVGCGKSSLLAAITgelhRLCGW--------------VAVSELSKGFGLATQEPWIQCATIRDNILFGK-TFD 65
Cdd:cd03254 30 ETVAIVGPTGAGKTTLINLLM----RFYDPqkgqilidgidirdISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRpNAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANhLLHRCILG 145
Cdd:cd03254 106 DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-LIQEALEK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 146 VLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03254 185 LMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
628-844 |
6.24e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.11 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLP--NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELR 702
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEpF--LFSGTIRENLdpqglhedrALwqALEQCHLSEVAV--------AMGGLdGELGER-GQNLSLGQRQL 771
Cdd:PRK11153 82 RQIGMIFQH-FnlLSSRTVFDNV---------AL--PLELAGTPKAEIkarvtellELVGL-SDKADRyPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 772 LCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 844
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRsileLLKD-INREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
644-852 |
6.58e-24 |
|
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: 102.34 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ-LAVIPQEPFLFSG-T 718
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASV 794
Cdd:cd03294 119 VLENvafgLEVQGVPRAEREERAAE-------ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 795 D-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:cd03294 192 DplirrEMQDELLR---LQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
644-840 |
8.27e-24 |
|
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: 100.52 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAVIPQEPFLFSG-TIREN 722
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 LDP-QGLH--EDRALWQALEqchlsEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD 799
Cdd:cd03266 99 LEYfAGLYglKGDELTARLE-----ELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 800 QLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:cd03266 173 RALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
628-838 |
8.37e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 99.18 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD--NVDTSQLELAELRSQL 705
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSG-TIRENldpqglhedralwqaleqchlsevaVAMGgldgelgergqnLSLGQRQLLCLARALLTDAKI 784
Cdd:cd03229 79 GMVFQDFALFPHlTVLEN-------------------------IALG------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 785 LCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGR 838
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
645-806 |
1.05e-23 |
|
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: 99.86 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAVIPQEPFLFSG-TIRENL 723
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 D-----PQGLHEDRALWQALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:COG4133 97 RfwaalYGLRADREAIDEALEAV----------GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
....*...
gi 1039753393 799 DQLLQQTI 806
Cdd:COG4133 167 VALLAELI 174
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
644-841 |
1.31e-23 |
|
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: 105.92 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFlfsG--- 717
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDPF---Gsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 -------TIRENLDPQGLHEDRA-----LWQALEqchlsEVavamgGLDGELGERGQN-LSLGQRQLLCLARALLTDAKI 784
Cdd:COG4172 377 prmtvgqIIAEGLRVHGPGLSAAerrarVAEALE-----EV-----GLDPAARHRYPHeFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 785 LCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTI--LnSDRVLVLQAGRVVE 841
Cdd:COG4172 447 LVLDEPTSALDvsvQA--QILDllRDLQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
644-852 |
1.50e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.50 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPF--L---- 714
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPYasLnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 -FSGTIRENLDPQGLH-----EDRALwQALEQChlsevavamgGLDGELGER-GQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:COG4608 113 tVGDIIAEPLRIHGLAskaerRERVA-ELLELV----------GLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 788 DEATASVD---QKtdQ---LLQ--QticKRFaNKTVLTIAHRLNT---IlnSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:COG4608 182 DEPVSALDvsiQA--QvlnLLEdlQ---DEL-GLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-186 |
1.77e-23 |
|
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: 100.00 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAIT-------GEL----HRLCGwVAVSELSKGFGLATQEPWIQCATIRDNILFGKtFDAQL--Y 69
Cdd:cd03251 31 VALVGPSGSGKSTLVNLIPrfydvdsGRIlidgHDVRD-YTLASLRRQIGLVSQDVFLFNDTVAENIAYGR-PGATReeV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHRCILGVLSH 149
Cdd:cd03251 109 EEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD-TESERLVQAALERLMKN 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 150 TTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03251 188 RTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
644-840 |
2.06e-23 |
|
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: 97.50 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQepflfsgtiren 722
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 ldpqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQL 801
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039753393 802 LQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:cd03216 122 FK--VIRRLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
644-841 |
2.54e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQEPFLFSG-TIRE 721
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NL----DPQ--GLHEDRALWQALEQcHLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:COG1129 99 NIflgrEPRrgGLIDWRAMRRRARE-LLARL-----GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 796 QK-TDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:COG1129 173 EReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
639-837 |
2.61e-23 |
|
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: 98.94 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 639 PGLPNaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQ----LAVIPQEPFL 714
Cdd:cd03290 12 SGLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 FSGTIRENLDPQGLHEDRALWQALEQCHLS-EVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039753393 794 VD-QKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAG 837
Cdd:cd03290 171 LDiHLSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-158 |
4.67e-23 |
|
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: 103.98 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGK--TFDAQLYR 70
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqDEVRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELWA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 eVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHT 150
Cdd:TIGR02868 444 -ALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGR 521
|
....*...
gi 1039753393 151 TRLLCTHR 158
Cdd:TIGR02868 522 TVVLITHH 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
645-846 |
9.74e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFL-FSGTIRE-- 721
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 --NLDPQGL---HEDRALWQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALL------TDAKILCIDEA 790
Cdd:PRK13548 98 amGRAPHGLsraEDDALVAAALAQVDLAHLA----------GRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 791 TASVDqktdqLLQQ----TICKRFANK---TVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPS 846
Cdd:PRK13548 168 TSALD-----LAHQhhvlRLARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
627-848 |
1.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD----NVDTSQLELA 699
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 700 ELRSQLAVIPQ--EPFLFSGTIRENLD--PQ--GLHEDRALWQALEQchLSEVavamgGLDGELGERGQ-NLSLGQRQLL 772
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEfgPKnfGFSEDEAKEKALKW--LKKV-----GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKT-DQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
580-848 |
1.33e-22 |
|
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: 104.64 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 580 VSSFTQTEammVSVERLEEYSCDVPQEPhsqplQSPHQQRISWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLG 659
Cdd:TIGR00957 597 ISSIVQAS---VSLKRLRIFLSHEELEP-----DSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVA 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 660 IVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlelaELRSQLAVIPQEPFLFSGTIREN-LDPQGLHEDRaLWQAL 738
Cdd:TIGR00957 669 VVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENiLFGKALNEKY-YQQVL 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 739 EQCHL-SEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ-LLQQTICKR--FANKT 814
Cdd:TIGR00957 735 EACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKhIFEHVIGPEgvLKNKT 814
|
250 260 270
....*....|....*....|....*....|....
gi 1039753393 815 VLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:TIGR00957 815 RILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-182 |
2.46e-22 |
|
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: 96.41 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAitgeLHRLcgwvavSELSKG--------------------FGLATQEPWIQCATIRDNI-LFG 61
Cdd:cd03244 33 VGIVGRTGSGKSSLLLA----LFRL------VELSSGsilidgvdiskiglhdlrsrISIIPQDPVLFSGTIRSNLdPFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 KTFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHR 141
Cdd:cd03244 103 EYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD-ALIQK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 142 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPP 182
Cdd:cd03244 181 TIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
627-846 |
2.55e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTS--QLELAEL 701
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 702 RSQLAVIPQEP--FLFSGTIRENLD--PQ--GLHEDRALWQALEqchlsevAVAMGGLDGE-LGERGQ-NLSLGQRQLLC 773
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAfgPInlGLSEEEIENRVKR-------AMNIVGLDYEdYKDKSPfELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 774 LARALLTDAKILCIDEATASVDQKT-DQLLQQ--TICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPS 846
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGrDEILNKikELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-853 |
6.31e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 96.26 E-value: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPNA---GRVLLDNVD--TSQLELAELRSQLAVIPQEPFLFS 716
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 GTIREN----LDPQGLHEDRAL----WQALEQCHL-SEVAvamgglDgELGERGQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:COG1117 106 KSIYDNvaygLRLHGIKSKSELdeivEESLRKAALwDEVK------D-RLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 788 DEATASVD----QKTDQLLQQtICKRFankTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSALRNQPH 853
Cdd:COG1117 179 DEPTSALDpistAKIEELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQIFTNPK 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-186 |
8.50e-22 |
|
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: 95.25 E-value: 8.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITG----ELHRLC------GWVAVSELSKGFGLATQEPWIQCATIRDNILFGKTfdAQLYRE 71
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRfyvpENGRVLvdghdlALADPAWLRRQVGVVLQENVLFNRSIRDNIALADP--GMSMER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLS 148
Cdd:cd03252 108 VIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHAIMRNMHDICA 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039753393 149 HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03252 187 GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
628-852 |
9.26e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 9.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL-ELAELRSQLA 706
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQEP-FLFSG-TIRENL--DPQGLhedraLWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLafGPENL-----CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 783 KILCIDEATASVDQKTDQLLQQTIcKRF--ANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERI-KKLheKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
628-846 |
1.23e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.85 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEP-FLFSGTIREN-----LDPQGLHED---RALWQALEQCHLSEVavamggLDGElgerGQNLSLGQRQLLCLARAL 778
Cdd:PRK13635 86 VFQNPdNQFVGATVQDdvafgLENIGVPREemvERVDQALRQVGMEDF------LNRE----PHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 779 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPS 846
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
645-839 |
5.17e-21 |
|
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: 92.61 E-value: 5.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElRSQLAVI--PQEPFLFSG-TIRE 721
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NLDP--QGLHEDRALWQA-----LEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASV 794
Cdd:cd03218 95 NILAvlEIRGLSKKEREEkleelLEEFHITHLR----------KSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753393 795 DQKTDQLLQQTIcKRFANKT--VLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:cd03218 165 DPIAVQDIQKII-KILKDRGigVLITDHNVRETLSiTDRAYIIYEGKV 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
628-839 |
6.90e-21 |
|
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: 92.09 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ 704
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 705 LAVIPQEPFLFSG-TIREN--LDPQGLHEDRALWQ-----ALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLAR 776
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENvaFALEVTGVPPREIRkrvpaALELV----------GLSHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 777 ALLTDAKILCIDEATASVDQKTD----QLLQQtICKRFANKTVLTIAHRL-NTIlnSDRVLVLQAGRV 839
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKK-INKAGTTVVVATHAKELvDTT--RHRVIALERGKL 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
627-851 |
7.24e-21 |
|
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: 93.77 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYRPGLPNaldgVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlelaELRSQLA 706
Cdd:cd03291 39 NLFFSNLCLVGAPVLKN----INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQEPFLFSGTIRENLdPQGLHEDRALWQA-LEQCHLSEVAVAMGGLDGE-LGERGQNLSLGQRQLLCLARALLTDAKI 784
Cdd:cd03291 102 FSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTvLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 785 LCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:cd03291 181 YLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
645-848 |
1.86e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEP-FLFSGTIREN- 722
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGATVEDd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 ----LDPQGL-HED--RALWQALEqchlsevAVAMGGLDGELGERgqnLSLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:PRK13650 103 vafgLENKGIpHEEmkERVNEALE-------LVGMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 796 QKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK13650 173 PEGRLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-195 |
1.89e-20 |
|
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: 96.36 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVS-----ELSKGFGLATQEPWIQCATIRDNI-LFGKTfDAQlyrE 71
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSqwdreELGRHIGYLPQDVELFDGTIAENIaRFGDA-DPE---K 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA--DVAnhlLHRCILG 145
Cdd:COG4618 437 VVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDegEAA---LAAAIRA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 146 VLSH-TTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPTA 195
Cdd:COG4618 513 LKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-186 |
2.10e-20 |
|
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: 91.14 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLL-------------AAITGELHRLcgwVAVSELSKGFGLATQEPWIQCATIRDNILFGK--TFDAQ 67
Cdd:cd03253 30 VAIVGPSGSGKSTILrllfrfydvssgsILIDGQDIRE---VTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRpdATDEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVL 147
Cdd:cd03253 107 VI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT-HTEREIQAALRDVS 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 148 SHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03253 185 KGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
643-847 |
2.57e-20 |
|
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: 90.96 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 643 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLA--VIPQEPFLFSG 717
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARHVgfVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 TIREN----LDPQGLHEDRALWQALeqchLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:COG4181 106 TALENvmlpLELAGRRDARARARAL----LERV-----GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 794 VDQKT-----DQLLQQTickRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSA 847
Cdd:COG4181 177 LDAATgeqiiDLLFELN---RERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
644-840 |
6.15e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD----NVDTSQlelAELRSQLAVIPQEPFLFSG-T 718
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvRIRSPR---DAIALGIGMVHQHFMLVPNlT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IRENL-----DPQGLHEDRAlwQALEQchLSEVAVAMGgLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAs 793
Cdd:COG3845 97 VAENIvlglePTKGGRLDRK--AARAR--IRELSERYG-LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 794 V--DQKTDQLLQqtICKRFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV 840
Cdd:COG3845 171 VltPQEADELFE--ILRRLAAegKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-181 |
6.59e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.39 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAI-------TGE-------LHRLcgwvAVSELSKGFGLATQEPWIQCATIRDNILFGKTfDA- 66
Cdd:PRK10789 343 MLGICGPTGSGKSTLLSLIqrhfdvsEGDirfhdipLTKL----QLDSWRSRLAVVSQTPFLFSDTVANNIALGRP-DAt 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 67 -QLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcilg 145
Cdd:PRK10789 418 qQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN---- 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039753393 146 vLS----HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGP 181
Cdd:PRK10789 494 -LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
645-852 |
9.62e-20 |
|
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: 89.32 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSqlELAELRSQLAVIPQEPFLFSG-TIRENL 723
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DpQGL---HEDRAlwQALEQCHlsEVAvAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 800
Cdd:cd03299 93 A-YGLkkrKVDKK--EIERKVL--EIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 801 LLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:cd03299 167 KLREELKKirKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
630-851 |
1.53e-19 |
|
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: 94.59 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 630 FQDVVLVYRPGLPNaldgVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlelaELRSQLAVIP 709
Cdd:TIGR01271 431 FSNFSLYVTPVLKN----ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 710 QEPFLFSGTIRENLdPQGLHEDRALWQA-LEQCHLSEVAVAMGGLDGE-LGERGQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:TIGR01271 494 QTSWIMPGTIKDNI-IFGLSYDEYRYTSvIKACQLEEDIALFPEKDKTvLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 788 DEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:TIGR01271 573 DSPFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
648-834 |
1.92e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.33 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 648 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENL--- 723
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 ----------------------------------------------DPQGLHEDRALWQALEQCHLSEVAVAM------- 750
Cdd:PTZ00265 484 lyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVSKKVlihdfvs 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 751 ---GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTI 825
Cdd:PTZ00265 564 alpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTI 643
|
....*....
gi 1039753393 826 LNSDRVLVL 834
Cdd:PTZ00265 644 RYANTIFVL 652
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
42-176 |
1.98e-19 |
|
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: 87.91 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 42 LATQEPWIQCATIRDNILFG-KTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKAL 120
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 121 YLLDDPLAAVDADvANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 176
Cdd:cd03248 172 LILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
638-852 |
3.77e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 638 RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS----QLAVIPQEPF 713
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 714 LFSGTIRenLDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:PRK10070 117 LMPHMTV--LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 794 VDQKTDQLLQQTICKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
628-821 |
5.08e-19 |
|
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: 84.90 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnvdtsqlELAElRSQLAV 707
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPE-GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSGTIRENLdpqglhedRALWQaleqchlsevavamggldgelgergQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:cd03223 69 LPQRPYLPLGTLREQL--------IYPWD-------------------------DVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 1039753393 788 DEATASVDQKTDQLLQQTICKRFAnkTVLTIAHR 821
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
628-840 |
5.29e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.18 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPglPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtSQLElAELRSQLAV 707
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLD-IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSG-TIRENL----DPQGLHEDRALWQA---LEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALL 779
Cdd:cd03269 75 LPEERGLYPKmKVIDQLvylaQLKGLKKEEARRRIdewLERLELSEYA----------NKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 780 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-180 |
6.03e-19 |
|
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: 85.06 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE---------LSKGFGLATQEPWIQCATIRDNIlfgktfdaqlyrevl 73
Cdd:cd03247 31 IALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekaLSSLISVLNQRPYLFDTTLRNNL--------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 74 eacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhRCILGVLSHTTRL 153
Cdd:cd03247 96 -----------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLI 151
|
170 180
....*....|....*....|....*..
gi 1039753393 154 LCTHRTEYLERADVVLLMEAGQLVRTG 180
Cdd:cd03247 152 WITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-185 |
6.35e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.09 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSE-----LSKGFGLATQEPWIQCATIRDNILFGKTF--DAQL 68
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLqnlyqptGGQV--LLDGVPLVQydhhyLHRQVALVGQEPVLFSGSVRENIAYGLTDtpDEEI 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 YREVLEACAlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVaNHLLH--RCILGv 146
Cdd:TIGR00958 588 MAAAKAANA-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQesRSRAS- 664
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 147 lshTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:TIGR00958 665 ---RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
652-840 |
2.84e-18 |
|
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: 84.47 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 652 VEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLAVIPQEPFLFSG-TIRENLdpqGLHE 730
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNV---GLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 731 DRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ---TIC 807
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlvlDLH 175
|
170 180 190
....*....|....*....|....*....|....
gi 1039753393 808 KRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:cd03298 176 AETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
627-848 |
3.23e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLvyrpglpnaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLA 706
Cdd:PRK09536 10 SVEFGDTTV---------LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQE---PFLFSG-TI--------RENLDPQGLHEDRALWQALEQCHLSEVAvamgglDGELGErgqnLSLGQRQLLCL 774
Cdd:PRK09536 81 SVPQDtslSFEFDVrQVvemgrtphRSRFDTWTETDRAAVERAMERTGVAQFA------DRPVTS----LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 775 ARALLTDAKILCIDEATASVDQKtDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDIN-HQVRTLELVRRLVDdgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADV 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
645-843 |
3.95e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelRSQLAVIPQEPFLFSG-TIRENL 723
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DpQGLHEDRALWQALEQC-----HLSEVAVAMGGLDGELGERG--------------------------QNLSLGQRQLL 772
Cdd:COG0488 83 L-DGDAELRALEAELEELeaklaEPDEDLERLAELQEEFEALGgweaearaeeilsglgfpeedldrpvSELSGGWRRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANkTVLTIAHrlntilnsDRVLvLQ--AGRVVELD 843
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL-KNYPG-TVLVVSH--------DRYF-LDrvATRILELD 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
628-845 |
5.43e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEP-FLFSGTIRENLDPQGL------HED--RALWQALEQCHLSEVAvamgglDGElgerGQNLSLGQRQLLCLARAL 778
Cdd:PRK13648 88 VFQNPdNQFVGSIVKYDVAFGLenhavpYDEmhRRVSEALKQVDMLERA------DYE----PNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 779 LTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 845
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
644-795 |
8.12e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.96 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD--NVDTSQLELAELRSQLAVIPQEPFLFSG-TIR 720
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglKLTDDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 EN--LDP---QGLHEDRALWQALEqcHLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:cd03262 95 ENitLAPikvKGMSKAEAEERALE--LLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
645-840 |
1.31e-17 |
|
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: 81.83 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLF-RLLEPNA-GRVLLDNVdtsQLELAELRSQLAVIPQEPFLFSG-TIRE 721
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVsGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NLDpqglhedralwqaleqchlseVAVAMGGLDGelgergqnlslGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 801
Cdd:cd03213 102 TLM---------------------FAAKLRGLSG-----------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 802 LQQTIcKRFA--NKTVLTIAHRL-NTILNS-DRVLVLQAGRVV 840
Cdd:cd03213 150 VMSLL-RRLAdtGRTIICSIHQPsSEIFELfDKLLLLSQGRVI 191
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
334-596 |
1.60e-17 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 84.47 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 334 AASNGTADVH----FYLIVYATIAGVNSLCTL--LRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFS 407
Cdd:cd18600 55 SSSNTYAVIVtftsSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 408 SDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLAD 487
Cdd:cd18600 135 KDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 488 TLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLVLS 567
Cdd:cd18600 215 SLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILT 291
|
250 260
....*....|....*....|....*....
gi 1039753393 568 YALSLTGLLSGLVSSFTQTEAMMVSVERL 596
Cdd:cd18600 292 LAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
624-841 |
1.71e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 624 TQGSVEFQDVVLVYrPGLpNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTS-QLELAELR 702
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQE----PFLfsgTIRENLD----PQG---LHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQL 771
Cdd:PRK11288 79 AGVAIIYQElhlvPEM---TVAENLYlgqlPHKggiVNRRLLNYEAREQ--LEHL-----GVDIDPDTPLKYLSIGQRQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 772 LCLARALLTDAKILCIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
644-840 |
1.79e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQL--AVIPQEPFLFSG-TIR 720
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLdPQGLHEDRALW--QALEQCHLSEVAVAMG---GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:PRK09700 99 ENL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLlrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039753393 796 QK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:PRK09700 178 NKeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-186 |
1.94e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.80 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAIT-------GEL----HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGK--TFDAQLy 69
Cdd:PRK11160 369 VALLGRTGCGKSTLLQLLTrawdpqqGEIllngQPIADY-SEAALRQAISVVSQRVHLFSATLRDNLLLAApnASDEAL- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhRCILGVLSH 149
Cdd:PRK11160 447 IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-ELLAEHAQN 524
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 150 TTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK11160 525 KTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
649-848 |
2.12e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.11 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 649 TFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElRSqLAVIPQEPFLFSG-TIREN----L 723
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DPqGLHEDRALWQALEQchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD----QKTD 799
Cdd:COG3840 97 RP-GLKLTAEQRAQVEQ------ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 800 QLLQQtICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:COG3840 170 DLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
645-846 |
2.83e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG-TIRE-- 721
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRElv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 --------NLDPQGLHEDRAL-WQALEQCHLSEVAVamggldgelgERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PRK11231 98 aygrspwlSLWGRLSAEDNARvNQAMEQTRINHLAD----------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 793 SVD-------QKTDQLLQQtickrfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPS 846
Cdd:PRK11231 168 YLDinhqvelMRLMRELNT------QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPE 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
627-848 |
3.25e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVD-TSQ---LELA 699
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 700 ELRSQLAVIPQ--EPFLFSGTIRENL--DPQ--GLHEDRALWQALEQchlsevaVAMGGLDGELGERGQ-NLSLGQRQLL 772
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVafGPQnfGVSQEEAEALAREK-------LALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKTDQLLqQTICKRF--ANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
644-852 |
3.41e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 81.51 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAelRSQLAVIPQEPFLFSG-TIREN 722
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 ----LDPQGLHEDRALWQALEQCHLsevaVAMGGLdgeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:cd03300 93 iafgLRLKKLPKAEIKERVAEALDL----VQLEGY---ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 799 DQLLQQTIcKRFANK---TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:cd03300 166 RKDMQLEL-KRLQKElgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-189 |
4.06e-17 |
|
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: 80.98 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFGKTF----DAQ 67
Cdd:cd03293 32 FVALVGPSGCGKSTLLRIIAGLERptsgevLVDG-EPVTGPGPDRGYVFQQdallPW---LTVLDNVALGLELqgvpKAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHlLHR 141
Cdd:cd03293 108 ARERAEELLEL--------------VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ-LQE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 142 CILGVLSHT--TRLLCTHRTE---YLerADVVLLMeagqlvrTGPPSEILPLV 189
Cdd:cd03293 173 ELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVL-------SARPGRIVAEV 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
628-851 |
4.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.48 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEP--FLFSGTIRENL--DPQGLHEDRAlwQALEQCHLSEVAVAMggldGELGERG-QNLSLGQRQLLCLARALLTDA 782
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVafGPVNMGLDKD--EVERRVEEALKAVRM----WDFRDKPpYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 783 KILCIDEATASVDQKTDQLLqQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETL-MEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2-128 |
5.00e-17 |
|
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: 78.84 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWV----------AVSELSKGFGLATQEPWIQCA-TIRDNILFG--------K 62
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddERKSLRKEIGYVFQDPQLFPRlTVRENLRLGlllkglskR 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 63 TFDAQLYrEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 128
Cdd:pfam00005 93 EKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
654-840 |
5.25e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 86.37 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 654 PGEKLGIV-GRTGSGKSSLFLVLFRLLEPNAGRVLldnvdtsqlelAElRSqLAVIPQEPFLFSGTIRENL---DPqglh 729
Cdd:PTZ00243 684 PRGKLTVVlGATGSGKSTLLQSLLSQFEISEGRVW-----------AE-RS-IAYVPQQAWIMNATVRGNIlffDE---- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 730 EDRA-LWQALEQCHL-SEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL-QQTI 806
Cdd:PTZ00243 747 EDAArLADAVRVSQLeADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVvEECF 826
|
170 180 190
....*....|....*....|....*....|....
gi 1039753393 807 CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 840
Cdd:PTZ00243 827 LGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
628-848 |
6.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVY-RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLA 706
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQEP-FLFSGTIREN-----LDPQGLHEDRALWQaleqchLSEVAVAMGGLDGELGERGQnLSLGQRQLLCLARALLT 780
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDdvafgMENQGIPREEMIKR------VDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 781 DAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
637-836 |
6.82e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 637 YRPGLPNALDGVTFRVEPGE-KLgIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLF 715
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEfKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 716 SGTIRENL-----------DPQGLHEDRALWqaleqchlsevavamgGLDGELGERGQN-LSLGQRQLLCLARALLTDAK 783
Cdd:PRK10247 94 GDTVYDNLifpwqirnqqpDPAIFLDDLERF----------------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 784 ILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQA 836
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-180 |
7.77e-17 |
|
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: 80.26 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGeLHRLCG---------WVAVSELSKGFGLATQE----PWIqcaTIRDNILFG----KTF 64
Cdd:cd03259 28 FLALLGPSGCGKTTLLRLIAG-LERPDSgeilidgrdVTGVPPERRNIGMVFQDyalfPHL---TVAENIAFGlklrGVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 DAQLYREVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcIL 144
Cdd:cd03259 104 KAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREE-LK 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 145 GVLS--HTTRLLCTH-RTEYLERADVVLLMEAGQLVRTG 180
Cdd:cd03259 175 ELQRelGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-186 |
8.78e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.80 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAitgeLHRlcgwvaVSELSKG-----------FGLAT---------QEPWIQCATIRDNI-LFG 61
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNA----LFR------IVELEKGrimiddcdvakFGLTDlrrvlsiipQSPVLFSGTVRFNIdPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 KTFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVaNHLLHR 141
Cdd:PLN03232 1335 EHNDADLW-EALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQR 1412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753393 142 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-185 |
9.50e-17 |
|
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: 80.46 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQE-PWIQCATIRDNILFG----------- 61
Cdd:cd03296 30 LVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedATDVPvqeRNVGFVFQHyALFRHMTVFDNVAFGlrvkprserpp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL--- 138
Cdd:cd03296 110 EAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELrrw 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 139 ---LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03296 179 lrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
645-841 |
1.19e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE--PNA---GRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG-T 718
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IRENLdPQGLH-----------EDRALWqALEQCHLSEvavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:PRK14247 99 IFENV-ALGLKlnrlvkskkelQERVRW-ALEKAQLWD------EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 788 DEATASVDQKTDQLLQQTICKRFANKTVLTIAH------RLntilnSDRVLVLQAGRVVE 841
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
628-840 |
1.26e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV---LLDNVDTSQLELAE- 700
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 701 --------------------LRSQLAVIPQ--EPFLFSGTIRENL--DPQ--GLHEDRALWQALEQchlsevaVAMGGLD 754
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIifGPVsmGVSKEEAKKRAAKY-------IELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 755 GELGERGQ-NLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQqtICKRF--ANKTVLTIAHRLNTILN-SD 829
Cdd:PRK13651 156 ESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILE--IFDNLnkQGKTIILVTHDLDNVLEwTK 233
|
250
....*....|.
gi 1039753393 830 RVLVLQAGRVV 840
Cdd:PRK13651 234 RTIFFKDGKII 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
645-852 |
1.43e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE------PNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSG- 717
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 TIREN----LDPQGLHEDRALWQALEQChLSEVAVAMGGLDgELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:PRK14246 106 SIYDNiaypLKSHGIKEKREIKKIVEEC-LRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 794 VDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
627-852 |
1.66e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 79.69 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLA 706
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQEPFLFSG-TIRENLdPQGLHEDRALWQALEQCHLSEVA--VAMGGLDGeLGERGQN-LSLGQRQLLCLARALLTDA 782
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV-AFGLRVKPRSERPPEAEIRAKVHelLKLVQLDW-LADRYPAqLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 783 KILCIDEATASVDQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-174 |
2.03e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 80.13 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFG-------KTFD 65
Cdd:COG1116 40 VALVGPSGCGKSTLLRLIAGLEKptsgevLVDG-KPVTGPGPDRGVVFQEpallPW---LTVLDNVALGlelrgvpKAER 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHlLHRCILG 145
Cdd:COG1116 116 RERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLR 183
|
170 180 190
....*....|....*....|....*....|....
gi 1039753393 146 VL--SHTTRLLCTHRTE---YLerADVVLLMEAG 174
Cdd:COG1116 184 LWqeTGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
645-806 |
3.38e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTsqlELAELRSQLAVI----PQEPFLfsgTIR 720
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLghrnAMKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLdpqglhedrALWQALEQCHLSEVAVAMG--GLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEavGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*...
gi 1039753393 799 DQLLQQTI 806
Cdd:PRK13539 163 VALFAELI 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-182 |
9.96e-16 |
|
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: 76.68 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrE 71
Cdd:cd03369 37 IGIVGRTGAGKSTLILALfrfleaeEGKIEidgIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIY-G 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEacalnddlsilpagdqteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTT 151
Cdd:cd03369 116 ALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIREEFTNST 176
|
170 180 190
....*....|....*....|....*....|.
gi 1039753393 152 RLLCTHRTEYLERADVVLLMEAGQLVRTGPP 182
Cdd:cd03369 177 ILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
628-846 |
1.31e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNV----DTSQLELAE 700
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 701 LRSQLAVIPQEP--FLFSGTIRENL--DPQ--GLHEDRALWQALEQchlsevaVAMGGLDGELGERGQ-NLSLGQRQLLC 773
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQnfGIPKEKAEKIAAEK-------LEMVGLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 774 LARALLTDAKILCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPS 846
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
632-839 |
1.37e-15 |
|
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: 75.55 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 632 DVVLVYRP-GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQ-LAVIP 709
Cdd:cd03215 2 EPVLEVRGlSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 710 QEPF---LFSG-TIRENLdpqglhedralwqALEQcHLSevavamGGldgelgergqNLslgqrQLLCLARALLTDAKIL 785
Cdd:cd03215 82 EDRKregLVLDlSVAENI-------------ALSS-LLS------GG----------NQ-----QKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 786 CIDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLI-RELAdaGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-211 |
1.59e-15 |
|
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: 80.33 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGEL---HRLCGWVAV----------SELSKGFGLATQEPWIQ--CATIRDNILFG----KT 63
Cdd:COG1123 35 VALVGESGSGKSTLALALMGLLphgGRISGEVLLdgrdllelseALRGRRIGMVFQDPMTQlnPVTVGDQIAEAlenlGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHR-C 142
Cdd:COG1123 115 SRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLlR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 143 ILGVLSHTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEILPLVQ---AVPTAWAEKEQVATSGQSPSV 211
Cdd:COG1123 187 ELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAAAEP 259
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-176 |
2.18e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.03 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLL-------AAITGELhrLCGWVAVSELSKGFGLATQE----PWiqcATIRDNI---LFGKTFDAQL 68
Cdd:PRK11247 41 VAVVGRSGCGKSTLLrllagleTPSAGEL--LAGTAPLAEAREDTRLMFQDarllPW---KKVIDNVglgLKGQWRDAAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 yrEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV---ANHLLHRciLG 145
Cdd:PRK11247 116 --QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrieMQDLIES--LW 180
|
170 180 190
....*....|....*....|....*....|..
gi 1039753393 146 VLSHTTRLLCTHR-TEYLERADVVLLMEAGQL 176
Cdd:PRK11247 181 QQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
628-840 |
2.33e-15 |
|
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: 76.66 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVY--RPglpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV--LLDNvDTSQLELAELRS 703
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGE-RRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 704 QLAVI-P--QEPFLFSGTIRE--------------NLDPQglHEDRAlWQALEQCHLSEVAvamggldgelGERGQNLSL 766
Cdd:COG1119 79 RIGLVsPalQLRFPRDETVLDvvlsgffdsiglyrEPTDE--QRERA-RELLELLGLAHLA----------DRPFGTLSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 767 GQRQLLCLARALLTDAKILCIDEATASVDQK-TDQLLQ--QTICKRFAnKTVLTIAHRLNTILNS-DRVLVLQAGRVV 840
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLAllDKLAAEGA-PTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
582-841 |
2.53e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 582 SFTQTEAMMVSVERLeeYSCDVPQEPhSQPLQSPHQQRISWLTQGSvefqdvvlvyRPGLPNaldgVTFRVEPGEKLGIV 661
Cdd:PLN03232 587 SLQRIEELLLSEERI--LAQNPPLQP-GAPAISIKNGYFSWDSKTS----------KPTLSD----INLEIPVGSLVAIV 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 662 GRTGSGKSSLFLVLFRLLEPnagrvlldnVDTSQLELaelRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQC 741
Cdd:PLN03232 650 GGTGEGKTSLISAMLGELSH---------AETSSVVI---RGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 742 HLSEVAVAMGGLD-GELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQLLQQTICKRFANKTVLTIA 819
Cdd:PLN03232 718 ALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVT 797
|
250 260
....*....|....*....|..
gi 1039753393 820 HRLNTILNSDRVLVLQAGRVVE 841
Cdd:PLN03232 798 NQLHFLPLMDRIILVSEGMIKE 819
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-186 |
2.65e-15 |
|
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: 76.22 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELH------RLCGWV----AVSELSKGFGLATQEPWIQ--CATIRDNILFG--------K 62
Cdd:COG1122 30 VAIIGPNGSGKSTLLRLLNGLLKptsgevLVDGKDitkkNLRELRRKVGLVFQNPDDQlfAPTVEEDVAFGpenlglprE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 63 TFDAQLyREVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLH 140
Cdd:COG1122 110 EIRERV-EEALELVGLEHlaDRPPH-------------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753393 141 rcILGVL--SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG1122 176 --LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
644-841 |
2.70e-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: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA----GRVLLDNVDTSQLELAELR----SQLAVIPQEPF-- 713
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRrirgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 714 ---LFS-GT-IRENLDP-QGLHEDRALWQALEQchLSEVavamgGL-DGE--LGERGQNLSLGQRQLLCLARALLTDAKI 784
Cdd:COG4172 105 lnpLHTiGKqIAEVLRLhRGLSGAAARARALEL--LERV-----GIpDPErrLDAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 785 LCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:COG4172 178 LIADEPTTALDvtvQA--QILDllKDLQREL-GMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
628-840 |
2.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.20 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQL 705
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEP--FLFSGTIRENLD----PQGLHEDralwqalEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALL 779
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgavNLKLPED-------EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 780 TDAKILCIDEATASVDQK-TDQLLQqtICKRFANKTVLTI---AHRLNTI-LNSDRVLVLQAGRVV 840
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMgVSEIMK--LLVEMQKELGLTIiiaTHDIDIVpLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
628-852 |
2.99e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQLELAELRSQ 704
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 705 LAVIPQEP-FLFSGTIRENLDPQGLhEDRALWQALEQCHLSEVAVAMGGLDGELGERgQNLSLGQRQLLCLARALLTDAK 783
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 784 ILCIDEATASVDQK-TDQLLQqtICKRFANK---TVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK13640 164 IIILDESTSMLDPAgKEQILK--LIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-176 |
3.38e-15 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 75.24 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSELSKGFGLATQEP-WIQcATIRDNILF-----GKTFDA 66
Cdd:COG4619 29 VAITGPSGSGKSTLLRALadldpptSGEIYldgKPLSAMPPPEWRRQVAYVPQEPaLWG-GTVRDNLPFpfqlrERKFDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 67 QLYREVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGV 146
Cdd:COG4619 108 ERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RRVEELLREY 176
|
170 180 190
....*....|....*....|....*....|...
gi 1039753393 147 LSH--TTRLLCTHRTEYLER-ADVVLLMEAGQL 176
Cdd:COG4619 177 LAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
654-840 |
4.02e-15 |
|
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: 75.02 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 654 PGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNV---DTSQ-LELAELRSQLAVIPQEPFLFSG-TIRENLDpQGL 728
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLA-FGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 729 hedRALWQALEQCHLSEVAVAMGgLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK 808
Cdd:cd03297 101 ---KRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1039753393 809 RFA--NKTVLTIAHRLNTI-LNSDRVLVLQAGRVV 840
Cdd:cd03297 177 IKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-198 |
4.07e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.17 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI--TGELHRLCGWV--------AVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrE 71
Cdd:PLN03130 1268 VGIVGRTGAGKSSMLNALfrIVELERGRILIdgcdiskfGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-E 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTT 151
Cdd:PLN03130 1347 SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCT 1425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 152 RLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILP--------LVQAVPTAWAE 198
Cdd:PLN03130 1426 MLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnegsafskMVQSTGAANAQ 1480
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
635-849 |
4.18e-15 |
|
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: 75.10 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 635 LVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAVIPQEPFL 714
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 FSG-TIRENLDPQGlhedrAL----WQALEQcHLSEVAVAMGGLDGElGERGQNLSLGQRQLLCLARALLTDAKILCIDE 789
Cdd:cd03265 85 DDElTGWENLYIHA-----RLygvpGAERRE-RIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 790 ATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTI-LNSDRVLVLQAGRVVELDSPSALR 849
Cdd:cd03265 158 PTIGLDPQTrAHVWEyiEKLKEEF-GMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
627-851 |
7.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVD----TSQLELA 699
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 700 ELRSQLAVIPQ--EPFLFSGTI-RENL-DPQGLHEDralwqaleqchLSEVAVAMGGLDGELGERGQNLSL-------GQ 768
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVeREIIfGPKNFKMN-----------LDEVKNYAHRLLMDLGFSRDVMSQspfqmsgGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 769 RQLLCLARALLTDAKILCIDEATASVDQKT-DQLLqqTICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 843
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSkRQVM--RLLKSLQtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
....*...
gi 1039753393 844 SPSALRNQ 851
Cdd:PRK13646 229 SPKELFKD 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-175 |
7.69e-15 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 74.43 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQ--CATIRDNILFG-------KT 63
Cdd:cd03225 30 VLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkELRRKVGLVFQNPDDQffGPTVEEEVAFGlenlglpEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcI 143
Cdd:cd03225 110 EIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--L 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1039753393 144 LGVL--SHTTRLLCTHRTEYLER-ADVVLLMEAGQ 175
Cdd:cd03225 177 LKKLkaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-180 |
8.46e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.46 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAitgeLHRL--------------CGWVAVSELSKGFGLATQEPWIQCATIRDNILFGKT--FDA 66
Cdd:PRK13657 364 VAIVGPTGAGKSTLINL----LQRVfdpqsgrilidgtdIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 67 QLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGV 146
Cdd:PRK13657 440 EM-RAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-ETEAKVKAALDEL 517
|
170 180 190
....*....|....*....|....*....|....
gi 1039753393 147 LSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 180
Cdd:PRK13657 518 MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-175 |
8.87e-15 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 72.66 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGwvavselskgfglatqepwiqcatirdNILFGKTFDAQLYREvleacALNDD 81
Cdd:cd00267 27 IVALVGPNGSGKSTLLRAIAGLLKPTSG---------------------------EILIDGKDIAKLPLE-----ELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 LSILPagdQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGVL-SHTTRLLCTHRTE 160
Cdd:cd00267 75 IGYVP---Q---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVIIVTHDPE 141
|
170
....*....|....*.
gi 1039753393 161 YLERA-DVVLLMEAGQ 175
Cdd:cd00267 142 LAELAaDRVIVLKDGK 157
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-186 |
8.88e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELS-----KGFGLATQEPWIQCATIRDNILFGKTFDAQLYREV 72
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrPLSSLShsvlrQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 73 LEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTR 152
Cdd:PRK10790 450 LETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTL 528
|
170 180 190
....*....|....*....|....*....|....
gi 1039753393 153 LLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-185 |
9.08e-15 |
|
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: 74.52 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 1 MLVGIVGKVGCGKSSLL------------AAITGELH----RLCGW-VAVSELSKGFGLATQEPWIQCATIRDNILFG-- 61
Cdd:cd03260 27 EITALIGPSGCGKSTLLrllnrlndlipgAPDEGEVLldgkDIYDLdVDVLELRRRVGMVFQKPNPFPGSIYDNVAYGlr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 ------KTFDAQLYREVLEACALNDDLSilpagDQTevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVA 135
Cdd:cd03260 107 lhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP-IS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 136 NHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03260 177 TAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
2-180 |
9.83e-15 |
|
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: 73.87 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-----ELSKGFGLATQEPWI-----QCA-----TIRDNILFGKTF-- 64
Cdd:cd03297 25 VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKKINLPPQQRKIglvfqQYAlfphlNVRENLAFGLKRkr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 ---DAQLYREVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLH 140
Cdd:cd03297 105 nreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 141 --RCILGVLsHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 180
Cdd:cd03297 173 elKQIKKNL-NIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
639-852 |
1.09e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 639 PGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDT---SQLELAELRSQLAVIPQEPFlf 715
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 716 sgtirENLDP-----QGLHEDRALWQALEQCHLSEVAVAMG---GLDGELGERGQNL-SLGQRQLLCLARALLTDAKILC 786
Cdd:PRK11308 103 -----GSLNPrkkvgQILEEPLLINTSLSAAERREKALAMMakvGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 787 IDEATASVD-----QKTDQL--LQQTIckrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK11308 178 ADEPVSALDvsvqaQVLNLMmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
635-804 |
1.30e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 635 LVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDnvdtsQLELAELRSQlaviPQEPFL 714
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN-----GTPLAEQRDE----PHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 FSG---------TIRENLD---PQGLHEDRALWQALEQChlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:TIGR01189 77 YLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAV----------GLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180
....*....|....*....|..
gi 1039753393 783 KILCIDEATASVDQKTDQLLQQ 804
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAG 168
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-186 |
1.35e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.95 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELS---KGFGLATQEPwiqcA-----TIRDNILFG----KT 63
Cdd:COG1118 30 LVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLFTNLPpreRRVGFVFQHY----AlfphmTVAENIAFGlrvrPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEacaLnddLSIL---------PAgdQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 134
Cdd:COG1118 106 SKAEIRARVEE---L---LELVqlegladryPS--Q---------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 135 ANHL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG1118 169 RKELrrwlrrLHDEL-----GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
609-852 |
1.98e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 609 SQPLQSPHQQRISWLTQGSVefQDVVlvyrpglpnalDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePN------ 682
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTV--RTVV-----------NDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvyp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 683 ------AGRVLLDnvdTSQLELAELR-SQLAVIPQEPfLFSGTIRENLDPQgLHEDRALWQALEQchlsEVAVA--MGGL 753
Cdd:PRK15134 68 sgdirfHGESLLH---ASEQTLRGVRgNKIAMIFQEP-MVSLNPLHTLEKQ-LYEVLSLHRGMRR----EAARGeiLNCL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 754 D--------GELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD----QLLQQTicKRFANKTVLTIAHR 821
Cdd:PRK15134 139 DrvgirqaaKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLREL--QQELNMGLLFITHN 216
|
250 260 270
....*....|....*....|....*....|..
gi 1039753393 822 LNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK15134 217 LSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
644-852 |
2.01e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL---DNVDTSQLELAELRSQLAVIPQEPfLFSgtir 720
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDP-LAS---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 enLDPQGLHED------RALWQALEQCHLSEVAVAM----GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEA 790
Cdd:PRK15079 111 --LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkvGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 791 TASVD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK15079 189 VSALDvsiqAQVVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-176 |
2.14e-14 |
|
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: 71.86 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILfgktfdaqlyrev 72
Cdd:cd03246 31 LAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpNELGDHVGYLPQDDELFSGSIAENIL------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 73 leacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTR 152
Cdd:cd03246 98 ----------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATR 149
|
170 180
....*....|....*....|....
gi 1039753393 153 LLCTHRTEYLERADVVLLMEAGQL 176
Cdd:cd03246 150 IVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
644-838 |
2.29e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNA---GRVLLD-------NV-DTSQLELAELRSQLAVIPQEp 712
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEgeelqasNIrDTERAGIAIIHQELALVKEL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 713 flfsgTIREN------LDPQGLHEDRALWQALEQChLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILC 786
Cdd:PRK13549 98 -----SVLENiflgneITPGGIMDYDAMYLRAQKL-LAQL-----KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 787 IDEATASV-DQKTDQLLqqTICKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGR 838
Cdd:PRK13549 167 LDEPTASLtESETAVLL--DIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
644-845 |
2.34e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.35 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLE-LAELRSQLAVIPQEP-FLFSGTIRE 721
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 N---LDPQGL----HEDRA-LWQALEQCHLSEVAVAMGGLdgelgergqnLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:PRK13633 105 EdvaFGPENLgippEEIRErVDESLKKVGMYEYRRHAPHL----------LSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 794 VDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 845
Cdd:PRK13633 175 LDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
645-841 |
3.23e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRS-----QL-------AVIPQEp 712
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqdsisAVNPRK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 713 flfsgTIRENLDpQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PRK10419 107 -----TVREIIR-EPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 793 SVD-----QKTDQL--LQQ---TICkrfanktvLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:PRK10419 181 NLDlvlqaGVIRLLkkLQQqfgTAC--------LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
644-852 |
5.09e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.72 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVdtsqlELAELRSQ----LAVIP--QEPFLF-S 716
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-----HIEGLPGHqiarMGVVRtfQHVRLFrE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 GTIRENL-DPQGLH------------------EDRALWQA---LEQCHLSEVAVAMGGldgelgergqNLSLGQRQLLCL 774
Cdd:PRK11300 95 MTVIENLlVAQHQQlktglfsgllktpafrraESEALDRAatwLERVGLLEHANRQAG----------NLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 775 ARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 244
|
.
gi 1039753393 852 P 852
Cdd:PRK11300 245 P 245
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
335-569 |
5.17e-14 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 73.06 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 335 ASNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVD 414
Cdd:pfam00664 33 GDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 415 DSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPV 494
Cdd:pfam00664 113 DGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRT 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 495 LRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLVLSYA 569
Cdd:pfam00664 193 VKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
644-845 |
5.20e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAelrsqLAVIPQepflFSGtiREN- 722
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELG-----AGFHPE----LTG--RENi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 --------LDPQglhEDRALwqaLEQChlseVAVAmggldgELGE------RgqNLSLGQRQLLCLARALLTDAKILCID 788
Cdd:COG1134 110 ylngrllgLSRK---EIDEK---FDEI----VEFA------ELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 789 EATASVD----QKTDQLLQQticKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:COG1134 172 EVLAVGDaafqKKCLARIRE---LRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
644-841 |
7.57e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFlfsgtir 720
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPN------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLDPQgLHEDRALWQALE--QCHLS------EVAVAMG--GLDGELGER-GQNLSLGQRQLLCLARALLTDAKILCIDE 789
Cdd:PRK15134 373 SSLNPR-LNVLQIIEEGLRvhQPTLSaaqreqQVIAVMEevGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 790 ATASVDqKTDQLLQQTICKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:PRK15134 452 PTSSLD-KTVQAQILALLKSLQQKHQLAylfISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
645-853 |
9.13e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL-AELRSQLAVIPQEPFLFSG------ 717
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlsvydn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 -----TIRENLDPQGlHEDRALwQALEQCHLSEVAVAMggldgelgerGQNLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PRK10895 99 lmavlQIRDDLSAEQ-REDRAN-ELMEEFHIEHLRDSM----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 793 SVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQPH 853
Cdd:PRK10895 167 GVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
644-843 |
9.55e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.41 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL-AELRSQLAVIpqEPFLFSGTIReN 722
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRLL-G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 LDPQglhEDRALWQALEQchLSevavamggldgELGERGQ----NLSLGQRQLLCLARALLTDAKILCIDEATASVD--- 795
Cdd:cd03220 114 LSRK---EIDEKIDEIIE--FS-----------ELGDFIDlpvkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaaf 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 796 -QKTDQLLQQTICKrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 843
Cdd:cd03220 178 qEKCQRRLRELLKQ---GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
627-848 |
1.04e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-LLDNVDTSQLELAelRSQL 705
Cdd:PRK13536 41 AIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLA--RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFL-FSGTIRENLDPQGLH---EDRALWQALEQchLSEVAvamgGLDGELGERGQNLSLGQRQLLCLARALLTD 781
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLVFGRYfgmSTREIEAVIPS--LLEFA----RLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHAL 259
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-186 |
1.28e-13 |
|
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: 71.61 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCA-TIRDNILFGKT------- 63
Cdd:COG1120 29 VTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsrRELARRIAYVPQEPPAPFGlTVRELVALGRYphlglfg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 -FDAQLYREVLEACAlnddlsilpagdQTEVG---EKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDadvANHL 138
Cdd:COG1120 109 rPSAEDREAVEEALE------------RTGLEhlaDRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSHLD---LAHQ 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 139 LHrcILGVLSHTTR------LLCTH------RTeylerADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG1120 174 LE--VLELLRRLARergrtvVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-186 |
1.29e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAIT-------GEL----HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGKTfdAQLYRE 71
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTrfydideGEIlldgHDLRDY-TLASLRNQVALVSQNVHLFNDTIANNIAYART--EQYSRE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLE-----ACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVanhllHRCILGV 146
Cdd:PRK11176 449 QIEeaarmAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES-----ERAIQAA 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039753393 147 LS----HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK11176 523 LDelqkNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
644-844 |
1.38e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPN---AGRVLLD--NVDTSQLELAELRSQLAVIPQEPFLFS 716
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 GTIREN----LDPQGLHEDRALWQALEQChLSEVAVAMGGLDgELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDKQVLDEAVEKS-LKGASIWDEVKD-RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 793 SVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 844
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
584-841 |
1.56e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 584 TQTEAMMVSVERLEE--------YSCDVPQEPhSQPLQSPHQQRISWLTQGSvefqdvvlvyRPGLPNaldgVTFRVEPG 655
Cdd:PLN03130 579 TQAVNANVSLKRLEElllaeervLLPNPPLEP-GLPAISIKNGYFSWDSKAE----------RPTLSN----INLDVPVG 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 656 EKLGIVGRTGSGKSSLFLVLFRLLEPNAgrvlldnvDTSqlelAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALW 735
Cdd:PLN03130 644 SLVAIVGSTGEGKTSLISAMLGELPPRS--------DAS----VVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYE 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 736 QALEQCHLS-EVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQQTICKRFANK 813
Cdd:PLN03130 712 RAIDVTALQhDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDaHVGRQVFDKCIKDELRGK 791
|
250 260
....*....|....*....|....*...
gi 1039753393 814 TVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:PLN03130 792 TRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
628-845 |
2.02e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.59 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN----VDTSQLELAE 700
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 701 LRSQLAVIPQ--EPFLFSGTIRENL--DPQ--GLHEDRALWQALEqchlsevAVAMGGLDGELGERGQ-NLSLGQRQLLC 773
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMnfGVSEEDAKQKARE-------MIELVGLPEELLARSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 774 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
643-845 |
2.47e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 643 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAEL---------RSQLAVIPQEP- 712
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 713 ------FLFSGTIRENLDPQGL-HEDRALWQALEQchLSEVAVAMGGLDgelgERGQNLSLGQRQLLCLARALLTDAKIL 785
Cdd:PRK11701 100 dglrmqVSAGGNIGERLMAVGArHYGDIRATAGDW--LERVEIDAARID----DLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 786 CIDEATA----SVDQKTDQLLQQTIckRFANKTVLTIAHRLNTI-LNSDRVLVLQAGRVVE-------LDSP 845
Cdd:PRK11701 174 FMDEPTGgldvSVQARLLDLLRGLV--RELGLAVVIVTHDLAVArLLAHRLLVMKQGRVVEsgltdqvLDDP 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
628-846 |
2.68e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQL 705
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEP--FLFSGTIRE-------NLdpqGLHED---RALWQALEqchlsevAVAMGGLDgelGERGQNLSLGQRQLLC 773
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEdvafgplNL---GLSKEeveKRVKEALK-------AVGMEGFE---NKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 774 LARALLTDAKILCIDEATASVD----QKTDQLLQQTickrfaNKTVLTI---AHRLNTI-LNSDRVLVLQAGRVVELDSP 845
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDL------NKEGITIiisTHDVDLVpVYADKVYVMSDGKIIKEGTP 221
|
.
gi 1039753393 846 S 846
Cdd:PRK13639 222 K 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
591-849 |
2.80e-13 |
|
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: 73.29 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 591 VSVERLEEYSCDVPQEPHSQPLQSPHQQRISWltqGSVEFQDVVLVYrpglPNALDGVTFRV-------EPGEKLGIVGR 663
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPAPADF---QTLELRGVTYRY----PGEDGDEGFTLgpidltiRRGELVFIVGG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 664 TGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFsgtiRENLDPQGLHEDRALWQALEQCHL 743
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 744 SE-VAVAmgglDGELGERgqNLSLGQRQLLCLARALLTDAKILCIDEATAsvDQktD---------QLLQQTicKRfANK 813
Cdd:COG4615 443 DHkVSVE----DGRFSTT--DLSQGQRKRLALLVALLEDRPILVFDEWAA--DQ--DpefrrvfytELLPEL--KA-RGK 509
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039753393 814 TVLTIAH-----RLntilnSDRVLVLQAGRVVELDSPSALR 849
Cdd:COG4615 510 TVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
644-840 |
3.40e-13 |
|
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: 70.05 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-LLDNVDTSQLElaELRSQLAVI------------PQ 710
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRK--KFLRRIGVVfgqktqlwwdlpVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 711 EPFLFSGTIReNLDPQGLHEDRAlwqaleqcHLSEvavaMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEA 790
Cdd:cd03267 114 DSFYLLAAIY-DLPPARFKKRLD--------ELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 791 TASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:cd03267 181 TIGLDVVAQENIRNFL--KEYNRergtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-176 |
3.68e-13 |
|
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: 69.44 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAIT-------GELhRLCGwVAVSELSKG----------------FGLatqepwIQCATIRDNIL 59
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGgldrptsGEV-RVDG-TDISKLSEKelaafrrrhigfvfqsFNL------LPDLTALENVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 60 FGKTF-------DAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 132
Cdd:cd03255 105 LPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEPTGNLDS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039753393 133 DVANHLLHrcILGVLSH---TTRLLCTHRTEYLERADVVLLMEAGQL 176
Cdd:cd03255 174 ETGKEVME--LLRELNKeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-170 |
3.78e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 33 VSELSKGFGLATQEPWIQCATIRDNILFGKTfDAQLyREVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 109
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 110 LARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLLCT--HRTEYLERADVVLL 170
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVV 1430
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
637-841 |
4.14e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 637 YRPGL-----PNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtSQLELAE--LRSQ-LAVI 708
Cdd:PRK15112 16 YRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGDysYRSQrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 709 PQEPF-----------LFSGTIRENLDPQGLHEDRALWQALEQchlsevavaMGGLDGELGERGQNLSLGQRQLLCLARA 777
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQ---------VGLLPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 778 LLTDAKILCIDEATASVD-----QKTDQLLQ----QTICKRFANKTVLTIAHRlntilnSDRVLVLQAGRVVE 841
Cdd:PRK15112 164 LILRPKVIIADEALASLDmsmrsQLINLMLElqekQGISYIYVTQHLGMMKHI------SDQVLVMHQGEVVE 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
644-852 |
4.20e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.72 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVD-TSQLELAELRsqLAVIPQEPFLFSG-TIRE 721
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERR--VGFVFQHYALFPHmTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 N----LDPQGLHEDRALWQALEQchLSEVavamgGLDGeLGER--GQnLSLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:COG1118 95 NiafgLRVRPPSKAEIRARVEEL--LELV-----QLEG-LADRypSQ-LSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 796 QK-TDQL---LQQTIcKRFaNKTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:COG1118 166 AKvRKELrrwLRRLH-DEL-GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
628-843 |
4.63e-13 |
|
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: 69.21 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLAV 707
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEPFLFSG-TIRENLdPQGLHEDRALWQALEQcHLSEVAvAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILC 786
Cdd:cd03301 77 VFQNYALYPHmTVYDNI-AFGLKLRKVPKDEIDE-RVREVA-ELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 787 IDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 843
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
640-845 |
4.86e-13 |
|
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: 72.53 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 640 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-------LLDNVDTSQLELAELRSQLAVIPQEP 712
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 713 FLFS-GTIRENL-DPQGLH--EDRALWQALeqchlseVAVAMGGLDGE-----LGERGQNLSLGQRQLLCLARALLTDAK 783
Cdd:TIGR03269 375 DLYPhRTVLDNLtEAIGLElpDELARMKAV-------ITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 784 ILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
631-850 |
4.91e-13 |
|
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: 73.51 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 631 QDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTsQLELAELRSQLAVIPQ 710
Cdd:TIGR01257 932 KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 711 EPFLFSG-TIRENLdpqgLHEDRALWQALEQCHLS-EVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 788
Cdd:TIGR01257 1011 HNILFHHlTVAEHI----LFYAQLKGRSWEEAQLEmEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 789 EATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTI-LNSDRVLVLQAGRVVELDSPSALRN 850
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
644-848 |
5.30e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIPQEPFLFSG-TIRE 721
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NLDPQGLHEDRALWQAleqcHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 801
Cdd:PRK11614 100 NLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753393 802 LQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK11614 176 IFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
640-841 |
6.34e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.91 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 640 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---------GRVLLdnvDTSQLELAELRS-QLAVIP 709
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGriggsatfnGREIL---NLPEKELNKLRAeQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 710 QEPFlfsgtirENLDPQ-----------GLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARAL 778
Cdd:PRK09473 104 QDPM-------TSLNPYmrvgeqlmevlMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 779 LTDAKILCIDEATASVDQkTDQ-----LLQQTicKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVVE 841
Cdd:PRK09473 177 LCRPKLLIADEPTTALDV-TVQaqimtLLNEL--KREFNTAIIMITHDLGVVAGIcDKVLVMYAGRTME 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
607-844 |
6.58e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 607 PHSQPLQSPHQQRISWLtqgSVEFQDvvlvYRPGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV 686
Cdd:PRK10261 2 PHSDELDARDVLAVENL---NIAFMQ----EQQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 687 LLDN----------VDTSQLELAELR----SQLAVIPQEP-------FLFSGTIRENLD-PQGLHEDRALWQA---LEQC 741
Cdd:PRK10261 74 QCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQEPmtslnpvFTVGEQIAESIRlHQGASREEAMVEAkrmLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 742 HLSEvAVAMggldgeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD-QLLQQ-TICKRFANKTVLTIA 819
Cdd:PRK10261 154 RIPE-AQTI------LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLiKVLQKEMSMGVIFIT 226
|
250 260
....*....|....*....|....*.
gi 1039753393 820 HRLNTILN-SDRVLVLQAGRVVELDS 844
Cdd:PRK10261 227 HDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-190 |
6.70e-13 |
|
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: 69.07 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-------------ELSKGFGLATQepwiQCA-----TIRDNILFG--- 61
Cdd:cd03261 29 LAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgedisglseaelyRLRRRMGMLFQ----SGAlfdslTVFENVAFPlre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 -KTFDAQLYREV----LEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD---AD 133
Cdd:cd03261 105 hTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 134 VANHLLHRciLGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL----PLVQ 190
Cdd:cd03261 174 VIDDLIRS--LKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRasddPLVR 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
649-851 |
6.96e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 649 TFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAelRSQLAVIPQEPFLFSG-TIRENLDpQG 727
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIG-LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 728 LHEDRALwQALEQCHLSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD----QKTDQLLQ 803
Cdd:PRK10771 96 LNPGLKL-NAAQREKLHAIARQM-GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753393 804 QtICKRfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:PRK10771 174 Q-VCQE-RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-186 |
7.46e-13 |
|
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: 69.12 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELSK----------GFGLatqePWIQcaTIRDNILFgktFdA 66
Cdd:COG4555 30 TGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPREarrqigvlpdERGL----YDRL--TVRENIRY---F-A 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 67 QLYREVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILG 145
Cdd:COG4555 100 ELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-ARRLLREILRA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 146 VLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG4555 178 LKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
4-198 |
1.05e-12 |
|
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: 70.51 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 4 GIVGKVGCGKSSLLAAITGELHRLCGWVAVSElskgfglatqEPWIQCA-------------------------TIRDNI 58
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG----------EVLQDSArgiflpphrrrigyvfqearlfphlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 59 LFG-----KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 133
Cdd:COG4148 99 LYGrkrapRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 134 VANHLLHrcILGVLSHTTR---LLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEILPLVQAVPTAWAE 198
Cdd:COG4148 168 RKAEILP--YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGE 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
645-798 |
1.34e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLEL---AELRSQ-LAVIPQEPFLFSG-TI 719
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 720 RENLDPQGLHEDRALWQALEQCHLSEVAVamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAV---GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
591-843 |
1.96e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 591 VSVERLEEYSCDVPQEPHSQPLQSPHQQRIswltqgsvEFQDVVLVYrPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSS 670
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPRPQAFPDWQTL--------ELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 671 LFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTirenLDPQGLHEDRALWQA-LEQCHLSE-VAV 748
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHkLEL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 749 AmgglDGELgeRGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD--------QKTDQLLQQTickrfaNKTVLTIAH 820
Cdd:PRK10522 441 E----DGRI--SNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEM------GKTIFAISH 508
|
250 260
....*....|....*....|...
gi 1039753393 821 RLNTILNSDRVLVLQAGRVVELD 843
Cdd:PRK10522 509 DDHYFIHADRLLEMRNGQLSELT 531
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-186 |
1.97e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 67.81 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGLATQEPWIQCA--------------TIRDNILFG------ 61
Cdd:COG1121 34 FVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL------FGKPPRRARRRIGyvpqraevdwdfpiTVRDVVLMGrygrrg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 --KTFDAQLYREVLEACALnddLSILPAGDQTeVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 139
Cdd:COG1121 108 lfRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 140 HrcILGVLSH--TTRLLCTHRTEYLER-ADVVLLMeAGQLVRTGPPSEIL 186
Cdd:COG1121 180 E--LLRELRRegKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-186 |
2.52e-12 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 68.01 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrE 71
Cdd:cd03288 50 VGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgidisklplhTLRSRLSIILQDPILFSGSIRFNLdPECKCTDDRLW-E 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANhLLHRCILGVLSHTT 151
Cdd:cd03288 129 ALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN-ILQKVVMTAFADRT 207
|
170 180 190
....*....|....*....|....*....|....*
gi 1039753393 152 RLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03288 208 VVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
645-840 |
2.58e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAeLRSQLAV--IPQEPFLFSG-TIRE 721
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NL-----DPQGLHED-RALWQALeQCHLSeVAVAMGGLDgelgergqnlsLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:PRK15439 106 NIlfglpKRQASMQKmKQLLAAL-GCQLD-LDSSAGSLE-----------VADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039753393 796 Q-KTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:PRK15439 173 PaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
628-848 |
2.95e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV-LLDNVDTSQLELAelRSQLA 706
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHA--RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 707 VIPQ----EPFLfsgTIRENLDPQGLHEDRALWQALEQC-HLSEVAVAMGGLDGELGErgqnLSLGQRQLLCLARALLTD 781
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVpPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTICKRFAN-KTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
645-845 |
3.01e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQLAVIPQEP--FLFSGTIR 720
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 EN----LDPQGLHEDralwqalEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 796
Cdd:PRK13638 97 SDiafsLRNLGVPEA-------EITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 797 K-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:PRK13638 170 AgRTQMI--AIIRRIVAQgnHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
640-853 |
3.40e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 640 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLfRLLE-PNAGRVLLDN------VDTSQLELAELRSQLAVIPQE- 711
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 712 ---PFLfsgTIRENL--DP---QGLHEDRALWQA---LEQCHLSEVAvamggldgelgER-GQNLSLGQRQLLCLARALL 779
Cdd:PRK11124 92 nlwPHL---TVQQNLieAPcrvLGLSKDQALARAeklLERLRLKPYA-----------DRfPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 780 TDAKILCIDEATASVDQK-TDQL------LQQTickrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALrNQ 851
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEiTAQIvsiireLAET------GITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCF-TQ 230
|
..
gi 1039753393 852 PH 853
Cdd:PRK11124 231 PQ 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
645-852 |
3.98e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEP-----NAGRVLLDNVDT-SQLELAELRSQLAVIPQEPFLFSGT 718
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IREN-LDPQGLHE--DRALWQALEQCHLSEVAVaMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD 795
Cdd:PRK14271 117 IMDNvLAGVRAHKlvPRKEFRGVAQARLTEVGL-WDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 796 QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
628-852 |
4.90e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAV 707
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 708 IPQEP--FLFSGTIRENL--DPQGLHEDRALWQaleqcHLSEVAVAMGGLDgELGERG-QNLSLGQRQLLCLARALLTDA 782
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEETVA-----HRVSSALHMLGLE-ELRDRVpHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 783 KILCIDEATASVD-QKTDQLLqqtickRFANK-------TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK13652 157 QVLVLDEPTAGLDpQGVKELI------DFLNDlpetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-176 |
5.39e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.19 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAA------ITGELH-RLCGW--VAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYReV 72
Cdd:cd03289 33 VGLLGRTGSGKSTLLSAflrllnTEGDIQiDGVSWnsVPLQKWRKAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEIWK-V 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 73 LEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSHTTR 152
Cdd:cd03289 112 AEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTV 190
|
170 180
....*....|....*....|....
gi 1039753393 153 LLCTHRTEYLERADVVLLMEAGQL 176
Cdd:cd03289 191 ILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
586-852 |
7.03e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 586 TEAMMVSVERLEEYS-CDVPQE------PHSQPLQSPHQQRISWLTQGSVEFQDVVLVY--RPGLPN-------ALDGVT 649
Cdd:PRK10261 265 TRALLAAVPQLGAMKgLDYPRRfplislEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFplRSGLLNrvtrevhAVEKVS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 650 FRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDT-SQLELAELRSQLAVIPQEPF-------LFSGTI 719
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPYasldprqTVGDSI 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 720 RENLDPQGLHEDRAlwqalEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD---- 795
Cdd:PRK10261 425 MEPLRVHGLLPGKA-----AAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvsir 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 796 -QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK10261 500 gQIINLLLD---LQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
645-804 |
7.89e-12 |
|
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: 65.21 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLD 724
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 725 -PQGLHEDRALWQALEQCHLSEVAVAMGGldgelgergqNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ 803
Cdd:cd03231 96 fWHADHSDEQVEEALARVGLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
.
gi 1039753393 804 Q 804
Cdd:cd03231 166 E 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
645-847 |
9.11e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDTSQLElAELRsQLAVIPQEPFLFSG-TIR 720
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALP-AEQR-RIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLD---PQGLHedRALWQALEQCHLSEVavamgGLDGeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 796
Cdd:COG4136 95 ENLAfalPPTIG--RAQRRARVEQALEEA-----GLAG-FADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 797 K-TDQLLQQtickrfanktVLTIAHRLN--TILNS-DRVLVLQAGRVVELDSPSA 847
Cdd:COG4136 167 AlRAQFREF----------VFEQIRQRGipALLVThDEEDAPAAGRVLDLGNWQH 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
643-852 |
9.76e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 643 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLelAELRSQLAVIPQEPFLFSG-TIRE 721
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NLdPQGLHEDR--------ALWQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:PRK11607 111 NI-AFGLKQDKlpkaeiasRVNEMLGLVHMQEFA----------KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 794 VDQKTDQLLQQT---ICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK11607 180 LDKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
638-852 |
1.25e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 638 RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN---------------VDTSQLELaeLR 702
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvADKNQLRL--LR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 703 SQLAVIPQEPFLFSG-TIREN-----LDPQGLHEDRALWQALEqcHLSEVavamgGLDgelgERGQ-----NLSLGQRQL 771
Cdd:PRK10619 92 TRLTMVFQHFNLWSHmTVLENvmeapIQVLGLSKQEARERAVK--YLAKV-----GID----ERAQgkypvHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 772 LCLARALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSA 847
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPElVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQ 238
|
....*
gi 1039753393 848 LRNQP 852
Cdd:PRK10619 239 LFGNP 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-185 |
1.65e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 66.66 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 10 GCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQEPwiqcA-----TIRDNILFG-------KTFDAQLY 69
Cdd:COG3842 41 GCGKTTLLRMIAGFETPDSGRILldgrdVTGLPpekRNVGMVFQDY----AlfphlTVAENVAFGlrmrgvpKAEIRARV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARA-VYQEKALyLLDDPLAAVDADVANHL------LHRc 142
Cdd:COG3842 117 AELLELVGLEGLADRYPH-----------QLSGGQQQRVALARAlAPEPRVL-LLDEPLSALDAKLREEMreelrrLQR- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039753393 143 ILGVlshTTrLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:COG3842 184 ELGI---TF-IYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
643-851 |
1.69e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 643 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAVI------------PQ 710
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGVVfgqrsqlwwdlpAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 711 EPFLFSGTI--------RENLDpqglhedralwqaleqcHLSEvavaMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:COG4586 115 DSFRLLKAIyripdaeyKKRLD-----------------ELVE----LLDLGELLDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 783 KILCIDEATASVD----QKTDQLLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:COG4586 174 KILFLDEPTIGLDvvskEAIREFLKE-YNRER-GTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-180 |
1.72e-11 |
|
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: 64.98 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH---RLCGWVAV--SELSKG-----FGLATQ-EPWIQCATIRDNILFGKTF-----D 65
Cdd:cd03234 35 VMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFngQPRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAILrlprkS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLYREVLEACALNDDLSILPAGDQTEVGekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILG 145
Cdd:cd03234 115 SDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS--TLS 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 146 VLSHTTRL-LCT-H--RTEYLERADVVLLMEAGQLVRTG 180
Cdd:cd03234 188 QLARRNRIvILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-180 |
1.75e-11 |
|
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: 64.58 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELS---KGFGLATQE----PWIqcaTIRDNILFG----KTFDAQ 67
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAG-LEEptsgriYIGGRDVTDLPpkdRDIAMVFQNyalyPHM---TVYDNIAFGlklrKVPKDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------LHR 141
Cdd:cd03301 107 IDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMraelkrLQQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039753393 142 cILGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTG 180
Cdd:cd03301 179 -RLG----TTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-176 |
2.06e-11 |
|
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: 63.19 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGlatQEPWIQCATIRDNILFgktfdaqlyreVLEACALNDDL 82
Cdd:cd03230 29 YGLLGPNGAGKTTLIKIILGLLKPDSGEIKV------LG---KDIKKEPEEVKRRIGY-----------LPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 83 SilpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS--HTTRLLCTHRTE 160
Cdd:cd03230 89 T----------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTILLSSHILE 156
|
170
....*....|....*..
gi 1039753393 161 YLER-ADVVLLMEAGQL 176
Cdd:cd03230 157 EAERlCDRVAILNNGRI 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
645-849 |
2.88e-11 |
|
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: 64.74 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPG-----EKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTS-QLELAELRSQLAVipqEPFLFSGT 718
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTV---RDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IRENLDPQglhedralWQaleqchlSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKt 798
Cdd:cd03237 87 KDFYTHPY--------FK-------TEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 799 DQLLQQTICKRFA---NKTVLTIAHRLNTI-LNSDRVLVL--QAGRVVELDSPSALR 849
Cdd:cd03237 150 QRLMASKVIRRFAennEKTAFVVEHDIIMIdYLADRLIVFegEPSVNGVANPPQSLR 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
627-845 |
2.99e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.64 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 627 SVEFQDVVLVYRPGLPN---ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL------DNVDTSQLE 697
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 698 LA----------ELRSQLAVIPQEP--FLFSGTIRENLdpqgLHEDRALWQALEQCH-LSEVAVAMGGLDGELGERGQ-N 763
Cdd:PRK13631 101 TNpyskkiknfkELRRRVSMVFQFPeyQLFKDTIEKDI----MFGPVALGVKKSEAKkLAKFYLNKMGLDDSYLERSPfG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 764 LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 841
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEvADEVIVMDKGKILK 256
|
....
gi 1039753393 842 LDSP 845
Cdd:PRK13631 257 TGTP 260
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-180 |
3.02e-11 |
|
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: 63.71 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAV-----SELSKGFGLATQE---PWIQCATIRDNIL--------FGKTFD 65
Cdd:cd03235 27 FLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplEKERKRIGYVPQRrsiDRDFPISVRDVVLmglyghkgLFRRLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLYREVLEAcalnddlsiLPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcIL 144
Cdd:cd03235 107 KADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE--LL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 145 GVLSHTTR--LLCTH-RTEYLERADVVLLMeAGQLVRTG 180
Cdd:cd03235 176 RELRREGMtiLVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
645-852 |
3.23e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.06 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQ-LAVIPQEPFLFSG-TI 719
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 720 RENLdpqglhEDRALWQALEQCHLSEVAVAMGGLDGeLGER-----GQnLSLGQRQLLCLARALLTDAKILCIDEATASV 794
Cdd:PRK10535 104 AQNV------EVPAVYAGLERKQRLLRAQELLQRLG-LEDRveyqpSQ-LSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 795 DQKTdqllqqtickrfaNKTVLTIAHRLN------TILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK10535 176 DSHS-------------GEEVMAILHQLRdrghtvIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
645-852 |
3.87e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNV--DTS------QLELAELRSQLAVIPQEPFLFS 716
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTArslsqqKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 G-TIRENLDPQGL---HEDRALWQALEQCHLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PRK11264 99 HrTVLENIIEGPVivkGEPKEEATARARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 793 SVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK11264 174 ALDPELVGEVLNTI-RQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-186 |
4.39e-11 |
|
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: 64.05 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV--SELSKGFGLAT--------QEP-------WiqcaTIRDNI-----LF 60
Cdd:COG1124 34 FGLVGESGSGKSTLLRALAGLERPWSGEVTFdgRPVTRRRRKAFrrrvqmvfQDPyaslhprH----TVDRILaeplrIH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 61 GKTFDAQLYREVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVA 135
Cdd:COG1124 110 GLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 136 NhLLHRciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG1124 179 N-LLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-180 |
5.85e-11 |
|
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: 63.29 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV-------------SELSKGFGLATQE------PWIqcaTIRDNI----- 58
Cdd:cd03257 34 LGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrKIRRKEIQMVFQDpmsslnPRM---TIGEQIaeplr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 59 LFGKTFDAQLYREV--LEACALNDDLSIL---PAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 133
Cdd:cd03257 111 IHGKLSKKEARKEAvlLLLVGVGLPEEVLnryPH-----------ELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 134 VAnhllhRCILGVLSH------TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 180
Cdd:cd03257 180 VQ-----AQILDLLKKlqeelgLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
628-840 |
5.96e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYRPGlPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE---LRSQ 704
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 705 LAVIPQE-PFLFSGTIREN----LDPQGLHED---RALWQALEQchlsevavaMGGLDgelgeRGQN----LSLGQRQLL 772
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNvaipLIIAGASGDdirRRVSAALDK---------VGLLD-----KAKNfpiqLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKtdqlLQQTICKRFA--NK---TVLTIAHRLNTILNSD-RVLVLQAGRVV 840
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
644-851 |
6.45e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.36 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelrsqlavipqEPflFSGTIRENL 723
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG--------------------EP--LDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 dpqG-LHEDRAL---WQALEQchlsevAVAMGGLDG-----------------ELGERG----QNLSLGQRQLLCLARAL 778
Cdd:COG4152 74 ---GyLPEERGLypkMKVGEQ------LVYLARLKGlskaeakrradewlerlGLGDRAnkkvEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 779 LTDAKILCIDEATASVDQKTDQLLQQTIcKRFANK--TVLTIAHRLNTI--LnSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVI-RELAAKgtTVIFSSHQMELVeeL-CDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
390-600 |
6.57e-11 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 64.16 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 390 PVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLAnSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRE 469
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMG-PLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 470 LRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQrLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIAL 549
Cdd:cd18559 164 LKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVD-AKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAY 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 550 VQHQQglaNPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYS 600
Cdd:cd18559 243 VSRHS---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-185 |
7.46e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.71 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSElsKGFGLATQEPwiqcA-----TIRDNILFG----K 62
Cdd:COG3839 31 FLVLLGPSGCGKSTLLRMIagledptSGEILiggRDVTDLPPKD--RNIAMVFQSY----AlyphmTVYENIAFPlklrK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 63 TFDAQLYREVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 136
Cdd:COG3839 105 VPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 137 HL------LHRcilgVLSHTTrLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:COG3839 171 EMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
645-843 |
8.12e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVdtsqlelaelrsQLAVIPQEpflfsgtiRENL 723
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETV------------KIGYFDQH--------QEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DPqglheDRALWQALEQchlsevaVAMGGLDGEL----------GERGQ----NLSLGQRQLLCLARALLTDAKILCIDE 789
Cdd:COG0488 391 DP-----DKTVLDELRD-------GAPGGTEQEVrgylgrflfsGDDAFkpvgVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 790 ATASVDQKTDQLLQQTIcKRFANkTVLTIAH-R--LNTIlnSDRVLVLQAGRVVELD 843
Cdd:COG0488 459 PTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-195 |
8.38e-11 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 65.31 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITG--------------ELHRLCGwVAVSELSKGFGLATQEPWIQ---CATIRDNI-----LF 60
Cdd:COG1123 294 LGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSR-RSLRELRRRVQMVFQDPYSSlnpRMTVGDIIaeplrLH 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 61 GKTFDAQLY---REVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----A 132
Cdd:COG1123 373 GLLSRAERRervAELLERVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqA 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 133 DVANHLLH-RCILGVlshtTRLLCTH---RTEYLerADVVLLMEAGQLVRTGPPSEIL--P-------LVQAVPTA 195
Cdd:COG1123 442 QILNLLRDlQRELGL----TYLFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-180 |
9.00e-11 |
|
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: 61.68 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELhrlcgwvavsELSKGfglatqepwiqcaTIRdniLFGKTFDAQLYREVLEACAlndd 81
Cdd:cd03214 27 IVGILGPNGAGKSTLLKTLAGLL----------KPSSG-------------EIL---LDGKDLASLSPKELARKIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 82 lsILP-AGDQTEVG---EKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH---TTRL 153
Cdd:cd03214 77 --YVPqALELLGLAhlaDRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLARergKTVV 152
|
170 180 190
....*....|....*....|....*....|.
gi 1039753393 154 LCTHrteYLERA----DVVLLMEAGQLVRTG 180
Cdd:cd03214 153 MVLH---DLNLAaryaDRVILLKDGRIVAQG 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
645-846 |
9.68e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN---AGRVLLDNVdtsQLELAELRSQLAVIPQ-EPFLFSGTIR 720
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQdDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLDPQG-LHEDRALWQALEQCHLSEVAVAMGGLD------GELGeRGQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:TIGR00955 118 EHLMFQAhLRMPRRVTKKEKRERVDEVLQALGLRKcantriGVPG-RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 794 VDQKTDQLLQQTIcKRFANK--TVLTIAHRLNTIL--NSDRVLVLQAGRVVELDSPS 846
Cdd:TIGR00955 197 LDSFMAYSVVQVL-KGLAQKgkTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPD 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
645-842 |
9.93e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA-----GRVLL--DNVDTSQLELAELRSQLAVIPQEPFLFSG 717
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLfgRNIYSPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 -TIREN----------LDPQGLHEDRALWqALEQCHLSEvavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILC 786
Cdd:PRK14267 100 lTIYDNvaigvklnglVKSKKELDERVEW-ALKKAALWD------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 787 IDEATASVDQKTDQLLQQTICKRFANKTVLTIAHR-LNTILNSDRVLVLQAGRVVEL 842
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-180 |
1.45e-10 |
|
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: 61.74 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGLATQEPwiQCATIRDNILFgktfdAQLYREVLEACALNDDL 82
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLF-----AHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 83 SILPAGDQT------EVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhRCILGVLSHT 150
Cdd:cd03298 100 KLTAEDRQAievalaRVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-DLVLDLHAET 178
|
170 180 190
....*....|....*....|....*....|...
gi 1039753393 151 --TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 180
Cdd:cd03298 179 kmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
645-845 |
1.52e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVdtsqlELAELRSQLAVIPQEPFLFS-GTIREN- 722
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQDARLLPwKKVIDNv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 -LDPQGLHEDRALwQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 801
Cdd:PRK11247 103 gLGLKGQWRDAAL-QALAAVGLADRA----------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 802 LQQTICKRFANK--TVLTIAHRLN-TILNSDRVLVLQAGRV-----VELDSP 845
Cdd:PRK11247 172 MQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
53-185 |
1.53e-10 |
|
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: 62.25 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNILFG----KTFDAQLYREVLEACalndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLA 128
Cdd:cd03300 88 TVFENIAFGlrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 129 AVDADVANHL------LHRcILGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03300 160 ALDLKLRKDMqlelkrLQK-ELG----ITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
643-844 |
1.97e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 643 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE--PNAGRVlldnvdtsqlelaelrsqlaVIPQEPFLFSGTIR 720
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV--------------------DVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLDPQGLHEDRAlwQALEQCHLSEVAVamggldgeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 800
Cdd:COG2401 104 DAIGRKGDFKDAV--ELLNAVGLSDAVL--------WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753393 801 LLQ---QTICKRfANKTVLTIAHRLNTI--LNSDRVLVLQAGRVVELDS 844
Cdd:COG2401 174 RVArnlQKLARR-AGITLVVATHHYDVIddLQPDLLIFVGYGGVPEEKR 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
644-845 |
2.26e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRsQLAVIPQEPFLFSG-TIREN 722
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNTVFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 ----LDPQGLHED----RALwQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASV 794
Cdd:PRK09452 107 vafgLRMQKTPAAeitpRVM-EALRMVQLEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 795 DQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:PRK09452 176 DYKLRKQMQNEL-KALQRKLGITfvfVTHDQEEALTmSDRIVVMRDGRIEQDGTP 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
646-834 |
2.93e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 646 DGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLElAELRSQLAVI-----------PQEPFL 714
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLghqpgikteltALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 FSGTIRENLDpqglheDRALWQALEQCHLS---EVAVAmggldgelgergqNLSLGQRQLLCLARALLTDAKILCIDEAT 791
Cdd:PRK13538 97 FYQRLHGPGD------DEALWEALAQVGLAgfeDVPVR-------------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753393 792 ASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVL 834
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGgmVILTTHQDLPVASDKVRKLRL 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
644-846 |
2.96e-10 |
|
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: 63.67 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPNAGRVL---------------------------------L 688
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 689 DNVDTSQLELAELRSQLAVIPQEPFLFSG--TIREN----LDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQ 762
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAVD-------LIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 763 NLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
....*..
gi 1039753393 840 VELDSPS 846
Cdd:TIGR03269 248 KEEGTPD 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
644-840 |
3.83e-10 |
|
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: 63.31 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRlLEPNA---GRVLLDNVDTSQLELAEL-RSQLAVIPQEPFLFSG-T 718
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IRENL-------DPQGLHEDRALWQaleQCH--LSEVAVAMGGLDGELGERGqnlsLGQRQLLCLARALLTDAKILCIDE 789
Cdd:TIGR02633 95 VAENIflgneitLPGGRMAYNAMYL---RAKnlLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 790 ATASVDQKTDQLLQQTIcKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:TIGR02633 168 PSSSLTEKETEILLDII-RDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
639-841 |
4.23e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.25 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 639 PGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN--VDTSQLELAELRSQLAVIPQEPFLfs 716
Cdd:PRK11248 12 GGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAERGVVFQNEGLLPWRNVQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 GTIRENLDPQGLHEDRALWQALEqchlsevAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 796
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQ-------MLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 797 KTDQLLQQTICKRFAN--KTVLTIAHRLNTILNSDRVLVLQA---GRVVE 841
Cdd:PRK11248 162 FTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSpgpGRVVE 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
640-843 |
4.37e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 640 GLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIP----QEPFL 714
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 FSGTIREN--------------LDPQGlhEDRALWQALEQchlseVAVAMGGLDGELGergqNLSLGQRQLLCLARALLT 780
Cdd:COG1129 343 LDLSIRENitlasldrlsrgglLDRRR--ERALAEEYIKR-----LRIKTPSPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 781 DAKILCIDEATASVD--QKTD--QLLQQtickrFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV-ELD 843
Cdd:COG1129 412 DPKVLILDEPTRGIDvgAKAEiyRLIRE-----LAAegKAVIVISSELPELLgLSDRILVMREGRIVgELD 477
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-185 |
5.01e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAVSelskGFGLATQEPWIQC-------------ATIRDNILFGKTFDAQLYRE 71
Cdd:PRK11607 50 LLGASGCGKSTLLRMLAGFEQPTAGQIMLD----GVDLSHVPPYQRPinmmfqsyalfphMTVEQNIAFGLKQDKLPKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 72 VleACALNDDLSILPAgdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSH-- 149
Cdd:PRK11607 126 I--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE-VVDILERvg 200
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 150 TTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK11607 201 VTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-170 |
6.59e-10 |
|
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: 59.80 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSElsKGFGLATQEPWIQCA------------TIRDNILF-----GKTF 64
Cdd:COG4133 30 ALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG--EPIRDAREDYRRRLAylghadglkpelTVRENLRFwaalyGLRA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 DAQLYREVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCIl 144
Cdd:COG4133 108 DREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALLAELI- 174
|
170 180 190
....*....|....*....|....*....|
gi 1039753393 145 gvLSHTTR----LLCTHRTEYLERADVVLL 170
Cdd:COG4133 175 --AAHLARggavLLTTHQPLELAAARVLDL 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-186 |
7.59e-10 |
|
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: 60.48 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELH------------RLCGWVaVSELSKGFGLAT---QEPWIQCATIRDNILFGKtFDA-QL 68
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPptygndvrlfgeRRGGED-VWELRKRIGLVSpalQLRFPRDETVLDVVLSGF-FDSiGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 YREVLE-----ACALNDDLSILPAGDQTeVGekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHRCI 143
Cdd:COG1119 112 YREPTDeqrerARELLELLGLAHLADRP-FG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-LGARELLLALL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 144 --LGVLSHTTRLLCTHRTEyleraDV------VLLMEAGQLVRTGPPSEIL 186
Cdd:COG1119 186 dkLAAEGAPTLVLVTHHVE-----EIppgithVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
645-841 |
8.72e-10 |
|
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: 59.08 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVL--FRLLEPNAGRVLLDNVDTSQLELAElRSQLAVI--PQEPFLFSGTIR 720
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENLdpqglhedralwqaleqchLSEVAVamgGLDGelGERGQNLSLgqrQLLCLaralltDAKILCIDEATASVDQKTDQ 800
Cdd:cd03217 95 ADF-------------------LRYVNE---GFSG--GEKKRNEIL---QLLLL------EPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753393 801 LLQQTICK-RFANKTVLTIAHRLNtILN---SDRVLVLQAGRVVE 841
Cdd:cd03217 142 LVAEVINKlREEGKSVLIITHYQR-LLDyikPDRVHVLYDGRIVK 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
628-852 |
9.10e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 628 VEFQDVVLVYrpGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD--NVDTSQLELAELRSQL 705
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 706 AVIPQEPFLFSG-TIREN-----LDPQGLHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQLLCLARALL 779
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENvmfgpLRVRGASKEEAEKQAREL--LAKV-----GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 780 TDAKILCIDEATASVDQktdQLLQQ--TICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK09493 153 VKPKLMLFDEPTSALDP---ELRHEvlKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
644-851 |
9.14e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQ-LAVIPQEPFLF----SGT 718
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvpDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IRENL------DPQ---GLHEDRALWQALEQCHLSEVAVAMGGLDGELGergqNLSLGQRQLLCLARALLTDAKILCIDE 789
Cdd:COG3845 353 VAENLilgryrRPPfsrGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 790 ATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV-ELDSPSALRNQ 851
Cdd:COG3845 429 PTRGLDVGaIEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREE 493
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-175 |
9.30e-10 |
|
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: 58.74 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGLATQEPWIQCATIRDNIlfGKTF-DAQLYR--EVLEACALn 79
Cdd:cd03229 29 VALLGPSGSGKSTLLRCIAGLEEPDSGSILI------DGEDLTDLEDELPPLRRRI--GMVFqDFALFPhlTVLENIAL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 80 ddlsilpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------LHRcILGVlshtTRL 153
Cdd:cd03229 100 -------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVrallksLQA-QLGI----TVV 155
|
170 180
....*....|....*....|...
gi 1039753393 154 LCTHRTEYLER-ADVVLLMEAGQ 175
Cdd:cd03229 156 LVTHDLDEAARlADRVVVLRDGK 178
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
588-839 |
9.83e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 588 AMMVSVERLEEYscdvPQEPHsqplqsphqqriswlTQGSVEFQ-DVVLVYRPGLPNA--LDGVTFRVEPGEKLGIVGRT 664
Cdd:PRK13549 237 TMMVGRELTALY----PREPH---------------TIGEVILEvRNLTAWDPVNPHIkrVDDVSFSLRRGEILGIAGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 665 GSGKSSLFLVLFRLLE-PNAGRVLLDN--VDTSQLELA---------ELRSQLAVIPQ------------EPFLFSGTIR 720
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQAiaqgiamvpEDRKRDGIVPVmgvgknitlaalDRFTGGSRID 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 ENldpqglHEDRALWQALEQCHL----SEVAVAmggldgelgergqNLSLGQRQLLCLARALLTDAKILCIDEATASVD- 795
Cdd:PRK13549 378 DA------AELKTILESIQRLKVktasPELAIA-------------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDv 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 796 -------QKTDQLLQQTICkrfanktVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:PRK13549 439 gakyeiyKLINQLVQQGVA-------IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-185 |
1.05e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.25 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQE-PWIQCATIRDNILFGKTFDAQlyREV 72
Cdd:PRK10851 30 MVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdVSRLHardRKVGFVFQHyALFRHMTVFDNIAFGLTVLPR--RER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 73 LEACALNDDLSILPAGDQTE--VGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------LHRCIl 144
Cdd:PRK10851 108 PNAAAIKAKVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwlrqLHEEL- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039753393 145 gvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK10851 187 ----KFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
645-853 |
1.31e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA-----GRVLL--DNVDTSQLELAELRSQLAVIPQEPFLFSG 717
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfnQNIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 TIRENL---------DPQgLHEDRALWQALEQCHLSEvavamgGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 788
Cdd:PRK14258 103 SVYDNVaygvkivgwRPK-LEIDDIVESALKDADLWD------EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 789 EATASVD----QKTDQLLQQTICKrfANKTVLTIAHRLNTILN-SDRVLVLQA-----GRVVELDSPSALRNQPH 853
Cdd:PRK14258 176 EPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
649-821 |
1.39e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.69 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 649 TFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelRSQLAVIPQEPFLFSGTIREN-LDPQG 727
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQiIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 728 LHE-------DRALWQALEQCHLSEVAVAMGGLDGeLGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 800
Cdd:TIGR00954 541 SEDmkrrglsDKDLEQILDNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|.
gi 1039753393 801 LLQQtICKRFaNKTVLTIAHR 821
Cdd:TIGR00954 620 YMYR-LCREF-GITLFSVSHR 638
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-178 |
1.56e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 58.90 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAI-------TGELhRLCGwVAVSELSKG----------------FGLatqepwIQCATIRDNI 58
Cdd:COG1136 36 FVAIVGPSGSGKSTLLNILggldrptSGEV-LIDG-QDISSLSERelarlrrrhigfvfqfFNL------LPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 59 LF-------GKTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 131
Cdd:COG1136 108 ALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEPTGNLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 132 ADVANHllhrcILGVL------SHTTRLLCTHRTEYLERADVVLLMEAGQLVR 178
Cdd:COG1136 177 SKTGEE-----VLELLrelnreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-185 |
1.76e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAV--------------------------SELSKGFGLATQEPWIQC--ATIRD 56
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpyskkiknfKELRRRVSMVFQFPEYQLfkDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 57 NILFG-------KTFDAQLYREVLEACALNDD-LSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLA 128
Cdd:PRK13631 137 DIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 129 AVDADvANHLLHRCILGV-LSHTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13631 206 GLDPK-GEHEMMQLILDAkANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
53-180 |
1.77e-09 |
|
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: 61.37 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNILFGKT--FDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAV 130
Cdd:COG5265 447 TIAYNIAYGRPdaSEEEV-EAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 131 DAdvanhllH--RCILGVL-----SHTTrLLCTHRTEYLERADVVLLMEAGQLVRTG 180
Cdd:COG5265 526 DS-------RteRAIQAALrevarGRTT-LVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
644-848 |
2.09e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVePGEKL--------------GIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIP 709
Cdd:PRK10575 13 ALRNVSFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 710 QE-PFLFSGTIREnLDPQGlhedRALWQ-AL-----EQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDA 782
Cdd:PRK10575 92 QQlPAAEGMTVRE-LVAIG----RYPWHgALgrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 783 KILCIDEATASVD--QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSAL 848
Cdd:PRK10575 167 RCLLLDEPTSALDiaHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
53-185 |
2.16e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.35 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNILFG----KTFDAQLYREVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDP 126
Cdd:PRK09452 102 TVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 127 LAAVDA----DVANHL--LHRcILGVlshtTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK09452 172 LSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-185 |
2.39e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSL------LAAIT-GELHrLCGWVaVSELskgfglatqEPWIQ-CA------------TIRDNILFG--- 61
Cdd:PRK11650 35 LVGPSGCGKSTLlrmvagLERITsGEIW-IGGRV-VNEL---------EPADRdIAmvfqnyalyphmSVRENMAYGlki 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 -KTFDAQLYREVLEACALnddLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL-- 138
Cdd:PRK11650 104 rGMPKAEIEERVAEAARI---LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrl 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 139 ----LHRCiLGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK11650 176 eiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
648-839 |
2.42e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 648 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAE-LRSQLAVIP---QEPFLF-SGTIREN 722
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYlDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 LDPQgLHEDRALWQ--ALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 800
Cdd:PRK15439 362 VCAL-THNRRGFWIkpARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039753393 801 LLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:PRK15439 441 DIYQLI-RSIAaqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
648-840 |
2.64e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 648 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLePNAGRVLLDNVDTSQLELAEL---RSQLAviPQEPFLFSGTIRENLD 724
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 725 ---PQGLHEDRAlwqaleQCHLSEVAVAMgGLDGELGERGQNLSLGQRQLLCLARALLT-------DAKILCIDEATASV 794
Cdd:PRK03695 92 lhqPDKTRTEAV------ASALNEVAEAL-GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 795 D--QKT--DQLLQQtICKrfANKTVLTIAHRLN-TILNSDRVLVLQAGRVV 840
Cdd:PRK03695 165 DvaQQAalDRLLSE-LCQ--QGIAVVMSSHDLNhTLRHADRVWLLKQGKLL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
644-851 |
3.32e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL--DNVDTSQLELaelRSQLAVIPQEpflFS--G-- 717
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgQPVDAGDIAT---RRRVGYMSQA---FSlyGel 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 TIRENLDpqgLH-------EDRA---LWQALEQCHLSEVAvamggldgelGERGQNLSLGQRQLLCLARALLTDAKILCI 787
Cdd:NF033858 355 TVRQNLE---LHarlfhlpAAEIaarVAEMLERFDLADVA----------DALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 788 DEATASVD-QKTDQLLQQTIckRFANKTVLTI---AHRLNTILNSDRVLVLQAGRVVELDSPSALRNQ 851
Cdd:NF033858 422 DEPTSGVDpVARDMFWRLLI--ELSREDGVTIfisTHFMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
643-841 |
3.59e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 643 NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQL---ELAELRSQLAVIPQEPFLFSGTI 719
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 720 --RENLDPQGLHEDRALWQALEQchlsevAVAMGGLDGeLGER----GQNLSLGQRQLLCLARALLTDAKILCIDEATAS 793
Cdd:PRK10584 104 naLENVELPALLRGESSRQSRNG------AKALLEQLG-LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 794 VDQKT-DQL--LQQTICKRFANkTVLTIAHRLNTILNSDRVLVLQAGRVVE 841
Cdd:PRK10584 177 LDRQTgDKIadLLFSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-185 |
3.97e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE--------------LSKGFGLATQEPWIQC--ATIRDNILFG-KTF- 64
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknkklkpLRKKVGIVFQFPEHQLfeETVEKDICFGpMNFg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 ----DA-QLYREVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL- 138
Cdd:PRK13634 116 vseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMm 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 139 -----LHRcilgvLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13634 186 emfykLHK-----EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-183 |
3.97e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAI-------TGELHRLCGWVAVselskgfgLATQEPWIQCATIRDNILFGKT---FDAQLYREVLE 74
Cdd:COG4178 394 ITGPSGSGKSTLLRAIaglwpygSGRIARPAGARVL--------FLPQRPYLPLGTLREALLYPATaeaFSDAELREALE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 75 ACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLL 154
Cdd:COG4178 466 AVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPGTTVIS 539
|
170 180
....*....|....*....|....*....
gi 1039753393 155 CTHRTEYLERADVVLLMEAGQLVRTGPPS 183
Cdd:COG4178 540 VGHRSTLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
626-845 |
5.15e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 626 GSVEFQDVVLVYRPGLP---NALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQ-----LE 697
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 698 LAELRSQLAVIPQEP--FLFSGTIRENL--DPQGLHEDRAlwQALEQchLSEVaVAMGGLDGELGERGQ-NLSLGQRQLL 772
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKK--VPEL-LKLVQLPEDYVKRSPfELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-186 |
5.43e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.08 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQCA-TIRDNILFGKTfdaqLYR 70
Cdd:PRK09536 31 LVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsarAASRRVASVPQDTSLSFEfDVRQVVEMGRT----PHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACALNDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGV 146
Cdd:PRK09536 107 SRFDTWTETDRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 147 LSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK09536 187 DDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-186 |
5.94e-09 |
|
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: 57.35 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS---KGFGLATQE----PWIqcaTIRDNILFG----KTFDAQ 67
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKpdsgkiLLNG-KDITNLPpekRDISYVPQNyalfPHM---TVYKNIAYGlkkrKVDKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLlhRCILGVL 147
Cdd:cd03299 106 IERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL--REELKKI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 148 SH---TTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03299 176 RKefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-186 |
6.87e-09 |
|
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: 57.21 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSK---------------GFGLATQEpwiqcaTIRDNILF- 60
Cdd:cd03258 34 FGIIGRSGAGKSTLIRCING-LERptsgsvLVDGTDLTLLSGkelrkarrrigmifqHFNLLSSR------TVFENVALp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 61 ------GKTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 134
Cdd:cd03258 107 leiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 135 ANH---LLHR--CILGVlshtTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03258 176 TQSilaLLRDinRELGL----TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
639-843 |
8.26e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 639 PGLPnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVL--------FrllepnAGRVLLDNvdtsqlELAELRS------- 703
Cdd:NF040905 12 PGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsY------EGEILFDG------EVCRFKDirdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 704 QLAVIPQE----PFLfsgTIRENL---DPQG----LHEDRALWQALEQchLSEVavamgGLDGELGERGQNLSLGQRQLL 772
Cdd:NF040905 79 GIVIIHQElaliPYL---SIAENIflgNERAkrgvIDWNETNRRAREL--LAKV-----GLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 773 CLARALLTDAKILCIDEATASV-DQKTDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVE-LD 843
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQgiTSIIISHKLNEIRRvADSITVLRDGRTIEtLD 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
645-838 |
8.61e-09 |
|
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: 55.15 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTsqlelaelrsqLAVIPQepflfsgtirenld 724
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 725 pqglhedralwqaleqchlsevavamggldgelgergqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ 804
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 805 TIcKRFaNKTVLTIAH-R--LNTIlnSDRVLVLQAGR 838
Cdd:cd03221 112 AL-KEY-PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
100-186 |
8.69e-09 |
|
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: 56.93 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------LHRcilgvLSHTTRLLCTHRT-EYLERADVVLLME 172
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMK 210
|
90
....*....|....
gi 1039753393 173 AGQLVRTGPPSEIL 186
Cdd:cd03295 211 NGEIVQVGTPDEIL 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
639-840 |
1.07e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 639 PGLpNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLD----NVDTSQlelAELRSQLAVIPQEPFL 714
Cdd:PRK10982 9 PGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeiDFKSSK---EALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 F-SGTIRENL------------DPQGLHED-RALWQALeqchlsevavamgGLDGELGERGQNLSLGQRQLLCLARALLT 780
Cdd:PRK10982 85 VlQRSVMDNMwlgryptkgmfvDQDKMYRDtKAIFDEL-------------DIDIDPRAKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 781 DAKILCIDEATASVDQK-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKeVNHLF--TIIRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-133 |
1.08e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.34 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELH---RLCGWV--------AVSELSKGFGLATQEP-----WiqcaTIRDNILFG--KTFDA 66
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSpafSASGEVllngrrltALPAEQRRIGILFQDDllfphL----SVGENLAFAlpPTIGR 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 67 QLYREVLEAcALnddlsilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 133
Cdd:COG4136 108 AQRRARVEQ-AL------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
644-853 |
1.10e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.61 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN----AGRVLLDNVDTSQLELAELR----SQLAVIPQEPflf 715
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRkiigREIAMIFQEP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 716 sgtiRENLDP-----QGLHE------------DRALW---QALEQCHlsEVAV-----AMGGLDGELGErgqnlslGQRQ 770
Cdd:COG4170 99 ----SSCLDPsakigDQLIEaipswtfkgkwwQRFKWrkkRAIELLH--RVGIkdhkdIMNSYPHELTE-------GECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 771 LLCLARALLTDAKILCIDEATASVDQKTD----QLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQaqifRLLARL--NQLQGTSILLISHDLESISQwADTITVLYCGQTVESGPT 243
|
....*...
gi 1039753393 846 SALRNQPH 853
Cdd:COG4170 244 EQILKSPH 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
588-839 |
1.64e-08 |
|
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: 57.91 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 588 AMMVSVERLEEYscdvPQEPHsqplqsphqqriswltqgsvEFQDVVL------VYRPGLPNA--LDGVTFRVEPGEKLG 659
Cdd:TIGR02633 235 TMMVGREITSLY----PHEPH--------------------EIGDVILearnltCWDVINPHRkrVDDVSFSLRRGEILG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 660 IVGRTGSGKSSLFLVLFRLLEPN-AGRVLLDN--VDTSQLELAeLRSQLAVIPQE-------PFLFSG-----------T 718
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-IRAGIAMVPEDrkrhgivPILGVGknitlsvlksfC 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 719 IRENLDPQGlhEDRALWQALEQCHLSEVA--VAMGGLDGelgergqnlslGQRQLLCLARALLTDAKILCIDEATASVD- 795
Cdd:TIGR02633 370 FKMRIDAAA--ELQIIGSAIQRLKVKTASpfLPIGRLSG-----------GNQQKAVLAKMLLTNPRVLILDEPTRGVDv 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 796 -------QKTDQLLQQTIckrfankTVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:TIGR02633 437 gakyeiyKLINQLAQEGV-------AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-185 |
1.67e-08 |
|
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: 56.04 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS--ELSKGFGLATQEPWIQCATI--------R----DNILFGKTFDAQ 67
Cdd:cd03256 29 FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtDINKLKGKALRQLRRQIGMIfqqfnlieRlsvlENVLSGRLGRRS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYR---------EVLEACALNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL 138
Cdd:cd03256 109 TWRslfglfpkeEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 139 LHrcILGVLSHT---TRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03256 184 MD--LLKRINREegiTVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-186 |
1.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.64 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFGKTFDAQLYR 70
Cdd:PRK13642 36 VSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgelltaenvwNLRRKIGMVFQNPDNQFvgATVEDDVAFGMENQGIPRE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhRCILGVLS-- 148
Cdd:PRK13642 116 EMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM-RVIHEIKEky 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039753393 149 HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13642 191 QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-186 |
2.18e-08 |
|
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: 56.11 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELSKG----------------FGLATQEpwiqcaTIRDNILFG-- 61
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVlidgqDIAAMSRKelrelrrkkismvfqsFALLPHR------TVLENVAFGle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 -----KTFDAQLYREVLEACALNDDLSILPagDQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD----A 132
Cdd:cd03294 129 vqgvpRAEREERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 133 DVANHLLHrciLGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03294 198 EMQDELLR---LQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
644-839 |
2.30e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.17 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLE----PNAGRVLLDNVDTSQLELA----ELRSQLAVIPQEPFLF 715
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTVQREGRLArdirKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 716 SG-TIREN-----LDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDE 789
Cdd:PRK09984 99 NRlSVLENvligaLGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 790 ATASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRV 839
Cdd:PRK09984 179 PIASLDPESARIVMDTL--RDINQndgiTVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
100-180 |
2.65e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSHT--TRLLCTHRTEYLER-ADVVLLMEAGQL 176
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHI 219
|
....
gi 1039753393 177 VRTG 180
Cdd:PRK11124 220 VEQG 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-138 |
3.04e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.38 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelsKGFGLA--TQEPWI-QCATIRDNILFGKTFDAQL---YREVLEAC 76
Cdd:COG0488 27 IGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---KGLRIGylPQEPPLdDDLTVLDTVLDGDAELRALeaeLEELEAKL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 77 ALNDDLSILPAGDQTEVGEKGV--------------------------TLSGGQRARIALARAVYQEKALYLLDDPlaav 130
Cdd:COG0488 104 AEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEP---- 179
|
....*...
gi 1039753393 131 dadvANHL 138
Cdd:COG0488 180 ----TNHL 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-186 |
3.43e-08 |
|
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: 57.12 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 4 GIVGKVGCGKSSL---LAAIT----GELHRLCG--WVAVSELS-KGFGLATqePWIqcatirdNILFgKTFDAQLYREVL 73
Cdd:TIGR03269 314 GIVGTSGAGKTTLskiIAGVLeptsGEVNVRVGdeWVDMTKPGpDGRGRAK--RYI-------GILH-QEYDLYPHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 74 E------ACALNDDLSILPA-------GDQTEVGEKGV-----TLSGGQRARIALARAVYQEKALYLLDDPLAAVD---- 131
Cdd:TIGR03269 384 DnlteaiGLELPDELARMKAvitlkmvGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitk 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 132 ADVANHLLH-RCILGvlshTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:TIGR03269 464 VDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-206 |
3.57e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.90 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 4 GIVGKVGCGKSSLLAAITGELHRLCGWVAVSEL--------------SKGFGLATQEPWIQC--ATIRDNILFGKTfDAQ 67
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikpvRKKVGVVFQFPESQLfeETVLKDVAFGPQ-NFG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGV 146
Cdd:PRK13643 115 IPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ--LFES 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 147 LSHT--TRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEILPLVQ-------AVPTAWAEKEQVATSG 206
Cdd:PRK13643 190 IHQSgqTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflkahelGVPKATHFADQLQKTG 259
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
2-171 |
3.65e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.16 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSeLSKGFGLATQ---EPWIQCATIRDNILFGKTFDAQLYR-------- 70
Cdd:NF040873 20 LTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-GGARVAYVPQrseVPDSLPLTVRDLVAMGRWARRGLWRrltrddra 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 ---EVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLlhRCILGVL 147
Cdd:NF040873 99 avdDALERVGL-ADLAGRQLG----------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI--IALLAEE 165
|
170 180
....*....|....*....|....*.
gi 1039753393 148 SHTTR--LLCTHRTEYLERADVVLLM 171
Cdd:NF040873 166 HARGAtvVVVTHDLELVRRADPCVLL 191
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
650-806 |
3.70e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 650 FRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPqepflfsgTIRENLDP-QGL 728
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP--------GLKADLSTlENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 729 HedraLWQALEQCHLSEV---AVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQT 805
Cdd:PRK13543 104 H----FLCGLHGRRAKQMpgsALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
.
gi 1039753393 806 I 806
Cdd:PRK13543 180 I 180
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
654-845 |
4.04e-08 |
|
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: 53.15 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 654 PGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGtirenldpqglhedra 733
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 734 lwqaleqchlsevavamggldgelgergqnlsLGQRQLlcLARALLTDAKILCIDEATASVDQKTDQLLQQTIC------ 807
Cdd:smart00382 65 --------------------------------LRLRLA--LALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 808 -KRFANKTVLTIAHRLNTILnsDRVLVLQAGRVVELDSP 845
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-185 |
4.72e-08 |
|
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: 54.43 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelskGFGLATQEPWIQ-----CAtiRDNILFGK-------TFDAQLYR 70
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAARqslgyCP--QFDALFDEltvrehlRFYARLKG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACALNDDLsILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSH 149
Cdd:cd03263 105 LPKSEIKEEVEL-LLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAIWDLILEVRKG 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 150 TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03263 183 RSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
644-839 |
5.07e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRL--LEPNA---GRVLL--DNVDTSQLELAELRSQLAVIPQEPFLFS 716
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFhgKNLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 GTIRENL-------DPQGlHEDRALWQALEQCHL-SEVavamgglDGELGERGQNLSLGQRQLLCLARALLTDAKILCID 788
Cdd:PRK14243 105 KSIYDNIaygarinGYKG-DMDELVERSLRQAALwDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 789 EATASVDQ----KTDQLLQQtICKRFankTVLTIAHRLNtilnsdrvlvlQAGRV 839
Cdd:PRK14243 177 EPCSALDPistlRIEELMHE-LKEQY---TIIIVTHNMQ-----------QAARV 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-191 |
5.35e-08 |
|
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: 54.60 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCG--WVA---VSELS--------KGFGLATQepwiQCA-----TIRDNILFG--- 61
Cdd:COG1127 34 LAIIGGSGSGKSVLLKLIIGLLRPDSGeiLVDgqdITGLSekelyelrRRIGMLFQ----GGAlfdslTVFENVAFPlre 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 -KTFDAQLYRE----VLEACALNDDLSILPAgdqtevgEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD---AD 133
Cdd:COG1127 110 hTDLSEAEIRElvleKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPTAGLDpitSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 134 VANHLLHRC--ILGvlshTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL----PLVQA 191
Cdd:COG1127 179 VIDELIRELrdELG----LTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLasddPWVRQ 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-185 |
5.43e-08 |
|
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: 56.35 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGE----------LHRL-----CGWVAVSELSK------GFGLATQEP--WIQCATIRDN-- 57
Cdd:TIGR03269 29 LGILGRSGAGKSVLMHVLRGMdqyeptsgriIYHValcekCGYVERPSKVGepcpvcGGTLEPEEVdfWNLSDKLRRRir 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 58 ----ILFGKTFdaQLYRE--VLEAC--ALND-----DLSILPAGD---QTEVGEK----GVTLSGGQRARIALARAVYQE 117
Cdd:TIGR03269 109 kriaIMLQRTF--ALYGDdtVLDNVleALEEigyegKEAVGRAVDlieMVQLSHRithiARDLSGGEKQRVVLARQLAKE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 118 KALYLLDDPLAAVDADVANhLLHRCIL-GVL-SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:TIGR03269 187 PFLFLADEPTGTLDPQTAK-LVHNALEeAVKaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-180 |
6.46e-08 |
|
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: 54.08 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELH-------RLCGWVAVSELSKGFGLAtqepwiqcATIRDNILFG-------KTFDAQL 68
Cdd:cd03220 51 IGLIGRNGAGKSTLLRLLAGIYPpdsgtvtVRGRVSSLLGLGGGFNPE--------LTGRENIYLNgrllglsRKEIDEK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 YREVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-------DVANHLLHR 141
Cdd:cd03220 123 IDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAafqekcqRRLRELLKQ 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 142 C-ILGVLSH---TTRLLCthrteyleraDVVLLMEAGQLVRTG 180
Cdd:cd03220 192 GkTVILVSHdpsSIKRLC----------DRALVLEKGKIRFDG 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-185 |
6.56e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.81 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSEL---SKGFGLATQE----PWIQCAtirDNILFG----KTF 64
Cdd:PRK11000 32 VVFVGPSGCGKSTLLRMIagleditSGDL--FIGEKRMNDVppaERGVGMVFQSyalyPHLSVA---ENMSFGlklaGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 DAQLYREVLEACAlnddlsILPAGDQTEVGEKgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------ 138
Cdd:PRK11000 107 KEEINQRVNQVAE------VLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrieisr 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753393 139 LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK11000 179 LHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
646-852 |
6.58e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 646 DGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN----AGRVLLDNVdtsQLELAELRSQL-AVIPQEP---FLFSG 717
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRGRKiATIMQNPrsaFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 718 TI----RENLDPQGLHEDRA-LWQALEQCHLSEVAVAMGGLDGElgergqnLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PRK10418 97 TMhthaRETCLALGKPADDAtLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 793 SVD----QKTDQLLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK10418 170 DLDvvaqARILDLLESIVQKR--ALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
638-840 |
7.27e-08 |
|
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: 53.81 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 638 RPGLPNA--LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNA---GRVLLDNVDtSQLELAELRSQLAVIPQEP 712
Cdd:cd03233 14 GKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIP-YKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 713 FLFSG-TIRENLdpqglheDRALwqaleQCHLSEVAvamggldgelgeRGqnLSLGQRQLLCLARALLTDAKILCIDEAT 791
Cdd:cd03233 93 VHFPTlTVRETL-------DFAL-----RCKGNEFV------------RG--ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 792 ASVDQKTD-QLLQ--QTICKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVV 840
Cdd:cd03233 147 RGLDSSTAlEILKciRTMADVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-185 |
7.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.67 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV------------SELSKGFGLATQEPWIQC--ATIRDNILFGKT----F 64
Cdd:PRK13637 36 VGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkkvklSDIRKKVGLVFQYPEYQLfeETIEKDIAFGPInlglS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 DAQLYREVLEACALnddlsilpAG-DQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA----DVANHL 138
Cdd:PRK13637 116 EEEIENRVKRAMNI--------VGlDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 139 --LHRcilgvLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13637 188 keLHK-----EYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-186 |
8.24e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.61 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-----------ELSKGFGLATQEPWIQCA--TIRDNILFGKTFDAQLY 69
Cdd:PRK13644 31 IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklqGIRKLVGIVFQNPETQFVgrTVEEDLAFGPENLCLPP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSH 149
Cdd:PRK13644 111 IEIRKRV----DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 150 TTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13644 187 KTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-184 |
1.04e-07 |
|
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: 53.59 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITG--------------ELHRL------------CGWVAVSelskgFGLatqepwIQCATIRD 56
Cdd:COG4181 41 VAIVGASGSGKSTLLGLLAGldrptsgtvrlagqDLFALdedararlrarhVGFVFQS-----FQL------LPTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 57 NI-----LFGKTFDAQLYREVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD 131
Cdd:COG4181 110 NVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 132 ADVANHllhrcILGVL------SHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSE 184
Cdd:COG4181 179 AATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
53-186 |
1.22e-07 |
|
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: 53.32 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNIL-----FGKTFDAQlyREVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPL 127
Cdd:cd03218 91 TVEENILavleiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 128 AAVD----ADVAN---HLLHRCIlGVL--SHTTRllcthrtEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03218 162 AGVDpiavQDIQKiikILKDRGI-GVLitDHNVR-------ETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-186 |
1.31e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.22 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQEPwiqcA-----------------TIRDNILFG---- 61
Cdd:COG3840 28 VAILGPSGAGKSTLLNLIAGFLPPDSGRI----LWNGQDLTALPP----AerpvsmlfqennlfphlTVAQNIGLGlrpg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 ---KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD------- 131
Cdd:COG3840 100 lklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqem 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 132 ADVANHLLHRcilgvlSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG3840 169 LDLVDELCRE------RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
625-841 |
1.33e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 625 QGSVEFQDVVLVYRpglpnALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEpNAGRVLLDNVDTSQLELAEL--- 701
Cdd:PRK11022 8 KLSVHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRIsek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 702 -RSQL-----AVIPQEP-------FLFSGTIRENLDP-QGLHEDRALWQALEQCHLsevaVAMGGLDGELGERGQNLSLG 767
Cdd:PRK11022 82 eRRNLvgaevAMIFQDPmtslnpcYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQ----VGIPDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 768 QRQLLCLARALLTDAKILCIDEATASVD-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVVE 841
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDvtiqaQIIELLLE---LQQKENMALVLITHDLALVAEAaHKIIVMYAGQVVE 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-185 |
1.65e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAI------------TGEL----HRLCG-WVAVSELSKGFGLATQEPWIQCATIRDNILFGKTFDAQ 67
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrmndlnpevtiTGSIvyngHNIYSpRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCI 143
Cdd:PRK14239 116 KDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 144 LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK14239 192 LGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
623-843 |
1.82e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 623 LTQGSVEFQDVVLvyrpglpnaLDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLfrllepnAGRVLLD--------NVDTS 694
Cdd:PRK11147 6 IHGAWLSFSDAPL---------LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyeqDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 695 QL---------------------ELAE-------LRSQLAVIPQEPFLFS-GTIRENLDPQGlhedraLWQaLEQcHLSE 745
Cdd:PRK11147 70 RLqqdpprnvegtvydfvaegieEQAEylkryhdISHLVETDPSEKNLNElAKLQEQLDHHN------LWQ-LEN-RINE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 746 VAVAMgGLDGE--LGErgqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANKTVLtIAHrln 823
Cdd:PRK11147 142 VLAQL-GLDPDaaLSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQGSIIF-ISH--- 211
|
250 260
....*....|....*....|.
gi 1039753393 824 tilnsDRVLVLQ-AGRVVELD 843
Cdd:PRK11147 212 -----DRSFIRNmATRIVDLD 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
644-853 |
2.35e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN----AGRVLLDNVDTSQLELAELRS----QLAVIPQEPflf 715
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 716 sgtiRENLDP-----------------QGLHEDRALWQ---ALEQCH---LSEVAVAMGGLDGELGErgqnlslGQRQLL 772
Cdd:PRK15093 99 ----QSCLDPservgrqlmqnipgwtyKGRWWQRFGWRkrrAIELLHrvgIKDHKDAMRSFPYELTE-------GECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 773 CLARALLTDAKILCIDEATASVDQKTdqllQQTICKRFA------NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPS 243
|
....*...
gi 1039753393 846 SALRNQPH 853
Cdd:PRK15093 244 KELVTTPH 251
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
648-845 |
2.44e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 648 VTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQG 727
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 728 LHEDRALWQALEQCHLSEVAVAM--GGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD--QKTDQLLQ 803
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMqaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDisHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 804 QTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 845
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-184 |
2.90e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 52.36 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKG--------FGLATQEPW-IQCATIRDNILF-----GKTf 64
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERptsgqvLVNG-QDLSRLKRReipylrrrIGVVFQDFRlLPDRTVYENVALplrvtGKS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 65 DAQLYREVLEACALnddlsilpagdqteVG--EKG----VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN-- 136
Cdd:COG2884 111 RKEIRRRVREVLDL--------------VGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWei 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 137 -HLLHR-CILGvlshTTRLLCTHRTEYLERADV-VLLMEAGQLVRTGPPSE 184
Cdd:COG2884 177 mELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-186 |
3.49e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE-----------LSKGFGLATQEPWI-QCATIRDNILFGKTFDAQLY 69
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplharARRGIGYLPQEASIfRRLSVYDNLMAVLQIRDDLS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLE--ACALNDDLSILPAGDQTevgekGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD-------ADVANHLLH 140
Cdd:PRK10895 111 AEQREdrANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvidiKRIIEHLRD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753393 141 RCiLGVL--SHTTRllctHRTEYLERADVVllmEAGQLVRTGPPSEIL 186
Cdd:PRK10895 186 SG-LGVLitDHNVR----ETLAVCERAYIV---SQGHLIAHGTPTEIL 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-132 |
3.65e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.56 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWIqcaTIRDNILFGKTFD----AQ 67
Cdd:COG4525 35 FVVALGASGCGKTTLLNLIAGFLApssgeiTLDG-VPVTGPGADRGVVFQKdallPWL---NVLDNVAFGLRLRgvpkAE 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 68 LYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 132
Cdd:COG4525 111 RRARAEELLAL--------------VGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-185 |
3.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS--------------ELSKGFGLATQEPWIQC--ATIRDNILFG-KTFD 65
Cdd:PRK13641 36 VALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnknlkKLRKKVSLVFQFPEAQLfeNTVLKDVEFGpKNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQlyrevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI 143
Cdd:PRK13641 116 FS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 144 LGVLSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13641 190 DYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-186 |
4.08e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLL------------AAITGELhRLCGWVAVS------ELSKGFGLATQEP-WIQCATIRDNILFGKTFD 65
Cdd:PRK14267 35 LMGPSGCGKSTLLrtfnrllelneeARVEGEV-RLFGRNIYSpdvdpiEVRREVGMVFQYPnPFPHLTIYDNVAIGVKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 A---------QLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVAN 136
Cdd:PRK14267 114 GlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGT 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 137 HLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK14267 186 AKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
53-192 |
5.08e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.57 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNIL-----FGKTFDAQlyREVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPL 127
Cdd:COG1137 94 TVEDNILavlelRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 128 AAVD----ADVAN---HLLHRCIlGVL--SHTTRllcthrtEYLERADVVLLMEAGQLVRTGPPSEIL--PLVQAV 192
Cdd:COG1137 165 AGVDpiavADIQKiirHLKERGI-GVLitDHNVR-------ETLGICDRAYIISEGKVLAEGTPEEILnnPLVRKV 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-138 |
5.33e-07 |
|
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: 49.75 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKgFGLATQepwiqcatirdnilfgktfdaqlyrevleacalnddl 82
Cdd:cd03221 29 IGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-IGYFEQ------------------------------------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 83 silpagdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLaavdadvaNHL 138
Cdd:cd03221 71 -----------------LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-186 |
6.17e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAI-------TGEL-----HRLCGWVAVSELSKGFGLATQE----PWIqcaTIRDNILFG----- 61
Cdd:PRK09493 30 VVIIGPSGSGKSTLLRCInkleeitSGDLivdglKVNDPKVDERLIRQEAGMVFQQfylfPHL---TALENVMFGplrvr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 --KTFDA-QLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvanhL 138
Cdd:PRK09493 107 gaSKEEAeKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE----L 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 139 LHRcILGVLSH-----TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK09493 172 RHE-VLKVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
645-845 |
6.49e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLF-RLLEPNA-------GRVLLDNVDTSQLE---LAELRSQLAVIPQEPF 713
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDaprLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 714 LFSgtIRE-NLDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARAL---------LTDAK 783
Cdd:PRK13547 97 AFS--AREiVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 784 ILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSP 845
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVrrLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
100-185 |
8.92e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.03 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARA-VYQEKALyLLDDPLAAVDADvanhlLHRCI----------LGVlshtTRLLCTH-RTEYLERADV 167
Cdd:PRK11432 137 ISGGQQQRVALARAlILKPKVL-LFDEPLSNLDAN-----LRRSMrekirelqqqFNI----TSLYVTHdQSEAFAVSDT 206
|
90
....*....|....*...
gi 1039753393 168 VLLMEAGQLVRTGPPSEI 185
Cdd:PRK11432 207 VIVMNKGKIMQIGSPQEL 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
660-840 |
9.20e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 660 IVGRTGSGKSSLFLVLFRLLEPNAGRVLLDN---VDTSQ-LELAELRSQLAVIPQEPFLFSG-TIRENLDPQGLHEDRAL 734
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 735 WQALeqchlsevaVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQ--QTICKRFa 811
Cdd:PRK11144 109 FDKI---------VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPylERLAREI- 178
|
170 180 190
....*....|....*....|....*....|
gi 1039753393 812 NKTVLTIAHRLNTILN-SDRVLVLQAGRVV 840
Cdd:PRK11144 179 NIPILYVSHSLDEILRlADRVVVLEQGKVK 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
89-186 |
9.55e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.12 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 89 DQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-A 165
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvS 219
|
90 100
....*....|....*....|.
gi 1039753393 166 DVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK10619 220 SHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-185 |
1.04e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 6 VGKVGCGKSSLLAAITGELHRLCGWVAVSELS--------------KGFGLATQEPWIQC--ATIRDNILFG-------K 62
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirKKVGLVFQFPESQLfeETVLKDVAFGpqnfgvsQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 63 TFDAQLYREVLEACALNDDLsilpagdqteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL---- 138
Cdd:PRK13649 119 EEAEALAREKLALVGISESL----------FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELmtlf 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 139 --LHRcilgvlSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13649 189 kkLHQ------SGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-186 |
1.29e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.16 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAVSE---------------LSKGFGLATQEPWIQC--ATIRDNILFGKTFDAQ 67
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrLRKEIGLVFQFPEYQLfqETIEKDIAFGPVNLGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYREVLEACALNDDLSILPagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA----DVANHLLHrci 143
Cdd:PRK13645 122 NKQEAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFER--- 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039753393 144 LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13645 196 LNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
645-834 |
1.46e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVlldnVDTSQLELAELRSQLAVIPQEPFLFSGTIRenLD 724
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYLDTTLPLTVNRFLR--LR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 725 PqGLHEDRALwQALEQCHLSEVavamggLDGELgergQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ 804
Cdd:PRK09544 94 P-GTKKEDIL-PALKRVQAGHL------IDAPM----QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 1039753393 805 TI--CKRFANKTVLTIAHRLNTIL-NSDRVLVL 834
Cdd:PRK09544 162 LIdqLRRELDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-163 |
1.52e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRL--CGWVAVSELskgfglatqePWIQCATIRDNILFGKTFDAQLyrEVLEACALN 79
Cdd:COG2401 58 IVLIVGASGSGKSTLLRLLAGALKGTpvAGCVDVPDN----------QFGREASLIDAIGRKGDFKDAV--ELLNAVGLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 80 DDLSILPAGDQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH---TTRLLCT 156
Cdd:COG2401 126 DAVLWLRRFKE---------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR--NLQKLARragITLVVAT 194
|
....*..
gi 1039753393 157 HRTEYLE 163
Cdd:COG2401 195 HHYDVID 201
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
5-185 |
1.53e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAVSE-----LSKGFGLATQEPWI----QCA------TIRDNILFG-KTFDAQL 68
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIgyvfQDArlfphyKVRGNLRYGmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 YREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS 148
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 149 HTTR---LLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK11144 176 REINipiLYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
645-820 |
1.57e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVdtsqlelaelrsQLAVIPQEpflfsgtiRENL 723
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KLAYVDQS--------RDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DPqglheDRALWQaleqchlsEVAvamGGLD---------------GELGERGQ-------NLSLGQRQLLCLARALLTD 781
Cdd:TIGR03719 398 DP-----NKTVWE--------EIS---GGLDiiklgkreipsrayvGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSG 461
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 782 AKILCIDEATASVDQKTDQLLQQTICKrFANkTVLTIAH 820
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLN-FAG-CAVVISH 498
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-162 |
1.91e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.67 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAaITGELHRLCGWV-AVSELSKGFGLAtQEPWIQCATIRDNILFGKTFDAQLYR----EVLEACALN 79
Cdd:TIGR00954 483 ICGPNGCGKSSLFR-ILGELWPVYGGRlTKPAKGKLFYVP-QRPYMTLGTLRDQIIYPDSSEDMKRRglsdKDLEQILDN 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 80 DDLS-ILpagdQTEVGEKGV-----TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRC-----ILGVLS 148
Cdd:TIGR00954 561 VQLThIL----EREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCrefgiTLFSVS 636
|
170
....*....|....
gi 1039753393 149 HTTRLLCTHrtEYL 162
Cdd:TIGR00954 637 HRKSLWKYH--EYL 648
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-186 |
2.12e-06 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 50.11 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGfGLATQE-----------PWiqcaTIRDNILFG--- 61
Cdd:COG4559 29 LTAIIGPNGAGKSTLLKLLTGELTpssgevRLNG-RPLAAWSPW-ELARRRavlpqhsslafPF----TVEEVVALGrap 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 ----KTFDAQLYREVLEACalndDLSILPAGDQTevgekgvTLSGGQRARIALARAVYQ--------EKALyLLDDPLAA 129
Cdd:COG4559 103 hgssAAQDRQIVREALALV----GLAHLAGRSYQ-------TLSGGEQQRVQLARVLAQlwepvdggPRWL-FLDEPTSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 130 VD-------ADVANHLLHR-----CILGVLSHTTRllcthrteYlerADVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG4559 171 LDlahqhavLRLARQLARRgggvvAVLHDLNLAAQ--------Y---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-186 |
2.13e-06 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 49.74 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSK-GFGLATQEPWI-QCATIRDNILFGKTFDAQL 68
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLISGFLrptsgsvlfdgEDITGL-PPHEIARlGIGRTFQIPRLfPELTVLENVMVAAQARTGS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 Y-----------------REVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 131
Cdd:cd03219 107 GlllararreereareraEELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 132 ADVANHLLHRcILGV-LSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03219 176 PEETEELAEL-IRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
99-176 |
2.67e-06 |
|
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: 49.07 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 99 TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHllhrcILGVL-----SHTTRLLCTHRTEY-LERADVVLLME 172
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE-----VLDVMkdlaeEGMTMVVVTHEMGFaREVADRVIFMD 209
|
....
gi 1039753393 173 AGQL 176
Cdd:cd03262 210 DGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-186 |
3.12e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 49.38 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCG-----WvAVSELSKGFGLATQE-----PWiqcaTIRDNILFG---- 61
Cdd:PRK13548 30 VVAILGPNGAGKSTLLRALSGELSpdsgevRLNGrpladW-SPAELARRRAVLPQHsslsfPF----TVEEVVAMGraph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 ---KTFDAQLYREVLEACALnDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQ------EKALYLLDDPLAAVD- 131
Cdd:PRK13548 105 glsRAEDDALVAAALAQVDL-AHLA----------GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDl 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 132 ------ADVANHLLHRCILGVLS--H----TTRllcthrteYlerADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13548 174 ahqhhvLRLARQLAHERGLAVIVvlHdlnlAAR--------Y---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-135 |
3.44e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.63 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITG--------ELH------------RLCGWVAVSELSKGFgLATQEPWIQCATIRDNILFG 61
Cdd:PRK09984 32 MVALLGPSGSGKSTLLRHLSGlitgdksaGSHiellgrtvqregRLARDIRKSRANTGY-IFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 KTFDAQLYREVLEACALNDDLSILPAgdQTEVG------EKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 135
Cdd:PRK09984 111 ALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESA 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-186 |
3.55e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCG--WVA-------------VSELSKGFGLATQepwiqcATIRDNILFG-----K 62
Cdd:PRK10771 28 VAILGPSGAGKSTLLNLIAGFLTPASGslTLNgqdhtttppsrrpVSMLFQENNLFSH------LTVAQNIGLGlnpglK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 63 TFDAQlyREVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHl 138
Cdd:PRK10771 102 LNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 139 lhrcILGVLS------HTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK10771 168 ----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-131 |
4.06e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.40 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLL------------AAITGEL----HRL-CGWVAVSELSKGFGLATQEPWIQCATIRDNILFGKTF 64
Cdd:PRK14243 38 ITAFIGPSGCGKSTILrcfnrlndlipgFRVEGKVtfhgKNLyAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARI 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 65 DA------QLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 131
Cdd:PRK14243 118 NGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-186 |
4.28e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------------ELSKGFGLATQEP-WIQCATIRDNILFG-KT 63
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgkdifqidaiKLRKEVGMVFQQPnPFPHLSIYDNIAYPlKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEACalndDLSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLL 139
Cdd:PRK14246 118 HGIKEKREIKKIV----EECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753393 140 HRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK14246 193 EKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-185 |
4.31e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEP--WIQCATIRDNILFGKT---FD-- 65
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitkeniREVRKFVGLVFQNPddQIFSPTVEQDIAFGPInlgLDee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 --AQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcI 143
Cdd:PRK13652 113 tvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--F 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753393 144 LGVLSHT---TRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13652 180 LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
645-838 |
5.20e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPN--AGRVLLDNVDTSQlelaELRSQLAVIPQEPFLFSG-TIRE 721
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 722 NLD-------PQGLHEDRALWQAleQCHLSEVAVAMGG--LDGELGERGqnLSLGQRQLLCLARALLTDAKILCIDEATA 792
Cdd:PLN03211 160 TLVfcsllrlPKSLTKQEKILVA--ESVISELGLTKCEntIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753393 793 SVDQKTDQLLQQTICKrFAN--KTVLTIAHRLNTILNS--DRVLVLQAGR 838
Cdd:PLN03211 236 GLDATAAYRLVLTLGS-LAQkgKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-177 |
5.43e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 47.93 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGEL--HRLCGWVAVSelskgfGLATQEPWIQCATI---RDNILFGktfdaQL-YREVLE- 74
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLIN------GRPLDKRSFRKIIGyvpQDDILHP-----TLtVRETLMf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 75 ACALnddlsilpagdqtevgeKGvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSHTTR-L 153
Cdd:cd03213 106 AAKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRtI 164
|
170 180
....*....|....*....|....*..
gi 1039753393 154 LCT-H--RTEYLERADVVLLMEAGQLV 177
Cdd:cd03213 165 ICSiHqpSSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-195 |
7.12e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELSKGF-----GLAT--QEPWIQC--ATIRDNILFG----KT 63
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSKRGLlalrqQVATvfQDPEQQIfyTDIDSDIAFSlrnlGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEACALNDDLSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLH--R 141
Cdd:PRK13638 109 PEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAiiR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 142 CILGVLSHTtrLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEILPLVQAVPTA 195
Cdd:PRK13638 181 RIVAQGNHV--IISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-138 |
7.30e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELhrlcgwvavsELSKGfglatqepwiqcaTIRdnilFGKT-----FDaQLYREvleaca 77
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLAGEL----------EPDSG-------------TVK----LGETvkigyFD-QHQEE------ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 78 LNDDLSIL-------PAGDQTEV----------GEK-----GVtLSGGQRARIALARAVYQEKALYLLDDPlaavdadvA 135
Cdd:COG0488 390 LDPDKTVLdelrdgaPGGTEQEVrgylgrflfsGDDafkpvGV-LSGGEKARLALAKLLLSPPNVLLLDEP--------T 460
|
...
gi 1039753393 136 NHL 138
Cdd:COG0488 461 NHL 463
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-157 |
8.06e-06 |
|
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: 47.35 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelSKGFGLATQEPWIQCA------------TIRDNILFGKTFDAQLYR 70
Cdd:TIGR01189 29 LQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN--GTPLAEQRDEPHENILylghlpglkpelSALENLHFWAAIHGGAQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACALN--DDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcilgVLS 148
Cdd:TIGR01189 107 TIEDALAAVglTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL----LRA 172
|
170
....*....|...
gi 1039753393 149 HTTR----LLCTH 157
Cdd:TIGR01189 173 HLARggivLLTTH 185
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-191 |
8.52e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.47 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFGktfdaqlyr 70
Cdd:PRK13635 36 VAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseetvwDVRRQVGMVFQNPDNQFvgATVQDDVAFG--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 evLEACALNDDLSIlPAGDQ--TEVG------EKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-------DVA 135
Cdd:PRK13635 107 --LENIGVPREEMV-ERVDQalRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrrevlETV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 136 NHLLHRCILGVLShttrllCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQA 191
Cdd:PRK13635 184 RQLKEQKGITVLS------ITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
53-186 |
9.41e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.67 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNIL-FGKTFDAQLyREVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD 131
Cdd:PRK13536 130 TVRENLLvFGRYFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 132 ADvANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13536 205 PH-ARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
100-186 |
9.47e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.21 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVR 178
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
|
....*...
gi 1039753393 179 TGPPSEIL 186
Cdd:PRK11264 225 QGPAKALF 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-141 |
9.53e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELS-----KGFGLATQEPWIQCATIRDNILfgktFDAQLYREVLE 74
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLlfegeDISTLKpeiyrQQVSYCAQTPTLFGDTVYDNLI----FPWQIRNQQPD 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753393 75 ACALNDDLSI--LPagdqTEVGEKGVT-LSGGQRARIALARAV-YQEKALyLLDDPLAAVDAD---VANHLLHR 141
Cdd:PRK10247 114 PAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLqFMPKVL-LLDEITSALDESnkhNVNEIIHR 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-132 |
1.15e-05 |
|
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: 47.10 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQEPWIQCA--------------TIRDNILFgktfdaql 68
Cdd:cd03231 29 LQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGllylghapgikttlSVLENLRF-------- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 69 yrevleACALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 132
Cdd:cd03231 97 ------WHADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
100-186 |
1.16e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 47.68 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVanhllhrciLGVL-----SHTTRLLCTH-----RteylERA 165
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvGEV---------LDVMrdlakEGMTMVVVTHemgfaR----EVA 203
|
90 100
....*....|....*....|.
gi 1039753393 166 DVVLLMEAGQLVRTGPPSEIL 186
Cdd:COG1126 204 DRVVFMDGGRIVEEGPPEEFF 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-186 |
1.21e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.60 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLL------------AAITGELHrLCGW----VAVSELSKGFGLATQEP-WIQCATIRDNILFGKTFD-- 65
Cdd:PRK14247 34 LMGPSGSGKSTLLrvfnrlielypeARVSGEVY-LDGQdifkMDVIELRRRVQMVFQIPnPIPNLSIFENVALGLKLNrl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 -------AQLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHL 138
Cdd:PRK14247 113 vkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753393 139 LHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK14247 185 IESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-142 |
1.39e-05 |
|
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: 46.38 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAI-------TGELHRLCGwvavselSKGFGLAtQEPWIQCATIRDNIlfgktfdaqlyrevleaca 77
Cdd:cd03223 32 ITGPSGTGKSSLFRALaglwpwgSGRIGMPEG-------EDLLFLP-QRPYLPLGTLREQL------------------- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 78 lnddlsILPAGDqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRC 142
Cdd:cd03223 85 ------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
97-188 |
1.57e-05 |
|
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: 46.75 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 97 GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD-------ADVANHLL--HRCILgVLSHTTRLLcthrtEYLeRADV 167
Cdd:cd03217 102 NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalrlvAEVINKLReeGKSVL-IITHYQRLL-----DYI-KPDR 174
|
90 100
....*....|....*....|.
gi 1039753393 168 VLLMEAGQLVRTGPPSEILPL 188
Cdd:cd03217 175 VHVLYDGRIVKSGDKELALEI 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-180 |
1.61e-05 |
|
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: 46.80 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 4 GIVGKVGCGKSSLLAAITGELHRLCGWVAV---------SELSKGFGLATQEP-WIQCATIRD-----NILFG---KTFD 65
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpQKLRRRIGYLPQEFgVYPNFTVREfldyiAWLKGipsKEVK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLyREVLEACALNDdlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVdaDVANHLLHRCILG 145
Cdd:cd03264 109 ARV-DEVLELVNLGD-----------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEERIRFRNLLS 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753393 146 VLSHT-TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 180
Cdd:cd03264 175 ELGEDrIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
100-192 |
1.88e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.39 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDA----DVANHLLHrciLGVLSHTTRLLCTHRTEYLERADVVLLMEAGQ 175
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGK 221
|
90
....*....|....*..
gi 1039753393 176 LVRTGPPSEILPLVQAV 192
Cdd:PRK13633 222 VVMEGTPKEIFKEVEMM 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
645-852 |
1.95e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.79 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAElrSQLAVIPQEPFLFSG-TIREN- 722
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGENv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 723 ---LDPQGLHEDRALWQALEqchlsevAVAMGGLDGeLGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:PRK11432 100 gygLKMLGVPKEERKQRVKE-------ALELVDLAG-FEDRYvDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 799 DQLLQQTI---CKRFaNKTVLTIAH-RLNTILNSDRVLVLQAGRVVELDSPSALRNQP 852
Cdd:PRK11432 172 RRSMREKIrelQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-186 |
2.88e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.57 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITgELHRLCGWVAVSELSKGFGLATQEPWIQCATIRDNI--LFGKT--FDAQLYREVLEACA 77
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVsmVHPKPnlFPMSVYDNVAYGVK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 78 LN--------DDL--SILPAGD-----QTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA---NHLL 139
Cdd:PRK14258 114 IVgwrpkleiDDIveSALKDADlwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLI 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 140 HRciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEA-----GQLVRTGPPSEIL 186
Cdd:PRK14258 194 QS--LRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-171 |
2.94e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 78 LNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHRCILGVLSHTTR--LLC 155
Cdd:PTZ00265 558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRitIII 636
|
90
....*....|....*.
gi 1039753393 156 THRTEYLERADVVLLM 171
Cdd:PTZ00265 637 AHRLSTIRYANTIFVL 652
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-154 |
4.20e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAvseLSKGFGL------------ATQEPWIQCATIRDNILfgktfdAQLYR 70
Cdd:PRK10636 341 IGLLGRNGAGKSTLIKLLAGELAPVSGEIG---LAKGIKLgyfaqhqleflrADESPLQHLARLAPQEL------EQKLR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 71 EVLEACALNddlsilpaGDQteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI-----LG 145
Cdd:PRK10636 412 DYLGGFGFQ--------GDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIdfegaLV 481
|
....*....
gi 1039753393 146 VLSHTTRLL 154
Cdd:PRK10636 482 VVSHDRHLL 490
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
53-186 |
4.33e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.34 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 53 TIRDNIL-FGKTF--DAQLYREVLEACAlndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAA 129
Cdd:PRK13537 96 TVRENLLvFGRYFglSAAAARALVPPLL---EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753393 130 VDADvANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-164 |
4.54e-05 |
|
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: 45.48 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWV-------------AVSELSKGFGLATQE-PWIQCATIRDNILFGKTFDAQ 67
Cdd:cd03292 29 FVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgrAIPYLRRKIGVVFQDfRLLPDRNVYENVAFALEVTGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 LYRE-------VLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHllh 140
Cdd:cd03292 109 PPREirkrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE--- 174
|
170 180
....*....|....*....|....*....
gi 1039753393 141 rcILGVLSH-----TTRLLCTHRTEYLER 164
Cdd:cd03292 175 --IMNLLKKinkagTTVVVATHAKELVDT 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
594-806 |
4.77e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 594 ERLEEYSCDVPQEPHSQPLQSPHQQRISwLTQGSVEFQDvvlvyRPglpnALDGVTFRVEPGEKLGIVGRTGSGKSSLF- 672
Cdd:PRK10938 235 EQLEGVQLPEPDEPSARHALPANEPRIV-LNNGVVSYND-----RP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLs 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 673 -------------LVLF---RllepNAGRVLLD-----NVDTSQLELaELRsqlavipqepflFSGTIReNLDPQGLHED 731
Cdd:PRK10938 305 litgdhpqgysndLTLFgrrR----GSGETIWDikkhiGYVSSSLHL-DYR------------VSTSVR-NVILSGFFDS 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 732 RALWQAL--EQCHLSEVAVAMGGLDGELGERG-QNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTI 806
Cdd:PRK10938 367 IGIYQAVsdRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-132 |
5.11e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.85 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFGKTFdAQLYRE 71
Cdd:PRK11248 29 LLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDG-KPVEGPGAERGVVFQNegllPW---RNVQDNVAFGLQL-AGVEKM 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 72 VLEACALnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 132
Cdd:PRK11248 104 QRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-186 |
5.11e-05 |
|
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: 45.50 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS------KGFGLATQEPWI-QCATIRDNILFGktfdAQLY 69
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIMGLLPprsgsiRFDG-RDITGLPpherarAGIGYVPEGRRIfPELTVEENLLLG----AYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLEACALNDDLSILPAGDQTEvGEKGVTLSGGQRARIALARAVYQEKALYLLDDP---LA-AVDADVANHLLHRCILG 145
Cdd:cd03224 104 RRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEAIRELRDEG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039753393 146 VlshtTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 186
Cdd:cd03224 183 V----TILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-180 |
5.33e-05 |
|
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: 45.44 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSE----------LSKGFGLAtqePWIqcaTIRDNILFgktFd 65
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEpdagfaTVDGFDVVKEpaearrrlgfVSDSTGLY---DRL---TARENLEY---F- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLY---REVLEAcALNDDLSILPAGDQTEVGEKGvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL--- 139
Cdd:cd03266 103 AGLYglkGDELTA-RLEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRefi 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753393 140 -HRCILGvlshTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 180
Cdd:cd03266 180 rQLRALG----KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
99-142 |
5.54e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.18 E-value: 5.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1039753393 99 TLSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVANHLLHRC 142
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARLEALLAQHA 176
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-188 |
5.83e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.58 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITG----------------------ELHRLCGWVAVSELSKGfGLATQEPWIQCATIRDNIL 59
Cdd:TIGR00955 53 LLAVMGSSGAGKTTLMNALAFrspkgvkgsgsvllngmpidakEMRAISAYVQQDDLFIP-TLTVREHLMFQAHLRMPRR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 60 FGKTFDAQLYREVLEacalndDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 137
Cdd:TIGR00955 132 VTKKEKRERVDEVLQ------ALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753393 138 LLHrcILGVLSHTTR-LLCT-HR--TEYLERADVVLLMEAGQLVRTGPPSEILPL 188
Cdd:TIGR00955 205 VVQ--VLKGLAQKGKtIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-133 |
8.99e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.48 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAVselsKGFGLATQEPWIQCA------------TIRDNILFGKTFDAQLYREV 72
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKL----DGGDIDDPDVAEACHylghrnamkpalTVAENLEFWAAFLGGEELDI 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 73 LEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 133
Cdd:PRK13539 109 AAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
100-179 |
9.05e-05 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 43.57 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVL--SHTTRLLCTHR-TEYLERADVVLLMEAGQL 176
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLraQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
...
gi 1039753393 177 VRT 179
Cdd:cd03216 161 VGT 163
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-183 |
9.62e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 45.11 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQ--CATIRDNILFG----KTFDA 66
Cdd:PRK13647 34 TALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmgrevnaeneKWVRSKVGLVFQDPDDQvfSSTVWDDVAFGpvnmGLDKD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 67 QLYREVLEAcalnddlsiLPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLlhRCILG 145
Cdd:PRK13647 114 EVERRVEEA---------LKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL--MEILD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753393 146 VLSH--TTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPS 183
Cdd:PRK13647 183 RLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-185 |
1.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.16 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--------------KGFGLATQEPWIQC--ATIRDNILFG-KTFDAQ 67
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrKRIGMVFQFPESQLfeDTVEREIIFGpKNFKMN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 68 L-------YREVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLH 140
Cdd:PRK13646 118 LdevknyaHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ-SKRQVM 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753393 141 RCI--LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13646 186 RLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-185 |
1.10e-04 |
|
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: 44.28 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 4 GIVGKVGCGKSS-------LLAAITGELHrLCGWVAVSE---LSKGFGLATQEPWIQCA-TIRDNI-LFGKTFD------ 65
Cdd:cd03265 30 GLLGPNGAGKTTtikmlttLLKPTSGRAT-VAGHDVVREpreVRRRIGIVFQDLSVDDElTGWENLyIHARLYGvpgaer 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 66 AQLYREVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCIL 144
Cdd:cd03265 109 RERIDELLDFVGL------------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753393 145 GVLSH-TTRLLCTHrteYLERA----DVVLLMEAGQLVRTGPPSEI 185
Cdd:cd03265 177 LKEEFgMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
100-176 |
1.67e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.04 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVD---ADVANHLLHRciLGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 176
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGE--LNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
314-429 |
2.48e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 44.07 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 314 LLLFSPGNLYTPLLSTPL--HKAASNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPV 391
Cdd:cd18572 5 LVVAALSELAIPHYTGAVidAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039753393 392 TFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSV 429
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
644-825 |
3.12e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 644 ALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIpqepflfsgtirENL 723
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 724 DPQGlhedraLWQALEQCHLSEVA---VAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TD 799
Cdd:PRK13545 107 ELKG------LMMGLTKEKIKEIIpeiIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTfTK 180
|
170 180
....*....|....*....|....*.
gi 1039753393 800 QLLQQTICKRFANKTVLTIAHRLNTI 825
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
101-210 |
3.36e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 101 SGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVAN---------HLLHRCI---LGVLSHTtrllcthrteyler 164
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNlmmdlqqelGLSYVFIshdLSVVEHI-------------- 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 165 ADVVLLMEAGQLVRTGPPSEIL--P-------LVQAVPTAWAE--KEQVATSGQSPS 210
Cdd:PRK11308 222 ADEVMVMYLGRCVEKGTKEQIFnnPrhpytqaLLSATPRLNPDdrRERIKLTGELPS 278
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
100-186 |
3.71e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.87 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI-LGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLV 177
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVV 244
|
....*....
gi 1039753393 178 RTGPPSEIL 186
Cdd:PRK10070 245 QVGTPDEIL 253
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
100-186 |
3.94e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVL--SHTTRLLCTHRTEY-LERADVVLLMEAGQL 176
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKI 243
|
90
....*....|
gi 1039753393 177 VRTGPPSEIL 186
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-185 |
4.13e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.18 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 5 IVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFG---KTFDAQLY 69
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteenvwDIRHKIGMVFQNPDNQFvgATVEDDVAFGlenKGIPHEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 RE-VLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhRCILGVLS 148
Cdd:PRK13650 118 KErVNEALEL--------VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI-KTIKGIRD 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753393 149 --HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13650 189 dyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-131 |
4.25e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.95 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGL----------ATQEPWIQCATIRDNILFGKTFDAQLYRE 71
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpqSEEVDWSFPVLVEDVVMMGRYGHMGWLRR 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 72 --------VLEACALNDDLSIlpagDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD 131
Cdd:PRK15056 115 akkrdrqiVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
99-180 |
4.54e-04 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 42.27 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 99 TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQL 176
Cdd:cd03269 128 ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
....
gi 1039753393 177 VRTG 180
Cdd:cd03269 207 VLYG 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
652-797 |
4.60e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.74 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 652 VEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV--------LLDNVDTSQLE--LAELRS-QLAVI--PQE----PFL 714
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSELQnyFTKLLEgDVKVIvkPQYvdliPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 715 FSGTIRENLDPQglHEDRALWQALEQCHLSEVavamggLDGELgergQNLSLGQRQLLCLARALLTDAKILCIDEATASV 794
Cdd:cd03236 103 VKGKVGELLKKK--DERGKLDELVDQLELRHV------LDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
...
gi 1039753393 795 DQK 797
Cdd:cd03236 171 DIK 173
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2-192 |
4.91e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLC--GWVAVS------ELSKGFGLATQepwiqcatirDNILFGKTfdaqLYREVL 73
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANnrkptkQILKRTGFVTQ----------DDILYPHL----TVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 74 EACALNDDLSILPAGDQTEVGEK-----GVT--------------LSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 134
Cdd:PLN03211 162 VFCSLLRLPKSLTKQEKILVAESviselGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753393 135 ANHLLHrcILGVLSHTTRLLCTHRTEYLERA----DVVLLMEAGQLVRTGPPSEILPLVQAV 192
Cdd:PLN03211 242 AYRLVL--TLGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
70-186 |
4.94e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 42.75 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 70 REVLEACALND-DLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdvanhLLHRCILGVL- 147
Cdd:PRK10419 132 SEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL-----VLQAGVIRLLk 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039753393 148 -----SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK10419 196 klqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKL 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
100-193 |
5.41e-04 |
|
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: 43.52 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHllhrcILGVLShttRLLCTHRTEYL----------ERADVVL 169
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ-----ILDLLR---DLQREHGLAYLfishdlavvrALAHRVM 497
|
90 100 110
....*....|....*....|....*....|...
gi 1039753393 170 LMEAGQLVRTGPPSEIL--P-------LVQAVP 193
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFdaPqhpytraLLAAAP 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-138 |
8.42e-04 |
|
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: 43.00 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLL---AAI----TGElhrlcgwvAVSELSKGFGLATQEPWI-QCATIRDNILFG------------- 61
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLrimAGVdkdfNGE--------ARPQPGIKVGYLPQEPQLdPTKTVRENVEEGvaeikdaldrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 ---------KTFDAQLYR-----EVLEACA---LNDDLSI------LPAGDQtevgeKGVTLSGGQRARIALARAVYQEK 118
Cdd:TIGR03719 106 isakyaepdADFDKLAAEqaelqEIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKP 180
|
170 180
....*....|....*....|....
gi 1039753393 119 ALYLLDDPLAAVDAD-VA---NHL 138
Cdd:TIGR03719 181 DMLLLDEPTNHLDAEsVAwleRHL 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-195 |
8.56e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.39 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVA----------------VSELSKGFGLATQEPWIQCATIRDNILFG---- 61
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvllggrsifnyrdVLEFRRRVGMLFQRPNPFPMSIMDNVLAGvrah 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 62 KTFDAQLYREVLEAC--------ALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 133
Cdd:PRK14271 129 KLVPRKEFRGVAQARltevglwdAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPT 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753393 134 VANHlLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEILPLVQAVPTA 195
Cdd:PRK14271 198 TTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
52-187 |
9.36e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.09 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 52 ATIRDNILFGKTFDA-------QLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLD 124
Cdd:PRK13640 100 ATVGDDVAFGLENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILD 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 125 DPLAAVDA-------DVANHLLHRCILGVLShttrllCTHRTEYLERADVVLLMEAGQLVRTGPPSEILP 187
Cdd:PRK13640 169 ESTSMLDPagkeqilKLIRKLKKKNNLTVIS------ITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2-186 |
9.86e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.12 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELH--------RLCGWVAVSelskGFGLATQEP---------WIQCA------TIRDNI 58
Cdd:PRK13547 29 VTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN----GEPLAAIDAprlarlravLPQAAqpafafSAREIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 59 LFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ--------EKALY-LLDDPLAA 129
Cdd:PRK13547 105 LLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaQPPRYlLLDEPTAA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753393 130 VDADVANHLLH--RCI-----LGVLS--HTTRLLCTHrteylerADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK13547 185 LDLAHQHRLLDtvRRLardwnLGVLAivHDPNLAARH-------ADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
645-821 |
1.00e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQlELAELRSQLAVIPQE----PFLfsgTIR 720
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsginPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 721 EN--LDpqgLHEDRALWQALEQCHLSEVAVAmggLDGELGErgqnLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 798
Cdd:PRK13540 93 ENclYD---IHFSPGAVGITELCRLFSLEHL---IDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 1039753393 799 DQLLQQTI-CKRFANKTVLTIAHR 821
Cdd:PRK13540 163 LLTIITKIqEHRAKGGAVLLTSHQ 186
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
638-795 |
1.48e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 638 RPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNvdtsqlelaelRSQLAVIPQE-PFLFS 716
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQEtPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 717 GTIRENLDpqGLHEDRALWQALEQCHLSE----VAVAMGGLDG----------------------ELGERGQNLSLGQRQ 770
Cdd:PRK10636 79 PALEYVID--GDREYRQLEAQLHDANERNdghaIATIHGKLDAidawtirsraasllhglgfsneQLERPVSDFSGGWRM 156
|
170 180
....*....|....*....|....*
gi 1039753393 771 LLCLARALLTDAKILCIDEATASVD 795
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-154 |
1.49e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 3 VGIVGKVGCGKSSLLAAITGELHRLCGWV--------AVSELSKGFGL-ATQEPWIQCATIRDNILfgktfdAQLYREVL 73
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmAVFSQHHVDGLdLSSNPLLYMMRCFPGVP------EQKLRAHL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 74 EACALNDDLSILPAgdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCIL---GVL--S 148
Cdd:PLN03073 612 GSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLfqgGVLmvS 681
|
....*.
gi 1039753393 149 HTTRLL 154
Cdd:PLN03073 682 HDEHLI 687
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
99-140 |
1.54e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1039753393 99 TLSGGQRARIALARAVYQEKALYLLDDPlaavdadvANHL-LH 140
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLdLH 378
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
101-168 |
1.55e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 101 SGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL---------HRCILGVLSH---TTRLLCtHRTEYLERADVV 168
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILallkslqqkHQLAYLFISHdlhVVRALC-HQVIVLRQGEVV 505
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
100-185 |
1.87e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 41.32 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnhllhRCILGVLS------HTTRLLCTHRTEYLER-ADVVLLME 172
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATT-----RSILELLKdinrelGLTIVLITHEMDVVKRiCDRVAVID 215
|
90
....*....|...
gi 1039753393 173 AGQLVRTGPPSEI 185
Cdd:PRK11153 216 AGRLVEQGTVSEV 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
660-828 |
2.15e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 660 IVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLelaelrsqlavipQEPFLfsGTIRENLdpqGLH------EDRA 733
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKPYC--TYIGHNL---GLKlemtvfENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 734 LWQAL-EQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTIC-KRFA 811
Cdd:PRK13541 93 FWSEIyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANS 172
|
170
....*....|....*..
gi 1039753393 812 NKTVLTIAHRLNTILNS 828
Cdd:PRK13541 173 GGIVLLSSHLESSIKSA 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
646-798 |
2.91e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 646 DGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLL-DNVdtsqlelaelrsQLAVIPQEpflfsgtiRENLD 724
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV------------KLAYVDQS--------RDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 725 PqglheDRALWQaleqchlsEVAvamGGLD---------------GELGERGQ-------NLSLGQRQLLCLARALLTDA 782
Cdd:PRK11819 401 P-----NKTVWE--------EIS---GGLDiikvgnreipsrayvGRFNFKGGdqqkkvgVLSGGERNRLHLAKTLKQGG 464
|
170
....*....|....*.
gi 1039753393 783 KILCIDEATASVDQKT 798
Cdd:PRK11819 465 NVLLLDEPTNDLDVET 480
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-185 |
3.02e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 40.45 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 2 LVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS------------ELSKGFGLATQEPWIQ--CATIRDNILFG----KT 63
Cdd:PRK13639 30 MVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikydkksllEVRKTVGIVFQNPDDQlfAPTVEEDVAFGplnlGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEACAlnddlsilpagdqtEVGEKGVT------LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 137
Cdd:PRK13639 110 SKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753393 138 LLHrcILGVLSH--TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 185
Cdd:PRK13639 176 IMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
100-210 |
3.21e-03 |
|
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: 40.42 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 100 LSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVANHLLHRC---------I---LGVLSHTtrllcthrteyle 163
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQrelglailfIthdLGVVAEI------------- 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 164 rADVVLLMEAGQLVRTGPPSEIL-----P----LVQAVPTAWAEKEQVAT-SGQSPS 210
Cdd:COG0444 218 -ADRVAVMYAGRIVEEGPVEELFenprhPytraLLSSIPRLDPDGRRLIPiPGEPPS 273
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
640-834 |
3.44e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 640 GLPNALDG-VTFR-------------VEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV--------LLDNVDTSQL- 696
Cdd:PRK13409 70 NLPEELEEePVHRygvngfklyglpiPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRFRGTELq 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 697 ----ELAELRSQLAVIPQE----PFLFSGTIRENLDpqglhedralwQALEQCHLSEVAVAMGgLDGELGERGQNLSLGQ 768
Cdd:PRK13409 150 nyfkKLYNGEIKVVHKPQYvdliPKVFKGKVRELLK-----------KVDERGKLDEVVERLG-LENILDRDISELSGGE 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 769 RQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLnTILN--SDRVLVL 834
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
98-169 |
3.99e-03 |
|
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: 38.88 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 98 VTLSGGQRARIALARAV----YQEKALYLLDDPLAAVDADVANHLLhRCILGVLSHTTRLLC-THRTEYLERADVVL 169
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHLVKGAQVIViTHLPELAELADKLI 151
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
99-186 |
5.10e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.53 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 99 TLSGGQRARIALARAVYQ-------EKALYLLDDPLAAVD-ADVA--NHLLHR-CILGVlshtTRLLCTH---RTeyLER 164
Cdd:PRK03695 126 QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDvAQQAalDRLLSElCQQGI----AVVMSSHdlnHT--LRH 199
|
90 100
....*....|....*....|..
gi 1039753393 165 ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK03695 200 ADRVWLLKQGKLLASGRRDEVL 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
645-707 |
5.83e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 5.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVL-----FRLLEpnaGRVLLDNVDTSQLElAELRSQLAV 707
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKILE---GDILFKGESILDLE-PEERAHLGI 86
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
645-686 |
6.63e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 6.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1039753393 645 LDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRV 686
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-186 |
9.06e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 39.00 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 4 GIVGKVGCGKSSLL-------AAITGELhRLCGWVAVSELSKGFG-----LATQEPWIQCATIRDNILFGK--------T 63
Cdd:PRK10575 41 GLIGHNGSGKSTLLkmlgrhqPPSEGEI-LLDAQPLESWSSKAFArkvayLPQQLPAAEGMTVRELVAIGRypwhgalgR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 64 FDAQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVD----AD 133
Cdd:PRK10575 120 FGAADREKVEEAISL--------------VGLKPLahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753393 134 VANhLLHRcilgvLSHT---TRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 186
Cdd:PRK10575 186 VLA-LVHR-----LSQErglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
94-175 |
9.16e-03 |
|
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: 38.07 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753393 94 GEKGVTLSGGQRARIALARAVYQE--KALYLLDDPLAAVDADVANHLLhRCI--LGVLSHTTrLLCTHRTEYLERADVVL 169
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLL-EVIkgLIDLGNTV-ILIEHNLDVLSSADWII 159
|
....*.
gi 1039753393 170 LMEAGQ 175
Cdd:cd03238 160 DFGPGS 165
|
|
| |
