|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
670-1065 |
0e+00 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 713.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 670 HQPSYTLYNMFDDLILLAKGGLIVYNGPVKSVEDYFSTLGITVPERVNPPDHYIDILEGIVKPE--SGINAKHFPLHWML 747
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEGIVKPStsSGVDYKQLPVRWML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 748 YNGYEVPNDMKDDLKAIGEQR---PHLGSSPSAGSTPHCLP-----HVRNAFAEERDRIEHHLSKPKDLSSRRTPGVIRQ 819
Cdd:pfam19055 81 HNGYPVPPDMLQNADGIAASSgenSSNGTNPGVGSEEQSFAgelwqDVKSNVELKRDHIRHNFLKSKDLSNRRTPGVFRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 820 YKYYLGRVTKQRLREARLLAVDFLILGLAGICLGTIAKLSDPNFGMPGYIYTIIAVSLLCKIAALRSFSLERLQYLRERE 899
Cdd:pfam19055 161 YRYFLGRVGKQRLREARIQAVDYLILLLAGACLGTLAKVSDETFGALGYTYTIIAVSLLCKIAALRSFSLDKLQYWRESA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 900 SGMSSLAYFLARDTIDHFSTIVKPIVYLSMFYYFNNPRSTITDNYIILLALVYCVTGIGYTFAICFNPGSAQLCSALIPV 979
Cdd:pfam19055 241 SGMSSLAYFLAKDTIDHFNTVIKPLVYLSMFYFFNNPRSSFADNYIVLLCLVYCVTGIAYALAIFFEPGPAQLWSVLLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 980 VLTLLSTQNNTPAILNR---LCYPKWALEGFIIVNAKRYPGVWLITRCGLLFRSRFDIHHYMLCILVLFMYGLFFRIVAF 1056
Cdd:pfam19055 321 VLTLIATQTNDSKFLKVlanLCYPKWALEAFVIANAERYSGVWLITRCGALMKSGYDLHDWGLCLVILILYGVLSRIIAF 400
|
....*....
gi 1002258264 1057 VALILVKKR 1065
Cdd:pfam19055 401 FCMVTFQKK 409
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
472-696 |
4.25e-72 |
|
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: 237.45 E-value: 4.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEFKDLTLSL------GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIRSYK 545
Cdd:cd03213 2 VTLSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGFVPQDDVVHGNLTVEENLWFSAKCrlsattahrhkvltvervidsldlqgvrsslvgtvekRGISGGQRKRVNVGI 625
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKL-------------------------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 626 EMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGLIvYNG 696
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVI-YFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
469-1059 |
1.45e-70 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 247.65 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 469 RPLLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVA-GYKVSGSVLVNGRHDNIRSYKKI 547
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkGVKGSGSVLLNGMPIDAKEMRAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTV-EKRGISGGQRKRVNVGIE 626
Cdd:TIGR00955 101 SAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 627 MVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGlIVYNGPVKSVEDYFS 706
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGR-VAYLGSPDQAVPFFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 707 TLGITVPERVNPPDHYIDILEGIvkpesginakhfplhwmlyngyevPNDMKDDLKAIGEQRPHLGSSPSAGSTphclph 786
Cdd:TIGR00955 260 DLGHPCPENYNPADFYVQVLAVI------------------------PGSENESRERIEKICDSFAVSDIGRDM------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 787 VRNAFAEERDriEHHLSKPKDLSSRRT--PGVIRQYKYYLGRVTKQRLREARLLAVDFLILGLAGICLGTIaklsdpNFG 864
Cdd:TIGR00955 310 LVNTNLWSGK--AGGLVKDSENMEGIGynASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLI------YLG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 865 MP----------GYIYTIIA-VSLLCKIAALRSFSLERLQYLRERESGMSSL-AYFLARDTIDHFSTIVKPIVYLSMFYY 932
Cdd:TIGR00955 382 QGltqkgvqninGALFLFLTnMTFQNVFPVINVFTAELPVFLRETRSGLYRVsAYFLAKTIAELPLFIILPALFTSITYW 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 933 FNNPRSTITdNYIILLALVYCV----TGIGYTFAICFNpgSAQLCSALIPVVLT---LLS----TQNNTPAILNRLCYPK 1001
Cdd:TIGR00955 462 MIGLRSGAT-HFLTFLFLVTLVanvaTSFGYLISCAFS--STSMALTVGPPFVIpflLFGgffiNSDSIPVYFKWLSYLS 538
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 1002 W---ALEGFII---VNAKRYP-------GVWLITRCGLLFRSRFDIHHYMLCILVLFMYGLFFRIVAFVAL 1059
Cdd:TIGR00955 539 WfryGNEGLLInqwSDVDNIEctsanttGPCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFAL 609
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
469-958 |
3.97e-49 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 186.24 E-value: 3.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 469 RPLLKVEFK--DLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIRSYKK 546
Cdd:PLN03211 62 KRILGHKPKisDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IiGFVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTVEKRGISGGQRKRVNVGIE 626
Cdd:PLN03211 142 T-GFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 627 MVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGLIvYNGPVKSVEDYFS 706
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL-FFGKGSDAMAYFE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 707 TLGITVPERVNPPDHYIDILEGIVKPEsGINAKhfplhwmlyngyEVPNdMKDDLkaIGEQRPHLGSSPSAGSTPHCLPH 786
Cdd:PLN03211 300 SVGFSPSFPMNPADFLLDLANGVCQTD-GVSER------------EKPN-VKQSL--VASYNTLLAPKVKAAIEMSHFPQ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 787 VRNAFAEERDRIEHHLSKPKDLSSRrtpgvIRQYKYYLGRVTKQRLREA-RLLAVDFLIlgLAGICLGTIAKLSD----- 860
Cdd:PLN03211 364 ANARFVGSASTKEHRSSDRISISTW-----FNQFSILLQRSLKERKHESfNTLRVFQVI--AAALLAGLMWWHSDfrdvq 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 861 PNFGMPGYIYTIIAVslLCKIAALRSFSLERLQYLRERESGMSSL-AYFLARDTIDHFSTIVKPIVYLSMFYYFNNPRST 939
Cdd:PLN03211 437 DRLGLLFFISIFWGV--FPSFNSVFVFPQERAIFVKERASGMYTLsSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPE 514
|
490 500
....*....|....*....|..
gi 1002258264 940 ITD---NYIILLALVYCVTGIG 958
Cdd:PLN03211 515 LGAfllTLLVLLGYVLVSQGLG 536
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
472-696 |
2.22e-47 |
|
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: 168.99 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEFKDLTLS----LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKV-AGYKVSGSVLVNGRHDNIRSYKK 546
Cdd:cd03234 2 RVLPWWDVGLKaknwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeGGGTTSGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDS-LDLQGVRSSLVgtvekRGISGGQRKRVNVGI 625
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLV-----KGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 626 EMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGlIVYNG 696
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE-IVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
408-983 |
7.37e-47 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 183.39 E-value: 7.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 408 GEIVAGKDRSAPKGKHRsthtqifkyayGEIEKEKVRQQENKNLTFTGVLSMVSE-------QQKEITRPLLkvEFKDLT 480
Cdd:TIGR00956 700 GEILVFRRGSLKRAKKA-----------GETSASNKNDIEAGEVLGSTDLTDESDdvndekdMEKESGEDIF--HWRNLT 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 481 LSLGKKK----LLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKV-AGYKVSGSVLVNGRHDNiRSYKKIIGFVPQDD 555
Cdd:TIGR00956 767 YEVKIKKekrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVtTGVITGGDRLVNGRPLD-SSFQRSIGYVQQQD 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 556 VVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTVEKrGISGGQRKRVNVGIEMVMEPSLLI 635
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPKLLL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 636 -LDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGLIVYNGPV----KSVEDYFSTLGI 710
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLgensHTIINYFEKHGA 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 711 T-VPERVNPPDhyidilegivkpesginakhfplhWMLyngyEVpndmkddlkaigeqrphLGSSPSAGSTPHCLPHVRN 789
Cdd:TIGR00956 1005 PkCPEDANPAE------------------------WML----EV-----------------IGAAPGAHANQDYHEVWRN 1039
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 790 -----AFAEERDRIEHHLSKPKDLS-----SRRTPGVIRQYKYYLGRVTKQRLREARLLAVDFLILGLAGICLGTIAKLS 859
Cdd:TIGR00956 1040 sseyqAVKNELDRLEAELSKAEDDNdpdalSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKV 1119
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 860 DPN--------FGMpgYIYTIIAVSLLCKIaaLRSF-SLERLQYLRERESGM-SSLAYFLARDTID-----HFSTIVKPI 924
Cdd:TIGR00956 1120 GTSlqglqnqmFAV--FMATVLFNPLIQQY--LPPFvAQRDLYEVRERPSRTfSWLAFIAAQITVEipynlVAGTIFFFI 1195
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 925 VYLSMFYYFNNPRSTITDNYIILLALVYCVTGIGYT----FAICFNPgSAQLCSALIPVVLTL 983
Cdd:TIGR00956 1196 WYYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFStlgqMVISFNP-NADNAAVLASLLFTM 1257
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
476-696 |
4.71e-43 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 155.09 E-value: 4.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 476 FKDLTLSL----GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIrSYKKIIGFV 551
Cdd:cd03232 6 WKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDK-NFQRSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEENLWFSAKCRlsattahrhkvltvervidsldlqgvrsslvgtvekrGISGGQRKRVNVGIEMVMEP 631
Cdd:cd03232 85 EQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002258264 632 SLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGLIVYNG 696
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
474-640 |
8.61e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 8.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR--HDNIRSYKKIIGFV 551
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT--SGEVRVLGEdvARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEENLWFSAKCR-LSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVME 630
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYgLPRKEARER----IDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHD 149
|
170
....*....|
gi 1002258264 631 PSLLILDEPT 640
Cdd:COG1131 150 PELLILDEPT 159
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
475-718 |
1.20e-37 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 153.85 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIRSYKKIIGFVPQD 554
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 555 DVVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTVEKRGISGGQRKRVNVGIEMVMEPSLL 634
Cdd:PLN03140 962 DIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 635 ILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLYNMFDDLILLAKGGLIVYNGPV-----KSVEDYFSTLG 709
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLgrnshKIIEYFEAIPG 1121
|
250
....*....|
gi 1002258264 710 I-TVPERVNP 718
Cdd:PLN03140 1122 VpKIKEKYNP 1131
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
489-640 |
2.55e-33 |
|
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: 125.84 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRH---DNIRSYKKIIGFVPQDDVVHGNLTVEE 565
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT--EGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002258264 566 NLWFSAKCRlsaTTAHRHKVLTVERVIDSLDLQGVRSSLVGtVEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:pfam00005 79 NLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVG-ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
483-696 |
4.46e-31 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 121.22 E-value: 4.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 483 LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGY-KVSGSVLVNG--RHDNIRSYKKIIGFVPQDDVVHG 559
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvSVEGDIHYNGipYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 NLTVEENLWFSAKCrlsattahrhkvltvervidsldlQGVRSSlvgtvekRGISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:cd03233 97 TLTVRETLDFALRC------------------------KGNEFV-------RGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 640 TSGLDSSSSQLLLRALRH--EALEGVNVcAVVHQPSYTLYNMFDDLILLAkGGLIVYNG 696
Cdd:cd03233 146 TRGLDSSTALEILKCIRTmaDVLKTTTF-VSLYQASDEIYDLFDKVLVLY-EGRQIYYG 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
474-640 |
3.75e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRhdNIRSYKKIIGFVPQ 553
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP--PTSGTVRLFGK--PPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DDVVHGN--LTVEE----NLWFSAKCRLSATTAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEM 627
Cdd:COG1121 83 RAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREA---VDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARAL 154
|
170
....*....|...
gi 1002258264 628 VMEPSLLILDEPT 640
Cdd:COG1121 155 AQDPDLLLLDEPF 167
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
474-701 |
1.79e-28 |
|
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: 115.53 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSYK-----KII 548
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS--SGEVLLDGR--DLASLSrrelaRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHGNLTVEENL------WFSAKCRLSAttAHRHKVltvERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVn 622
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELValgrypHLGLFGRPSA--EDREAV---EEALERTGLEHLADRPVDE-----LSGGERQRV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 623 vGIEMVM--EPSLLILDEPTsgldssssqlllralRHEALE---------GVNVCAVVHQPsytlyNM----FDDLILLA 687
Cdd:COG1120 147 -LIARALaqEPPLLLLDEPTshld--------lahQLEVLEllrrlarerGRTVVMVLHDL-----NLaaryADRLVLLK 212
|
250
....*....|....
gi 1002258264 688 KGGlIVYNGPVKSV 701
Cdd:COG1120 213 DGR-IVAQGPPEEV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
475-640 |
3.17e-28 |
|
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: 114.18 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR--HDNIRSYKKIIGFVP 552
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGEdvRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QDDVVHGNLTVEENLWFSAKCRLSATTAHRHKvltVERVIDSLDLQGVRSSLVGtvekrGISGGQRKRVNVGIEMVMEPS 632
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKR---IEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPK 152
|
....*...
gi 1002258264 633 LLILDEPT 640
Cdd:COG4555 153 VLLLDEPT 160
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
485-720 |
6.77e-28 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 122.14 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 485 KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYK--VSGSVLVNG--RHDNIRSYKKIIGFVPQDDVVHGN 560
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigVEGVITYDGitPEEIKKHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 561 LTVEENLWFSAKCRlsaTTAHRHKVLT----VERVID----SLDLQGVRSSLVGTVEKRGISGGQRKRVNVGIEMVMEPS 632
Cdd:TIGR00956 153 LTVGETLDFAARCK---TPQNRPDGVSreeyAKHIADvymaTYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 633 LLILDEPTSGLDSSSsqlllralrheALEGVNV---CAV---------VHQPSYTLYNMFDDLILLAKgGLIVYNGPVKS 700
Cdd:TIGR00956 230 IQCWDNATRGLDSAT-----------ALEFIRAlktSANildttplvaIYQCSQDAYELFDKVIVLYE-GYQIYFGPADK 297
|
250 260
....*....|....*....|
gi 1002258264 701 VEDYFSTLGITVPERVNPPD 720
Cdd:TIGR00956 298 AKQYFEKMGFKCPDRQTTAD 317
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
472-640 |
9.01e-28 |
|
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: 112.14 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRH-DNIRSYKKI--- 547
Cdd:cd03224 1 LEVE--NLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR--SGSIRFDGRDiTGLPPHERArag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQDDVVHGNLTVEENLwfsakcRLSATTAHRHKV-LTVERVIDSL-DLQGVRSSLVGTvekrgISGGQRKRVNVGI 625
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENL------LLGAYARRRAKRkARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIAR 145
|
170
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:cd03224 146 ALMSRPKLLLLDEPS 160
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
474-640 |
5.38e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 108.25 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR--HDNIRSYKKIIGFV 551
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD--SGEIKVLGKdiKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEENLWFsakcrlsattahrhkvltvervidsldlqgvrsslvgtvekrgiSGGQRKRVNVGIEMVMEP 631
Cdd:cd03230 79 PEEPSLYENLTVRENLKL--------------------------------------------SGGMKQRLALAQALLHDP 114
|
....*....
gi 1002258264 632 SLLILDEPT 640
Cdd:cd03230 115 ELLILDEPT 123
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
474-639 |
8.10e-27 |
|
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: 109.15 E-value: 8.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAgykvSGSVLVNGR-HDNIRSYKKIIGF 550
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPD----SGEILIDGRdVTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVME 630
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRAR---VRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALARE 148
|
....*....
gi 1002258264 631 PSLLILDEP 639
Cdd:cd03259 149 PSLLLLDEP 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
474-640 |
9.66e-27 |
|
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: 109.20 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGrVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRH--DNIRSYKKIIGFV 551
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP--PSSGTIRIDGQDvlKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEENLWFSAKC-RLSATTAHRhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVME 630
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLkGIPSKEVKA----RVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGD 148
|
170
....*....|
gi 1002258264 631 PSLLILDEPT 640
Cdd:cd03264 149 PSILIVDEPT 158
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
485-715 |
9.96e-27 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 118.41 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 485 KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKV-AGYKVSGSVLVNGRHDNIRSYKKIIGFVPQDDVVHGNLTV 563
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 564 EENLWFSAKCRLSATtahRHKVLT----------------VERVIDSLDLQGVRSSL------------------VGTVE 609
Cdd:PLN03140 257 KETLDFSARCQGVGT---RYDLLSelarrekdagifpeaeVDLFMKATAMEGVKSSLitdytlkilgldickdtiVGDEM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 610 KRGISGGQRKRVNVGiEMVMEPS-LLILDEPTSGLDSSSSQLLLRALRHEA-LEGVNVCAVVHQPSYTLYNMFDDLILLA 687
Cdd:PLN03140 334 IRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVhLTEATVLMSLLQPAPETFDLFDDIILLS 412
|
250 260
....*....|....*....|....*...
gi 1002258264 688 KGGlIVYNGPVKSVEDYFSTLGITVPER 715
Cdd:PLN03140 413 EGQ-IVYQGPRDHILEFFESCGFKCPER 439
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
475-639 |
1.35e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.72 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVA-GYKVSGSVLVNGRH-DNIRSYKKIIGFVP 552
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpAFSASGEVLLNGRRlTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QDDVVHGNLTVEENLWFSakcrLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVgieMVM--- 629
Cdd:COG4136 83 QDDLLFPHLSVGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVAL---LRAlla 150
|
170
....*....|
gi 1002258264 630 EPSLLILDEP 639
Cdd:COG4136 151 EPRALLLDEP 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
484-640 |
1.42e-26 |
|
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: 108.75 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGR--HDNIRSYKKIIGFVPQDDVVHGNL 561
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTAYINGYsiRTDRKAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 562 TVEENLWFSAKCR-LSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03263 91 TVREHLRFYARLKgLPKSEIKEE----VELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
475-640 |
2.10e-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: 105.31 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRHdnIRSYKKIIGFVPQD 554
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT--SGSIRVFGKP--LEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 555 DVVHGN--LTVEE----NLWfsAKCRL--SATTAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIE 626
Cdd:cd03235 77 RSIDRDfpISVRDvvlmGLY--GHKGLfrRLSKADKAK---VDEALERVGLSELADRQIGE-----LSGGQQQRVLLARA 146
|
170
....*....|....
gi 1002258264 627 MVMEPSLLILDEPT 640
Cdd:cd03235 147 LVQDPDLLLLDEPF 160
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
474-640 |
9.19e-25 |
|
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: 104.12 E-value: 9.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG-------RHDNIRSYKK 546
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--PDSGEVLIDGedisglsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 iIGFVPQDDVVHGNLTVEENLWFsakcRLSATTAHRHKVLTvERVIDSLDLQGVRsslvGTVEKR--GISGGQRKRVNVG 624
Cdd:cd03261 79 -MGMLFQSGALFDSLTVFENVAF----PLREHTRLSEEEIR-EIVLEKLEAVGLR----GAEDLYpaELSGGMKKRVALA 148
|
170
....*....|....*.
gi 1002258264 625 IEMVMEPSLLILDEPT 640
Cdd:cd03261 149 RALALDPELLLYDEPT 164
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
470-640 |
1.13e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.91 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRH-DNIRSYKKI- 547
Cdd:COG0410 2 PMLEVE--NLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRSGSIRFDGEDiTGLPPHRIAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 --IGFVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRhkvlTVERVIDsL--DLQGVRSSLVGTvekrgISGGQRKRVNV 623
Cdd:COG0410 78 lgIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRA----DLERVYE-LfpRLKERRRQRAGT-----LSGGEQQMLAI 147
|
170
....*....|....*..
gi 1002258264 624 GIEMVMEPSLLILDEPT 640
Cdd:COG0410 148 GRALMSRPKLLLLDEPS 164
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
475-640 |
1.40e-24 |
|
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: 102.93 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNG---RHDNIRSYKKIIG 549
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG--LLGPTSGEVLVDGkdlTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FV---PQDDVVhgNLTVEENLWFSAKCR-LSATTAHRhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGI 625
Cdd:cd03225 79 LVfqnPDDQFF--GPTVEEEVAFGLENLgLPEEEIEE----RVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAG 147
|
170
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:cd03225 148 VLAMDPDILLLDEPT 162
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
470-640 |
2.37e-24 |
|
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: 101.79 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR--HDNIRSYKKI 547
Cdd:COG4133 1 MMLEAE--NLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP--PSAGEVLWNGEpiRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQDDVVHGNLTVEENLWFSAkcRLSATTAHRhkvLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEM 627
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWA--ALYGLRADR---EAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLL 146
|
170
....*....|...
gi 1002258264 628 VMEPSLLILDEPT 640
Cdd:COG4133 147 LSPAPLWLLDEPF 159
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
472-640 |
5.45e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 101.74 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKV-SGSVLVNGRH-DNIRSYKKI-- 547
Cdd:cd03219 1 LEVR--GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF---LRPtSGSVLFDGEDiTGLPPHEIArl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 -IGFVPQDDVVHGNLTVEENL----------WFSAKCRLSATTAHRHKVltvERVIDSLDLQGVRSSLVGTvekrgISGG 616
Cdd:cd03219 76 gIGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERA---EELLERVGLADLADRPAGE-----LSYG 147
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPA 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
468-640 |
1.17e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 101.27 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKV-SGSVLVNGRhdnirsykK 546
Cdd:COG0411 1 SDPLLEVR--GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF---YRPtSGRILFDGR--------D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGfVPQDDVVH-------------GNLTVEENL-----------WFSAKCRLSATTAHRHKVL-TVERVIDSLDLQGVR 601
Cdd:COG0411 68 ITG-LPPHRIARlgiartfqnprlfPELTVLENVlvaaharlgrgLLAALLRLPRARREEREAReRAEELLERVGLADRA 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002258264 602 SSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG0411 147 DEPAGN-----LSYGQQRRLEIARALATEPKLLLLDEPA 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
477-701 |
8.34e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.03 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 477 KDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSYK-----KIIGFV 551
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS--SGEVRLNGR--PLAAWSpwelaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEEnlwFSAKCRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVN-------VG 624
Cdd:COG4559 81 PQHSSLAFPFTVEE---VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQT-----LSGGEQQRVQlarvlaqLW 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002258264 625 IEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSytLYNMFDDLILLAKGGLIVYNGPVKSV 701
Cdd:COG4559 153 EPVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
474-640 |
1.90e-22 |
|
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: 97.36 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR------HDNIRSYKKI 547
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR--PDSGEILVDGQditglsEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQddvvHG----NLTVEENLWFS--AKCRLSATTAHrhkvltvERVIDSLDLQGvrssLVGTVEKR--GISGGQRK 619
Cdd:COG1127 84 IGMLFQ----GGalfdSLTVFENVAFPlrEHTDLSEAEIR-------ELVLEKLELVG----LPGAADKMpsELSGGMRK 148
|
170 180
....*....|....*....|...
gi 1002258264 620 RvnVGI--EMVMEPSLLILDEPT 640
Cdd:COG1127 149 R--VALarALALDPEILLYDEPT 169
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
474-640 |
3.97e-22 |
|
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: 96.10 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---NAVTGKVAGYKVSGSVLVNGR-----HDNIRSYK 545
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllNRLNDLIPGAPDEGEVLLDGKdiydlDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGFVPQD-DVVHGnlTVEENLWFSAKCRLSATTAHRHkvltvERVIDSLDLQG----VRSSLVGtvekRGISGGQRKR 620
Cdd:cd03260 81 RRVGMVFQKpNPFPG--SIYDNVAYGLRLHGIKLKEELD-----ERVEEALRKAAlwdeVKDRLHA----LGLSGGQQQR 149
|
170 180
....*....|....*....|
gi 1002258264 621 VNVGIEMVMEPSLLILDEPT 640
Cdd:cd03260 150 LCLARALANEPEVLLLDEPT 169
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
474-640 |
7.84e-22 |
|
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: 95.48 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLS-LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNG---RHDNIRSYKKIIG 549
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT--SGEVLVDGkdiTKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQD-D--VVhgNLTVEENLWFSAKCR-LSATTAHRhkvlTVERVIDSLDLQGVR----SSLvgtvekrgiSGGQRKRV 621
Cdd:COG1122 79 LVFQNpDdqLF--APTVEEDVAFGPENLgLPREEIRE----RVEEALELVGLEHLAdrppHEL---------SGGQKQRV 143
|
170 180
....*....|....*....|
gi 1002258264 622 NV-GIeMVMEPSLLILDEPT 640
Cdd:COG1122 144 AIaGV-LAMEPEVLVLDEPT 162
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
469-640 |
2.36e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 99.21 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 469 RPLLkvEFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKV-AGYKVSGSVLVNGR-----HDN 540
Cdd:COG1123 2 TPLL--EVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRdllelSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 541 IRSykKIIGFVPQDDVVHGN-LTVEENLWFSAKCRLSATTAHRhkvltvERVIDSLDLQGVRSSLvgtveKRGI---SGG 616
Cdd:COG1123 80 LRG--RRIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEAR------ARVLELLEAVGLERRL-----DRYPhqlSGG 146
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPT 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
475-694 |
3.51e-21 |
|
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: 92.11 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSYK-----KIIG 549
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS--SGEILLDGK--DLASLSpkelaRKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQddvvhgnltveenlwfsakcrlsattahrhkvltverVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVM 629
Cdd:cd03214 77 YVPQ-------------------------------------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002258264 630 EPSLLILDEPTSGLDSSSSQLLLRALRHEALE-GVNVCAVVHQPSYTLyNMFDDLILLAKGGLIVY 694
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAA-RYADRVILLKDGRIVAQ 179
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
471-640 |
6.44e-21 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 92.57 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 471 LLKVefKDLTLSL----GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRHDNIRS--- 543
Cdd:cd03257 1 LLEV--KNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG--LLKPTSGSIIFDGKDLLKLSrrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 ---YKKIIGFVPQD--DVVHGNLTVEENLwfsakcrlsATTAHRHKVLTVE---RVIDSLDLQGVrsSLVGTVEKR---G 612
Cdd:cd03257 77 rkiRRKEIQMVFQDpmSSLNPRMTIGEQI---------AEPLRIHGKLSKKearKEAVLLLLVGV--GLPEEVLNRyphE 145
|
170 180
....*....|....*....|....*...
gi 1002258264 613 ISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPT 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
474-640 |
7.35e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 92.94 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKK----KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR---HDNIRSYKK 546
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW--SGEVTFDGRpvtRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQD--DVVHGNLTVEENLwfsakcrlsATTAHRHKVLTVE-RVIDSLDLQGVRSSLVgtvEKRG--ISGGQRKRV 621
Cdd:COG1124 80 RVQMVFQDpyASLHPRHTVDRIL---------AEPLRIHGLPDREeRIAELLEQVGLPPSFL---DRYPhqLSGGQRQRV 147
|
170
....*....|....*....
gi 1002258264 622 NVGIEMVMEPSLLILDEPT 640
Cdd:COG1124 148 AIARALILEPELLLLDEPT 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
474-640 |
7.49e-21 |
|
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: 92.43 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGrHDNIRSYKKI---IGF 550
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK--PTSGRATVAG-HDVVREPREVrrrIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAkcRLSATTAHRHKVlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVME 630
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHA--RLYGVPGAERRE-RIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHR 149
|
170
....*....|
gi 1002258264 631 PSLLILDEPT 640
Cdd:cd03265 150 PEVLFLDEPT 159
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
456-640 |
8.68e-21 |
|
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: 97.91 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 456 VLSMVSEQQKEITRPL-----LKVEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvS 529
Cdd:COG4988 314 LLDAPEPAAPAGTAPLpaagpPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY--S 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 530 GSVLVNG---RHDNIRSYKKIIGFVPQDDVV-HGnlTVEENLwfsakcRLSATTAhrhkvlTVERVIDSLDLQGVRS--- 602
Cdd:COG4988 392 GSILINGvdlSDLDPASWRRQIAWVPQNPYLfAG--TIRENL------RLGRPDA------SDEELEAALEAAGLDEfva 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002258264 603 -------SLVGtvEK-RGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4988 458 alpdgldTPLG--EGgRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
473-639 |
1.11e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.85 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLS----LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRHdnIRSYKKII 548
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT--SGEVLVDGKP--VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHGNLTVEENLWFSAKCR-LSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRvnVGI-- 625
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRgVPKAERRER----ARELLELVGLAGFEDAYPHQ-----LSGGMRQR--VAIar 151
|
170
....*....|....
gi 1002258264 626 EMVMEPSLLILDEP 639
Cdd:COG1116 152 ALANDPEVLLMDEP 165
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
461-640 |
1.45e-20 |
|
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: 97.60 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 461 SEQQKEITRPLLK--VEFKDLTLSLG--KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvaGYKV-SGSVLVN 535
Cdd:COG2274 459 EEGRSKLSLPRLKgdIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG---LYEPtSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 536 G---RHDNIRSYKKIIGFVPQDDVV-HGnlTVEENLwfsakcRLSATTAhrhkvlTVERVIDSLDLQGVRS--------- 602
Cdd:COG2274 536 GidlRQIDPASLRRQIGVVLQDVFLfSG--TIRENI------TLGDPDA------TDEEIIEAARLAGLHDfiealpmgy 601
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002258264 603 -SLVGtvEK-RGISGGQRKRvnVGI--EMVMEPSLLILDEPT 640
Cdd:COG2274 602 dTVVG--EGgSNLSGGQRQR--LAIarALLRNPRILILDEAT 639
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
474-640 |
1.86e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.26 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKL----LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAgykvSGSVLVNGRH--------- 538
Cdd:COG1136 5 LELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPT----SGEVLIDGQDisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 DNIRSYKkiIGFVPQDdvvH---GNLTVEENLWFSAK-CRLSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgIS 614
Cdd:COG1136 81 ARLRRRH--IGFVFQF---FnllPELTALENVALPLLlAGVSRKERRER----ARELLERVGLGDRLDHRPSQ-----LS 146
|
170 180
....*....|....*....|....*.
gi 1002258264 615 GGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPT 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
475-640 |
3.50e-20 |
|
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: 88.46 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGR---HDNIRSYKKIIGFV 551
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL--KPTSGEILIDGKdiaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQddvvhgnltveenlwfsakcrlsattahrhkvltvervidsldlqgvrsslvgtvekrgISGGQRKRVNVGIEMVMEP 631
Cdd:cd00267 79 PQ-----------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
....*....
gi 1002258264 632 SLLILDEPT 640
Cdd:cd00267 100 DLLLLDEPT 108
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
475-640 |
4.98e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.28 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykVSGSVLVNGRhdNI---RSYKKI---I 548
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPV--KSGSIRLDGE--DItklPPHERAragI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHGNLTVEENLWFSAKCRlsattAHRHKvltveRVIDSL-DLQGVRSSLVGtveKRG--ISGGQRKRVNVGI 625
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAAL-----PRRSR-----KIPDEIyELFPVLKEMLG---RRGgdLSGGQQQQLAIAR 144
|
170
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:TIGR03410 145 ALVTRPKLLLLDEPT 159
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
474-640 |
5.77e-20 |
|
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: 88.21 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLG--KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNG---RHDNIRSYKKII 548
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT--SGEILIDGvdlRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHgNLTVEENLwfsakcrlsattahrhkvltvervidsldlqgvrsslvgtvekrgISGGQRKRVNVGIEMV 628
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI---------------------------------------------LSGGQRQRIAIARALL 112
|
170
....*....|..
gi 1002258264 629 MEPSLLILDEPT 640
Cdd:cd03228 113 RDPPILILDEAT 124
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
474-639 |
1.11e-19 |
|
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: 88.68 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLS----LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSYKKIIG 549
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT--SGEVLVDGE--PVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVM 629
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARER---AEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAV 148
|
170
....*....|
gi 1002258264 630 EPSLLILDEP 639
Cdd:cd03293 149 DPDVLLLDEP 158
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
474-640 |
1.50e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLS-LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKV-SGSVLVNGRhdNIRSYK-----K 546
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF---YDPtSGRILIDGV--DIRDLTleslrR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVV-HGnlTVEENLwfsakcRLSATTAHRHKVLT------VERVIDSLDlQGVRsSLVGtveKRGI--SGGQ 617
Cdd:COG1132 415 QIGVVPQDTFLfSG--TIRENI------RYGRPDATDEEVEEaakaaqAHEFIEALP-DGYD-TVVG---ERGVnlSGGQ 481
|
170 180
....*....|....*....|....*
gi 1002258264 618 RKRvnVGI--EMVMEPSLLILDEPT 640
Cdd:COG1132 482 RQR--IAIarALLKDPPILILDEAT 504
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
474-640 |
1.78e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLS-LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKV-SGSVLVNGRhdNIR--SYKKI-- 547
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE---ERPtSGQVLVNGQ--DLSrlKRREIpy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ----IGFVPQDdvvHG---NLTVEENLWFSakcrLSATTAHRHKVLT-VERVIDSLDLQGVRSSLVGTVekrgiSGGQRK 619
Cdd:COG2884 77 lrrrIGVVFQD---FRllpDRTVYENVALP----LRVTGKSRKEIRRrVREVLDLVGLSDKAKALPHEL-----SGGEQQ 144
|
170 180
....*....|....*....|.
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPT 640
Cdd:COG2884 145 RVAIARALVNRPELLLADEPT 165
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
474-640 |
1.79e-19 |
|
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: 88.83 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKK--LLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTgkvAGYKV-SGSVLVNGrHD----NIRSYKK 546
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP---RFYDVdSGRILIDG-HDvrdyTLASLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDdVVHGNLTVEENLWFS------AKCRLSATTAHRHKVltvervIDSLDlQGVRSSlvgtVEKRGI--SGGQR 618
Cdd:cd03251 77 QIGLVSQD-VFLFNDTVAENIAYGrpgatrEEVEEAARAANAHEF------IMELP-EGYDTV----IGERGVklSGGQR 144
|
170 180
....*....|....*....|..
gi 1002258264 619 KRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03251 145 QRIAIARALLKDPPILILDEAT 166
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
474-640 |
2.06e-19 |
|
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: 86.86 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR-----HDNIRSYKKII 548
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE--PDSGSILIDGEdltdlEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHGNLTVEENLWFsakcrlsattahrhkvltvervidsldlqgvrsslvgtvekrGISGGQRKRVNVGIEMV 628
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALA 116
|
170
....*....|..
gi 1002258264 629 MEPSLLILDEPT 640
Cdd:cd03229 117 MDPDVLLLDEPT 128
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
474-639 |
2.35e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.93 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAvtgkVAG-YKV-SGSVLVNGR-HDNIRSYKKIIGF 550
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRM----IAGfETPdSGRILLDGRdVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCR-LSATTAHRhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVM 629
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRgVPKAEIRA----RVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAP 152
|
170
....*....|
gi 1002258264 630 EPSLLILDEP 639
Cdd:COG3842 153 EPRVLLLDEP 162
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
477-692 |
7.53e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.16 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 477 KDLTLSLGKK-KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRHDNIRSYKKIIGFVPQDd 555
Cdd:cd03226 3 ENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG--LIKESSGSILLNGKPIKAKERRKSIGYVMQD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 556 vVHGNL---TVEENLWFSAKcRLSATTAhrhkvlTVERVIDSLDLQGVRsslvgtvEK--RGISGGQRKRVNVGIEMVME 630
Cdd:cd03226 80 -VDYQLftdSVREELLLGLK-ELDAGNE------QAETVLKDLDLYALK-------ERhpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002258264 631 PSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYtLYNMFDDLILLAKGGLI 692
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
474-640 |
1.21e-18 |
|
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: 85.62 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLG----KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVagykVSGSVLVNGRhdNIRSYKKI 547
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRP----TSGEVRVDGT--DISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ---------IGFVPQDDVVHGNLTVEENLwfsakcRLSATTAHRHKVLTVER---VIDSLDLQGVRSSLVGTvekrgISG 615
Cdd:cd03255 75 elaafrrrhIGFVFQSFNLLPDLTALENV------ELPLLLAGVPKKERRERaeeLLERVGLGDRLNHYPSE-----LSG 143
|
170 180
....*....|....*....|....*
gi 1002258264 616 GQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPT 168
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
475-705 |
3.50e-18 |
|
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: 84.93 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLG-KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykVSGSVLVNG------RHDNIRSYKKI 547
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP--TSGSVLIDGtdinklKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQDDVVHGNLTVEENLwfsakcrLSATTAHRHKVLTVERVIDSLDLQGVRSSL--VGTVEK---RG--ISGGQRKR 620
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENV-------LSGRLGRRSTWRSLFGLFPKEEKQRALAALerVGLLDKayqRAdqLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 621 VNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALE-GVNVCAVVHQPSYTLYNmFDDLILLaKGGLIVYNGPVK 699
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREY-ADRIVGL-KDGRIVFDGPPA 230
|
....*.
gi 1002258264 700 SVEDYF 705
Cdd:cd03256 231 ELTDEV 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
468-640 |
4.29e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 88.81 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVefKDLTLS-----LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAgykvSGSVLVNGR--- 537
Cdd:COG1123 257 AEPLLEV--RNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllRPT----SGSILFDGKdlt 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 ---HDNIRSYKKIIGFVPQDdvVHGNL----TVEENLWFSAKCRLSATTAHRHkvltvERVIDSLDLQGvrssLVGTVEK 610
Cdd:COG1123 331 klsRRSLRELRRRVQMVFQD--PYSSLnprmTVGDIIAEPLRLHGLLSRAERR-----ERVAELLERVG----LPPDLAD 399
|
170 180 190
....*....|....*....|....*....|...
gi 1002258264 611 R---GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1123 400 RyphELSGGQRQRVAIARALALEPKLLILDEPT 432
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
464-640 |
5.63e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 88.50 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 464 QKEITR-PLLKVEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR---H 538
Cdd:TIGR02857 311 KAPVTAaPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNGVplaD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 DNIRSYKKIIGFVPQDDVVHgNLTVEENLWFSakcRLSATTAhrhkvlTVERVIDSLDLQGVRSSLVGTVEK------RG 612
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLF-AGTIAENIRLA---RPDASDA------EIREALERAGLDEFVAALPQGLDTpigeggAG 458
|
170 180
....*....|....*....|....*...
gi 1002258264 613 ISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
474-640 |
5.72e-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: 83.73 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---NAVTGKVAGYKVSGSVLVNGRHDNIRSYKKIIGF 550
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrciNLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKcrlsaTTAHRHKVLTVERVIDSLDlqgvrssLVGTVEK-----RGISGGQRKRVNVGI 625
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPI-----KVKGMSKAEAEERALELLE-------KVGLADKadaypAQLSGGQQQRVAIAR 148
|
170
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:cd03262 149 ALAMNPKVMLFDEPT 163
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
498-639 |
8.65e-18 |
|
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: 83.11 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 498 PGRVTAVMGPSGAGKTTFLNAVTG--KV-AGY-KVSGSVLVNGRHD-NIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAK 572
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPdGGTiVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 573 crlsattAHRHKVLT--VERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:cd03297 102 -------RKRNREDRisVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEP 158
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
474-640 |
8.72e-18 |
|
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: 83.23 E-value: 8.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKK-KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG------RHDNIRSYKK 546
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGTIRVNGqdvsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHGNLTVEENLWFSAKCrlsatTAHRHKVLTvERVIDSLDLQGVRSSLVGTVEkrGISGGQRKRVNVGIE 626
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEV-----TGVPPREIR-KRVPAALELVGLSHKHRALPA--ELSGGEQQRVAIARA 150
|
170
....*....|....
gi 1002258264 627 MVMEPSLLILDEPT 640
Cdd:cd03292 151 IVNSPTILIADEPT 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
470-639 |
8.77e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagyKV-SGSVLVNGRhdNI------- 541
Cdd:COG1137 2 MTLEAE--NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV---KPdSGRIFLDGE--DIthlpmhk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 RSyKKIIGFVPQDDVVHGNLTVEENLW-------FSAKCRlsattahRHKvltVERVIDSLDLQGVRSSLVGTvekrgIS 614
Cdd:COG1137 75 RA-RLGIGYLPQEASIFRKLTVEDNILavlelrkLSKKER-------EER---LEELLEEFGITHLRKSKAYS-----LS 138
|
170 180
....*....|....*....|....*
gi 1002258264 615 GGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEP 163
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
477-701 |
9.33e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 9.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 477 KDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSYK-----KIIGFV 551
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGR--PLADWSpaelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQddvvHGNL----TVEENLWFSakcRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVgtvekRGISGGQRKRVNvgIEM 627
Cdd:PRK13548 82 PQ----HSSLsfpfTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDLAHLAGRDY-----PQLSGGEQQRVQ--LAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 628 VM--------EPSLLILDEPTSgldssssqlllralrheAL------------------EGVNVCAVVHqpSYTLYNMFD 681
Cdd:PRK13548 148 VLaqlwepdgPPRWLLLDEPTS-----------------ALdlahqhhvlrlarqlaheRGLAVIVVLH--DLNLAARYA 208
|
250 260
....*....|....*....|
gi 1002258264 682 DLILLAKGGLIVYNGPVKSV 701
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEV 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
472-640 |
1.54e-17 |
|
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: 83.15 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEfkDLTLSLGKKKLlRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRH-DNIRSYKKIIGF 550
Cdd:cd03299 1 LKVE--NLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDSGKILLNGKDiTNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRLsattahRHKVLTVERVIDSLDLQGVRSSLVGTVEKrgISGGQRKRVNVGIEMVME 630
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRK------VDKKEIERKVLEIAEMLGIDHLLNRKPET--LSGGEQQRVAIARALVVN 147
|
170
....*....|
gi 1002258264 631 PSLLILDEPT 640
Cdd:cd03299 148 PKILLLDEPF 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
474-640 |
1.67e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 82.26 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRH--DNIRSYKKIiGFV 551
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIK--PDSGEITFDGKSyqKNIEALRRI-GAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEENLWFSAKcrlsattAHRHKVLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEP 631
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLAR-------LLGIRKKRIDEVLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNP 145
|
....*....
gi 1002258264 632 SLLILDEPT 640
Cdd:cd03268 146 DLLILDEPT 154
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
472-639 |
5.74e-17 |
|
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: 81.44 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagyKV-SGSVLVNGR---HDNIrsYKKI 547
Cdd:cd03218 1 LRAE--NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV---KPdSGKILLDGQditKLPM--HKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ---IGFVPQDDVVHGNLTVEENLwfsaKCRLSATT---AHRHKVLtvERVIDSLDLQGVRSSLVGTvekrgISGGQRKRV 621
Cdd:cd03218 74 rlgIGYLPQEASIFRKLTVEENI----LAVLEIRGlskKEREEKL--EELLEEFHITHLRKSKASS-----LSGGERRRV 142
|
170
....*....|....*...
gi 1002258264 622 NVGIEMVMEPSLLILDEP 639
Cdd:cd03218 143 EIARALATNPKFLLLDEP 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
475-639 |
7.70e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.95 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLlrSINGELRPGRVTAVMGPSGAGKTTFLNAvtgkVAGYKV--SGSVLVNGR-HDNIRSYKKIIGFV 551
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNL----IAGFLPpdSGRILWNGQdLTALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNLTVEEN--LWFSAKCRLSAttAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVM 629
Cdd:COG3840 77 FQENNLFPHLTVAQNigLGLRPGLKLTA--EQRAQ---VEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVR 146
|
170
....*....|
gi 1002258264 630 EPSLLILDEP 639
Cdd:COG3840 147 KRPILLLDEP 156
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
475-640 |
9.23e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 80.25 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR---HDNIRSYKKIIGFV 551
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT--SGEIYLDGKplsAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 552 PQDDVVHGNlTVEENLwfsakcrlSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTVEKRgISGGQRKRVNVGIEMVMEP 631
Cdd:COG4619 80 PQEPALWGG-TVRDNL--------PFPFQLRERKFDRERALELLERLGLPPDILDKPVER-LSGGERQRLALIRALLLQP 149
|
....*....
gi 1002258264 632 SLLILDEPT 640
Cdd:COG4619 150 DVLLLDEPT 158
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
474-640 |
1.07e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 80.81 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAgykvSGSVLVNG-----RHDNIRSYKK 546
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleEPD----SGTITVDGedltdSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQddvvHGNL----TVEENLwfsakcrlsaTTAHRhKVL------TVERVIDSLDLqgvrsslVGTVEKRG---- 612
Cdd:COG1126 78 KVGMVFQ----QFNLfphlTVLENV----------TLAPI-KVKkmskaeAEERAMELLER-------VGLADKADaypa 135
|
170 180 190
....*....|....*....|....*....|.
gi 1002258264 613 -ISGGQRKRVnvGI--EMVMEPSLLILDEPT 640
Cdd:COG1126 136 qLSGGQQQRV--AIarALAMEPKVMLFDEPT 164
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
484-640 |
1.21e-16 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 82.05 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGrHDNIRSYKKI---IGFVPQDDVVHGN 560
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLR--PTSGTARVAG-YDVVREPRKVrrsIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 561 LTVEENLWFSAKCR-LSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:TIGR01188 81 LTGRENLEMMGRLYgLPKDEAEER----AEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
.
gi 1002258264 640 T 640
Cdd:TIGR01188 152 T 152
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
474-694 |
1.35e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.63 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRHDNIRSYKKIiGFVPQ 553
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD--SGEVLFDGKPLDIAARNRI-GYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DDVVHGNLTVEENLWFSAKCR-LSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPS 632
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKgLKKEEARRR----IDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002258264 633 LLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSyTLYNMFDDLILLAKGGLIVY 694
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLY 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
474-640 |
1.64e-16 |
|
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: 80.51 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSG-SVLVNGR---HDNIRSYKKIIG 549
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL--PPTYGnDVRLFGErrgGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQD--DVVHGNLTVEENLwfsakcrLSA-----------TTAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGG 616
Cdd:COG1119 82 LVSPAlqLRFPRDETVLDVV-------LSGffdsiglyrepTDEQRER---ARELLELLGLAHLADRPFGT-----LSQG 146
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPT 170
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
499-696 |
1.76e-16 |
|
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: 79.46 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 499 GRVTAVMGPSGAGKTTFLNAvtgkVAGYKV--SGSVLVNGR-HDNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAKCRL 575
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNL----IAGFETpqSGRVLINGVdVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 576 SATTAHRHKvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEPtsgldsssSQLLLRAL 655
Cdd:cd03298 100 KLTAEDRQA---IEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEP--------FAALDPAL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002258264 656 RHEALEGVN-VCA--------VVHQPSYTLyNMFDDLILLAKgGLIVYNG 696
Cdd:cd03298 164 RAEMLDLVLdLHAetkmtvlmVTHQPEDAK-RLAQRVVFLDN-GRIAAQG 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
474-640 |
1.79e-16 |
|
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: 79.97 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLG-KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkVAGYKV-SGSVLVNGRhdNIRSYK-----K 546
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL---FRFYDVsSGSILIDGQ--DIREVTldslrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHgNLTVEENLWFSakcRLSAT---------TAHRHKvlTVERVIDSLDlqgvrsSLVGtveKRG--ISG 615
Cdd:cd03253 76 AIGVVPQDTVLF-NDTIGYNIRYG---RPDATdeevieaakAAQIHD--KIMRFPDGYD------TIVG---ERGlkLSG 140
|
170 180
....*....|....*....|....*
gi 1002258264 616 GQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEAT 165
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
473-640 |
2.20e-16 |
|
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: 79.58 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKKKL-LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKVS-GSVLVNGRhdNIRSYKKI--- 547
Cdd:cd03254 2 EIEFENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF---YDPQkGQILIDGI--DIRDISRKslr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 --IGFVPQDDVVHgNLTVEENLWFS------AKCRLSATTAHRHKVltVERVIDSLDLQgvrsslvgtVEKRG--ISGGQ 617
Cdd:cd03254 77 smIGVVLQDTFLF-SGTIMENIRLGrpnatdEEVIEAAKEAGAHDF--IMKLPNGYDTV---------LGENGgnLSQGE 144
|
170 180
....*....|....*....|...
gi 1002258264 618 RKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEAT 167
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
488-672 |
2.29e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 488 LLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLvngRHDNIRsykkiIGFVPQ----DDVVhgNLTV 563
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR--PTSGTVR---RAGGAR-----VAYVPQrsevPDSL--PLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 564 EE----NLWfSAKCRLSATTAHRHKVltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:NF040873 75 RDlvamGRW-ARRGLWRRLTRDDRAA--VDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|...
gi 1002258264 640 TSGLDSSSSQLLLRALRHEALEGVNVCAVVHQP 672
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
475-639 |
2.35e-16 |
|
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: 78.72 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkVAGYKV-SGSVLVNGrhDNIRsykkiigfvpq 553
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEVtEGEILFKG--EDIT----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 ddvvhgNLTVEEnlwfsaKCRLSATTAHRHKVltvervidslDLQGVR-SSLVGTVEKrGISGGQRKRVNVGIEMVMEPS 632
Cdd:cd03217 68 ------DLPPEE------RARLGIFLAFQYPP----------EIPGVKnADFLRYVNE-GFSGGEKKRNEILQLLLLEPD 124
|
....*..
gi 1002258264 633 LLILDEP 639
Cdd:cd03217 125 LAILDEP 131
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
474-639 |
2.47e-16 |
|
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: 78.84 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYKV--SGSVLVNGRHDN-IRSYKKIIGF 550
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMI----AGLEEptSGRIYIGGRDVTdLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRlsattaHRHKVLTVERVIDSLDLQGVrSSLVGTVEKRgISGGQRKRVNVGIEMVME 630
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLR------KVPKDEIDERVREVAELLQI-EHLLDRKPKQ-LSGGQRQRVALGRAIVRE 148
|
....*....
gi 1002258264 631 PSLLILDEP 639
Cdd:cd03301 149 PKVFLMDEP 157
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
476-640 |
3.16e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 476 FKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGrhdNIRsykkiIGFVPQDD 555
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD--SGEVSIPK---GLR-----IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 556 VVHGNLTVEENLwFSAKCRLSATTAHRHKVLT------------------------------VERVIDSLDLQGV-RSSL 604
Cdd:COG0488 71 PLDDDLTVLDTV-LDGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEdLDRP 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002258264 605 VGTVekrgiSGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG0488 150 VSEL-----SGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
474-704 |
3.38e-16 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 79.26 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGK-KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG------RHDNIRSYKK 546
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE--PSSGSILLEGtditklRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHGNLTVEENLWFSakcRLSATTA--------HRHKVltvERVIDSLDLQGvrssLVGTVEKRG--ISGG 616
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHG---RLGYKPTwrsllgrfSEEDK---ERALSALERVG----LADKAYQRAdqLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALE-GVNVCAVVHQPSYTLynMFDDLILLAKGGLIVYN 695
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAK--KYADRIVGLKAGEIVFD 227
|
....*....
gi 1002258264 696 GPVKSVEDY 704
Cdd:TIGR02315 228 GAPSELDDE 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
474-639 |
3.65e-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: 79.31 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYK--VSGSVLVNGR---HDNIRsyKKII 548
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLI----AGLErpDSGTILFGGEdatDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKVltVERVIDSLDLqgVRSSLVGTVEKRGISGGQRKRVNVGIEMV 628
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEI--RAKVHELLKL--VQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170
....*....|.
gi 1002258264 629 MEPSLLILDEP 639
Cdd:cd03296 153 VEPKVLLLDEP 163
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
474-639 |
4.74e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.89 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAvtgkVAG-YKVS-GSVLVNGRH-DNIRSYKKIIGF 550
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRM----IAGlEDPTsGEILIGGRDvTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCR-LSATTAHRHkvltVERVIDSLDLQGVRSSLVgtvekRGISGGQRKRVNVGIEMVM 629
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRkVPKAEIDRR----VREAAELLGLEDLLDRKP-----KQLSGGQRQRVALGRALVR 150
|
170
....*....|
gi 1002258264 630 EPSLLILDEP 639
Cdd:COG3839 151 EPKVFLLDEP 160
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
474-640 |
4.88e-16 |
|
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: 82.51 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSYK-----K 546
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ--SGSITLGGV--DLRDLDeddlrR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQD-DVVHGnlTVEENLwfsakcRL---SATTAHRHKVLT-------VERVIDSLDlqgvrsSLVGtvEK-RGIS 614
Cdd:COG4987 410 RIAVVPQRpHLFDT--TLRENL------RLarpDATDEELWAALErvglgdwLAALPDGLD------TWLG--EGgRRLS 473
|
170 180
....*....|....*....|....*...
gi 1002258264 615 GGQRKRVnvGIEMVM--EPSLLILDEPT 640
Cdd:COG4987 474 GGERRRL--ALARALlrDAPILLLDEPT 499
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
474-640 |
5.28e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 78.95 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNG------RHDNIRSYKK 546
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT--SGEILVDGqdvtalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHGNLTVEEN----------LWFSAKCRLSAttAHRHKVLTV-ERViDSLDLQGVR-SSLvgtvekrgiS 614
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNvlagrlgrtsTWRSLLGLFPP--EDRERALEAlERV-GLADKAYQRaDQL---------S 148
|
170 180
....*....|....*....|....*...
gi 1002258264 615 GGQRKRVnvGIE--MVMEPSLLILDEPT 640
Cdd:COG3638 149 GGQQQRV--AIAraLVQEPKLILADEPV 174
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
474-639 |
5.98e-16 |
|
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: 78.43 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYKV--SGSVLVNGRH-DNIRSYKKIIGF 550
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLI----AGFETptSGEILLDGKDiTNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKcrlsatTAHRHKVLTVERVIDSLDLqgVRSSLVGTVEKRGISGGQRKRVNVGIEMVME 630
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLR------LKKLPKAEIKERVAEALDL--VQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
....*....
gi 1002258264 631 PSLLILDEP 639
Cdd:cd03300 149 PKVLLLDEP 157
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
474-639 |
7.12e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.19 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhD---NIRSYKKIIGF 550
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD--SGRIVLNGR-DlftNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKvltVERVIDSLDLQGvrsslvgtVEKR---GISGGQRKRVNVGIEM 627
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRAR---VEELLELVQLEG--------LADRypsQLSGGQRQRVALARAL 148
|
170
....*....|..
gi 1002258264 628 VMEPSLLILDEP 639
Cdd:COG1118 149 AVEPEVLLLDEP 160
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
475-639 |
1.19e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvAGYKV-SGSVLVNGrhDNI-------RSYKK 546
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEVtSGSILLDG--EDIlelspdeRARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 I-IGFvpQDDVVHGNLTVEENLwfsakcrLSATTAHRHKVLTV----ERVIDSLDLQGVRSSLVgtveKR----GISGGQ 617
Cdd:COG0396 79 IfLAF--QYPVEIPGVSVSNFL-------RTALNARRGEELSAreflKLLKEKMKELGLDEDFL----DRyvneGFSGGE 145
|
170 180
....*....|....*....|....*.
gi 1002258264 618 RKRvnvgIEM----VMEPSLLILDEP 639
Cdd:COG0396 146 KKR----NEIlqmlLLEPKLAILDET 167
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
478-639 |
2.70e-15 |
|
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: 78.60 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 478 DLTLSLGKKKLlrSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKV---AGY-KVSGSVLVNGRHD-NIRSYKKIIGFVP 552
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLErpdSGRiRLGGEVLQDSARGiFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QDDVVHGNLTVEENLWFSAKcRlsATTAHRHkvLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPS 632
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRK-R--APRAERR--ISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPR 153
|
....*..
gi 1002258264 633 LLILDEP 639
Cdd:COG4148 154 LLLMDEP 160
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
467-640 |
3.21e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 467 ITRPLLKVefKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---NAVTGKVAGYKVSGSVLVNGRhdNIRS 543
Cdd:PRK14239 1 MTEPILQV--SDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPEVTITGSIVYNGH--NIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 -------YKKIIGFVPQddvvHGN---LTVEENLWFSAkcrlsattahRHKVLTVERVIDsldlQGVRSSLVGT-----V 608
Cdd:PRK14239 77 prtdtvdLRKEIGMVFQ----QPNpfpMSIYENVVYGL----------RLKGIKDKQVLD----EAVEKSLKGAsiwdeV 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002258264 609 EKR------GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK14239 139 KDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
474-640 |
7.22e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPG-RVtAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLvngRHDNIRsykkiIGFVP 552
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPD--SGTVK---LGETVK-----IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QD-DVVHGNLTVEENLWfsakcRLS--ATTAHRHKVL--------TVERVIDSLdlqgvrsslvgtvekrgiSGGQRKRV 621
Cdd:COG0488 385 QHqEELDPDKTVLDELR-----DGApgGTEQEVRGYLgrflfsgdDAFKPVGVL------------------SGGEKARL 441
|
170
....*....|....*....
gi 1002258264 622 NVGIEMVMEPSLLILDEPT 640
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
489-640 |
8.56e-15 |
|
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: 74.71 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG--RHDNIRSYKKIIGFVPQDDVVHGNLTVEEN 566
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE--PDAGFATVDGfdVVKEPAEARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002258264 567 LWFSAkcRLSATTAHRHKVlTVERVIDSLDLQGVRSSLVGtvekrGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03266 99 LEYFA--GLYGLKGDELTA-RLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
474-701 |
1.20e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.79 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAV---------TGKVAGYKVSGSVLVNGRHDNIRSY 544
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagTIRVGDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQDDVVHGNLTVEEN-----LWFSAKCRLSATTAHRhkvltveRVIDSLDLQGVRSSLvgtveKRGISGGQRK 619
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENiiegpVIVKGEPKEEATARAR-------ELLAKVGLAGKETSY-----PRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTlYNMFDDLILLAKgGLIVYNGPVK 699
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA-RDVADRAIFMDQ-GRIVEQGPAK 229
|
..
gi 1002258264 700 SV 701
Cdd:PRK11264 230 AL 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
474-640 |
1.88e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.11 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKK---KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAV------TgkvagykvSGSVLVNGRHD---NI 541
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydpT--------SGEILLDGVDIrdlNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 RSYKKIIGFVPQDDVVHgNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQGvrSSLVGTvekRG--ISGGQRK 619
Cdd:cd03249 73 RWLRSQIGLVSQEPVLF-DGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGY--DTLVGE---RGsqLSGGQKQ 146
|
170 180
....*....|....*....|.
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03249 147 RIAIARALLRNPKILLLDEAT 167
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
474-640 |
2.37e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR---HDNIRSYKKIIG 549
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK--PTSGSVLIRGEpitKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQ--DDVVHGNlTVEENLWFsAKCRL---SATTAHRhkvltVERVIDSLDLQGVRSSLvgtveKRGISGGQRKRVNVG 624
Cdd:PRK13652 82 LVFQnpDDQIFSP-TVEQDIAF-GPINLgldEETVAHR-----VSSALHMLGLEELRDRV-----PHHLSGGEKKRVAIA 149
|
170
....*....|....*.
gi 1002258264 625 IEMVMEPSLLILDEPT 640
Cdd:PRK13652 150 GVIAMEPQVLVLDEPT 165
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
473-701 |
2.54e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGY---KVSGSVLVNGR---HDNIRSYKK 546
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpeaRVSGEVYLDGQdifKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHGNLTVEENLWFSAKC-RLSATTAHRHkvltvERVIDSLDlqgvRSSLVGTVEKR------GISGGQRK 619
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLnRLVKSKKELQ-----ERVRWALE----KAQLWDEVKDRldapagKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRhEALEGVNVCAVVHQPSYTLynMFDDLILLAKGGLIVYNGPVK 699
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFL-ELKKDMTIVLVTHFPQQAA--RISDYVAFLYKGQIVEWGPTR 230
|
..
gi 1002258264 700 SV 701
Cdd:PRK14247 231 EV 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
477-692 |
2.61e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 477 KDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR---HDNIRSYKKIIGFVPQ 553
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQSGTVFLGDKpisMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DDVVHGNLTVEE------NLWFSAKCRLSATTAHRhkvltVERVIDsldlqgvRSSLVGTVEKR--GISGGQRKRVNVGI 625
Cdd:PRK11231 84 HHLTPEGITVRElvaygrSPWLSLWGRLSAEDNAR-----VNQAME-------QTRINHLADRRltDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 626 EMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVH---QPS-YTlynmfDDLILLAKGGLI 692
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASrYC-----DHLVVLANGHVM 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
474-640 |
3.01e-14 |
|
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: 77.02 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG------RHDNIRsykK 546
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGvpvsslDQDEVR---R 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 IIGFVPQDDVVHGNlTVEENLWFSAKcrlSATTAHRHKVLTVERVIDSLD-LQGVRSSLVGTVEKRgISGGQRKRVNVGI 625
Cdd:TIGR02868 410 RVSVCAQDAHLFDT-TVRENLRLARP---DATDEELWAALERVGLADWLRaLPDGLDTVLGEGGAR-LSGGERQRLALAR 484
|
170
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:TIGR02868 485 ALLADAPILLLDEPT 499
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
495-639 |
3.43e-14 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 72.96 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 495 ELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNGRHDniRSYKKIIGFVPQD---------DVVHGNLTVEE 565
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPPAK--GTVKVAGASP--GKGWRHIGYVPQRhefawdfpiSVAHTVMSGRT 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002258264 566 NL--WFSAKCRLS-ATTAHrhkvltverVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:TIGR03771 78 GHigWLRRPCVADfAAVRD---------ALRRVGLTELADRPVGE-----LSGGQRQRVLVARALATRPSVLLLDEP 140
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
457-640 |
5.07e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 457 LSMVSEQQKEITRPL-----LKVEFKDLT-LSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgYKvsG 530
Cdd:PRK11174 328 LETPLAHPQQGEKELasndpVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQ--G 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 531 SVLVNG---RHDNIRSYKKIIGFVPQD-DVVHGnlTVEENLWFSakcRLSATTAHRHKVLT-------VERVIDSLDLQ- 598
Cdd:PRK11174 405 SLKINGielRELDPESWRKHLSWVGQNpQLPHG--TLRDNVLLG---NPDASDEQLQQALEnawvsefLPLLPQGLDTPi 479
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002258264 599 GVRSSlvgtvekrGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11174 480 GDQAA--------GLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
484-640 |
5.72e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 71.69 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR---HD--NIRSYKKIIGFVPQD-DVV 557
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLR--PQSGAVLIDGEpldYSrkGLLERRQRVGLVFQDpDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 558 HGNLTVEENLWFSAK-CRLSATTAHRHkvltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLIL 636
Cdd:TIGR01166 81 LFAADVDQDVAFGPLnLGLSEAEVERR----VREALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLLL 151
|
....
gi 1002258264 637 DEPT 640
Cdd:TIGR01166 152 DEPT 155
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
473-640 |
5.92e-14 |
|
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: 72.24 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYK-VSGSVLVNGrHDnIRSY----- 544
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL---YKpTSGSVLLDG-TD-IRQLdpadl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQDDV-VHGnlTVEENLWFSAkcrLSATTahrhkvltvERVIDSLDLQGVrSSLVGTVEK----------RGI 613
Cdd:cd03245 77 RRNIGYVPQDVTlFYG--TLRDNITLGA---PLADD---------ERILRAAELAGV-TDFVNKHPNgldlqigergRGL 141
|
170 180
....*....|....*....|....*..
gi 1002258264 614 SGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPT 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
484-691 |
1.00e-13 |
|
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: 70.32 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRhdNIRS-----YKKIIGFVPQDDvvh 558
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PTSGRVRLDGA--DISQwdpneLGDHVGYLPQDD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 559 gnltveeNLwFSakcrlsattahrhkvltvervidsldlqgvrsslvGTVEKRGISGGQRKRVNVGIEMVMEPSLLILDE 638
Cdd:cd03246 86 -------EL-FS-----------------------------------GSIAENILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 639 PTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSytLYNMFDDLILLAKGGL 691
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
475-640 |
1.17e-13 |
|
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: 70.85 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGRHDN--IRSYKKIIGFVP 552
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL--RPDSGEVRWNGTPLAeqRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QDDVVHGNLTVEENLWFSAKcrlsattAHRHKVLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPS 632
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAA-------IHGGAQRTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRP 147
|
....*...
gi 1002258264 633 LLILDEPT 640
Cdd:TIGR01189 148 LWILDEPT 155
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
473-640 |
1.26e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.99 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---NAVTGKVAGYKVSGSVLVNGRhdNIRSyKKI-- 547
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPGARVEGEILLDGE--DIYD-PDVdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ------IGFVPQ----------DDV-----VHGNLT-------VEE-----NLWfsakcrlsattahrhkvltvERVIDS 594
Cdd:COG1117 88 velrrrVGMVFQkpnpfpksiyDNVayglrLHGIKSkseldeiVEEslrkaALW--------------------DEVKDR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002258264 595 LDLQGVrsslvgtvekrGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1117 148 LKKSAL-----------GLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
474-671 |
1.55e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.28 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---NAVTGKVAGYKVSGSVLVNGRHDNIRSYKKIIGF 550
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKVltvervidSLDLQGVrsslVGTVEKRG-----ISGGQRKRVNVGI 625
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQ--------ARELLAK----VGLAERAHhypseLSGGQQQRVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002258264 626 EMVMEPSLLILDEPTsgldssssQLLLRALRHEAL--------EGVNVCAVVHQ 671
Cdd:PRK09493 150 ALAVKPKLMLFDEPT--------SALDPELRHEVLkvmqdlaeEGMTMVIVTHE 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
475-672 |
1.59e-13 |
|
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: 70.60 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR--HDNIRSYKKIIGFVP 552
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP--PLAGRVLLNGGplDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QDDVVHGNLTVEENLWFSakCRLSATTahrhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPS 632
Cdd:cd03231 80 HAPGIKTTLSVLENLRFW--HADHSDE-------QVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002258264 633 LLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQP 672
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
488-640 |
1.67e-13 |
|
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: 71.36 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 488 LLRSINGELRPGRVTAVMGPSGAGKTTflnaVTGKVAGYKV--SGSVLVNGrHD----NIRSYKKIIGFVPQDDVVHgNL 561
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKST----LTKLIQRFYVpeNGRVLVDG-HDlalaDPAWLRRQVGVVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 562 TVEENLwfsakcRLSATTAHRHKVLTVERVIDS----LDLQGVRSSLVGTvEKRGISGGQRKRVNVGIEMVMEPSLLILD 637
Cdd:cd03252 91 SIRDNI------ALADPGMSMERVIEAAKLAGAhdfiSELPEGYDTIVGE-QGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
...
gi 1002258264 638 EPT 640
Cdd:cd03252 164 EAT 166
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
468-640 |
1.72e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIRSYKKI 547
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQDDVVHGNLTVEENLW-FSAKCRLSATTahrhkvltVERVIDSLdLQGVRSSLVGTVEKRGISGGQRKRVNVGIE 626
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLvFGRYFGMSTRE--------IEAVIPSL-LEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170
....*....|....
gi 1002258264 627 MVMEPSLLILDEPT 640
Cdd:PRK13536 187 LINDPQLLILDEPT 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
474-640 |
2.37e-13 |
|
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: 70.69 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLT----LSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRH------DNIRS 543
Cdd:cd03258 2 IELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--LERPTSGSVLVDGTDltllsgKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 YKKIIGFVPQddvvHGNL----TVEENLWFSAKcrlsatTAHRHKVLTVERVIDSLDLqgvrsslVGTVEKRG-----IS 614
Cdd:cd03258 80 ARRRIGMIFQ----HFNLlssrTVFENVALPLE------IAGVPKAEIEERVLELLEL-------VGLEDKADaypaqLS 142
|
170 180
....*....|....*....|....*.
gi 1002258264 615 GGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEAT 168
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
479-640 |
2.78e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 479 LTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKI---IGFVPQDD 555
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT--PAHGHVWLDGEHIQHYASKEVarrIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 556 VVHGNLTVEEnlwfsakcrLSATTAHRHKVLTV-------ERVIDSLDLQGVRSSLVGTVEKrgISGGQRKRVNVGIEMV 628
Cdd:PRK10253 91 TTPGDITVQE---------LVARGRYPHQPLFTrwrkedeEAVTKAMQATGITHLADQSVDT--LSGGQRQRAWIAMVLA 159
|
170
....*....|..
gi 1002258264 629 MEPSLLILDEPT 640
Cdd:PRK10253 160 QETAIMLLDEPT 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
474-701 |
3.52e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKI---IGF 550
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT--PTAGTVLVAGDDVEALSARAAsrrVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFsakcrlsATTAHRHKVLT--------VERVIDSLDLQGVRSSLVGTVekrgiSGGQRKRVN 622
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEM-------GRTPHRSRFDTwtetdraaVERAMERTGVAQFADRPVTSL-----SGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 623 VGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHqpSYTLYNMF-DDLILLAKGGlIVYNGPVKSV 701
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGR-VRAAGPPADV 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-640 |
5.05e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 462 EQQKEITRPLLKVEfkdltlSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRHDNI 541
Cdd:COG1129 247 KRAAAPGEVVLEVE------GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG--ADPADSGEIRLDGKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 RSYKK-I---IGFVPQDDVVHG---NLTVEENL------WFSAKCRLSATTAHRHkvltVERVIDSLDlqgVRSS----L 604
Cdd:COG1129 319 RSPRDaIragIAYVPEDRKGEGlvlDLSIRENItlasldRLSRGGLLDRRRERAL----AEEYIKRLR---IKTPspeqP 391
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002258264 605 VGTvekrgISGG-QRKrVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1129 392 VGN-----LSGGnQQK-VVLAKWLATDPKVLILDEPT 422
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
498-639 |
5.19e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 71.68 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 498 PGR-VTAVMGPSGAGKTTFLNAVTGKVAGYK----VSGSVLVNGRHDNIRS-YKKIIGFVPQDDVVHGNLTVEENLWFSA 571
Cdd:TIGR02142 21 PGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEgeivLNGRTLFDSRKGIFLPpEKRRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 572 K-CRLSATTAhrhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:TIGR02142 101 KrARPSERRI------SFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
499-703 |
5.95e-13 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 69.12 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 499 GRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGR-HDNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAKCRLSA 577
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFI--EPASGSIKVNDQsHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 578 TTAHRHKVLTVERvidSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRH 657
Cdd:TIGR01277 102 NAEQQEKVVDAAQ---QVGIADYLDRLPEQ-----LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002258264 658 EALE-GVNVCAVVHQPSytlynmfdDLILLAKGGLIVYNGPVKSVED 703
Cdd:TIGR01277 174 LCSErQRTLLMVTHHLS--------DARAIASQIAVVSQGKIKVVSD 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
474-640 |
6.17e-13 |
|
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: 67.09 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLvngRHDNIRsykkiIGFVPQ 553
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD--EGIVT---WGSTVK-----IGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 ddvvhgnltveenlwfsakcrlsattahrhkvltvervidsldlqgvrsslvgtvekrgISGGQRKRVNVGIEMVMEPSL 633
Cdd:cd03221 71 -----------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
....*..
gi 1002258264 634 LILDEPT 640
Cdd:cd03221 92 LLLDEPT 98
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
500-640 |
7.04e-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: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 500 RVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR--HDNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAKCRlsa 577
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLVGGKdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK--- 1031
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 578 TTAHRHKVLTVERVIDSLDLQGVRSSlvgtvEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
468-639 |
7.43e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVefKDLTLSLGKkklLRSING---ELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYK-VSGSVLVNGRHDNIRS 543
Cdd:PRK11300 2 SQPLLSV--SGLMMRFGG---LLAVNNvnlEVREQEIVSLIGPNGAGKTTVFNCLTGF---YKpTGGTILLRGQHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 YKKI--IGFVP--QDDVVHGNLTVEENLwFSAKCR---------LSATTAHRHKVL-TVERVIDSLDLQGVRSslVGTVE 609
Cdd:PRK11300 74 GHQIarMGVVRtfQHVRLFREMTVIENL-LVAQHQqlktglfsgLLKTPAFRRAESeALDRAATWLERVGLLE--HANRQ 150
|
170 180 190
....*....|....*....|....*....|
gi 1002258264 610 KRGISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
474-639 |
1.07e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.14 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRHDNIRSYKKIiGFVPQ 553
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD--SGEVLWDGEPLDPEDRRRI-GYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DDVVHGNLTVEENLWFSAKCR-LSATTAHRhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPS 632
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKgLSKAEAKR----RADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPE 149
|
....*..
gi 1002258264 633 LLILDEP 639
Cdd:COG4152 150 LLILDEP 156
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
474-639 |
1.74e-12 |
|
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: 68.48 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGK-KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRhdNIRSYKKI----- 547
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE--PTSGEIFIDGE--DIREQDPVelrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQDDVVHGNLTVEENL--------WFSAKCRlsattahrhkvltvERVIDSLDLQGVRSSLVGTVEKRGISGGQRK 619
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIalvpkllkWPKEKIR--------------ERADELLALVGLDPAEFADRYPHELSGGQQQ 142
|
170 180
....*....|....*....|
gi 1002258264 620 RVNVGIEMVMEPSLLILDEP 639
Cdd:cd03295 143 RVGVARALAADPPLLLMDEP 162
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
461-640 |
2.18e-12 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 71.44 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 461 SEQQKEITRPLL--KVEFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYK-VSGSVLVN 535
Cdd:TIGR03375 449 PEGTRFLHRPRLqgEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGL---YQpTEGSVLLD 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 536 GrHDnIRSY-----KKIIGFVPQDDVV-HGnlTVEENLWFSAkcrLSATTAHRHKVLT---VERVI----DSLDLQgvrs 602
Cdd:TIGR03375 526 G-VD-IRQIdpadlRRNIGYVPQDPRLfYG--TLRDNIALGA---PYADDEEILRAAElagVTEFVrrhpDGLDMQ---- 594
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002258264 603 slVGtvEK-RGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR03375 595 --IG--ERgRSLSGGQRQAVALARALLRDPPILLLDEPT 629
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
474-640 |
2.63e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG-------RHDNIRsykk 546
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTH--PDAGSISLCGepvpsraRHARQR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 iIGFVPQDDVVHGNLTVEENLW-FSAKCRLSATTAHrhkvltvERVIDSLDLQGVRSSLVGTVekRGISGGQRKRVNVGI 625
Cdd:PRK13537 82 -VGVVPQFDNLDPDFTVRENLLvFGRYFGLSAAAAR-------ALVPPLLEFAKLENKADAKV--GELSGGMKRRLTLAR 151
|
170
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:PRK13537 152 ALVNDPDVLVLDEPT 166
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
471-640 |
3.08e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 68.93 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 471 LLKVefKDLTLSLG-KKKLLRSING---ELRPGRVTAVMGPSGAGKTTFLNAVTGKV-AGYKVSGSVLVNGRhdNI---- 541
Cdd:COG0444 1 LLEV--RNLKVYFPtRRGVVKAVDGvsfDVRRGETLGLVGESGSGKSTLARAILGLLpPPGITSGEILFDGE--DLlkls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 -RSYKKI----IGFVPQD-----DVVHgnlTVEENLwfsakcrlsATTAHRHKVLT----VERVIDSLDLQGVRSSlvgt 607
Cdd:COG0444 77 eKELRKIrgreIQMIFQDpmtslNPVM---TVGDQI---------AEPLRIHGGLSkaeaRERAIELLERVGLPDP---- 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002258264 608 vEKRG------ISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG0444 141 -ERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPT 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
469-640 |
3.47e-12 |
|
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: 65.92 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 469 RPLLKVEfkDLTLslgkKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRHDNIRSYKKI- 547
Cdd:cd03215 2 EPVLEVR--GLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA--SGEITLDGKPVTRRSPRDAi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ---IGFVPQDDVVHG---NLTVEENLwfsakcrlsattahrhkvltvervidsldlqGVRSSLvgtvekrgiSGGQRKRV 621
Cdd:cd03215 74 ragIAYVPEDRKREGlvlDLSVAENI-------------------------------ALSSLL---------SGGNQQKV 113
|
170
....*....|....*....
gi 1002258264 622 NVGIEMVMEPSLLILDEPT 640
Cdd:cd03215 114 VLARWLARDPRVLILDEPT 132
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
489-639 |
3.64e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.96 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRhdNIRSYKKIIGFVPQDDVVHGNLTVEENLW 568
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA--PSSGEITLDGV--PVTGPGADRGVVFQKDALLPWLNVLDNVA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002258264 569 FSAKCR-LSAttAHRHKVltVERVIDSLDLQGVrsslvgtvEKRGI---SGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:COG4525 99 FGLRLRgVPK--AERRAR--AEELLALVGLADF--------ARRRIwqlSGGMRQRVGIARALAADPRFLLMDEP 161
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
477-640 |
3.97e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 477 KDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKIIGFVPQDDV 556
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGDIDDPDVAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 557 VHGNLTVEENLWFSAKCRLSATTAhrhkvltVERVIDSLDLQGVrsslvGTVEKRGISGGQRKRVNVGIEMVMEPSLLIL 636
Cdd:PRK13539 84 MKPALTVAENLEFWAAFLGGEELD-------IAAALEAVGLAPL-----AHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
....
gi 1002258264 637 DEPT 640
Cdd:PRK13539 152 DEPT 155
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
474-640 |
4.79e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.57 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKK----LLRSINGELRPGRVTAVMGPSGAGKTTFL---NA---VTgkvagykvSGSVLVNGR------ 537
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLlerPT--------SGSVLVDGVdltals 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 HDNIRSYKKIIGFVPQddvvHGNL----TVEENLWFSAKCrlsattAHRHKVLTVERVIDSLDlqgvrssLVGTVEKRG- 612
Cdd:COG1135 74 ERELRAARRKIGMIFQ----HFNLlssrTVAENVALPLEI------AGVPKAEIRKRVAELLE-------LVGLSDKADa 136
|
170 180 190
....*....|....*....|....*....|....
gi 1002258264 613 ----ISGGQRKRvnVGI--EMVMEPSLLILDEPT 640
Cdd:COG1135 137 ypsqLSGGQKQR--VGIarALANNPKVLLCDEAT 168
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
474-639 |
5.55e-12 |
|
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: 65.95 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKK-----LLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGRhdnirsykkiI 548
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGEL--EKLSGSVSVPGS----------I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHgNLTVEENLWFSAKcrlsattaHRHKVLtvERVIDS----LDLQgvrsSLVG----TVEKRGI--SGGQR 618
Cdd:cd03250 69 AYVSQEPWIQ-NGTIRENILFGKP--------FDEERY--EKVIKAcalePDLE----ILPDgdltEIGEKGInlSGGQK 133
|
170 180
....*....|....*....|.
gi 1002258264 619 KRVNVGIEMVMEPSLLILDEP 639
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDP 154
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
474-640 |
9.18e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVlvngrhdnIRSYKKIIGFVPQ 553
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA--PDEGVI--------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 ddvvhgnltveenlwfsaKCRLSATTAhrhkvLTVERVidsLDLQ-GVRSSLVGTVEKR------------GISGGQRKR 620
Cdd:PRK09544 75 ------------------KLYLDTTLP-----LTVNRF---LRLRpGTKKEDILPALKRvqaghlidapmqKLSGGETQR 128
|
170 180
....*....|....*....|
gi 1002258264 621 VNVGIEMVMEPSLLILDEPT 640
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPT 148
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
473-640 |
1.13e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.57 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKK---KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKVS-GSVLVNGR----HDNiRSY 544
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF---YQPQgGQVLLDGKpisqYEH-KYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQDDVVHGNlTVEENLWFS-AKCRL-----SATTAHRHKVLtvervidsldlQGVRSSLVGTVEKRG--ISGG 616
Cdd:cd03248 87 HSKVSLVGQEPVLFAR-SLQDNIAYGlQSCSFecvkeAAQKAHAHSFI-----------SELASGYDTEVGEKGsqLSGG 154
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEAT 178
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
465-640 |
1.32e-11 |
|
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: 68.59 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 465 KEITRPLLKVEFKDLTLSLG--KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNG---RHD 539
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY--EPDSGQILLDGhdlADY 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 540 NIRSYKKIIGFVPQDdVVHGNLTVEENLWFSAKcrlsaTTAHRHKVLTVER------VIDSLDLqGVRSSlVGTVEKRgI 613
Cdd:TIGR02203 400 TLASLRRQVALVSQD-VVLFNDTIANNIAYGRT-----EQADRAEIERALAaayaqdFVDKLPL-GLDTP-IGENGVL-L 470
|
170 180
....*....|....*....|....*..
gi 1002258264 614 SGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEAT 497
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
474-640 |
1.39e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykVSGSVLVNGRH----DNIRSYKKIIG 549
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRA--TSGRIVFDGKDitdwQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHGNLTVEENLwfsakcRLSATTAHRHKVLT-VERVIDSLD-LQGVRSSLVGTvekrgISGGQRKRVNVGIEM 627
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENL------AMGGFFAERDQFQErIKWVYELFPrLHERRIQRAGT-----MSGGEQQMLAIGRAL 152
|
170
....*....|...
gi 1002258264 628 VMEPSLLILDEPT 640
Cdd:PRK11614 153 MSQPRLLLLDEPS 165
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
484-639 |
1.84e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 67.85 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAgykvSGSVLVNGRhdNIRSYKK-----IIGFVPQDdv 556
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvwPPT----AGSVRLDGA--DLSQWDReelgrHIGYLPQD-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 557 VH---GnlTVEENLwfsakCRLSATTAhrhkvltvERVIDSLDLQGVR---SSL-------VGtVEKRGISGGQRKRV-- 621
Cdd:COG4618 415 VElfdG--TIAENI-----ARFGDADP--------EKVVAAAKLAGVHemiLRLpdgydtrIG-EGGARLSGGQRQRIgl 478
|
170 180
....*....|....*....|....
gi 1002258264 622 ------NvgiemvmePSLLILDEP 639
Cdd:COG4618 479 aralygD--------PRLVVLDEP 494
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
496-640 |
1.85e-11 |
|
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: 68.89 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 496 LRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRH--DNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAkc 573
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA-- 2037
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 574 RLSATTAHRhkvltVERV----IDSLDLQGVRSSLVGTVekrgiSGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR01257 2038 RLRGVPAEE-----IEKVanwsIQSLGLSLYADRLAGTY-----SGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
489-640 |
2.24e-11 |
|
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: 65.05 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGrhdnIRSYKKIIGFVPQDDVVHG-------NL 561
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL--QPTSGEVRVAG----LVPWKRRKKFLRRIGVVFGqktqlwwDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 562 TVEENLWFSAKC-RLSATTAHRhkvlTVERVIDSLDLQGVRSSLVgtvekRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03267 111 PVIDSFYLLAAIyDLPPARFKK----RLDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
474-639 |
2.32e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.56 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGrhDNI------RSY--K 545
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIA--PDHGEILFDG--ENIpamsrsRLYtvR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGFVPQDDVVHGNLTVEENLWFSAK--CRLSATTAHRHKVLTVERVidsldlqGVRSSlvGTVEKRGISGGQRKRVNV 623
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLRehTQLPAPLLHSTVMMKLEAV-------GLRGA--AKLMPSELSGGMARRAAL 154
|
170
....*....|....*.
gi 1002258264 624 GIEMVMEPSLLILDEP 639
Cdd:PRK11831 155 ARAIALEPDLIMFDEP 170
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
484-694 |
3.30e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 66.99 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNG---RHDNIRSYKKIIGFVPQD-DVVHG 559
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVG--IWPPTSGSVRLDGadlKQWDRETFGKHIGYLPQDvELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 nlTVEENLwfsakCRLSattahrhKVLTVERVIDSLDLQGVRSSLVG-------TVEKRGI--SGGQRKRVNVGIEMVME 630
Cdd:TIGR01842 407 --TVAENI-----ARFG-------ENADPEKIIEAAKLAGVHELILRlpdgydtVIGPGGAtlSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002258264 631 PSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSytLYNMFDDLILLAKGGLIVY 694
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGRIARF 534
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
468-639 |
3.35e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVefKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgYKV-SGSVLVNGRhdNI----- 541
Cdd:CHL00131 4 NKPILEI--KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPA-YKIlEGDILFKGE--SIldlep 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 --RSYKKI-IGFvpQDDVVHGNLTVEENLwfsakcRLSATTAHRHKVLT-------VERVIDSLDLQGVRSSLVGTVEKR 611
Cdd:CHL00131 79 eeRAHLGIfLAF--QYPIEIPGVSNADFL------RLAYNSKRKFQGLPeldplefLEIINEKLKLVGMDPSFLSRNVNE 150
|
170 180
....*....|....*....|....*....
gi 1002258264 612 GISGGQRKRvNVGIEM-VMEPSLLILDEP 639
Cdd:CHL00131 151 GFSGGEKKR-NEILQMaLLDSELAILDET 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
462-640 |
4.14e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 67.15 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 462 EQQKEIT-----RPLL----KVEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTT-------Flnavtgkva 524
Cdd:COG5265 337 DQPPEVAdapdaPPLVvgggEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTlarllfrF--------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 525 gYKV-SGSVLVNGRhdNIR-----SYKKIIGFVPQDDVVHgNLTVEENLWFSakcRLSATTAhrhkvlTVERVIDSLDLQ 598
Cdd:COG5265 408 -YDVtSGRILIDGQ--DIRdvtqaSLRAAIGIVPQDTVLF-NDTIAYNIAYG---RPDASEE------EVEAAARAAQIH 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 599 GVRSSL-------VGtveKRG--ISGGQRKRvnVGIEMVM--EPSLLILDEPT 640
Cdd:COG5265 475 DFIESLpdgydtrVG---ERGlkLSGGEKQR--VAIARTLlkNPPILIFDEAT 522
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
474-639 |
4.15e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYK--VSGSVLVNG-RHDNIRSYKKIIGF 550
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI----AGLEdiTSGDLFIGEkRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRlSATTAHRHKvlTVERVIDSLDLQGVrsslvgtVEKR--GISGGQRKRVNVGIEMV 628
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLA-GAKKEEINQ--RVNQVAEVLQLAHL-------LDRKpkALSGGQRQRVAIGRTLV 149
|
170
....*....|.
gi 1002258264 629 MEPSLLILDEP 639
Cdd:PRK11000 150 AEPSVFLLDEP 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
468-640 |
6.03e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLkvEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRHDNIRSYKKI 547
Cdd:COG1129 1 AEPLL--EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD--SGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ----IGFVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQgVR-SSLVGTvekrgISGGQRKRVn 622
Cdd:COG1129 77 qaagIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLD-IDpDTPVGD-----LSVAQQQLV- 149
|
170 180
....*....|....*....|..
gi 1002258264 623 vgiE----MVMEPSLLILDEPT 640
Cdd:COG1129 150 ---EiaraLSRDARVLILDEPT 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
484-639 |
8.57e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKiiGFVPQDDVVHGNLTV 563
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 564 EENLWFSAKCRLSATTAHRHKVLtveRVIDSLDLQGvrsslvgtVEKRGI---SGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAH---QMLKKVGLEG--------AEKRYIwqlSGGQRQRVGIARALAANPQLLLLDEP 155
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
477-703 |
1.02e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 477 KDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR-------HDNIRsykKIIG 549
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP--RDAGNIIIDDEdisllplHARAR---RGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHGNLTVEENLWFSAKCRLSATTAHRHKvlTVERVIDSLDLQGVRSSLvgtveKRGISGGQRKRVNVGIEMVM 629
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQRED--RANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002258264 630 EPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTLyNMFDDLILLAKGGLIVYNGPVKSVED 703
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
474-640 |
1.07e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLN-------AVTGK--VAGYKVSGSVLVNgrHDNIRSY 544
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRvlnlletPDSGQlnIAGHQFDFSQKPS--EKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQDDVVHGNLTVEENLwFSAKCRL-----SATTAHRHKVLTVERVIDSLDlqgvRSSLvgtvekrGISGGQRK 619
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENL-IEAPCKVlglskEQAREKAMKLLARLRLTDKAD----RFPL-------HLSGGQQQ 148
|
170 180
....*....|....*....|.
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPT 169
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
474-639 |
1.20e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAvtgkVAGYKV--SGSVLVNGR-HDNIRSYKKIIGF 550
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRL----IAGFETpdSGRIMLDGQdITHVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRlsattahrhKVLTVE---RVIDSLDLqgVRSSLVGTVEKRGISGGQRKRVNVGIEM 627
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQ---------KTPAAEitpRVMEALRM--VQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170
....*....|..
gi 1002258264 628 VMEPSLLILDEP 639
Cdd:PRK09452 160 VNKPKVLLLDES 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
475-639 |
1.46e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 475 EFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGRhdNIRSykkiigfvpQD 554
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD--AGEVLWQGE--PIRR---------QR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 555 DVVHGN-------------LTVEENLWFSakCRLsattahrHKVLTVERVIDSLD---LQGVRSSLVGTvekrgISGGQR 618
Cdd:PRK13538 70 DEYHQDllylghqpgikteLTALENLRFY--QRL-------HGPGDDEALWEALAqvgLAGFEDVPVRQ-----LSAGQQ 135
|
170 180
....*....|....*....|.
gi 1002258264 619 KRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEP 156
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
489-639 |
1.65e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.48 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRhdnirsykKIIGFVPQDDVVHGN------LT 562
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG--LAQPTSGGVILEGK--------QITEPGPDRMVVFQNysllpwLT 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 563 VEENLWFSAKCRLsattAHRHKVLTVERVIDSLDLQGVRSSlvgtVEKR--GISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:TIGR01184 71 VRENIALAVDRVL----PDLSKSERRAIVEEHIALVGLTEA----ADKRpgQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-640 |
1.67e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 478 DLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTF---LNAVTGKVAGYKVSGSVLVNGRhdNIRSYKKIIGFVPQD 554
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFlrtLNRMNDKVSGYRYSGDVLLGGR--SIFNYRDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 555 DVVHGN-----LTVEENLwfsakcrLSATTAHrhkvltveRVIDSLDLQGV---RSSLVG---TVEKR------GISGGQ 617
Cdd:PRK14271 104 GMLFQRpnpfpMSIMDNV-------LAGVRAH--------KLVPRKEFRGVaqaRLTEVGlwdAVKDRlsdspfRLSGGQ 168
|
170 180
....*....|....*....|...
gi 1002258264 618 RKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPT 191
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
474-640 |
1.75e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.98 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvagYKV----SGSVLVNG---RHDNIRSYK 545
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL------QRVfdpqSGRILIDGtdiRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGFVPQDDVVHgNLTVEENLWF------SAKCRLSATTAHRHKVltVERVIDSLDlqgvrsSLVGtveKRG--ISGGQ 617
Cdd:PRK13657 409 RNIAVVFQDAGLF-NRSIEDNIRVgrpdatDEEMRAAAERAQAHDF--IERKPDGYD------TVVG---ERGrqLSGGE 476
|
170 180
....*....|....*....|...
gi 1002258264 618 RKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEAT 499
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
471-696 |
3.11e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.95 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 471 LLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGS--------VLVNGR-HDNI 541
Cdd:PRK09984 4 IIRVE--KLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShiellgrtVQREGRlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 RSYKKIIGFVPQDDVVHGNLTVEENLWFSAkcrLSATTAHRHKVLTVERVIDSLDLQGV-RSSLVGTVEKR--GISGGQR 618
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGA---LGSTPFWRTCFSWFTREQKQRALQALtRVGMVHFAHQRvsTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 619 KRVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRH-EALEGVNVCAVVHQPSYTLynMFDDLILLAKGGLIVYNG 696
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYAL--RYCERIVALRQGHVFYDG 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
495-639 |
3.37e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 495 ELRPGRVTAVMGPSGAGKTTFLNAvtgkVAGYKV--SGSVLVNGR-HDNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSA 571
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNL----IAGFLTpaSGSLTLNGQdHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002258264 572 KCRLSATTAHRHKvltVERVIDSLDLQGVRSSLVGTVekrgiSGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK10771 97 NPGLKLNAAQREK---LHAIARQMGIEDLLARLPGQL-----SGGQRQRVALARCLVREQPILLLDEP 156
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
452-640 |
3.68e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 452 TFTGVLSMVSEQ---QKEITRPLLKVEFKDLTLSL-GKKKL-LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTgkvAGY 526
Cdd:PRK11176 317 TLFAILDLEQEKdegKRVIERAKGDIEFRNVTFTYpGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLT---RFY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 527 KV-SGSVLVNGRhdNIRSYK-----KIIGFVPQDdvVH-GNLTVEENLWFSAKCRLS-------ATTAHRHKVltVERVI 592
Cdd:PRK11176 394 DIdEGEILLDGH--DLRDYTlaslrNQVALVSQN--VHlFNDTIANNIAYARTEQYSreqieeaARMAYAMDF--INKMD 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002258264 593 DSLDlqgvrsSLVGtveKRGI--SGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11176 468 NGLD------TVIG---ENGVllSGGQRQRIAIARALLRDSPILILDEAT 508
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
474-640 |
3.80e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 62.08 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGK-----KKLLRSINGELRPGRVTAVMGPSGAGKTTF---LNAVTgkvagYKVSGSVLVNGRH------D 539
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLiqhLNGLL-----KPTSGTVTIDGRDitakkkK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 540 NIRSYKKIIGFVPQ------------DDVVHG--NLTVEENlwfSAKcrlsattahrhkvltvERVIDSLDLQGVRSSLV 605
Cdd:TIGR04521 76 KLKDLRKKVGLVFQfpehqlfeetvyKDIAFGpkNLGLSEE---EAE----------------ERVKEALELVGLDEEYL 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002258264 606 gtveKR---GISGGQRKRVNV-GIeMVMEPSLLILDEPT 640
Cdd:TIGR04521 137 ----ERspfELSGGQMRRVAIaGV-LAMEPEVLILDEPT 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
489-640 |
6.97e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.40 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR-----HDNIRSYKKIIGFVPQD-DVVHGNLT 562
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK--PSSGRILFDGKpidysRKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 563 VEENLWFSA-KCRLSATTAHRHkvltVERVIDSLDLQGVRSSlvgtvEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK13636 100 VYQDVSFGAvNLKLPEDEVRKR----VDNALKRTGIEHLKDK-----PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
474-638 |
7.18e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGrhdnirsyKKIIGFVPQ 553
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKG--------KDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DDVVHG-----NLTVE----ENLWFsAKCRLSATTAHRHKVLT--------VERVIDSLDLQgvrSSLVGTVEKRGISGG 616
Cdd:PRK09580 74 DRAGEGifmafQYPVEipgvSNQFF-LQTALNAVRSYRGQEPLdrfdfqdlMEEKIALLKMP---EDLLTRSVNVGFSGG 149
|
170 180
....*....|....*....|..
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDE 638
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDE 171
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
470-640 |
7.32e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.14 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVE--FKDLTL-SLGKKKL--LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvaGYKV-SGSVLVngRHDN--- 540
Cdd:COG4778 3 TLLEVEnlSKTFTLhLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---NYLPdSGSILV--RHDGgwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 541 ------------IRsyKKIIGFVPQ----------DDVV------HG---------------NLTVEENLWfsakcRLSA 577
Cdd:COG4778 78 dlaqaspreilaLR--RRTIGYVSQflrviprvsaLDVVaeplleRGvdreearararellaRLNLPERLW-----DLPP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 578 TTahrhkvltvervidsldlqgvrsslvgtvekrgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4778 151 AT---------------------------------FSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
474-640 |
8.96e-10 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 58.59 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSykkiigfvPQ 553
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK--PDSGEILVDGKEVSFAS--------PR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DdvvhgnltveenlwfsakcrlsattAHRHKVLTVervidsldLQgvrsslvgtvekrgISGGQRKRVNVGIEMVMEPSL 633
Cdd:cd03216 71 D-------------------------ARRAGIAMV--------YQ--------------LSVGERQMVEIARALARNARL 103
|
....*..
gi 1002258264 634 LILDEPT 640
Cdd:cd03216 104 LILDEPT 110
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
461-639 |
1.12e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 461 SEQQKEITrPLLkvEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYK--VSGSVLVNGRH 538
Cdd:PRK11607 10 AKTRKALT-PLL--EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRML----AGFEqpTAGQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 -DNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAKC-RLSattahrhKVLTVERVIDSLDLqgVRSSLVGTVEKRGISGG 616
Cdd:PRK11607 83 lSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQdKLP-------KAEIASRVNEMLGL--VHMQEFAKRKPHQLSGG 153
|
170 180
....*....|....*....|...
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEP 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
468-640 |
1.64e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKI 547
Cdd:PRK11701 3 DQPLLSVR--GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA--PDAGEVHYRMRDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 ------------IGFVPQD-------DVVHGNLTVEenlwfsakcRLSATTAhRHKVltvervidslDLQGVRSSLVGTV 608
Cdd:PRK11701 79 seaerrrllrteWGFVHQHprdglrmQVSAGGNIGE---------RLMAVGA-RHYG----------DIRATAGDWLERV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002258264 609 E---------KRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11701 139 EidaariddlPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
474-639 |
2.56e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.10 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG---KVAGYKVSGSVLVNGRHDNIRSykkiIGF 550
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehQTSGHIRFHGTDVSRLHARDRK----VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKC-----RLSATtAHRHKVLTVervidsldLQGVRSSLVGTVEKRGISGGQRKRVNVGI 625
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVlprreRPNAA-AIKAKVTQL--------LEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170
....*....|....
gi 1002258264 626 EMVMEPSLLILDEP 639
Cdd:PRK10851 150 ALAVEPQILLLDEP 163
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
474-640 |
2.67e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLN-------AVTGK--VAGYKVSGSVLVNGRhdNIRSY 544
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRvlnllemPRSGTlnIAGNHFDFSKTPSDK--AIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQDDVVHGNLTVEENLwFSAKCR---LSATTAHRH--KVLTVERVIDSLD---LQgvrsslvgtvekrgISGG 616
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNL-IEAPCRvlgLSKDQALARaeKLLERLRLKPYADrfpLH--------------LSGG 145
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPT 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
474-639 |
2.75e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYK--VSGSVLVNGRHDNIRSYK-KIIGF 550
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLV----AGLEkpTEGQIFIDGEDVTHRSIQqRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKcRLSATTAHRhkvltVERVIDSL---DLQGVRSSLVGTvekrgISGGQRKRVNVGIEM 627
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLK-MLGVPKEER-----KQRVKEALelvDLAGFEDRYVDQ-----ISGGQQQRVALARAL 151
|
170
....*....|..
gi 1002258264 628 VMEPSLLILDEP 639
Cdd:PRK11432 152 ILKPKVLLFDEP 163
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
486-640 |
3.61e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.29 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 486 KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG-----RHDNIRSYKKIIGFV---PQDDVV 557
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK--PTSGKIIIDGvditdKKVKLSDIRKKVGLVfqyPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 558 HGnlTVEENLWFSAKCR-LSATTAHRhkvltveRVIDSLDLQGVRSSLVGTVEKRGISGGQRKRVNVGIEMVMEPSLLIL 636
Cdd:PRK13637 98 EE--TIEKDIAFGPINLgLSEEEIEN-------RVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
....
gi 1002258264 637 DEPT 640
Cdd:PRK13637 169 DEPT 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
474-640 |
4.90e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRH----DNIRSYKKIIG 549
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINynklDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHGNLTVEENLWFSakcrlsattahRH---KVLTVErVID----------SLDLQGVRSSLVGTVEKRGISgg 616
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIG-----------RHltkKVCGVN-IIDwremrvraamMLLRVGLKVDLDEKVANLSIS-- 149
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPT 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
473-697 |
5.30e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.44 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTgkVAGYKVSGSVLVNGRH-------------- 538
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN--FLEKPSEGSIVVNGQTinlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 --DNIRSYKKIIGFVPQDDVVHGNLTVEENLwFSAKCRLSATTAHRHKvltvERVIDSLDLQGVRSSLVGTVEKRgISGG 616
Cdd:PRK10619 83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEAR----ERAVKYLAKVGIDERAQGKYPVH-LSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYTlYNMFDDLILLAKgGLIVYNG 696
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA-RHVSSHVIFLHQ-GKIEEEG 234
|
.
gi 1002258264 697 P 697
Cdd:PRK10619 235 A 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
464-640 |
5.37e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 464 QKEITRPLLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDN--- 540
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP--PDSGTLEIGGNPCArlt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 541 -IRSYKKIIGFVPQDDVVHGNLTVEENLWFsakcRLSATTAHRHKvltVERVIDSLDLQGVRSSLVGTVEKrgisgGQRK 619
Cdd:PRK15439 80 pAKAHQLGIYLVPQEPLLFPNLSVKENILF----GLPKRQASMQK---MKQLLAALGCQLDLDSSAGSLEV-----ADRQ 147
|
170 180
....*....|....*....|.
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPT 168
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
470-639 |
7.71e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVefKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL------NAVTGKVagyKVSGSVLVNGR------ 537
Cdd:PRK14258 6 PAIKV--NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEV---RVEGRVEFFNQniyerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 ------------------------HDNIRSYKKIIGFVPQ---DDVVHGNLTVEEnLWFSAKCRLsattahrHKvltver 590
Cdd:PRK14258 81 vnlnrlrrqvsmvhpkpnlfpmsvYDNVAYGVKIVGWRPKleiDDIVESALKDAD-LWDEIKHKI-------HK------ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002258264 591 viDSLDLqgvrsslvgtvekrgiSGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK14258 147 --SALDL----------------SGGQQQRLCIARALAVKPKVLLMDEP 177
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
417-640 |
8.33e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 417 SAPKGkhrsTHTQIFKYAYGEIEKEKVRQQENKnLTFTgvlsmVSEQQKEITRPLLkVEFKDLTLSLGKKKLlRSINGEL 496
Cdd:PRK13409 295 SKPKG----VRVGINEYLKGYLPEENMRIRPEP-IEFE-----ERPPRDESERETL-VEYPDLTKKLGDFSL-EVEGGEI 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 497 RPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVngrhdNIR-SYKkiigfvPQ---DDVvhgNLTVEENLwFSAK 572
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLK--PDEGEVDP-----ELKiSYK------PQyikPDY---DGTVEDLL-RSIT 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 573 CRLSaTTAHRHKV---LTVERVIDSldlqgvrsslvgtvEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK13409 426 DDLG-SSYYKSEIikpLQLERLLDK--------------NVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
474-640 |
8.81e-09 |
|
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: 56.17 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLG--KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRH-----DNIRSYkk 546
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK--PQQGEITLDGVPvsdleKALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 547 iIGFVPQDDVVHgNLTVEENLwfsakcrlsattahrhkvltvervidsldlqGVRsslvgtvekrgISGGQRKRVNVGIE 626
Cdd:cd03247 77 -ISVLNQRPYLF-DTTLRNNL-------------------------------GRR-----------FSGGERQRLALARI 112
|
170
....*....|....
gi 1002258264 627 MVMEPSLLILDEPT 640
Cdd:cd03247 113 LLQDAPIVLLDEPT 126
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-640 |
9.18e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNA------------VTGKVagyKVSGSVLVNGRHDNI 541
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEV---RLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 RSYKKIiGFVPQDDVVHGNLTVEENLWFSAKcrLSATTAHRHKVltVERVIDSLDlqgvRSSLVGTVEKR------GISG 615
Cdd:PRK14267 82 EVRREV-GMVFQYPNPFPHLTIYDNVAIGVK--LNGLVKSKKEL--DERVEWALK----KAALWDEVKDRlndypsNLSG 152
|
170 180
....*....|....*....|....*
gi 1002258264 616 GQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPT 177
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
474-640 |
9.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.78 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGK-KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG---RHDN--IRSYKKI 547
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK--PTSGEVLIKGepiKYDKksLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQ--DDVVHGNlTVEENLWFSA-KCRLSATTAHRhkvltveRVIDSLDlqgvRSSLVGTVEK--RGISGGQRKRVN 622
Cdd:PRK13639 80 VGIVFQnpDDQLFAP-TVEEDVAFGPlNLGLSKEEVEK-------RVKEALK----AVGMEGFENKppHHLSGGQKKRVA 147
|
170
....*....|....*...
gi 1002258264 623 VGIEMVMEPSLLILDEPT 640
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPT 165
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
474-640 |
1.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.44 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGK-KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNGRH---DNIRSYKKIIG 549
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQR--GRVKVMGREvnaENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQD--DVVHGNlTVEENLWFSA-KCRLSATTAHRHkvltVERVIDSLDLQGVRsslvgtvEK--RGISGGQRKRVNVG 624
Cdd:PRK13647 83 LVFQDpdDQVFSS-TVWDDVAFGPvNMGLDKDEVERR----VEEALKAVRMWDFR-------DKppYHLSYGQKKRVAIA 150
|
170
....*....|....*.
gi 1002258264 625 IEMVMEPSLLILDEPT 640
Cdd:PRK13647 151 GVLAMDPDVIVLDEPM 166
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
461-640 |
1.07e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 59.37 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 461 SEQQKEITRPLLKVEFKDLTLSLG-KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkVAGYKV-SGSVLVNGRH 538
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLL---VGFFQArSGEILLNGFS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 -DNI--RSYKKIIGFVPQDDVVHGNlTVEENLWFSAKcrlsattahrhKVLTVERVIDSLDL-----------QGVRSSL 604
Cdd:TIGR01193 538 lKDIdrHTLRQFINYLPQEPYIFSG-SILENLLLGAK-----------ENVSQDEIWAACEIaeikddienmpLGYQTEL 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002258264 605 vgTVEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR01193 606 --SEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
504-639 |
1.16e-08 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 57.89 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 504 VMGPSGAGKTTFLNAVtgkvAGYKV--SGSVLVNGRH-DNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAKCRlsATTA 580
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLL----AGFEQpdSGSIMLDGEDvTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMR--KVPR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 581 HRHKvltvERVIDSLDLqgVRSSLVGTVEKRGISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:TIGR01187 75 AEIK----PRVLEALRL--VQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEP 127
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-640 |
1.26e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 479 LTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGY----KVSGSVLVNGRH----DNIRsYKKIIGF 550
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskiKVDGKVLYFGKDifqiDAIK-LRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRlsATTAHRHKVLTVERVIDSLDL-QGVRSSLVGTVEKrgISGGQRKRVNVGIEMVM 629
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSH--GIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQ--LSGGQQQRLTIARALAL 170
|
170
....*....|.
gi 1002258264 630 EPSLLILDEPT 640
Cdd:PRK14246 171 KPKVLLMDEPT 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
474-736 |
1.33e-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: 58.66 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIRSYKKIIGFVPQ 553
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 D-DVVHGNLTVEE-NLWFSAK-----------CRLSATTAHRHKVLTVERVIDSLDLQGVRSS--------LVGTVE--- 609
Cdd:TIGR03269 81 PcPVCGGTLEPEEvDFWNLSDklrrrirkriaIMLQRTFALYGDDTVLDNVLEALEEIGYEGKeavgravdLIEMVQlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 610 -----KRGISGGQRKRVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLlralrHEAL-EGV---NVCAVV--HQPSyTLYN 678
Cdd:TIGR03269 161 rithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLV-----HNALeEAVkasGISMVLtsHWPE-VIED 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 679 MFDDLILLAKGGLIVYNGPVKSVEDYFST-----------LGITVPERVNPPDHYIDILEGIVKPESGI 736
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAVFMEGvsevekeceveVGEPIIKVRNVSKRYISVDRGVVKAVDNV 303
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
473-640 |
1.33e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.97 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSL---GKKKLLRSINGELRPGRVTAVMGPSGAGKTT-------FLNAVTGKVAgykVSGSVLVNGRHdniR 542
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaallqnLYQPTGGQVL---LDGVPLVQYDH---H 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 543 SYKKIIGFVPQDDVVHGNlTVEENLWFS------AKCRLSATTAHRHKVLT-VERVIDsldlqgvrsSLVGtvEKRG-IS 614
Cdd:TIGR00958 552 YLHRQVALVGQEPVLFSG-SVRENIAYGltdtpdEEIMAAAKAANAHDFIMeFPNGYD---------TEVG--EKGSqLS 619
|
170 180
....*....|....*....|....*.
gi 1002258264 615 GGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEAT 645
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
474-713 |
1.68e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.12 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVL----VNGRHDNIRSYKKI 547
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKItvdgITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQD-DVVHGNLTVEENLWFSAKCRlsatTAHRHKVLT-VERVIDSLDLQGVRSSlvgtvEKRGISGGQRKRVNVGI 625
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAFGLENR----AVPRPEMIKiVRDVLADVGMLDYIDS-----EPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 626 EMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALE-GVNVCAVVHQPSYTlyNMFDDLILLAKGGLIVYNGPVK--SVE 702
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEifSKV 234
|
250
....*....|.
gi 1002258264 703 DYFSTLGITVP 713
Cdd:PRK13640 235 EMLKEIGLDIP 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
469-640 |
1.70e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.26 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 469 RPLLkvEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGrHD----NIRSY 544
Cdd:PRK10247 5 SPLL--QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PTSGTLLFEG-EDistlKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQDDVVHGNlTVEENLWFSAKCrlsattahRHKVLTVERVIDSLDlqgvRSSLVGTVEKRGI---SGGQRKRV 621
Cdd:PRK10247 80 RQQVSYCAQTPTLFGD-TVYDNLIFPWQI--------RNQQPDPAIFLDDLE----RFALPDTILTKNIaelSGGEKQRI 146
|
170
....*....|....*....
gi 1002258264 622 NVGIEMVMEPSLLILDEPT 640
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEIT 165
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
468-640 |
2.18e-08 |
|
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: 58.16 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEfkDLTLSLGK----KKLLRSINGELRPGRVTAVMGPSGAGKT-TFLnAVTGKV--AGYKVSGSVLVNGR--- 537
Cdd:COG4172 3 SMPLLSVE--DLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLpdPAAHPSGSILFDGQdll 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 HDNIRSYKKI----IGFVPQD-----DVVHgnlTVEENLwfsakcrlsATTAHRHKVLT----VERVIDSLDLQGVRSSl 604
Cdd:COG4172 80 GLSERELRRIrgnrIAMIFQEpmtslNPLH---TIGKQI---------AEVLRLHRGLSgaaaRARALELLERVGIPDP- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002258264 605 vgtvEKR------GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4172 147 ----ERRldayphQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
479-534 |
3.27e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 3.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002258264 479 LTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLV 534
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV 91
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
468-640 |
5.49e-08 |
|
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: 54.75 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEFKDLTLSLGKKKL--LRSINGELRPGRVTAVMGPSGAGKTTFLnavtGKVAGYKV--SGSVLVNGrHD---- 539
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLL----GLLAGLDRptSGTVRLAG-QDlfal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 540 ------NIRSYKkiIGFVPQDDVVHGNLTVEENlwfsakcrlsattahrhkvltverVIDSLDLQGVRSSL--------- 604
Cdd:COG4181 80 dedaraRLRARH--VGFVFQSFQLLPTLTALEN------------------------VMLPLELAGRRDARararaller 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002258264 605 VGtVEKR------GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4181 134 VG-LGHRldhypaQLSGGEQQRVALARAFATEPAILFADEPT 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
474-640 |
8.39e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvaGYKV-SGSVLVNGRHDNIRSYKK-I---I 548
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYG---LYQPdSGEILIDGKPVRIRSPRDaIalgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQddvvH----GNLTVEENLWFSAK----CRLSATTAHRHkvltVERVIDSLDLQgVR-SSLVGTvekrgISGGQRK 619
Cdd:COG3845 83 GMVHQ----HfmlvPNLTVAENIVLGLEptkgGRLDRKAARAR----IRELSERYGLD-VDpDAKVED-----LSVGEQQ 148
|
170 180
....*....|....*....|....*
gi 1002258264 620 RVnvgiEMV----MEPSLLILDEPT 640
Cdd:COG3845 149 RV----EILkalyRGARILILDEPT 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
456-640 |
1.04e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 456 VLSMVSEQQKEITRPLLKVEfkDLTL-SLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAgykvSGSV 532
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVE--NLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlrPPA----SGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 533 LVNGR---HDNIRS-YKKIIGFVPQDDVVHG---NLTVEENL--------WFSAKCRLSATTAHRHkvltVERVIDSLDl 597
Cdd:COG3845 316 RLDGEditGLSPRErRRLGVAYIPEDRLGRGlvpDMSVAENLilgryrrpPFSRGGFLDRKAIRAF----AEELIEEFD- 390
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002258264 598 qgVRSSLVGTvEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG3845 391 --VRTPGPDT-PARSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
464-698 |
1.09e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 464 QKEITRPLLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLnavtgKVAGYK---VSGSVLVNGR--- 537
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-----KMLGRHqppSEGEILLDAQple 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 HDNIRSYKKIIGFVPQDDVVHGNLTVEENL------WFSAKCRLSAttAHRHKVltvERVIDSLDLQGVRSSLVGTvekr 611
Cdd:PRK10575 77 SWSSKAFARKVAYLPQQLPAAEGMTVRELVaigrypWHGALGRFGA--ADREKV---EEAISLVGLKPLAHRLVDS---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 612 gISGGQRKRVNVGIEMVMEPSLLILDEPTSGL-DSSSSQLLLRALRHEALEGVNVCAVVHQpsytlYNMF----DDLILL 686
Cdd:PRK10575 148 -LSGGERQRAWIAMLVAQDSRCLLLDEPTSALdIAHQVDVLALVHRLSQERGLTVIAVLHD-----INMAarycDYLVAL 221
|
250
....*....|..
gi 1002258264 687 AKGGLIVYNGPV 698
Cdd:PRK10575 222 RGGEMIAQGTPA 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
478-639 |
1.11e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 478 DLTLSLGKKKLlrSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNGR--HD-----NIRSYKKIIGF 550
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQK--GRIVLNGRvlFDaekgiCLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 551 VPQDDVVHGNLTVEENLWFSAKCRLSAttahrhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVME 630
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGMAKSMVA---------QFDKIVALLGIEPLLDRYPGS-----LSGGEKQRVAIGRALLTA 146
|
....*....
gi 1002258264 631 PSLLILDEP 639
Cdd:PRK11144 147 PELLLMDEP 155
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
479-701 |
1.23e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 479 LTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVA------GYKVSGSVLVNGRH----DNIRsYKKII 548
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprGARVTGDVTLNGEPlaaiDAPR-LARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQddvvhgnlTVEENLWFSAK----------CRLSATTAHRhkvlTVERVIDSLDLQGVrSSLVGTvEKRGISGGQR 618
Cdd:PRK13547 86 AVLPQ--------AAQPAFAFSAReivllgryphARRAGALTHR----DGEIAWQALALAGA-TALVGR-DVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 619 KRVNVGI---------EMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALE-GVNVCAVVHQPSytLYNMFDDLILLAK 688
Cdd:PRK13547 152 ARVQFARvlaqlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPN--LAARHADRIAMLA 229
|
250
....*....|...
gi 1002258264 689 GGLIVYNGPVKSV 701
Cdd:PRK13547 230 DGAIVAHGAPADV 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
485-640 |
1.54e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 485 KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGyKVSGSVLVNGRHDNIRSYKKII----GFVPQDDVVHG- 559
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG-KFEGNVFINGKPVDIRNPAQAIragiAMVPEDRKRHGi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 --NLTVEENLWFSAKCRLSattahrhkvlTVERVIDSLDLQGVRSSL----VGTVEK----RGISGGQRKRVNVGIEMVM 629
Cdd:TIGR02633 351 vpILGVGKNITLSVLKSFC----------FKMRIDAAAELQIIGSAIqrlkVKTASPflpiGRLSGGNQQKAVLAKMLLT 420
|
170
....*....|.
gi 1002258264 630 EPSLLILDEPT 640
Cdd:TIGR02633 421 NPRVLILDEPT 431
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
416-640 |
2.59e-07 |
|
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: 54.56 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 416 RSAPKGKHRSTHTQIfkYAYGEIEKEKVRQQENKNltftgvlsmvseqqkEITRPL------LKVEFKDLTLSLGKKKLL 489
Cdd:TIGR03719 276 RQSPKGRQAKSKARL--ARYEELLSQEFQKRNETA---------------EIYIPPgprlgdKVIEAENLTKAFGDKLLI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 490 RSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNgrhDNIRsykkiIGFVPQD-DVVHGNLTVeenlW 568
Cdd:TIGR03719 339 DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD--SGTIEIG---ETVK-----LAYVDQSrDALDPNKTV----W 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 569 fsakcrlsattahrhkvltvERVIDSLDLQgvrssLVGTVE------------------KR--GISGGQRKRVNVGIEMV 628
Cdd:TIGR03719 405 --------------------EEISGGLDII-----KLGKREipsrayvgrfnfkgsdqqKKvgQLSGGERNRVHLAKTLK 459
|
250
....*....|..
gi 1002258264 629 MEPSLLILDEPT 640
Cdd:TIGR03719 460 SGGNVLLLDEPT 471
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
482-639 |
4.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 482 SLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGyKVSGSVLVNGRhdnirsykkiIGFVPQDDVVHgNL 561
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-RSDASVVIRGT----------VAYVPQVSWIF-NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 562 TVEENLWFSakcrlSATTAHRHkvltvERVIDSLDLQGVRSSLVG----TVEKRG--ISGGQRKRVNVGIEMVMEPSLLI 635
Cdd:PLN03130 694 TVRDNILFG-----SPFDPERY-----ERAIDVTALQHDLDLLPGgdltEIGERGvnISGGQKQRVSMARAVYSNSDVYI 763
|
....
gi 1002258264 636 LDEP 639
Cdd:PLN03130 764 FDDP 767
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
488-640 |
6.75e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 488 LLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDN---------IRSYKkiIGFVPQDDVVH 558
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT--PTSGDVIFNGQPMSklssaakaeLRNQK--LGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 559 GNLTVEEN----LWFSAKCRLSATtahrhkvltvERVIDSLdlqgvrsSLVGtVEKRG------ISGGQRKRVNVGIEMV 628
Cdd:PRK11629 100 PDFTALENvampLLIGKKKPAEIN----------SRALEML-------AAVG-LEHRAnhrpseLSGGERQRVAIARALV 161
|
170
....*....|..
gi 1002258264 629 MEPSLLILDEPT 640
Cdd:PRK11629 162 NNPRLVLADEPT 173
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
472-640 |
7.31e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEFKDLTLSLGKK-----KLLRSINGELRPGRVTAVMGPSGAGKTTF---LNAV----TGKVAGY-------KVSGSV 532
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdTGTIEWIfkdeknkKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 533 LVNGRHDNI-----RSYKKIIGFVPQDDVVHG-------NLTVEENLWFSAkcrLSATTAhrhKVLTVERVIDSLDLQGV 600
Cdd:PRK13651 81 EKVLEKLVIqktrfKKIKKIKEIRRRVGVVFQfaeyqlfEQTIEKDIIFGP---VSMGVS---KEEAKKRAAKYIELVGL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002258264 601 RSSLVgtveKR---GISGGQRKRVNV-GIeMVMEPSLLILDEPT 640
Cdd:PRK13651 155 DESYL----QRspfELSGGQKRRVALaGI-LAMEPDFLVFDEPT 193
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
826-1010 |
7.52e-07 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 51.12 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 826 RVTKQRLREARLLAVDFLILGLAGICLGTI---AKLSDPNFGMPGYIYTIIAVSLLCKIAALR-SFSLERLQYLRERESG 901
Cdd:pfam01061 4 REFLRRWRDPSLGLWRLIQPILMALIFGTLfgnLGNQQGGLNRPGLLFFSILFNAFSALSGISpVFEKERGVLYRELASP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 902 MSSL-AYFLARDTIDHFSTIVKPIVYLSMFYYFNNPRSTITDNYIILLALV---YCVTGIGYTF-AICFNPGSAQLCSAL 976
Cdd:pfam01061 84 LYSPsAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLltaLAASSLGLFIsALAPSFEDASQLGPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002258264 977 IPVVLTLLS----TQNNTPAIL---NRLCYPKWALEGFIIV 1010
Cdd:pfam01061 164 VLLPLLLLSgffiPIDSMPVWWqwiYYLNPLTYAIEALRAN 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
489-640 |
1.00e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.67 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG-------RHDNIRSYKKIIGFVPQ-------- 553
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHV--PTQGSVRVDDtlitstsKNKDIKQIRKKVGLVFQfpesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 ----DDVVHGnltvEENLWFSAKcrlSATTAHRHKvltvervidsLDLQGVRSSLVgtvEKR--GISGGQRKRVNVGIEM 627
Cdd:PRK13649 101 etvlKDVAFG----PQNFGVSQE---EAEALAREK----------LALVGISESLF---EKNpfELSGGQMRRVAIAGIL 160
|
170
....*....|...
gi 1002258264 628 VMEPSLLILDEPT 640
Cdd:PRK13649 161 AMEPKILVLDEPT 173
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
470-639 |
1.13e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGRHDNIRSYKKIIG 549
Cdd:PRK13543 10 PLLAAH--ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLL--HVESGQIQIDGKTATRGDRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHGNLTVEENLWFSakCRLSAttahRHKVLTVERVIDSLDLQGVRSSLVgtvekRGISGGQRKRVNVGiEMVM 629
Cdd:PRK13543 86 YLGHLPGLKADLSTLENLHFL--CGLHG----RRAKQMPGSALAIVGLAGYEDTLV-----RQLSAGQKKRLALA-RLWL 153
|
170
....*....|.
gi 1002258264 630 EPS-LLILDEP 639
Cdd:PRK13543 154 SPApLWLLDEP 164
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
464-640 |
1.19e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 464 QKEITRPLLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRHDNIRS 543
Cdd:PRK09700 254 KENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAGGEIRLNGKDISPRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 ----YKKIIGFVPQ---DDVVHGNLTVEENLWFSAKCRLSATTA------HRHKVLTVERVIDSLDLQGvrSSLVGTVEK 610
Cdd:PRK09700 332 pldaVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGamglfhEVDEQRTAENQRELLALKC--HSVNQNITE 409
|
170 180 190
....*....|....*....|....*....|
gi 1002258264 611 rgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK09700 410 --LSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
473-640 |
1.27e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 50.57 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLS--LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykVSGSVLVNG-------RHDnIRS 543
Cdd:cd03244 2 DIEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL--SSGSILIDGvdiskigLHD-LRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 ykkIIGFVPQDDVVHGNlTVEENLWFSAKCrlsaTTAHRHKVLtvERV-----IDSLDLQgvrssLVGTVEKRG--ISGG 616
Cdd:cd03244 79 ---RISIIPQDPVLFSG-TIRSNLDPFGEY----SDEELWQAL--ERVglkefVESLPGG-----LDTVVEEGGenLSVG 143
|
170 180
....*....|....*....|....
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEAT 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
483-640 |
1.28e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.64 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 483 LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGrHDNIR-------SYKKIIGFVPQDD 555
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--IERPSAGKIWFSG-HDITRlknrevpFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 556 VVHGNLTVEENLwfsakcrlsattahrhkvlTVERVIDSLDLQGVRSSLVGTVEKRGI-----------SGGQRKRVNVG 624
Cdd:PRK10908 89 HLLMDRTVYDNV-------------------AIPLIIAGASGDDIRRRVSAALDKVGLldkaknfpiqlSGGEQQRVGIA 149
|
170
....*....|....*.
gi 1002258264 625 IEMVMEPSLLILDEPT 640
Cdd:PRK10908 150 RAVVNKPAVLLADEPT 165
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
470-640 |
1.32e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLTLSLGKKK-LLRSINGE----------LRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykvSGSVLVNGRH 538
Cdd:PRK15134 274 PLLDVE--QLQVAFPIRKgILKRTVDHnvvvknisftLRPGETLGLVGESGSGKSTTGLALLRLINS---QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 DNIRSYKKIIGFVPQDDVVHGN--------LTV----EENLWFSAKcRLSAttAHRHkvltvERVIDSLDLQGVRSslvg 606
Cdd:PRK15134 349 LHNLNRRQLLPVRHRIQVVFQDpnsslnprLNVlqiiEEGLRVHQP-TLSA--AQRE-----QQVIAVMEEVGLDP---- 416
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002258264 607 tvEKR-----GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK15134 417 --ETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
489-639 |
1.37e-06 |
|
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: 51.11 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDN---------IRSYKkiIGFVPQDDVVHG 559
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--PTSGKVLIDGQDIAamsrkelreLRRKK--ISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 NLTVEENLWFSAKCRlSATTAHRHkvltvERVIDSLDLQGvrssLVGTVEK--RGISGGQRKRVNVGIEMVMEPSLLILD 637
Cdd:cd03294 116 HRTVLENVAFGLEVQ-GVPRAERE-----ERAAEALELVG----LEGWEHKypDELSGGMQQRVGLARALAVDPDILLMD 185
|
..
gi 1002258264 638 EP 639
Cdd:cd03294 186 EA 187
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
462-640 |
1.38e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 462 EQQKEITRplLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLvngrhdni 541
Cdd:PRK15064 310 EQDKKLHR--NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE--PDSGTVK-------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 542 RSYKKIIGFVPQDdvvH-----GNLTVEEnlWfsakcrLSATTAHRHkvltvervidslDLQGVRSSLvG-------TVE 609
Cdd:PRK15064 378 WSENANIGYYAQD---HaydfeNDLTLFD--W------MSQWRQEGD------------DEQAVRGTL-GrllfsqdDIK 433
|
170 180 190
....*....|....*....|....*....|...
gi 1002258264 610 K--RGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK15064 434 KsvKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
489-713 |
1.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.14 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNG----RHDNIRSYKKIIGFVPQD-DVVHGNLTV 563
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK--GKVLVSGidtgDFSKLQGIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 564 EENLWFSAKCRLSATTAHRHKVltvERVIDSLDLQGVRSSlvgtvEKRGISGGQRKRVNVGIEMVMEPSLLILDEPTSGL 643
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRV---DRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 644 DSSSSQLLLRALRHEALEGVNVCAVVHQpsytLYNMFD-DLILLAKGGLIVYNGPVKSVEDYFS--TLGITVP 713
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHN----LEELHDaDRIIVMDRGKIVLEGEPENVLSDVSlqTLGLTPP 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
486-639 |
1.61e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 486 KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKVS-GSVLVNgrhdniRSykkiIGFVPQDDVVHgNLTVE 564
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQ---FEISeGRVWAE------RS----IAYVPQQAWIM-NATVR 738
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002258264 565 ENLWFSAKCRlsatTAHRHKVLTVERVidSLDLQGVRSSLVGTVEKRGI--SGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PTZ00243 739 GNILFFDEED----AARLADAVRVSQL--EADLAQLGGGLETEIGEKGVnlSGGQKARVSLARAVYANRDVYLLDDP 809
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
461-640 |
1.87e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.75 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 461 SEQQKEITRPLLkvEFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTgkvAGYKV-SGSVLVNGR 537
Cdd:PRK11160 328 TTSTAAADQVSL--TLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWDPqQGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 hdNIRSY-----KKIIGFVPQDdvVH-GNLTVEENLwfsakcRLSATTAHRHKVLTV-ERV-IDSL--DLQGVRSSL--V 605
Cdd:PRK11160 403 --PIADYseaalRQAISVVSQR--VHlFSATLRDNL------LLAAPNASDEALIEVlQQVgLEKLleDDKGLNAWLgeG 472
|
170 180 190
....*....|....*....|....*....|....*
gi 1002258264 606 GtvekRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11160 473 G----RQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
474-640 |
2.06e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDL--TLSLGKKKL--LRSINGELRPGRVTAVMGPSGAGKTTFLNAV------TgkvagykvSGSVLVNGRH----- 538
Cdd:PRK11153 2 IELKNIskVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerpT--------SGRVLVDGQDltals 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 -DNIRSYKKIIGFVPQddvvHGNL----TVEENLWFSAKcrlsatTAHRHKVLTVERVIDSLDLqgvrsslVGTVEKRG- 612
Cdd:PRK11153 74 eKELRKARRQIGMIFQ----HFNLlssrTVFDNVALPLE------LAGTPKAEIKARVTELLEL-------VGLSDKADr 136
|
170 180 190
....*....|....*....|....*....|..
gi 1002258264 613 ----ISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11153 137 ypaqLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
438-640 |
2.36e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 51.34 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 438 IEKEKVRQQENKNLTFTGVLSMVSEQQK----EITRPLLKV-EFKDLTLSL--GKKKLLRSINGELRPGRVTAVMGPSGA 510
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFMEGVSEVEKecevEVGEPIIKVrNVSKRYISVdrGVVKAVDNVSLEVKEGEIFGIVGTSGA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 511 GKTTFLNAVTGKVAgyKVSGSVLV----------NGRHDNIRSYKKIIGFVPQDDVVHGNLTVEENLWFSAKCRLSATTA 580
Cdd:TIGR03269 322 GKTTLSKIIAGVLE--PTSGEVNVrvgdewvdmtKPGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELA 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 581 HRHKVLTVERVidSLDLQGVRSSLVGTVEKrgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR03269 400 RMKAVITLKMV--GFDEEKAEEILDKYPDE--LSEGERHRVALAQVLIKEPRIVILDEPT 455
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
472-640 |
2.56e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.22 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEFKdltlslGKKKLLRSING----------ELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykvSGSVLVNGR---- 537
Cdd:COG4172 281 LKVWFP------IKRGLFRRTVGhvkavdgvslTLRRGETLGLVGESGSGKSTLGLALLRLIPS---EGEIRFDGQdldg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 --HDNIRSYKKIIGFVPQDDvvHGNL--------TVEENLWFSakcRLSATTAHRHkvltvERVIDSLDLQGvrssLVGT 607
Cdd:COG4172 352 lsRRALRPLRRRMQVVFQDP--FGSLsprmtvgqIIAEGLRVH---GPGLSAAERR-----ARVAEALEEVG----LDPA 417
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002258264 608 VEKRGI---SGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4172 418 ARHRYPhefSGGQRQRIAIARALILEPKLLVLDEPT 453
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
460-640 |
2.91e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 460 VSEQQKEITRPLLkVEFKDLTLSLGKKKLlrSIN-GELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVlvngrH 538
Cdd:COG1245 329 VHAPRREKEEETL-VEYPDLTKSYGGFSL--EVEgGEIREGEVLGIVGPNGIGKTTFAKILAGVLK--PDEGEV-----D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 539 DNIR-SYKkiigfvPQDDVVHGNLTVEENLWFSAKCRLSaTTAHRHKV---LTVERVIDSldlqgvrsslvgtvEKRGIS 614
Cdd:COG1245 399 EDLKiSYK------PQYISPDYDGTVEEFLRSANTDDFG-SSYYKTEIikpLGLEKLLDK--------------NVKDLS 457
|
170 180
....*....|....*....|....*.
gi 1002258264 615 GGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG1245 458 GGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
486-640 |
3.25e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.47 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 486 KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGR--HDNIRSYKKIIGfvpqddVVHGN--- 560
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIL--VPTSGEVRVLGYvpFKRRKEFARRIG------VVFGQrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 561 ----LTVEENL-WFSAKCRLSATTAHRhkvlTVERVIDSLDLQG-----VRS-SLvgtvekrgisgGQRKRVnvgiEMVM 629
Cdd:COG4586 107 lwwdLPAIDSFrLLKAIYRIPDAEYKK----RLDELVELLDLGElldtpVRQlSL-----------GQRMRC----ELAA 167
|
170
....*....|....*
gi 1002258264 630 ----EPSLLILDEPT 640
Cdd:COG4586 168 allhRPKILFLDEPT 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
484-638 |
4.36e-06 |
|
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: 49.07 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKvagYKV-SGSVLVNGRhdnIRSYKKI-IGFvpqddvvHGNL 561
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI---YPPdSGTVTVRGR---VSSLLGLgGGF-------NPEL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002258264 562 TVEENLWFSakCRLS-ATTAHRHKVltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDE 638
Cdd:cd03220 100 TGRENIYLN--GRLLgLSRKEIDEK--IDEIIEFSELGDFIDLPVKT-----YSSGMKARLAFAIATALEPDILLIDE 168
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
487-640 |
4.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.73 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 487 KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG---KVAGYKVSGSVLVNG--RHDNIRSYKKIIGFV---PQDDVVH 558
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVfqfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 559 GnlTVEENLWFSAKcRLSATTAHRHKVLTverviDSLDLQGVRSSLVgtvEKR--GISGGQRKRVNVGIEMVMEPSLLIL 636
Cdd:PRK13643 100 E--TVLKDVAFGPQ-NFGIPKEKAEKIAA-----EKLEMVGLADEFW---EKSpfELSGGQMRRVAIAGILAMEPEVLVL 168
|
....
gi 1002258264 637 DEPT 640
Cdd:PRK13643 169 DEPT 172
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
466-640 |
4.67e-06 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 49.41 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 466 EITRPLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---------NavtgkvagykvSGSVLVNG 536
Cdd:COG4598 3 DTAPPALEVR--DLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLrcinlletpD-----------SGEIRVGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 537 --------RH-----------DNIRSYkkiIGFVPQddvvHGNL----TVEENLwfsakcrlsaTTAHRHkVL------T 587
Cdd:COG4598 70 eeirlkpdRDgelvpadrrqlQRIRTR---LGMVFQ----SFNLwshmTVLENV----------IEAPVH-VLgrpkaeA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002258264 588 VERVIDSLDLqgvrsslVGTVEKRG-----ISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4598 132 IERAEALLAK-------VGLADKRDaypahLSGGQQQRAAIARALAMEPEVMLFDEPT 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
486-689 |
5.78e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 486 KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSgSVLVNGRhdnirsykkiIGFVPQDDVVHgNLTVEE 565
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVVIRGS----------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 566 NLWFSAKCRlsatTAHRHKVLTVERVIDSLDLQGVRSslVGTVEKRG--ISGGQRKRVNVGIEMVMEPSLLILDEPTSGL 643
Cdd:PLN03232 698 NILFGSDFE----SERYWRAIDVTALQHDLDLLPGRD--LTEIGERGvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002258264 644 DSSSSQLLLRALRHEALEGVNVCAVVHQPSYtlYNMFDDLILLAKG 689
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEG 815
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
489-639 |
6.98e-06 |
|
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: 48.48 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKI-------IGFVPQDDVVHgNL 561
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNKNESEPSFEATrsrnrysVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 562 TVEENLWFSakcrlSATTAHRHKVltverVIDSLDLQGVRSSL----VGTVEKRGI--SGGQRKRVNVGIEMVMEPSLLI 635
Cdd:cd03290 94 TVEENITFG-----SPFNKQRYKA-----VTDACSLQPDIDLLpfgdQTEIGERGInlSGGQRQRICVARALYQNTNIVF 163
|
....
gi 1002258264 636 LDEP 639
Cdd:cd03290 164 LDDP 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
473-640 |
7.34e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKKK---LLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHD----NIRSYK 545
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--PTEGDIIINDSHNlkdiNLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGFVPQDDVVHGNlTVEENLWFS--------------------------------AKC----RLSATTAHRHKVLTVE 589
Cdd:PTZ00265 460 SKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrAKCagdlNDMSNTTDSNELIEMR 538
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 590 R---VIDSLDLQGVR----------------SSLVGTVEKRgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PTZ00265 539 KnyqTIKDSEVVDVSkkvlihdfvsalpdkyETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEAT 607
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-571 |
7.48e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.54 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 476 FKDLTLSLGKKKL-----LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvagykV----SGSVLVNGRhdnIRSykk 546
Cdd:COG1134 24 LKELLLRRRRTRReefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG------IleptSGRVEVNGR---VSA--- 91
|
90 100
....*....|....*....|....*....
gi 1002258264 547 II----GFvpqddvvHGNLTVEENLWFSA 571
Cdd:COG1134 92 LLelgaGF-------HPELTGRENIYLNG 113
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
474-640 |
9.36e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNG---RHDNIR-SYKKIIG 549
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGsplKASNIRdTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHGNLTVEENLWFSAKCRLSAT-TAHRHKVLTVERVIDSLDLQGVRSSLvgTVEKRGisGGQRKRVNVGIEMV 628
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTR--PVGDYG--GGQQQLVEIAKALN 157
|
170
....*....|..
gi 1002258264 629 MEPSLLILDEPT 640
Cdd:TIGR02633 158 KQARLLILDEPS 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
474-640 |
9.74e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLnavtGKVAGYKV--SGSVLVNG------RHDNiRSYK 545
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLIAGARKiqQGRVEVLGgdmadaRHRR-AVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KiIGFVPQddvvhG-------NLTVEENLWFSAkcRL---SAttAHRhkvltvERVIDSL----DLQGVRSSLVGTvekr 611
Cdd:NF033858 77 R-IAYMPQ-----GlgknlypTLSVFENLDFFG--RLfgqDA--AER------RRRIDELlratGLAPFADRPAGK---- 136
|
170 180
....*....|....*....|....*....
gi 1002258264 612 gISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:NF033858 137 -LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
489-640 |
1.01e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRHDNIRSykkiigfvPQDDVVHG--------- 559
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG--ALPRTSGYVTLDGHEVVTRS--------PQDGLANGivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 ------NLTVEENLWFSAKCRLSATTAH-RHK--VLTVERVIDSLDLQG-VRSSLVGTvekrgISGGQRKRVNVGIEMVM 629
Cdd:PRK10762 338 rdglvlGMSVKENMSLTALRYFSRAGGSlKHAdeQQAVSDFIRLFNIKTpSMEQAIGL-----LSGGNQQKVAIARGLMT 412
|
170
....*....|.
gi 1002258264 630 EPSLLILDEPT 640
Cdd:PRK10762 413 RPKVLILDEPT 423
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
484-638 |
1.05e-05 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 48.26 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAGYKVS--GSVLVNGRHDNIRSYKKIIGFVPQD--DVV 557
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGleKPAQGTVSfrGQDLYQLDRKQRRAFRRDVQLVFQDspSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 558 HGNLTVEENLWFSAKCRLSATTAHRHkvltvERVIDSLDLQGVRSSLVGTVeKRGISGGQRKRVNVGIEMVMEPSLLILD 637
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRHLTSLDESEQK-----ARIAELLDMVGLRSEDADKL-PRQLSGGQLQRINIARALAVKPKLIVLD 175
|
.
gi 1002258264 638 E 638
Cdd:TIGR02769 176 E 176
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
503-640 |
1.08e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.57 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 503 AVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNGR---HDNIRSYKKIIGFVPQD-DVVHGNLTVEENLWFSAKcrlSAT 578
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEAE--SGQIIIDGDlltEENVWDIRHKIGMVFQNpDNQFVGATVEDDVAFGLE---NKG 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002258264 579 TAHRhkvLTVERVIDSLDLQGVrsSLVGTVEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK13650 112 IPHE---EMKERVNEALELVGM--QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
472-640 |
1.31e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEFKDLTLSLGK-----KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNG-------RHD 539
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK--PTTGTVTVDDitithktKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 540 NIRSYKKIIGFV---PQDDVVHGNltVEENLWFSAK---CRLSATTAHRHKVLtvervidsLDLQGVRSslVGTVEKRGI 613
Cdd:PRK13646 79 YIRPVRKRIGMVfqfPESQLFEDT--VEREIIFGPKnfkMNLDEVKNYAHRLL--------MDLGFSRD--VMSQSPFQM 146
|
170 180
....*....|....*....|....*..
gi 1002258264 614 SGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
478-713 |
1.54e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.08 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 478 DLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNGRHDN-----IRSYKKIIGFVP 552
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK--GAVLWQGKPLDyskrgLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 553 QDDVVHGNLT-VEENLWFSAKcrlSATTAHRHKVLTVERVIDSLDLQGVRSSLVgtvekRGISGGQRKRVNVGIEMVMEP 631
Cdd:PRK13638 84 QDPEQQIFYTdIDSDIAFSLR---NLGVPEAEITRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 632 SLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQPSYtLYNMFDDLILLAKGGLIVYNGP--VKSVEDYFSTLG 709
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAPgeVFACTEAMEQAG 234
|
....
gi 1002258264 710 ITVP 713
Cdd:PRK13638 235 LTQP 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
474-640 |
1.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSING---ELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNGRH---DNIRSYKKI 547
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGvsfSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFE--GKVKIDGELltaENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 548 IGFVPQD-DVVHGNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQgvrsslvgTVEKRGISGGQRKRVNVGIE 626
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK--------TREPARLSGGQKQRVAVAGI 154
|
170
....*....|....
gi 1002258264 627 MVMEPSLLILDEPT 640
Cdd:PRK13642 155 IALRPEIIILDEST 168
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
485-703 |
1.75e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.90 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 485 KKKLLRSINGELRPGRVTAVMGPSGAGKTTFL---NAV----TGK--VAGYKVSgsvlVNGRHDNIRSYKKIIGFVPQ-- 553
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALlkpsSGTitIAGYHIT----PETGNKNLKKLRKKVSLVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 ----------DDVVHGNLtveeNLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQgvrsslvgtvekrgISGGQRKRVNV 623
Cdd:PRK13641 95 eaqlfentvlKDVEFGPK----NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFE--------------LSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 624 GIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHqpsytlyNM------FDDLILLAKGGLIVYNGP 697
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH-------NMddvaeyADDVLVLEHGKLIKHASP 229
|
....*.
gi 1002258264 698 VKSVED 703
Cdd:PRK13641 230 KEIFSD 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
489-640 |
1.94e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykvSGSVLVNGRhdNIRSYK-----KIIGFVPQDDVVHGNLTV 563
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQ--PLEAWSaaelaRHRAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 564 EENLWFS--AKCRLSATTAhrhkvlTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVN-VGIEMVMEPS------LL 634
Cdd:PRK03695 87 FQYLTLHqpDKTRTEAVAS------ALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRlAAVVLQVWPDinpagqLL 155
|
....*.
gi 1002258264 635 ILDEPT 640
Cdd:PRK03695 156 LLDEPM 161
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
452-521 |
2.07e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 48.65 E-value: 2.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002258264 452 TFTGVLSMVSEQQKEITRPLLK----VEFKDLTLSL-GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG 521
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSedgaLALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
474-639 |
2.63e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGK-VAGYkvSGSVLVNGRH----DNIRSYKKII 548
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGY--SNDLTLFGRRrgsgETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDdvVHGNLTVeenlwfSAKCR---LSA---------TTAHRHKVLTVERvidsLDLQGVrSSLVGTVEKRGISGG 616
Cdd:PRK10938 339 GYVSSS--LHLDYRV------STSVRnviLSGffdsigiyqAVSDRQQKLAQQW----LDILGI-DKRTADAPFHSLSWG 405
|
170 180
....*....|....*....|...
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEP 428
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
489-639 |
2.75e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVagYKVSGSVLVNGRHDNIRSYKKIIGFVPQDDVVHGN--LTVEEN 566
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV--RLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSfpVLVEDV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002258264 567 LW---FSAKCRLSATTAHRHKVltVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK15056 101 VMmgrYGHMGWLRRAKKRDRQI--VTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
468-640 |
2.83e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 47.32 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR---HDNIRSY 544
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--PEAGTITVGGMvlsEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 545 KKIIGFVPQ--DDVVHGNlTVEENLWFSakcrLSATTAHRHKVltVERVIDSLDLQGVRSSLvgTVEKRGISGGQRKRVN 622
Cdd:PRK13635 80 RRQVGMVFQnpDNQFVGA-TVQDDVAFG----LENIGVPREEM--VERVDQALRQVGMEDFL--NREPHRLSGGQKQRVA 150
|
170
....*....|....*...
gi 1002258264 623 VGIEMVMEPSLLILDEPT 640
Cdd:PRK13635 151 IAGVLALQPDIIILDEAT 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
368-640 |
2.91e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 368 QEAPLFMNQELSDSAAFSAHQSTGEISEVMPSVVVDVSDDGeiVAGKDRSApKGKHRSTHTQIFKYAYGEIEKEKVRQQE 447
Cdd:PTZ00265 1074 QSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGS--YAGKLMSL-KGDSENAKLSFEKYYPLIIRKSNIDVRD 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 448 -------NKNLtFTGVLSMVSEQQKEITRPLLKVeFKDLTLSLGKKKllrsingelrpgrVTAVMGPSGAGKTTFL---- 516
Cdd:PTZ00265 1151 nggirikNKND-IKGKIEIMDVNFRYISRPNVPI-YKDLTFSCDSKK-------------TTAIVGETGSGKSTVMsllm 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 517 --------------NAVTGKVAG----------------------------------YKVSGSVLVNGRH---DNIRSYK 545
Cdd:PTZ00265 1216 rfydlkndhhivfkNEHTNDMTNeqdyqgdeeqnvgmknvnefsltkeggsgedstvFKNSGKILLDGVDicdYNLKDLR 1295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGFVPQDDVVHgNLTVEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQgvRSSLVGTVEKrGISGGQRKRVNVGI 625
Cdd:PTZ00265 1296 NLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNK--YDTNVGPYGK-SLSGGQKQRIAIAR 1371
|
330
....*....|....*
gi 1002258264 626 EMVMEPSLLILDEPT 640
Cdd:PTZ00265 1372 ALLREPKILLLDEAT 1386
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
485-640 |
4.02e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 485 KKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGyKVSGSVLVNGRHDNIRSYKKI----IGFVPQDDVVHG- 559
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG-RWEGEIFIDGKPVKIRNPQQAiaqgIAMVPEDRKRDGi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 --NLTVEENLWFSAKCRLSATTA--HRHKVLTVERVIDSLDlqgVRSSlvgTVEKR--GISGGQRKRVNVGIEMVMEPSL 633
Cdd:PRK13549 353 vpVMGVGKNITLAALDRFTGGSRidDAAELKTILESIQRLK---VKTA---SPELAiaRLSGGNQQKAVLAKCLLLNPKI 426
|
....*..
gi 1002258264 634 LILDEPT 640
Cdd:PRK13549 427 LILDEPT 433
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
486-716 |
5.22e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 486 KKLLRSINGELRPGRVTAVMGPSGAGKTTF---LNAV----TGKVagyKVSGSVLVNG-RHDNIRSYKKIIGFVPQddvv 557
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhLNGLlqptSGTV---TIGERVITAGkKNKKLKPLRKKVGIVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 558 hgnltVEENLWFSAkcrlsattahrhkvlTVERVI------------DSLDLQGVRSSLVGTVEK---RG---ISGGQRK 619
Cdd:PRK13634 93 -----FPEHQLFEE---------------TVEKDIcfgpmnfgvseeDAKQKAREMIELVGLPEEllaRSpfeLSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 620 RVNVGIEMVMEPSLLILDEPTsgldssssQLLLRALRHEALE---------GVNVCAVVHQ----PSYTlynmfDDLILL 686
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPT--------AGLDPKGRKEMMEmfyklhkekGLTTVLVTHSmedaARYA-----DQIVVM 219
|
250 260 270
....*....|....*....|....*....|..
gi 1002258264 687 AKGGLIVYNGP--VKSVEDYFSTLGITVPERV 716
Cdd:PRK13634 220 HKGTVFLQGTPreIFADPDELEAIGLDLPETV 251
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
489-639 |
5.51e-05 |
|
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: 47.63 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRhdnirsykkiIGFVPQDDVVHgNLTVEENLW 568
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD--KVEGHVHMKGS----------VAYVPQQAWIQ-NDSLRENIL 720
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 569 FSakcrlSATTAHRHKVlTVERVIDSLDLQGVRSSLVGTVEKRGI--SGGQRKRVNVGIEMVMEPSLLILDEP 639
Cdd:TIGR00957 721 FG-----KALNEKYYQQ-VLEACALLPDLEILPSGDRTEIGEKGVnlSGGQKQRVSLARAVYSNADIYLFDDP 787
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
470-640 |
6.50e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.26 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLT--------LSLGKKKLLRSING---ELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGR- 537
Cdd:COG4608 6 PLLEVR--DLKkhfpvrggLFGRTVGVVKAVDGvsfDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PTSGEILFDGQd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 -----HDNIRSYKKIIGFVPQD--DVVHGNLTVEENLwfSAKCRLsattahrHKVLTV----ERVIDSLDLQGVRSSLVG 606
Cdd:COG4608 82 itglsGRELRPLRRRMQMVFQDpyASLNPRMTVGDII--AEPLRI-------HGLASKaerrERVAELLELVGLRPEHAD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002258264 607 tvekR---GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:COG4608 153 ----RyphEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
464-640 |
6.54e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 464 QKEITRPLLKVEfkDLTlslGKKklLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRS 543
Cdd:PRK15439 261 QQAAGAPVLTVE--DLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP--ARGGRIMLNGKEINALS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 YKKII--GFV--PQDDVVHG------------NLTVEENLWFSAKCRLSATTAHRHKVLTVErvIDSLDlQGVrsslvgt 607
Cdd:PRK15439 332 TAQRLarGLVylPEDRQSSGlyldaplawnvcALTHNRRGFWIKPARENAVLERYRRALNIK--FNHAE-QAA------- 401
|
170 180 190
....*....|....*....|....*....|...
gi 1002258264 608 vekRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK15439 402 ---RTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
483-640 |
7.74e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 483 LGKKKLLRSING---ELRPGRVTAVMGPSGAGKTTFLNAVTgkVAGYKVSGSVLVNGR------HDNIRSYKKIIGFVPQ 553
Cdd:PRK11308 22 FKPERLVKALDGvsfTLERGKTLAVVGESGCGKSTLARLLT--MIETPTGGELYYQGQdllkadPEAQKLLRQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DDvvHGNL--------TVEENLWFSAKcrLSAttAHRhkvltVERVIDSLDLQGVRSslvgtvEKRG-----ISGGQRKR 620
Cdd:PRK11308 100 NP--YGSLnprkkvgqILEEPLLINTS--LSA--AER-----REKALAMMAKVGLRP------EHYDryphmFSGGQRQR 162
|
170 180
....*....|....*....|
gi 1002258264 621 VNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPV 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
487-640 |
7.92e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 487 KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKI----IGFVPQDDVVHGNLT 562
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ--KDSGSILFQGKEIDFKSSKEAlengISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002258264 563 VEENLWFSAKCRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
463-640 |
1.06e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 463 QQKEITRPLLKVefKDLTLSL----GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGY-KVSGSVLVNGR 537
Cdd:PRK09473 4 LAQQQADALLDV--KDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgRIGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 H---------DNIRSYKkiIGFVPQDDVVHGN--LTVEENLW--FSAKCRLSATTAHRHKVltveRVIDSLDLQGVRSSL 604
Cdd:PRK09473 82 EilnlpekelNKLRAEQ--ISMIFQDPMTSLNpyMRVGEQLMevLMLHKGMSKAEAFEESV----RMLDAVKMPEARKRM 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002258264 605 vgTVEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK09473 156 --KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
461-713 |
1.31e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 461 SEQQKEITRPLLK---VEFKDLTLSLGKK-----KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGK---------- 522
Cdd:PRK13631 6 MKKKLKVPNPLSDdiiLRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 523 ---VAGYKVSGSVLVNGRHD----NIRSYKKIIGFV---PQDDVVHGnlTVEENLWFSAkcrlsaTTAHRHKVLTVERVI 592
Cdd:PRK13631 86 gdiYIGDKKNNHELITNPYSkkikNFKELRRRVSMVfqfPEYQLFKD--TIEKDIMFGP------VALGVKKSEAKKLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 593 DSLDLQGVRSSLVgTVEKRGISGGQRKRVNVGIEMVMEPSLLILDEPTSGLDSSSSQLLLRALRHEALEGVNVCAVVHQP 672
Cdd:PRK13631 158 FYLNKMGLDDSYL-ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1002258264 673 SYTLyNMFDDLILLAKGGLIVYNGP--VKSVEDYFSTLGITVP 713
Cdd:PRK13631 237 EHVL-EVADEVIVMDKGKILKTGTPyeIFTDQHIINSTSIQVP 278
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
465-638 |
1.37e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.41 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 465 KEITRPLLKVEFKDLT-LSLGKKKLLRSIngelRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKvsGSVLVNG------R 537
Cdd:PRK10070 23 KYIEQGLSKEQILEKTgLSLGVKDASLAI----EEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR--GQVLIDGvdiakiS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 HDNIRSYK-KIIGFVPQDDVVHGNLTVEENLWFSAKcrLSATTAHRHKvltvERVIDSLDLQGVRSSLVGTVEKrgISGG 616
Cdd:PRK10070 97 DAELREVRrKKIAMVFQSFALMPHMTVLDNTAFGME--LAGINAEERR----EKALDALRQVGLENYAHSYPDE--LSGG 168
|
170 180
....*....|....*....|..
gi 1002258264 617 QRKRVNVGIEMVMEPSLLILDE 638
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDE 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
487-722 |
1.42e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.00 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 487 KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKV---AGYKVSGSVLVNGRHDNIRSYKKI---IGFV---PQDDVV 557
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiseTGQTIVGDYAIPANLKKIKEVKRLrkeIGLVfqfPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 558 HGnlTVEENLWFsAKCRLSATTAHRHKvltveRVIDSLDLqgvrSSLVGTVEKRG---ISGGQRKRVNVGIEMVMEPSLL 634
Cdd:PRK13645 105 QE--TIEKDIAF-GPVNLGENKQEAYK-----KVPELLKL----VQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 635 ILDEPTSGLDSSSSQL-LLRALRHEALEGVNVCAVVHQPSYTLyNMFDDLILLAKGGLIVYNGPVksveDYFSTLGITVP 713
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDfINLFERLNKEYKKRIIMVTHNMDQVL-RIADEVIVMHEGKVISIGSPF----EIFSNQELLTK 247
|
....*....
gi 1002258264 714 ERVNPPDHY 722
Cdd:PRK13645 248 IEIDPPKLY 256
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
463-558 |
1.64e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 463 QQKEITRPL--LKVEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDN 540
Cdd:TIGR00630 596 GRKKIEVPAerRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTS 675
|
90
....*....|....*...
gi 1002258264 541 IRSYKKIigfvpqDDVVH 558
Cdd:TIGR00630 676 IEGLEHL------DKVIH 687
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
484-638 |
2.21e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.29 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG--KVAGYKVS--GSVLVNGRHDNIRSYKKIIGFVPQDDV--V 557
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGleSPSQGNVSwrGEPLAKLNRAQRKAFRRDIQMVFQDSIsaV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 558 HGNLTVEENLWFSAKCRLSATTAHRhkvltVERVIDSLDLQGVRSSLVgtvEKR--GISGGQRKRVNVGIEMVMEPSLLI 635
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSLDKAER-----LARASEMLRAVDLDDSVL---DKRppQLSGGQLQRVCLARALAVEPKLLI 174
|
...
gi 1002258264 636 LDE 638
Cdd:PRK10419 175 LDE 177
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
472-639 |
2.21e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.70 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 472 LKVEFK---DLTLSLGKKKLLRSING---ELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGykVSGSVLVNGR------HD 539
Cdd:PRK15079 14 LKVHFDikdGKQWFWQPPKTLKAVDGvtlRLYEGETLGVVGESGCGKSTFARAIIGLVKA--TDGEVAWLGKdllgmkDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 540 NIRSYKKIIGFVPQDDVVHGN--LTVEENLwfsAKcRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTVEKRgISGGQ 617
Cdd:PRK15079 92 EWRAVRSDIQMIFQDPLASLNprMTIGEII---AE-PLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHE-FSGGQ 166
|
170 180
....*....|....*....|..
gi 1002258264 618 RKRVNVGIEMVMEPSLLILDEP 639
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEP 188
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
492-596 |
2.53e-04 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 43.75 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 492 INGELRPGRVTAVMGPSGAGKTTFLN--AVTGKVAGYKVsgsVLV--NGRHDNIRSYKKIIGFVPQDDVVHGNLTVeenL 567
Cdd:COG0467 13 LGGGLPRGSSTLLSGPPGTGKTTLALqfLAEGLRRGEKG---LYVsfEESPEQLLRRAESLGLDLEEYIESGLLRI---I 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 1002258264 568 WFSAKCRLSATTAHRHKVLT-VER------VIDSLD 596
Cdd:COG0467 87 DLSPEELGLDLEELLARLREaVEEfgakrvVIDSLS 122
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
474-640 |
3.91e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNgrhDNIRsykkiIGFVPQ 553
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD--SGTIKIG---ETVK-----LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 554 DdvvHGNLTVEENLWfsakcrlsattahrhkvltvERVIDSLDLqgvrsSLVGTVE-------------------KRGI- 613
Cdd:PRK11819 395 S---RDALDPNKTVW--------------------EEISGGLDI-----IKVGNREipsrayvgrfnfkggdqqkKVGVl 446
|
170 180
....*....|....*....|....*..
gi 1002258264 614 SGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
495-522 |
4.02e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.77 E-value: 4.02e-04
10 20 30
....*....|....*....|....*....|.
gi 1002258264 495 ELRP---GRVTAVMGPSGAGKTTFLNAVTGK 522
Cdd:cd01854 78 ELREllkGKTSVLVGQSGVGKSTLLNALLPE 108
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
487-640 |
5.14e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 487 KLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKIIG-----------FVPqdd 555
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQ--PDAGSILIDGQEMRFASTTAALAagvaiiyqelhLVP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 556 vvhgNLTVEENLWFSakcRLSATTAHRHKVLTVERVIDSLDLQGVRSSLVGTVekRGISGGQRKRVNVGIEMVMEPSLLI 635
Cdd:PRK11288 93 ----EMTVAENLYLG---QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPL--KYLSIGQRQMVEIAKALARNARVIA 163
|
....*
gi 1002258264 636 LDEPT 640
Cdd:PRK11288 164 FDEPT 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
473-639 |
5.51e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLS-LGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVtgkvAGYKV--SGSVLVNGRHDNIRSYK-KII 548
Cdd:PRK11650 3 GLKLQAVRKSyDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV----AGLERitSGEIWIGGRVVNELEPAdRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 549 GFVPQDDVVHGNLTVEENLWFSAKCR--LSATTAHRhkvltVERVIDSLDLQGV--RsslvgtvEKRGISGGQRKRVNVG 624
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKIRgmPKAEIEER-----VAEAARILELEPLldR-------KPRELSGGQRQRVAMG 146
|
170
....*....|....*
gi 1002258264 625 IEMVMEPSLLILDEP 639
Cdd:PRK11650 147 RAIVREPAVFLFDEP 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
559-640 |
5.74e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 559 GNLTVEENLWFSAkcRL----SATTAHRhkvltVERVIDSLDLQGVRSSLVGtvekrGISGGQRKRVNVGIEMVMEPSLL 634
Cdd:NF033858 352 GELTVRQNLELHA--RLfhlpAAEIAAR-----VAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELL 419
|
....*.
gi 1002258264 635 ILDEPT 640
Cdd:NF033858 420 ILDEPT 425
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
495-538 |
7.88e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 41.37 E-value: 7.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1002258264 495 ELRP---GRVTAVMGPSGAGKTTFLNAVTG----KVAGykVSGSvLVNGRH 538
Cdd:pfam03193 99 ALKEllkGKTTVLAGQSGVGKSTLLNALLPeldlRTGE--ISEK-LGRGRH 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
484-640 |
1.02e-03 |
|
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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 484 GKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYkvSGSVLVNgrhDNIRsykkiIGFVPQDDVVHGNLTV 563
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDF--NGEARPQ---PGIK-----VGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 564 EENLW---------------FSAKcrLSATTAHRHKVLT----VERVIDSLDLQGVRSSLV------------GTVEKrg 612
Cdd:TIGR03719 86 RENVEegvaeikdaldrfneISAK--YAEPDADFDKLAAeqaeLQEIIDAADAWDLDSQLEiamdalrcppwdADVTK-- 161
|
170 180
....*....|....*....|....*...
gi 1002258264 613 ISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
474-521 |
1.03e-03 |
|
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: 40.99 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002258264 474 VEFKDLTLSLGK-KKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTG 521
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
470-704 |
2.05e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 470 PLLKVEfkDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVlvnGRHDNIRsykkiIG 549
Cdd:PRK10636 311 PLLKME--KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA--PVSGEI---GLAKGIK-----LG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 550 FVPQDDVVHgnLTVEEnlwfsakcrlsatTAHRHKVLTVERVIDsldlQGVRSSLVG--------TVEKRGISGGQRKRV 621
Cdd:PRK10636 379 YFAQHQLEF--LRADE-------------SPLQHLARLAPQELE----QKLRDYLGGfgfqgdkvTEETRRFSGGEKARL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 622 NVGIEMVMEPSLLILDEPTSGLDSSSSQLLLralrhEAL---EGVNVcaVVHQPSYTLYNMFDDLILLAKGGLIVYNGpv 698
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALT-----EALidfEGALV--VVSHDRHLLRSTTDDLYLVHDGKVEPFDG-- 510
|
....*.
gi 1002258264 699 kSVEDY 704
Cdd:PRK10636 511 -DLEDY 515
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
499-640 |
2.14e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 41.28 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 499 GRVTAVMGPSGAGKTTFLNAVTGkVAGYKvSGSVLVNGR---HDNIRSYKKIIGFV---PQDDVVHGnlTVEENLWFSAK 572
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIG-IEKVK-SGEIFYNNQaitDDNFEKLRKHIGIVfqnPDNQFVGS--IVKYDVAFGLE 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002258264 573 crlSATTAHRHKVLTVERVIDSLDLQGVRSSlvgtvEKRGISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK13648 111 ---NHAVPYDEMHRRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
498-640 |
3.21e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 498 PGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRHDNIRSYKKI----IGFVPQDDVVHGNLTVEENLwFSAKC 573
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYT--RDAGSILYLGKEVTFNGPKSSqeagIGIIHQELNLIPQLTIAENI-FLGRE 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002258264 574 RLSATTAHRHKVLTVE--RVIDSLDLQGVRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK10762 106 FVNRFGRIDWKKMYAEadKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
468-640 |
4.28e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 468 TRPLLKVEfkDLTLSLGKKKLLRSINGEL----RPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKV---SGSVLVNGR--- 537
Cdd:PRK15134 2 TQPLLAIE--NLSVAFRQQQTVRTVVNDVslqiEAGETLALVGESGSGKSVTALSILRLLPSPPVvypSGDIRFHGEsll 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 538 HDNIRSYKKI----IGFVPQDDVVHGN--LTVEENLWFSakcrLSATTAHRHKVLTVErVIDSLDLQGVRSSlvgtvEKR 611
Cdd:PRK15134 80 HASEQTLRGVrgnkIAMIFQEPMVSLNplHTLEKQLYEV----LSLHRGMRREAARGE-ILNCLDRVGIRQA-----AKR 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1002258264 612 ------GISGGQRKRVNVGIEMVMEPSLLILDEPT 640
Cdd:PRK15134 150 ltdyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
498-550 |
4.32e-03 |
|
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: 38.89 E-value: 4.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 498 PGRVTAVMGPSGAGKTTFLNAVTGKvAGYKVSGSVLVNGRHDNIRSYKKIIGF 550
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-LGPPGGGVIYIDGEDILEEVLDQLLLI 52
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
481-639 |
4.38e-03 |
|
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: 40.23 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 481 LSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAgyKVSGSVLVNGRhdnirsykkiIGFVPQDD-VVHG 559
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELE--PSEGKIKHSGR----------ISFSSQFSwIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 560 nlTVEENLWFSAkcrlsATTAHRHKvltveRVIDSLDLQGVRSSLV---GTVEKRG---ISGGQRKRVNVGIEMVMEPSL 633
Cdd:cd03291 113 --TIKENIIFGV-----SYDEYRYK-----SVVKACQLEEDITKFPekdNTVLGEGgitLSGGQRARISLARAVYKDADL 180
|
....*.
gi 1002258264 634 LILDEP 639
Cdd:cd03291 181 YLLDSP 186
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
497-519 |
4.93e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 39.41 E-value: 4.93e-03
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-640 |
5.53e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 474 VEFKDLTLSLGKKKLLRSINGELRPGRVTAVMGPSGAGKTTflNAVTGKVAGYKVsgsvlvnGRHD--------NIRSYK 545
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R--GALPAHV*GPDA-------GRRPwrf*twcaNRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 546 KIIGF-VPQDDVVHGNLTVEENLWFSAKC-RLSATTAHRHKVLTVERVidSLDLQGVRSSlvgtvekRGISGGQRKRVNV 623
Cdd:NF000106 85 RTIG*hRPVR*GRRESFSGRENLYMIGR*lDLSRKDARARADELLERF--SLTEAAGRAA-------AKYSGGMRRRLDL 155
|
170
....*....|....*..
gi 1002258264 624 GIEMVMEPSLLILDEPT 640
Cdd:NF000106 156 AASMIGRPAVLYLDEPT 172
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
489-548 |
5.73e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 5.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGKVAGYKVSGSVLVNGRHDNIRSYK---KII 548
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEhldKVI 687
|
|
| RhaT |
COG0697 |
Permease of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and ... |
829-985 |
6.23e-03 |
|
Permease of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism, Amino acid transport and metabolism, General function prediction only];
Pssm-ID: 440461 [Multi-domain] Cd Length: 290 Bit Score: 39.83 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 829 KQRLREARLLAVdflILGLAGICLGTIAKLSDPNFGMPGYIYTIIAVslLCkiAALRSFSLERLqylRERESGMSSLAYF 908
Cdd:COG0697 115 GERLSRRRWLGL---LLGFAGVLLIVGPGGGGGGGSLLGDLLALLAA--LS--WALYTVLTRRL---SRRLDPLTLTFWQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 909 LArdtidhFSTIVkpivYLSMFYYFNNPRSTITDNYIILLALVYCVTGIGYTF---AICF-NPGSAQLCSALIPVVLTLL 984
Cdd:COG0697 185 ML------VGALL----LLPLALLTGLPLPLSAAAWLALLYLGLFGTALAYLLwfrALRRlGASRAAPLTYLEPVFAVLL 254
|
.
gi 1002258264 985 S 985
Cdd:COG0697 255 G 255
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
489-640 |
6.32e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 489 LRSINGELRPGRVTAVMGPSGAGKTTFLNAVTGkvAGYKVSGSVLVNGRHDNIRSYKKII--GFV-----PQDDVVHGNL 561
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG--IREKSAGTITLHGKKINNHNANEAInhGFAlvteeRRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 562 TVEENLWFSA----KCRLSATTAHRHKVLTvERVIDSLDLQG-VRSSLVGTvekrgISGGQRKRVNVGIEMVMEPSLLIL 636
Cdd:PRK10982 342 DIGFNSLISNirnyKNKVGLLDNSRMKSDT-QWVIDSMRVKTpGHRTQIGS-----LSGGNQQKVIIGRWLLTQPEILML 415
|
....
gi 1002258264 637 DEPT 640
Cdd:PRK10982 416 DEPT 419
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
473-640 |
8.09e-03 |
|
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: 38.93 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 473 KVEFKDLTLSLGKK--KLLRSINGELRPGRVTAVMGPSGAGKTT-------FLNAVTGKVagyKVSGsvlVNGRHDNIRS 543
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTlilalfrFLEAEEGKI---EIDG---IDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258264 544 YKKIIGFVPQDDVVhgnltveenlwFSAKCRlsaTTAHRHKVLTVERVIDSLDLQGVRSSLvgtvekrgiSGGQRKRVNV 623
Cdd:cd03369 80 LRSSLTIIPQDPTL-----------FSGTIR---SNLDPFDEYSDEEIYGALRVSEGGLNL---------SQGQRQLLCL 136
|
170
....*....|....*..
gi 1002258264 624 GIEMVMEPSLLILDEPT 640
Cdd:cd03369 137 ARALLKRPRVLVLDEAT 153
|
|
| |
