|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
57-663 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 774.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 57 LTEAQRFSSLPRRAAVNIEfRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM 136
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 137 KGA--VLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEK--DEGRREMVKEILTALGLLSCANTRTG 212
Cdd:TIGR00955 80 KGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 213 ------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYV 286
Cdd:TIGR00955 160 vpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 287 LSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSrlVRAVREGMCDSDHKRDLGGDAEVNPFLWH 366
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENE--SRERIEKICDSFAVSDIGRDMLVNTNLWS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 367 RPS---EEDSSSMEGCHsFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFL 443
Cdd:TIGR00955 318 GKAgglVKDSENMEGIG-YNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 444 FFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFA 523
Cdd:TIGR00955 397 FLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 524 ALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDR 603
Cdd:TIGR00955 477 FLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVD 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 604 --EDLHCDIDETCHFQKsEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER 663
Cdd:TIGR00955 557 niECTSANTTGPCPSSG-EVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
71-296 |
3.58e-101 |
|
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: 306.79 E-value: 3.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 71 AVNIEFRDLSYSVPEGPWwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET-GMKGAVLINGLPRDL 149
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPS---KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqekdegrremvkeiltalgllscantrtgSLSGGQRKRLAIALELV 229
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 230 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
95-656 |
3.56e-78 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 262.12 E-value: 3.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLPRDLRCFRKVScYIMQDDMLLPHLTVQE 173
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSAHLKLQE---KDEGRReMVKEILTALGLLSCANTRTGS-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PLN03211 160 TLVFCSLLRLPKsltKQEKIL-VAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 246 SASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEV 325
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 326 ASGE------------------YGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSeeDSSSMegchsfsASCL 387
Cdd:PLN03211 319 ANGVcqtdgvserekpnvkqslVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSS--DRISI-------STWF 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 388 TQFCILFKRTfLSIMRDSVLTHLRITShiGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMG 467
Cdd:PLN03211 390 NQFSILLQRS-LKERKHESFNTLRVFQ--VIAAALLAGLMWWHSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERA 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 468 VFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSL 547
Cdd:PLN03211 467 IFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDA 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 548 QVATFVGPVTAIPVLLFSGFFVsfDTIPTYLQWMSYISYVRYGFEGVILSIYGLDRED---LHCDIDE-----TCHFQKS 619
Cdd:PLN03211 547 KKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRIsslLGCSLPHgsdraSCKFVEE 624
|
570 580 590
....*....|....*....|....*....|....*..
gi 46592978 620 EAIlreldvENAKLYLDFIVLGIFFISLRLIAYFVLR 656
Cdd:PLN03211 625 DVA------GQISPATSVSVLIFMFVGYRLLAYLALR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
75-614 |
1.57e-70 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 249.64 E-value: 1.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM--KGAVLINGLPRDlRCF 152
Cdd:TIGR00956 761 HWRNLTYEVK-----IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 153 RKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEK--DEGRREMVKEILTALGLLSCANTRTG----SLSGGQRKRLAIAL 226
Cdd:TIGR00956 835 QRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSvsKSEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 227 ELVNNPP-VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQG-QCVY---RGKVCN- 300
Cdd:TIGR00956 915 ELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYfgdLGENSHt 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 301 LVPYLRDLGL-NCPTYHNPADFVMEV---ASGEYGDQ-------NSRLVRAVREgmcdsdhkrdlggdaEVNPFLWHRPS 369
Cdd:TIGR00956 995 IINYFEKHGApKCPEDANPAEWMLEVigaAPGAHANQdyhevwrNSSEYQAVKN---------------ELDRLEAELSK 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 370 EEDSSSMEGCHSFSASCLTQFCILFKRTFLSIMR--DSVLTHLRITshigiglligllylgigneakkvLSNS---GFLF 444
Cdd:TIGR00956 1060 AEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRtpDYLYSKFFLT-----------------------IFAAlfiGFTF 1116
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 445 F----SMLFL---MFAALMPTVLTFPLEMG-----------VFLREHLNYWYSLKAYYLAKTMADVPFQIMF-PVAYCSI 505
Cdd:TIGR00956 1117 FkvgtSLQGLqnqMFAVFMATVLFNPLIQQylppfvaqrdlYEVRERPSRTFSWLAFIAAQITVEIPYNLVAgTIFFFIW 1196
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 506 VYWM----TSQPSDAV--RFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQ 579
Cdd:TIGR00956 1197 YYPVgfywNASKTGQVheRGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWI 1276
|
570 580 590
....*....|....*....|....*....|....*
gi 46592978 580 WMSYISYVRYGFEGVILSIYGldredlhcDIDETC 614
Cdd:TIGR00956 1277 FMYRCSPFTYLVQALLSTGLA--------DVPVTC 1303
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
86-296 |
3.57e-66 |
|
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: 216.75 E-value: 3.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 86 GPWWR-------KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMK-GAVLINGLPRDLRCFRKVS 156
Cdd:cd03234 4 LPWWDvglkaknWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTsGQILFNGQPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 157 CYIMQDDMLLPHLTVQEAMMVSAHLKLQE-KDEGRREMVKEI--LTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPP 233
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRkSSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 234 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
74-296 |
2.41e-65 |
|
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: 213.26 E-value: 2.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETG-MKGAVLINGLPRDlRCF 152
Cdd:cd03232 4 LTWKNLNYTVPV-----KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 153 RKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqekdegrremvkeiltalgllscantrtgSLSGGQRKRLAIALELVNNP 232
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFSALLR------------------------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQ-GQCVYRG 296
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-605 |
2.24e-58 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 213.55 E-value: 2.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 8 PHGTNASSYSAEMTEPKSVCvSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQrfSSLPRRAAV------NIEFRDLSY 81
Cdd:PLN03140 799 SEETAEEMEGEEDSIPRSLS-SADGNNTREVAIQRMSNPEGLSKNRDSSLEAAN--GVAPKRGMVlpftplAMSFDDVNY 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 82 SVPEGPWWRKKGYK----TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETG--MKGAVLINGLPRDLRCFRKV 155
Cdd:PLN03140 876 FVDMPAEMKEQGVTedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGgyIEGDIRISGFPKKQETFARI 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 156 SCYIMQDDMLLPHLTVQEAMMVSAHLKLqEKDEGRRE---MVKEILTALGLLSCANTRTG-----SLSGGQRKRLAIALE 227
Cdd:PLN03140 955 SGYCEQNDIHSPQVTVRESLIYSAFLRL-PKEVSKEEkmmFVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVE 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 228 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQ-GQCVYRGKV----CNLV 302
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKII 1113
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 303 PYLRDL-GL-NCPTYHNPADFVMEVASgeygdqnsrLVRAVREGM-------CDSDHKRDlggDAEVNPFLWHRPSEEDs 373
Cdd:PLN03140 1114 EYFEAIpGVpKIKEKYNPATWMLEVSS---------LAAEVKLGIdfaehykSSSLYQRN---KALVKELSTPPPGASD- 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 374 ssMEGCHSFSASCLTQFCILFKRTFLSIMR--DSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNS-GFLFFSMLFL 450
Cdd:PLN03140 1181 --LYFATQYSQSTWGQFKSCLWKQWWTYWRspDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMViGAMYAAVLFV 1258
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 451 MFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTS 530
Cdd:PLN03140 1259 GINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSF 1338
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 531 LVAQSLGLLIGAASTSLQVAT-FVGPVTAIpVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGlDRED 605
Cdd:PLN03140 1339 LYFTYYGMMTVSLTPNQQVAAiFAAAFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG-DVED 1412
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
90-595 |
3.04e-51 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 192.25 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE---TGMKGAVLINGLPRD--LRCFRKVSCYIMQDDM 164
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhIGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 LLPHLTVQEAMMVSAHLK-------LQEKDEGRREMVKEILTALGLLSCANTRTGS-----LSGGQRKRLAIALELVNNP 232
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLN 311
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 312 CPTYHNPADFVMEVAS-------GEYGDQNSRLVRAVREGMCDSDHKRDLggDAEVNPFLWHRPSEEDSSSMEGCH---- 380
Cdd:TIGR00956 309 CPDRQTTADFLTSLTSpaerqikPGYEKKVPRTPQEFETYWRNSPEYAQL--MKEIDEYLDRCSESDTKEAYRESHvakq 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 381 --------SFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMF 452
Cdd:TIGR00956 387 skrtrpssPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAF 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 453 AALMPTVLTFplEMGVFLREHLNY-WYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSL 531
Cdd:TIGR00956 467 SSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTL 544
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 532 VAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVI 595
Cdd:TIGR00956 545 AMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
75-291 |
1.09e-47 |
|
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: 166.87 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---RDLRC 151
Cdd:cd03225 1 ELKNLSFSYP-------DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 152 FRKVSCYIMQ--DDMLLpHLTVQEAMMVSA-HLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 228
Cdd:cd03225 73 LRRKVGLVFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQ 291
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
74-301 |
1.31e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.55 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP--RD 148
Cdd:COG1131 1 IEVRGLT-----------KRYgdKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRPTS--GEVRVLGEDvaRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 228
Cdd:COG1131 68 PAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKE-ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKVCNL 301
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
393-595 |
1.08e-46 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 163.98 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 393 LFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKkVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLRE 472
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 473 HLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATF 552
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592978 553 VGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVI 595
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
74-293 |
4.50e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.91 E-value: 4.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP------R 147
Cdd:COG1136 5 LELRNLTKSYGTG-----EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVLIDGQDisslseR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSC-YIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 226
Cdd:COG1136 79 ELARLRRRHIgFVFQFFNLLPELTALENVALPLLLAGVSRKE-RRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 227 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHqpSAKLFELFDQLYVLSQGQCV 293
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTH--DPELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
74-291 |
8.05e-46 |
|
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: 161.89 E-value: 8.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP------R 147
Cdd:cd03255 1 IELKNLSKTYGGG-----GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFR--KVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:cd03255 75 ELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLLLA-GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSakLFELFDQLYVLSQGQ 291
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
74-297 |
1.68e-45 |
|
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: 161.35 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP---RDL 149
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQ--DDMLLpHLTVQEAMMVS-AHLKLqEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 226
Cdd:COG1122 71 RELRRKVGLVFQnpDDQLF-APTVEEDVAFGpENLGL-PREE-IRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 227 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGK 297
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGT 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
74-296 |
2.22e-40 |
|
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: 147.70 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYsvpegpwwrKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP--RDLRC 151
Cdd:COG4555 2 IEVENLSK---------KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-LKPDSGSILIDGEDvrKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 152 FRKVSCYIMQDDMLLPHLTVQEammvsaHLKL-----QEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 226
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLTVRE------NIRYfaelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 227 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
98-242 |
1.62e-39 |
|
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: 142.40 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP---RDLRCFRKVSCYIMQDDMLLPHLTVQEA 174
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 175 MMVSAHLKLQEKDEGRREMvKEILTALGLLSCANTR----TGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 242
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA-EEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
91-271 |
5.55e-39 |
|
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: 143.03 E-value: 5.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 91 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETGM-KGAVLING--LPRDLRCFRKVSCYIMQDDMLLP 167
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG--ELRPtSGTAYINGysIRTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 247
Cdd:cd03263 89 ELTVREHLRFYARLKGLPKSEIKEE-VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180
....*....|....*....|....
gi 46592978 248 SCFQVVSLMKGLaQGGRSIICTIH 271
Cdd:cd03263 168 SRRAIWDLILEV-RKGRSIILTTH 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
74-296 |
7.50e-39 |
|
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: 143.41 E-value: 7.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPR----- 147
Cdd:cd03261 1 IELRGLTKSF---------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 -DLRCFRKVSCYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSEEE--IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIICTiHQPSAkLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
74-297 |
1.13e-38 |
|
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: 143.09 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PR 147
Cdd:cd03256 1 IEVENLSKTYPNG--------KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGTdinklkGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSA------------HLKLQEKDEGRremvkEILTALGLLSCANTRTGSLS 215
Cdd:cd03256 72 ALRQLRRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrslfgLFPKEEKQRAL-----AALERVGLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 216 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLFelFDQLYVLSQGQCV 293
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIV 224
|
....
gi 46592978 294 YRGK 297
Cdd:cd03256 225 FDGP 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
74-294 |
2.23e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDlRCFR 153
Cdd:COG1121 7 IELENLTVSY---------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPR-RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 KVScYIMQD---DMLLPhLTVQE--AMMVSAHLKLQEK-DEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALE 227
Cdd:COG1121 76 RIG-YVPQRaevDWDFP-ITVRDvvLMGRYGRRGLFRRpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 228 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVY 294
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLVAH 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
74-296 |
2.74e-37 |
|
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: 139.41 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP------R 147
Cdd:COG1120 2 LEAENLSVGYGG---------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRcfRKVScYIMQDDMLLPHLTVQEAMMV--SAHLK----LQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKR 221
Cdd:COG1120 72 ELA--RRIA-YVPQEPPAPFGLTVRELVALgrYPHLGlfgrPSAED---REAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 222 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLFelFDQLYVLSQGQCVYRG 296
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
74-289 |
3.30e-37 |
|
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: 137.61 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSvpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLPRDLRC-- 151
Cdd:COG4133 3 LEAENLSCR---------RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-LLPPSAGEVLWNGEPIRDARed 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 152 FRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqeKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNN 231
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 232 PPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsakLFELFDQLYVLSQ 289
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
91-594 |
1.61e-36 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 147.30 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 91 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMK--GAVLINGLPRDLRCFRKVSCYIMQDDMLLPH 168
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGYRLNEFVPRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQEAMMVSA-------------HLKLQEKDEG--------------RREMVKE------ILTALGLLSCANTRTGS-- 213
Cdd:PLN03140 254 MTVKETLDFSArcqgvgtrydllsELARREKDAGifpeaevdlfmkatAMEGVKSslitdyTLKILGLDICKDTIVGDem 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 ---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSAKLFELFDQLYVLSQ 289
Cdd:PLN03140 334 irgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 290 GQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASG----EYGDQNSRLVRAVREGMCDSDHKR-----DLGGDAEV 360
Cdd:PLN03140 414 GQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKkdqeQYWADRNKPYRYISVSEFAERFKSfhvgmQLENELSV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 361 nPFlwHRPSEEDSSSMEGCHSFSASCLTQFCilFKRTFLSIMRDSVL----THLRITSHIGIGLLIGLLYLGIGNEAKKV 436
Cdd:PLN03140 494 -PF--DKSQSHKAALVFSKYSVPKMELLKAC--WDKEWLLMKRNAFVyvfkTVQIIIVAAIASTVFLRTEMHTRNEEDGA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 437 LSnSGFLFFSMLFLMF---AALMPTVLTFPlemgVFLRE-----HLNYWYSLKAYYLAktmadVPFQIMFPVAYCSIVYW 508
Cdd:PLN03140 569 LY-IGALLFSMIINMFngfAELALMIQRLP----VFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVVWVVITYY 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 509 MTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVR 588
Cdd:PLN03140 639 SIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLS 718
|
....*.
gi 46592978 589 YGFEGV 594
Cdd:PLN03140 719 YGFNAL 724
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
74-301 |
2.68e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.73 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGL------PR 147
Cdd:COG3638 3 LELRNLSKRYPGG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGQdvtalrGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMV---------SAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQ 218
Cdd:COG3638 74 ALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgrtstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 219 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPS-AKlfELFDQLYVLSQGQCVYRG 296
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDlAR--RYADRIIGLRDGRVVFDG 229
|
....*
gi 46592978 297 KVCNL 301
Cdd:COG3638 230 PPAEL 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
74-291 |
4.78e-36 |
|
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: 133.29 E-value: 4.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGYKTL--LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TgmKGAVLINGLP--RD 148
Cdd:cd03230 1 IEVRNLS-----------KRYGKKtaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpD--SGEIKVLGKDikKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRCFRKVSCYIMQDDMLLPHLTVQEammvsaHLKlqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALEL 228
Cdd:cd03230 68 PEEVKRRIGYLPEEPSLYENLTVRE------NLK-------------------------------LSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQ 291
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
90-296 |
5.27e-36 |
|
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: 134.31 E-value: 5.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET--GMKGAVLINGLPRD--LRCFRKVSCYIMQDDML 165
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPYKefAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 166 LPHLTVQEAMMVSAHLKlqekdegRREMVKEIltalgllscantrtgslSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:cd03233 95 FPTLTVRETLDFALRCK-------GNEFVRGI-----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46592978 246 SASCFQVVSLMKGLAQG-GRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
105-296 |
1.76e-35 |
|
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: 133.00 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 105 FNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScYIMQDDMLLPHLTVQE--AMM 176
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 177 VSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 256
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46592978 257 KGL-AQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 296
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
74-245 |
4.44e-35 |
|
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: 132.21 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDlRCF 152
Cdd:cd03293 1 LEVRNVSKTYGGG-----GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEPVT-GPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 153 RKVScYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNP 232
Cdd:cd03293 73 PDRG-YVFQQDALLPWLTVLDNVALGLELQGVPKAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170
....*....|...
gi 46592978 233 PVMFFDEPTSGLD 245
Cdd:cd03293 151 DVLLLDEPFSALD 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-298 |
5.70e-35 |
|
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: 139.27 E-value: 5.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP------ 146
Cdd:COG1123 261 LEVRNLSKRYPV----RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRCFRKVSCYIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGL-LSCANTRTGSLSGGQRKRLA 223
Cdd:COG1123 335 RSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 224 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIictihqpsakLF---------ELFDQLYVLSQGQCV 293
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTY----------LFishdlavvrYIADRVAVMYDGRIV 484
|
....*
gi 46592978 294 YRGKV 298
Cdd:COG1123 485 EDGPT 489
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
59-296 |
4.23e-34 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 138.81 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 59 EAQRFSSLPRRAAvNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmK 137
Cdd:COG2274 460 EGRSKLSLPRLKG-DIELENVSFRYPGDS-------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPT--S 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 138 GAVLINGL------PRDLRcfRKVScYIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGrremvk 195
Cdd:COG2274 530 GRILIDGIdlrqidPASLR--RQIG-VVLQDVFLFsgtirenitlgdPDATDEEiieaARLAGLHDFIEALPMG------ 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 196 eILTALGllscanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSa 275
Cdd:COG2274 601 -YDTVVG------EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS- 671
|
250 260
....*....|....*....|.
gi 46592978 276 kLFELFDQLYVLSQGQCVYRG 296
Cdd:COG2274 672 -TIRLADRIIVLDKGRIVEDG 691
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
74-296 |
5.00e-34 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 129.55 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING-----LPRD 148
Cdd:cd03257 2 LEVKNLSVSFP-----TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP-TSGSIIFDGkdllkLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LR--CFRKVScYIMQDDM--LLPHLTVQEAMM--VSAHLKLQEKDEgRREMVKEILTALGLLS-CANTRTGSLSGGQRKR 221
Cdd:cd03257 76 LRkiRRKEIQ-MVFQDPMssLNPRMTIGEQIAepLRIHGKLSKKEA-RKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 222 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
74-291 |
5.66e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.78 E-value: 5.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRD---- 148
Cdd:COG4619 1 LELEGLSFRV---------GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTS--GEIYLDGKPLSampp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 --LRcfRKVScYIMQDdmllPHL---TVQEAMMVSAHLKLQEKDegrREMVKEILTALGL-LSCANTRTGSLSGGQRKRL 222
Cdd:COG4619 70 peWR--RQVA-YVPQE----PALwggTVRDNLPFPFQLRERKFD---RERALELLERLGLpPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 223 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPsAKLFELFDQLYVLSQGQ 291
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
95-296 |
6.79e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 128.46 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGeLVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQ 172
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGqdVLKQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVSAHLK-LQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 251
Cdd:cd03264 91 EFLDYIAWLKgIPSKEVKAR--VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592978 252 VVSLMKGLAQgGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03264 169 FRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
74-245 |
8.40e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.82 E-value: 8.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPRDlRCFR 153
Cdd:COG1116 8 LELRGVSKRFP-----TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPVT-GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 KVScYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPP 233
Cdd:COG1116 81 DRG-VVFQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170
....*....|..
gi 46592978 234 VMFFDEPTSGLD 245
Cdd:COG1116 159 VLLMDEPFGALD 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
98-296 |
1.06e-33 |
|
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: 128.71 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVL-----INGLPRDLRC-------FRKVScyimqddm 164
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLfdgedITGLPPHEIArlgigrtFQIPR-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 LLPHLTVQEAMMVSAHLKLQE---------KDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVM 235
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 236 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
64-302 |
1.14e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 136.04 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 64 SSLPRRAAVNIEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYREtGMKGAVLIN 143
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGG--------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-PYSGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GLPR---DLRCFRKVSCYIMQDDMLlPHLTVQEammvsaHLKLQEKDEGRREM--------VKEILTAL--GLlscaNTR 210
Cdd:COG4988 398 GVDLsdlDPASWRRQIAWVPQNPYL-FAGTIRE------NLRLGRPDASDEELeaaleaagLDEFVAALpdGL----DTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 211 TGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTiHQPSakLFELFDQLYV 286
Cdd:COG4988 467 LGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILV 543
|
250
....*....|....*.
gi 46592978 287 LSQGQCVYRGKVCNLV 302
Cdd:COG4988 544 LDDGRIVEQGTHEELL 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
74-291 |
1.22e-33 |
|
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: 126.34 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPR---DL 149
Cdd:cd03228 1 IEFKNVSFSYPGRP-------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlYDPT--SGEILIDGVDLrdlDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQDDMLLpHLTVQEAMmvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELV 229
Cdd:cd03228 72 ESLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 230 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSakLFELFDQLYVLSQGQ 291
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
75-291 |
1.64e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.82 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP---RDLR 150
Cdd:cd00267 1 EIENLSFRYGG---------RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGlLKPT--SGEILIDGKDiakLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQddmllphltvqeammvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVN 230
Cdd:cd00267 70 ELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 231 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQ 291
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
93-291 |
2.40e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 127.25 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGlpRDLRCF----RKVScYIMQDDMLLPH 168
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDG--RDVTGVpperRNIG-MVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQEAmmVSAHLKLQEKDEG-RREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 247
Cdd:cd03259 87 LTVAEN--IAFGLKLRGVPKAeIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46592978 248 SCFQVVSLMKGL-AQGGRSIICTIHQPS-AklFELFDQLYVLSQGQ 291
Cdd:cd03259 165 LREELREELKELqRELGITTIYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
74-297 |
3.39e-33 |
|
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: 127.80 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP------R 147
Cdd:TIGR02315 2 LEVENLSKVYPNG--------KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-VEPSSGSILLEGTDitklrgK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQDDMLLPHLTVQEAMM---VSAHLKLQ-------EKDegrREMVKEILTALGLLSCANTRTGSLSGG 217
Cdd:TIGR02315 73 KLRKLRRRIGMIFQHYNLIERLTVLENVLhgrLGYKPTWRsllgrfsEED---KERALSALERVGLADKAYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 218 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLFElfDQLYVLSQGQCVYR 295
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFD 227
|
..
gi 46592978 296 GK 297
Cdd:TIGR02315 228 GA 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
75-296 |
3.83e-33 |
|
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: 125.63 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGlpRDLrcfrk 154
Cdd:cd03214 1 EVENLSVGYGG---------RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDG--KDL----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 155 vscyimqddmllphltvqeammvsAHLKLQEKdegRREM--VKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNP 232
Cdd:cd03214 64 ------------------------ASLSPKEL---ARKIayVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPS-AKLFelFDQLYVLSQGQCVYRG 296
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
74-307 |
5.20e-33 |
|
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: 127.02 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----L 145
Cdd:COG1127 6 IEVRNLT-----------KSFgdRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGqditgL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 PRD----LRcfRKVScYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQR 219
Cdd:COG1127 73 SEKelyeLR--RRIG-MLFQGGALFDSLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIICTiHQ-PSAklFELFDQLYVLSQGQCVYRG 296
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEG 224
|
250
....*....|....*
gi 46592978 297 KVCNLV----PYLRD 307
Cdd:COG1127 225 TPEELLasddPWVRQ 239
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
74-291 |
2.10e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.78 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----LPR 147
Cdd:COG2884 2 IRFENVSKRYPGG--------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 D----LRcfRKVScYIMQDDMLLPHLTVQE----AMMVsahLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQR 219
Cdd:COG2884 72 ReipyLR--RRIG-VVFQDFRLLPDRTVYEnvalPLRV---TGKSRKEIRRR--VREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsaklfELFDQL----YVLSQGQ 291
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL-----ELVDRMpkrvLELEDGR 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
73-296 |
3.51e-32 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 124.24 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGL------ 145
Cdd:cd03245 2 RIEFRNVSFSYPNQE-------IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTS--GSVLLDGTdirqld 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 PRDLRcfRKVScYIMQDdmllPHL---TVQEAMMvsahLKLQEKDEgrrEMVKEILTALGLLSCANT-----------RT 211
Cdd:cd03245 73 PADLR--RNIG-YVPQD----VTLfygTLRDNIT----LGAPLADD---ERILRAAELAGVTDFVNKhpngldlqigeRG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 212 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAqGGRSIICTIHQPSakLFELFDQLYVLSQGQ 291
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGR 215
|
....*
gi 46592978 292 CVYRG 296
Cdd:cd03245 216 IVADG 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
74-272 |
3.59e-32 |
|
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: 123.79 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGYKTL--LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGLP-- 146
Cdd:cd03262 1 IEIKNLH-----------KSFGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGLKlt 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 ---RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVsAHLKLQ--EKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKR 221
Cdd:cd03262 66 ddkKNINELRQKVGMVFQQFNLFPHLTVLENITL-APIKVKgmSKAEAE-ERALELLEKVGLADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592978 222 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQ 272
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-342 |
4.51e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.79 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGMKGAVLING-----LP 146
Cdd:COG1123 5 LEVRDLSVRYPGGD-------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGrdlleLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRCfRKVScYIMQDDM--LLPhLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:COG1123 78 EALRG-RRIG-MVFQDPMtqLNP-VTVGDQIAEALENLGLSRAE-ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPsAKLFELFDQLYVLSQGQCVYRGKVCNL-- 301
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIla 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 46592978 302 -------VPYLRDLGLNCPTYHNPADFVMEVA--SGEYGDQNSRLVRAVR 342
Cdd:COG1123 233 apqalaaVPRLGAARGRAAPAAAAAEPLLEVRnlSKRYPVRGKGGVRAVD 282
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
74-271 |
5.26e-32 |
|
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: 123.29 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP------R 147
Cdd:cd03292 1 IEFINVTKTYPNG--------TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:cd03292 72 AIPYLRRKIGVVFQDFRLLPDRNVYENVAFA----LEVTGVPPREIrkrVPAALELVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
78-271 |
1.45e-31 |
|
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: 121.98 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 78 DLSYSVPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPRDLRCFRKVS 156
Cdd:cd03226 4 NISFSYKKGT--------EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 157 CYIMQD-DMLLPHLTVQEAMMVSahLKLQEKDEGRREmvkEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVM 235
Cdd:cd03226 74 GYVMQDvDYQLFTDSVREELLLG--LKELDAGNEQAE---TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 46592978 236 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
74-291 |
1.81e-31 |
|
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: 120.75 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPRD 148
Cdd:cd03229 1 LELKNVSKRYGQ---------KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGedltdLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRCFRKVSCYIMQDDMLLPHLTVQEammvsahlklqekdegrremvkeiltalgllscaNTRTGsLSGGQRKRLAIALEL 228
Cdd:cd03229 71 LPPLRRRIGMVFQDFALFPHLTVLE----------------------------------NIALG-LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPsAKLFELFDQLYVLSQGQ 291
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
74-296 |
4.30e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP-----R 147
Cdd:PRK13639 2 LETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT--SGEVLIKGEPikydkK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:PRK13639 72 SLLEVRKTVGIVFQnpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpsAKLFELF-DQLYVLSQGQCVYRG 296
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
75-290 |
1.44e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.18 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLINGLPrdLRCFR 153
Cdd:cd03235 1 EVEDLTVSY---------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLlKPT--SGSIRVFGKP--LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 KVSCYIMQD---DMLLPhLTVQEAMM------VSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:cd03235 68 KRIGYVPQRrsiDRDFP-ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQG 290
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
74-273 |
2.11e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 126.76 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNIL-------AG-YRETGMKGAVLINGL 145
Cdd:PRK10535 5 LELKDIRRSYPSG-----EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 PRDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:PRK10535 80 LAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQP 273
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-308 |
2.49e-30 |
|
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: 119.52 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLR 150
Cdd:COG1124 2 LEVRNLSVSYGQGGRRV-----PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQDDM--LLPHLTVQEAmmVSAHLKLQEKDEgRREMVKEILTALGL-LSCANTRTGSLSGGQRKRLAIALE 227
Cdd:COG1124 76 AFRRRVQMVFQDPYasLHPRHTVDRI--LAEPLRIHGLPD-REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 228 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPSAKLFeLFDQLYVLSQGQCV---YRGKVCNLV- 302
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGRIVeelTVADLLAGPk 231
|
....*..
gi 46592978 303 -PYLRDL 308
Cdd:COG1124 232 hPYTREL 238
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
98-271 |
3.06e-30 |
|
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: 117.52 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP-----RDLRCFRKVSCYIMQ--DDMLLPHL 169
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQ--SGAVLIDGEPldysrKGLLERRQRVGLVFQdpDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 249
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERR--VREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|..
gi 46592978 250 FQVVSLMKGLAQGGRSIICTIH 271
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
98-297 |
3.24e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 118.69 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 173
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSAHLKLQEKDEGRREMVKEILTALGLLScaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 253
Cdd:cd03224 95 NLLLGAYARRRAKRKARLERVYELFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 254 SLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQCVYRGK 297
Cdd:cd03224 173 EAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
64-308 |
4.17e-30 |
|
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: 125.26 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 64 SSLPRRAAVNIEFRDLSYSVPEGPWWrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLIN 143
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRP-------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GLP-RDLR--CFRKVSCYIMQDdmllPHL---TVQEammvsaHLKLQEKDEGRREMVkEILTALGLLSCA-------NTR 210
Cdd:COG4987 396 GVDlRDLDedDLRRRIAVVPQR----PHLfdtTLRE------NLRLARPDATDEELW-AALERVGLGDWLaalpdglDTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 211 TGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYV 286
Cdd:COG4987 465 LGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILV 541
|
250 260
....*....|....*....|....*
gi 46592978 287 LSQGQCVYRGKVCNLV---PYLRDL 308
Cdd:COG4987 542 LEDGRIVEQGTHEELLaqnGRYRQL 566
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
73-298 |
6.29e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.93 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLSYSvpegpwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPR 147
Cdd:COG3840 1 MLRLDDLTYR-----------YGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGF-LPPDSGRILWNGqdltaLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLrcfRKVScYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:COG3840 69 AE---RPVS-MLFQENNLFPHLTVAQniGLGLRPGLKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLfeLFDQLYVLSQGQCVYRGKV 298
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAAR--IADRVLLVADGRIAADGPT 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
74-272 |
7.51e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.27 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLM---NILagyrETGMKGAVLINGL----P 146
Cdd:PRK09493 2 IEFKNVS---------KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVDGLkvndP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 R-DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSA-HLKLQEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:PRK09493 69 KvDERLIRQEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAE-KQARELLAKVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQ 272
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
98-291 |
1.45e-29 |
|
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: 117.83 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGlpRDL--------------RCFRKVScyimqd 162
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDG--RDItglpphriarlgiaRTFQNPR------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 dmLLPHLTVQEAMMVSAHLKLQE-------------KDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 228
Cdd:COG0411 90 --LFPELTVLENVLVAAHARLGRgllaallrlprarREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQ 291
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL-VMGLADRIVVLDFGR 230
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
59-293 |
2.67e-29 |
|
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: 123.82 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 59 EAQRFSSLPRRAAvNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmK 137
Cdd:TIGR03375 450 EGTRFLHRPRLQG-EIEFRNVSFAYPGQE-------TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGlYQPT--E 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 138 GAVLINGL------PRDLRcfRKVScYIMQDDMLLpHLTVQEAMMVSAhlklQEKDEgrrEMVKEILTALGLLSCANT-- 209
Cdd:TIGR03375 520 GSVLLDGVdirqidPADLR--RNIG-YVPQDPRLF-YGTLRDNIALGA----PYADD---EEILRAAELAGVTEFVRRhp 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 210 ---------RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAqGGRSIICTIHQPSakLFEL 280
Cdd:TIGR03375 589 dgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS--LLDL 665
|
250
....*....|...
gi 46592978 281 FDQLYVLSQGQCV 293
Cdd:TIGR03375 666 VDRIIVMDNGRIV 678
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
74-271 |
3.06e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.25 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGYKTL--LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGLP-- 146
Cdd:COG1126 2 IEIENLH-----------KSFGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDlt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 ---RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVS-AHLKLQEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRL 222
Cdd:COG1126 67 dskKDINKLRRKVGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46592978 223 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
74-298 |
6.36e-29 |
|
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: 115.37 E-value: 6.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PR 147
Cdd:cd03258 2 IELKNVSKVFGDT-----GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALE 227
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAE-IEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 228 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 298
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTV 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
93-296 |
9.74e-29 |
|
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: 113.85 E-value: 9.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLPRDLRCFRKVSCyIMQDDMLLPHLTV 171
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDSGEITFDGKSYQKNIEALRRIGA-LIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSAHLKLqekdeGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 251
Cdd:cd03268 90 RENLRLLARLLG-----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592978 252 VVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03268 165 LRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
74-296 |
1.55e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.83 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGL------PR 147
Cdd:COG4559 2 LEAENLSVRL---------GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGEL-TPSSGEVRLNGRplaawsPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVscyimqddmlLP-------HLTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGG- 217
Cdd:COG4559 72 ELARRRAV----------LPqhsslafPFTVEEvvALGRAPHGSSAAQD---RQIVREALALVGLAHLAGRSYQTLSGGe 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 218 -QRKRLAIAL----ELVNNPP-VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPS-AKLFElfDQLYVLSQG 290
Cdd:COG4559 139 qQRVQLARVLaqlwEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYA--DRILLLHQG 216
|
....*.
gi 46592978 291 QCVYRG 296
Cdd:COG4559 217 RLVAQG 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
94-297 |
1.90e-28 |
|
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: 113.42 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 94 YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPR-DLRCFRKVSCYIMQDDMLLPHLTVQ 172
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-IEPASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVSAH--LKLQEKdegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:TIGR01277 89 QNIGLGLHpgLKLNAE---QQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46592978 251 QVVSLMKGLA-QGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGK 297
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGKIKVVSD 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
74-261 |
4.77e-28 |
|
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: 112.53 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPRD 148
Cdd:COG4181 9 IELRGLTKTVGTG-----AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGqdlfaLDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRC-FR--KVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:COG4181 83 ARArLRarHVG-FVFQSFQLLPTLTALENVMLPLELA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 261
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
74-298 |
1.19e-27 |
|
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: 112.10 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSvpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-----YRET----GMK-GAVLIn 143
Cdd:COG1119 4 LELRNVTVR---------RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptYGNDvrlfGERrGGEDV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 glpRDLRcfRK---VSCYIMQDdmLLPHLTVQEaMMVSA-------HLKLQEKDEGRremVKEILTALGLLSCANTRTGS 213
Cdd:COG1119 74 ---WELR--KRiglVSPALQLR--FPRDETVLD-VVLSGffdsiglYREPTDEQRER---ARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSAkLFELFDQLYVLSQGQC 292
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRV 221
|
....*.
gi 46592978 293 VYRGKV 298
Cdd:COG1119 222 VAAGPK 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
91-296 |
1.70e-27 |
|
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: 111.10 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 91 KKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----LPRDLRCfRKVSCYIMQD 162
Cdd:cd03218 7 SKRYgkRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGKILLDGqditkLPMHKRA-RLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 DMLLPHLTVQEAMMvsAHLKLQEKD-EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 241
Cdd:cd03218 84 ASIFRKLTVEENIL--AVLEIRGLSkKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 242 SGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 296
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEG 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
93-273 |
1.83e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 110.35 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQ 172
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVSAHLKlqekdEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 252
Cdd:PRK13539 92 ENLEFWAAFL-----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|..
gi 46592978 253 VSLMKG-LAQGGRSIICTiHQP 273
Cdd:PRK13539 167 AELIRAhLAQGGIVIAAT-HIP 187
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
74-245 |
2.68e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 113.65 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LP 146
Cdd:COG3842 6 LELENVS-----------KRYgdVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGrdvtgLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 ---RDLrcfrkvsCYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKR 221
Cdd:COG3842 74 pekRNV-------GMVFQDYALFPHLTVAEN--VAFGLRMRgvPKAE-IRARVAELLELVGLEGLADRYPHQLSGGQQQR 143
|
170 180
....*....|....*....|....
gi 46592978 222 LAIALELVNNPPVMFFDEPTSGLD 245
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALD 167
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
90-301 |
3.04e-27 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 110.15 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGLP--RDLRCFRKVSCYIMQDDMLL 166
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQEAMMVsaHLKLQE-KDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:cd03265 86 DELTGWENLYI--HARLYGvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 246 SASCFQVVSLMKGL-AQGGRSIICTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVCNL 301
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
93-245 |
6.20e-27 |
|
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: 109.63 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP-RDLRCFRKVSCYIMQDDMLLPHLTV 171
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 172 QEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
98-245 |
8.31e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.09 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------LPRDlrcfRKVScyiM--QDDMLLPHL 169
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL-EDPTSGEILIGGrdvtdlPPKD----RNIA---MvfQSYALYPHM 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 170 TVQEAMmvSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:COG3839 91 TVYENI--AFPLKLRkvPKAE-IDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
107-296 |
1.34e-26 |
|
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: 108.15 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 107 SGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------------PRDlrcfRKVScYIMQDDMLLPHLTVQEA 174
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 175 MMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 254
Cdd:cd03297 96 LAFGLKRKRNRED---RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 255 LMKGLAQ--GGRSIICTiHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03297 173 ELKQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
96-246 |
1.69e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.01 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 96 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-------LPRDlrcfRKVScYIMQDDMLLPH 168
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGrdlftnlPPRE----RRVG-FVFQHYALFPH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 169 LTVQEAmmVSAHLKLQEKDEG-RREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:COG1118 90 MTVAEN--IAFGLRVRPPSKAeIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
95-247 |
6.81e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETG--MKGAVLINGlpRDLRCF----RKVScYIMQDDMLLPH 168
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNG--RRLTALpaeqRRIG-ILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQE--AMMVSAHLKLQEkdegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:COG4136 91 LSVGEnlAFALPPTIGRAQ----RRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 46592978 247 A 247
Cdd:COG4136 167 A 167
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
95-296 |
9.47e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 106.76 E-value: 9.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNIL----AGYRETG---MKGAVLINGLPRDLRCFRKVSCYIMQDDM 164
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLeqpeAGTIRVGditIDTARSLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 LLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 244
Cdd:PRK11264 96 LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592978 245 DSASCFQVVSLMKGLAQGGRSIICTIHQPS-AKlfELFDQLYVLSQGQCVYRG 296
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQG 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
66-287 |
1.11e-25 |
|
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: 111.61 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 66 LPRRAAVNIEFRDLSYSVPegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL 145
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYP--------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 PR---DLRCFRKVSCYIMQddmlLPHLTvqeAMMVSAHLKLQEKDeGRREMVKEILTALGLLSCA-------NTRTGS-- 213
Cdd:TIGR02857 385 PLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRLARPD-ASDAEIREALERAGLDEFVaalpqglDTPIGEgg 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 214 --LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPsaKLFELFDQLYVL 287
Cdd:TIGR02857 457 agLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
108-247 |
1.65e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.43 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGlpRDLRCF----RKVScYIMQDDMLLPHLTVQEAMMVSAH--L 181
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFL-TPASGSLTLNG--QDHTTTppsrRPVS-MLFQENNLFSHLTVAQNIGLGLNpgL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 182 KLqekDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 247
Cdd:PRK10771 101 KL---NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
73-296 |
1.86e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLSYSVPEGPWwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP------ 146
Cdd:COG1132 339 EIEFENVSFSYPGDRP--------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDirdltl 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRcfRKVScYIMQDDMLLpHLTVQE-----------------AMMVSAHLKLQEKDEGRREMVKEiltalgllscant 209
Cdd:COG1132 410 ESLR--RQIG-VVPQDTFLF-SGTIREnirygrpdatdeeveeaAKAAQAHEFIEALPDGYDTVVGE------------- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 210 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIIctI-HQPSAklFELFDQLYVLS 288
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV--IaHRLST--IRNADRILVLD 548
|
....*...
gi 46592978 289 QGQCVYRG 296
Cdd:COG1132 549 DGRIVEQG 556
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
92-273 |
5.98e-25 |
|
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: 102.82 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 92 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP----RDLRcfRKVSCYIMQDDMLLP 167
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPlaeqRDEP--HENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTVQEAMMVSAHLKlqekdEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 247
Cdd:TIGR01189 87 ELSALENLHFWAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 46592978 248 SCFQVVSLMKGLAQGGRSIICTIHQP 273
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
74-291 |
1.04e-24 |
|
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: 101.14 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP---RDLR 150
Cdd:cd03246 1 LEVENVSFRYPGAEPP-------VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADisqWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQDDMLLPHlTVQEAMmvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVN 230
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 231 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSakLFELFDQLYVLSQGQ 291
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
98-257 |
2.20e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 102.03 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING-----LPRDLRCFrkvsCYIMQDDMLLPHLTVQ 172
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGkditnLPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 252
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
....*
gi 46592978 253 VSLMK 257
Cdd:cd03299 169 REELK 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
74-261 |
4.47e-24 |
|
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: 101.10 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMK----GAVLING----- 144
Cdd:cd03260 1 IELRDLNVYY---------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGkdiyd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 145 ---LPRDLRcfRKVScYIMQDDMLLPhLTVQEAmmVSAHLKLQE--KDEGRREMVKEILTALGLLSCANTRTG--SLSGG 217
Cdd:cd03260 72 ldvDVLELR--RRVG-MVFQKPNPFP-GSIYDN--VAYGLRLHGikLKEELDERVEEALRKAALWDEVKDRLHalGLSGG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 218 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 261
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
92-273 |
5.39e-24 |
|
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: 100.26 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 92 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRD-LRCFRKVSC-YIMQDDMLLPHL 169
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPLDfQRDSIARGLlYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAMMVSAhlklqekDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 249
Cdd:cd03231 89 SVLENLRFWH-------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 46592978 250 FQVVSLMKGLAQGGRSIICTIHQP 273
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
73-296 |
5.93e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 100.76 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---RDL 149
Cdd:cd03254 2 EIEFENVNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQDDMLLPHlTVQEAMMVSahlklqeKDEGRREMVKEILTAL-----------GLLSCANTRTGSLSGGQ 218
Cdd:cd03254 73 KSLRSMIGVVLQDTFLFSG-TIMENIRLG-------RPNATDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 219 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTiHQPSAKLFElfDQLYVLSQGQCVYRG 296
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
96-273 |
1.22e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 96 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYREtgmkgavlinglPRDLRCFRKVSC---YIMQ---DDMLLPhL 169
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------------PTSGTVRRAGGArvaYVPQrseVPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAMMVS--AHLKLQEK-DEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:NF040873 73 TVRDLVAMGrwARRGLWRRlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIHQP 273
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
98-263 |
1.48e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL---------PRDLRCFRKVSCYIMQDDML 165
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 166 LPHLTVQEAMmVSAHLKL--QEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:COG4161 94 WPHLTVMENL-IEAPCKVlgLSKEQAR-EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|
gi 46592978 244 LDSASCFQVVSLMKGLAQGG 263
Cdd:COG4161 172 LDPEITAQVVEIIRELSQTG 191
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
98-301 |
1.74e-23 |
|
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: 101.31 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGL-----PRDLR-----CFRKVSCYimqDDmll 166
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGYdvvrePRKVRrsigiVPQYASVD---ED--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 phLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:TIGR01188 81 --LTGRENLEMMGRLYGLPKDE-AEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIHQpsakLFE---LFDQLYVLSQGQCVYRGKVCNL 301
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
74-293 |
1.79e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL------PR 147
Cdd:PRK13548 3 LEARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVscyimqddmlLPH-------LTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGG- 217
Cdd:PRK13548 73 ELARRRAV----------LPQhsslsfpFTVEEvvAMGRAPHGLSRAED---DALVAAALAQVDLAHLAGRDYPQLSGGe 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 218 -QRKRLAIAL----ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHqpSAKLFELF-DQLYVLSQG 290
Cdd:PRK13548 140 qQRVQLARVLaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQG 217
|
...
gi 46592978 291 QCV 293
Cdd:PRK13548 218 RLV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
74-296 |
2.37e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 99.23 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRkkgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP-RD--LR 150
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV-------LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDGHDvRDytLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKvSCYIMQDDMLLPHLTVQE-----------------AMMVSAHLKLQEKDEGRREMVKEiltalgllscantRTGS 213
Cdd:cd03251 73 SLRR-QIGLVSQDVFLFNDTVAEniaygrpgatreeveeaARAANAHEFIMELPEGYDTVIGE-------------RGVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYVLSQGQCV 293
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIV 215
|
...
gi 46592978 294 YRG 296
Cdd:cd03251 216 ERG 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
74-293 |
4.06e-23 |
|
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: 98.91 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL------PR 147
Cdd:cd03295 1 IEFENVTKRYGGG--------KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRcfRKVScYIMQDDMLLPHLTVQEAmmVSAHLKLQE-KDEGRREMVKEILTALGL--LSCANTRTGSLSGGQRKRLAI 224
Cdd:cd03295 72 ELR--RKIG-YVIQQIGLFPHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSaKLFELFDQLYVLSQGQCV 293
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDID-EAFRLADRIAIMKNGEIV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
93-296 |
4.88e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.74 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPRDLRCFRKVScYIMQDDMLLPHLTV 171
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPD--SGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 251
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592978 252 VVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
97-245 |
1.55e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.81 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 97 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---------RDLRCfRKVScYIMQDDMLLP 167
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTVQE--AM-MVSAHLKLQEKDEGRREMvkeiLTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 244
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
.
gi 46592978 245 D 245
Cdd:PRK11629 177 D 177
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
74-297 |
1.57e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 96.92 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGlpRDLR--- 150
Cdd:cd03253 1 IEFENVTFAYDPG--------RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDG--QDIRevt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 --CFRKVSCYIMQDDMLL----------PHLTVQEAMMVSA------HLKLQEKDEGRREMVKEiltalgllscantRTG 212
Cdd:cd03253 70 ldSLRRAIGVVPQDTVLFndtigyniryGRPDATDEEVIEAakaaqiHDKIMRFPDGYDTIVGE-------------RGL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 213 SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPS----AklfelfDQLYVLS 288
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLStivnA------DKIIVLK 209
|
....*....
gi 46592978 289 QGQCVYRGK 297
Cdd:cd03253 210 DGRIVERGT 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
74-246 |
2.01e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP-----RD 148
Cdd:COG4525 4 LTVRHVSVRYPGG-----GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 lrcfRKVscyIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 226
Cdd:COG4525 78 ----RGV---VFQKDALLPWLNVLDN--VAFGLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180
....*....|....*....|
gi 46592978 227 ELVNNPPVMFFDEPTSGLDS 246
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDA 167
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
98-296 |
2.72e-22 |
|
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: 95.51 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL-----PRDLRcfRKVScyIMQDDM-LLPHLTV 171
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFdvvkePAEAR--RRLG--FVSDSTgLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSAHLKLQEKDE--GRremVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 249
Cdd:cd03266 96 RENLEYFAGLYGLKGDEltAR---LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46592978 250 FQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
71-273 |
2.96e-22 |
|
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: 100.90 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 71 AVNIEFRDLSYSVPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---R 147
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAP--------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVSCYIMQDdmllPHL---TVQEAMMVSahlklqeKDEGRREMVKEILTALGLL-------SCANTRTG----S 213
Cdd:TIGR02868 403 DQDEVRRRVSVCAQD----AHLfdtTVRENLRLA-------RPDATDEELWAALERVGLAdwlralpDGLDTVLGeggaR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGlAQGGRSIICTIHQP 273
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
106-263 |
3.00e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 106 NSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLINGL---------PRDLRCFRKVSCYIMQDDMLLPHLTVQEAMm 176
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 177 VSAHLKLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 255
Cdd:PRK11124 104 IEAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
....*...
gi 46592978 256 MKGLAQGG 263
Cdd:PRK11124 184 IRELAETG 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
74-245 |
3.64e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.23 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS--YSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL--- 145
Cdd:COG1135 2 IELENLSktFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 ---PRDLRCFR-KVScYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQR 219
Cdd:COG1135 71 alsERELRAARrKIG-MIFQHFNLLSSRTVAEN--VALPLEIAgvPKAE-IRKRVAELLELVGLSDKADAYPSQLSGGQK 146
|
170 180
....*....|....*....|....*.
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
89-291 |
4.28e-22 |
|
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: 95.01 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 89 WRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LP---RDLrcfrkvsCYIM 160
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGrdvtdLPpkdRDI-------AMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 161 QDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592978 241 TSGLDSASCFQVVSLMKGLAQG-GRSIICTIH-QPSAklFELFDQLYVLSQGQ 291
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
98-296 |
4.64e-22 |
|
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: 95.43 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGlpRD---LRCFRKVS---CYIMQDDMLLPHLTV 171
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL-LPPRSGSIRFDG--EDitgLPPHRIARlgiGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSAHL-KLQEKDEGRREMVKEILTALGLLscANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL-----D 245
Cdd:COG0410 96 EENLLLGAYArRDRAEVRADLERVYELFPRLKER--RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592978 246 sascfQVVSLMKGLAQGGRSIICtIHQPSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:COG0410 174 -----EIFEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
98-246 |
5.32e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 95.48 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScYIMQDDMLLPHLTV 171
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEdatdvpVQE----RNVG-FVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAmmVSAHLKLQEKDEGR-----REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:cd03296 92 FDN--VAFGLRVKPRSERPpeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
75-296 |
5.57e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.52 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLING-----LP 146
Cdd:COG0396 2 EIKNLHVSVEG---------KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGedileLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRC----FrkvscYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGR--REMVKEILTALGL----LS-CANtrtGSLS 215
Cdd:COG0396 71 PDERAragiF-----LAFQYPVEIPGVSVSNFLRTALNARRGEELSARefLKLLKEKMKELGLdedfLDrYVN---EGFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 216 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVS-LMKGLAQGGRSIICTIHQPsaKLFELF--DQLYVLSQGQC 292
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRI 219
|
....
gi 46592978 293 VYRG 296
Cdd:COG0396 220 VKSG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
98-267 |
7.11e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDLRCFRK-----VSCyIMQDDMLLPHLTV 171
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagIAI-IHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSahlklQEKDEG----RREMVK---EILTALGL-LScANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:COG1129 97 AENIFLG-----REPRRGglidWRAMRRrarELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180
....*....|....*....|....
gi 46592978 244 LDSASCFQVVSLMKGLAQGGRSII 267
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
74-297 |
7.77e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.86 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSV-PEGPWwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLPR---DL 149
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--------ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-VPENGRVLVDGHDLalaDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQDDMLLP----------------HLTVQEAMMVSAHLKLQEKDEGRREMVKEiltalgllscantRTGS 213
Cdd:cd03252 72 AWLRRQVGVVLQENVLFNrsirdnialadpgmsmERVIEAAKLAGAHDFISELPEGYDTIVGE-------------QGAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYVLSQGQCV 293
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIV 215
|
....
gi 46592978 294 YRGK 297
Cdd:cd03252 216 EQGS 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
76-245 |
8.57e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 76 FRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLInglPRDLRcfrkV 155
Cdd:COG0488 1 LENLSKSFGG---------RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVSI---PKGLR----I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 156 ScYIMQDDMLLPHLTV-QEAMMVSAHLK--LQEKDEGRREM----------------------------VKEILTALGLL 204
Cdd:COG0488 64 G-YLPQEPPLDDDLTVlDTVLDGDAELRalEAELEELEAKLaepdedlerlaelqeefealggweaearAEEILSGLGFP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46592978 205 SC-ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:COG0488 143 EEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
74-245 |
9.95e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LP 146
Cdd:PRK09452 15 VELRGIS-----------KSFdgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDGqdithVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRCFRKVscyiMQDDMLLPHLTVQEAmmVSAHLKLQE--KDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:PRK09452 83 AENRHVNTV----FQSYALFPHMTVFEN--VAFGLRMQKtpAAE-ITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 46592978 225 ALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
90-272 |
1.03e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.04 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLING----LPRD------------LRCFR 153
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGqtinLVRDkdgqlkvadknqLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 KVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGS-LSGGQRKRLAIALELVNNP 232
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQ 272
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
93-296 |
1.29e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyR-ETGMKGAVLINGLPRDLRCFRKVSCYIMqddmLLP-HLT 170
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RlLTPQSGTVFLGDKPISMLSSRQLARRLA----LLPqHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 171 VQEAMMV--------SAHL----KLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFD 238
Cdd:PRK11231 87 TPEGITVrelvaygrSPWLslwgRLSAED---NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 239 EPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH---QPSaklfELFDQLYVLSQGQCVYRG 296
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
74-296 |
1.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRD----- 148
Cdd:PRK13636 6 LKVEELNYNYSDG--------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPIDysrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 226
Cdd:PRK13636 77 LMKLRESVGMVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKR--VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 227 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHqpSAKLFELF-DQLYVLSQGQCVYRG 296
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQG 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
74-313 |
2.35e-21 |
|
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: 94.44 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGL------- 145
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKA----LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 --PRDLRcfRKVScYIMQddmlLPH-----LTVQEAMMVSAH-LKLQEKDEGRRemVKEILTALGL------LSCAntrt 211
Cdd:TIGR04521 75 kkLKDLR--KKVG-LVFQ----FPEhqlfeETVYKDIAFGPKnLGLSEEEAEER--VKEALELVGLdeeyleRSPF---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 212 gSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSaKLFELFDQLYVLSQG 290
Cdd:TIGR04521 142 -ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKG 219
|
250 260
....*....|....*....|....*.
gi 46592978 291 QCVYRGK---VCNLVPYLRDLGLNCP 313
Cdd:TIGR04521 220 KIVLDGTpreVFSDVDELEKIGLDVP 245
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
98-271 |
2.38e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 94.10 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL----------------PRDLRCFRKVSCY 158
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 159 IMQDDMLLPHLTVQE-AMMVSAHLKLQEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFF 237
Cdd:COG4598 100 VFQSFNLWSHMTVLEnVIEAPVHVLGRPKAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190
....*....|....*....|....*....|....
gi 46592978 238 DEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
77-293 |
5.66e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 77 RDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP------RDLR 150
Cdd:PRK10419 7 SGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQDDM--LLPHLTV----QEAMMvsaHLkLQEKDEGRREMVKEILTALGL-LSCANTRTGSLSGGQRKRLA 223
Cdd:PRK10419 86 AFRRDIQMVFQDSIsaVNPRKTVreiiREPLR---HL-LSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 224 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHqpSAKLFELFDQ-LYVLSQGQCV 293
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITH--DLRLVERFCQrVMVMDNGQIV 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
92-296 |
9.06e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 92 KGYK--TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGmkgAVLING-----LPRDLRCFRKVScYIMQD 162
Cdd:PRK10895 11 KAYKgrRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDedislLPLHARARRGIG-YLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 242
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46592978 243 GLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 296
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
98-306 |
1.00e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 91.37 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPRDLRCFRKVscYIMQDDMLLPHLTVQE--AM 175
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 176 MVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS- 254
Cdd:TIGR01184 78 AVDRVLPDLSKSE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEe 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46592978 255 LMKGLAQGGRSIICTIHQPSAKLFeLFDQLYVLSQGQCVYRGKVCNlVPYLR 306
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE-VPFPR 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
91-245 |
1.38e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.24 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 91 KKGYK--TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagyreTGM----KGAVLING-----LPRDLRC-------- 151
Cdd:COG1137 10 VKSYGkrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI-----VGLvkpdSGRIFLDGedithLPMHKRArlgigylp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 152 -----FRKvscyimqddmllphLTVQEAMMvsAHLKLQEKD-EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:COG1137 85 qeasiFRK--------------LTVEDNIL--AVLELRKLSkKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180
....*....|....*....|
gi 46592978 226 LELVNNPPVMFFDEPTSGLD 245
Cdd:COG1137 149 RALATNPKFILLDEPFAGVD 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
98-296 |
1.38e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.00 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY----RETGMKGAVLING------LPRDLRCFRKVSCYIMQDDMLLP 167
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTvqregrLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTVQEAMMVSA-------HLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:PRK09984 100 RLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 241 TSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 296
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
99-322 |
1.51e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 99 KGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE--TG--MKGAVLINGLPRDLRCFRKVscyiMQDDMLLPHLTVQEA 174
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGVGMV----FQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 175 MmvSAHLKLQEKDEG----RREMVKEILTALGLLscaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:PRK11000 96 M--SFGLKLAGAKKEeinqRVNQVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 251 Q----VVSLMKGLaqgGRSIICTIH-QPSAklFELFDQLYVLSQGQCVYRGKVCNLvpylrdlglncptYHNPAD-FV 322
Cdd:PRK11000 171 QmrieISRLHKRL---GRTMIYVTHdQVEA--MTLADKIVVLDAGRVAQVGKPLEL-------------YHYPANrFV 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-261 |
1.82e-20 |
|
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: 92.81 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL----MNILAGYRETGmkGAVLINGL---- 145
Cdd:COG0444 2 LEVRNLKVYFP-----TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGITS--GEILFDGEdllk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 --PRDLRCFR--KVScYIMQDDM--LLPHLTVQEAMM--VSAHLKLQEKDegRREMVKEILTALGLlSCANTRTGS---- 213
Cdd:COG0444 75 lsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQIAepLRIHGGLSKAE--ARERAIELLERVGL-PDPERRLDRyphe 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMKGLAQ 261
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiQA---QILNLLKDLQR 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
74-297 |
2.13e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLsysvpegpwwRKK-GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING--LPRDLR 150
Cdd:PRK13537 8 IDFRNV----------EKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGepVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQDDMLLPHLTVQEAMMV-SAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELV 229
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLLVfGRYFGLSAAAA--RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 230 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH-QPSAKlfELFDQLYVLSQGQCVYRGK 297
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHfMEEAE--RLCDRLCVIEEGRKIAEGA 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
88-297 |
2.49e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 88 WWRKKGyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP-----RDLRCFRKVSCYIMQD 162
Cdd:PRK13638 8 WFRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-QKGAVLWQGKPldyskRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 -DMLLPHLTVQEAMMVS-AHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:PRK13638 86 pEQQIFYTDIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 241 TSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGK 297
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGA 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
73-297 |
2.67e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLSYSVPEGPwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP-RDLR 150
Cdd:TIGR00958 478 LIEFQDVSFSYPNRP------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlYQPTG--GQVLLDGVPlVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 C---FRKVScyIMQDDMLLPHLTVQEAM----------MVSAHLKLQEKDEGRREMVKEILTALGllscantRTGS-LSG 216
Cdd:TIGR00958 550 HhylHRQVA--LVGQEPVLFSGSVRENIaygltdtpdeEIMAAAKAANAHDFIMEFPNGYDTEVG-------EKGSqLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 217 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKglaQGGRSIICTIHQPSakLFELFDQLYVLSQGQCVYRG 296
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKGSVVEMG 695
|
.
gi 46592978 297 K 297
Cdd:TIGR00958 696 T 696
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
74-296 |
2.83e-20 |
|
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: 88.52 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDL--RC 151
Cdd:cd03247 1 LSINNVSFSYPEQE-------QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 152 FRKVSCYIMQDdmllPHL---TVQEAMmvsahlklqekdeGRRemvkeiltalgllscantrtgsLSGGQRKRLAIALEL 228
Cdd:cd03247 73 LSSLISVLNQR----PYLfdtTLRNNL-------------GRR----------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYVLSQGQCVYRG 296
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
65-296 |
2.97e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.91 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 65 SLPRRAAVNIEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRetgmkGAVL 141
Cdd:PRK11174 341 ELASNDPVTIEAEDLEILSPDG--------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 142 INGLPR---DLRCFRKVSCYIMQDDmLLPHLTVQEAMMVSAHlklQEKDEG-----RREMVKEILTAL--GLLSCANTRT 211
Cdd:PRK11174 408 INGIELrelDPESWRKHLSWVGQNP-QLPHGTLRDNVLLGNP---DASDEQlqqalENAWVSEFLPLLpqGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 212 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTiHQpsakLFEL--FDQLYVLSQ 289
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ----LEDLaqWDQIWVMQD 558
|
....*..
gi 46592978 290 GQCVYRG 296
Cdd:PRK11174 559 GQIVQQG 565
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
93-329 |
3.37e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM-KGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTV 171
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgKITVLGVPVPARARLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMV-SAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:PRK13536 132 RENLLVfGRYFGMSTRE--IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 251 QVVSLMKGLAQGGRSIICTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVCNLVpylrDLGLNCPtyhnpadfVMEVASGE 329
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTHfMEEAE--RLCDRLCVLEAGRKIAEGRPHALI----DEHIGCQ--------VIEIYGGD 275
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
66-296 |
4.36e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 66 LPRRAAVNIEFRDLSYSVP--EGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTlmNILAGYRETGMKGAVLIN 143
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPirKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GLP------RDLRCFRKVSCYIMQD--DMLLPHLTVQEamMVSAHLKLQEKD---EGRREMVKEILTALGLLSCANTR-T 211
Cdd:PRK15134 346 GQPlhnlnrRQLLPVRHRIQVVFQDpnSSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 212 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQ 291
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
....*
gi 46592978 292 CVYRG 296
Cdd:PRK15134 504 VVEQG 508
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
98-293 |
6.06e-20 |
|
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: 87.10 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGlprdlrcfRKVScyimqddmllpHLTVQEAM- 175
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlYKPDS--GEILVDG--------KEVS-----------FASPRDARr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 176 ----MVSahlklQekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 251
Cdd:cd03216 75 agiaMVY-----Q-----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592978 252 VVSLMKGLAQGGRSIICTIHqpsaKLFELF---DQLYVLSQGQCV 293
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
74-297 |
6.13e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGL---PRDL 149
Cdd:PRK13632 8 IKVENVSFSYPNS-------ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGItisKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQD-DMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:PRK13632 79 KEIRKKIGIIFQNpDNQFIGATVEDDIAFG----LENKKVPPKKMkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSAKLfeLFDQLYVLSQGQCVYRGK 297
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQGK 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
74-297 |
6.25e-20 |
|
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: 89.52 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP-RDL--R 150
Cdd:cd03249 1 IEFKNVSFRYPSRP------DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGVDiRDLnlR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQDDMLL------------PHLTVQEAM----MVSAHLKLQEKDEGRREMVKEiltalgllscantRTGSL 214
Cdd:cd03249 74 WLRSQIGLVSQEPVLFdgtiaenirygkPDATDEEVEeaakKANIHDFIMSLPDGYDTLVGE-------------RGSQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 215 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVvslMKGL--AQGGRSIICTIHQPS----AklfelfDQLYVLS 288
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV---QEALdrAMKGRTTIVIAHRLStirnA------DLIAVLQ 211
|
....*....
gi 46592978 289 QGQCVYRGK 297
Cdd:cd03249 212 NGQVVEQGT 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
95-290 |
7.43e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP-RDLRCFRKVscyIMQDDMLLPHLTVQE 173
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPvEGPGAERGV---VFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 253
Cdd:PRK11248 90 NVAFGLQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 46592978 254 SLMKGLAQG-GRSIICTIHQPSAKLFeLFDQLYVLSQG 290
Cdd:PRK11248 169 TLLLKLWQEtGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
101-245 |
1.21e-19 |
|
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: 89.24 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGmkGAVLINGLP---------RDLRcfRKVSCYIMQDDMLLPHLT 170
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTS--GKVLIDGQDiaamsrkelRELR--RKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 171 VQEAmmVSAHLKLQ-EKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:cd03294 119 VLEN--VAFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
98-297 |
1.26e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.74 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETGMKGAVLINGLP------RDLRCFRkvsCYIMQDDMLLPhltv 171
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 qeAMMVSAHLKLQEKDEGRREMVK----EILTALGLLSCANTRTGSLSGG--QRKRLAIALELV---NNPP--VMFFDEP 240
Cdd:COG4138 83 --AMPVFQYLALHQPAGASSEAVEqllaQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 241 TSGLDSAScfQVV--SLMKGLAQGGRSIICTIHQPSAKLFELfDQLYVLSQGQCVYRGK 297
Cdd:COG4138 161 MNSLDVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGE 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
66-296 |
1.56e-19 |
|
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: 92.44 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 66 LPRRAAVNIEFRDLS--YSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL-MNILagyRETGMKGAVLI 142
Cdd:COG4172 268 VPPDAPPLLEARDLKvwFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL---RLIPSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 143 NGLP------RDLRCFRK---VscyIMQDDM--LLPHLTV----QEAMMVsahLKLQEKDEGRREMVKEILTALGLLscA 207
Cdd:COG4172 345 DGQDldglsrRALRPLRRrmqV---VFQDPFgsLSPRMTVgqiiAEGLRV---HGPGLSAAERRARVAEALEEVGLD--P 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 208 NTRT---GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIictihqpsAKLF------ 278
Cdd:COG4172 417 AARHrypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHGL--------AYLFishdla 487
|
250 260
....*....|....*....|.
gi 46592978 279 ---ELFDQLYVLSQGQCVYRG 296
Cdd:COG4172 488 vvrALAHRVMVMKDGKVVEQG 508
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
74-298 |
1.90e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG----YRETGMKGAVLING---LP 146
Cdd:PRK14247 4 IEIRDLKVSF---------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGqdiFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRCFRKVSCYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEGRREM---VKEILTALGLLSCANTR----TGSLSGGQR 219
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNLSIFEN--VALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPsAKLFELFDQLYVLSQGQCVYRGKV 298
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGPT 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
105-291 |
2.07e-19 |
|
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: 93.54 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 105 FNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLK 182
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGkdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 183 LQEKDEGRREMvKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG 262
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180
....*....|....*....|....*....
gi 46592978 263 GRSIICTIHQPSAKLfeLFDQLYVLSQGQ 291
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGR 1137
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
77-271 |
2.24e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.31 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 77 RDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLINGLPR---DLRCF- 152
Cdd:PRK10575 15 RNVSFRVPG---------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLeswSSKAFa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 153 RKVScYIMQDdmlLPH---LTVQEAMMVSA---HLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 226
Cdd:PRK10575 85 RKVA-YLPQQ---LPAaegMTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46592978 227 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIH 271
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
74-296 |
2.53e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.39 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS-----YSVPEG-------PWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAV 140
Cdd:cd03267 1 IEVSNLSksyrvYSKEPGligslksLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 141 LINGL-P--RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGG 217
Cdd:cd03267 79 RVAGLvPwkRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKR-LDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 218 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIH--QPSAKlfeLFDQLYVLSQGQCVY 294
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEA---LARRVLVIDKGRLLY 234
|
..
gi 46592978 295 RG 296
Cdd:cd03267 235 DG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
74-298 |
2.64e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLP---RDLR 150
Cdd:PRK13652 4 IETRDLCYSY--------SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL-KPTSGSVLIRGEPitkENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 228
Cdd:PRK13652 75 EVRKFVGLVFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 298
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
55-297 |
3.19e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 55 NNLTEAQ---RFS--SLPRRAAVNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA 129
Cdd:PRK11160 315 NEITEQKpevTFPttSTAAADQVSLTLNNVSFTYPDQP-------QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 130 GYRETGmKGAVLINGLPrdLRCFRkvscyimqDDMLLPHLTV--QEAMMVSAHLK---LQEKDEGRREMVKEILTALGLL 204
Cdd:PRK11160 388 RAWDPQ-QGEILLNGQP--IADYS--------EAALRQAISVvsQRVHLFSATLRdnlLLAAPNASDEALIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 205 SCANTRTG----------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQps 274
Cdd:PRK11160 457 KLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR-- 533
|
250 260
....*....|....*....|...
gi 46592978 275 AKLFELFDQLYVLSQGQCVYRGK 297
Cdd:PRK11160 534 LTGLEQFDRICVMDNGQIIEQGT 556
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
74-271 |
4.02e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyRETGM-KGAVLINGLP------ 146
Cdd:COG4604 2 IEIKNVSKRY---------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGLDvattps 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRcfRKVScyIM-QDDMLLPHLTVQEamMVS----AHLK--LQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQR 219
Cdd:COG4604 71 RELA--KRLA--ILrQENHINSRLTVRE--LVAfgrfPYSKgrLTAED---REIIDEAIAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIH 271
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
95-245 |
4.84e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.45 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLING-----LPRDLRcfrkvSCYI---MQDDML 165
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGkdvtkLPEYKR-----AKYIgrvFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 166 --LPHLTVQEAMMVSAH------LKLQEKDEgRREMVKEILTALGL-----LscaNTRTGSLSGGQRKRLAIALELVNNP 232
Cdd:COG1101 92 gtAPSMTIEENLALAYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLMATLTKP 167
|
170
....*....|...
gi 46592978 233 PVMFFDEPTSGLD 245
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
74-291 |
5.07e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 86.37 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP---RDL 149
Cdd:cd03248 12 VKFQNVTFAYPTRP------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfYQPQG--GQVLLDGKPisqYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQDDMLLPH---------LTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGllscanTRTGSLSGGQRK 220
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVG------EKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 221 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSakLFELFDQLYVLSQGQ 291
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLS--TVERADQILVLDGGR 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
98-296 |
8.55e-19 |
|
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: 85.65 E-value: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 173
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDiTKLPPHERARagiAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSahlkLQEKDEGRREMVKEILTALGLL-SCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL------DS 246
Cdd:TIGR03410 95 NLLTG----LAALPRRSRKIPDEIYELFPVLkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsiikDI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46592978 247 AscfQVVSLMKglAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:TIGR03410 171 G---RVIRRLR--AEGGMAIL-LVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
65-297 |
1.40e-18 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 90.19 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 65 SLPRRAAvNIEFRDLSYSV-PEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLIN 143
Cdd:TIGR01846 448 ALPELRG-AITFENIRFRYaPDSP--------EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVD 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GL------PRDLRcfRKVSCyIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltal 201
Cdd:TIGR01846 518 GVdlaiadPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAPFEHvihaAKLAGAHDFISELPQGYNTEVGE----- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 202 gllscantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELF 281
Cdd:TIGR01846 590 --------KGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLST--VRAC 658
|
250
....*....|....*.
gi 46592978 282 DQLYVLSQGQCVYRGK 297
Cdd:TIGR01846 659 DRIIVLEKGQIAESGR 674
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
98-245 |
2.17e-18 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 89.25 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLRCFRKVSCYIMQDDMLLP------- 167
Cdd:TIGR03797 469 LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDlagLDVQAVRRQLGVVLQNGRLMSgsifeni 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 ----HLTVQEAMMVSAHLKLqekDEGRREMvkeiltALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:TIGR03797 548 aggaPLTLDEAWEAARMAGL---AEDIRAM------PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
..
gi 46592978 244 LD 245
Cdd:TIGR03797 619 LD 620
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
74-296 |
2.52e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.73 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETgmKGAVLING-----L 145
Cdd:cd03217 1 LEIKDLHVSVGG---------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGeditdL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 PRDLRcFRKVSCYIMQDDMLLPHLTVQEAmmvsahlkLQEKDEGrremvkeiltalgllscantrtgsLSGGQRKRLAIA 225
Cdd:cd03217 70 PPEER-ARLGIFLAFQYPPEIPGVKNADF--------LRYVNEG------------------------FSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpsAKLFELF--DQLYVLSQGQCVYRG 296
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
74-314 |
2.99e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL----PRDL 149
Cdd:PRK13644 2 IRLENVSYSYPDG--------TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGIdtgdFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQD-DMLLPHLTVQEAMMVSAHLKLQEKDEGRReMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 228
Cdd:PRK13644 73 QGIRKLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpsakLFELF--DQLYVLSQGQCVYRGKVCNLV--PY 304
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN----LEELHdaDRIIVMDRGKIVLEGEPENVLsdVS 227
|
250
....*....|
gi 46592978 305 LRDLGLNCPT 314
Cdd:PRK13644 228 LQTLGLTPPS 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
74-245 |
5.59e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLIN-GLprdlrcf 152
Cdd:COG0488 316 LELEGLSKSYGD---------KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVKLGeTV------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 153 rKVScYIMQD-DMLLPHLTVQEAMMvsahlklQEKDEGRREMVKEILTALgLLS--CANTRTGSLSGGQRKRLAIALELV 229
Cdd:COG0488 379 -KIG-YFDQHqEELDPDKTVLDELR-------DGAPGGTEQEVRGYLGRF-LFSgdDAFKPVGVLSGGEKARLALAKLLL 448
|
170
....*....|....*.
gi 46592978 230 NNPPVMFFDEPTSGLD 245
Cdd:COG0488 449 SPPNVLLLDEPTNHLD 464
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
90-298 |
6.32e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.78 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDLRCFRKVScYimqddM---- 164
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPDS--GEVLWDGEPLDPEDRRRIG-Y-----Lpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 -LLPHLTVQEAMMVSAHLKLQEKDEGRREMvKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:COG4152 81 gLYPKMKVGEQLVYLARLKGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 244 LDSAScfqvVSLMKG----LAQGGRSIICTIHQ-PSAKlfELFDQLYVLSQGQCVYRGKV 298
Cdd:COG4152 160 LDPVN----VELLKDvireLAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSGSV 213
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
95-298 |
6.73e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 83.46 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLING-----LPRDLRCfRKVSCYIMQDDMLL 166
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsYEVTS--GTILFKGqdlleLEPDERA-RAGLFLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQEAMMVSAHLKLQEKDEGR------REMVKEILTALGL---LSCANTRTGsLSGGQRKRLAIALELVNNPPVMFF 237
Cdd:TIGR01978 90 PGVSNLEFLRSALNARRSARGEEPldlldfEKLLKEKLALLDMdeeFLNRSVNEG-FSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 238 DEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsaKLFELF--DQLYVLSQGQCVYRGKV 298
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSGDV 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
113-245 |
7.21e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 85.24 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 113 IMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPRDLRCFRKVscyiMQDDMLLPHLTVQEAmmVSAHLKLQEKD 187
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMRKVP 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 188 -EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:TIGR01187 74 rAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
98-293 |
1.26e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDlrcFRKVS-------CYIMQDDMLLPHL 169
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMR---FASTTaalaagvAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAMMVsAHL--KLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:PRK11288 95 TVAENLYL-GQLphKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCV 293
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGRYV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
109-291 |
1.27e-17 |
|
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: 84.78 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 109 ELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGlprdlRCF-------------RKVScYIMQDDMLLPHLTVQEam 175
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNG-----RTLfdsrkgiflppekRRIG-YVFQEARLFPHLSVRG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 176 mvsaHLKLQEKD---EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 252
Cdd:TIGR02142 95 ----NLRYGMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46592978 253 VSLMKGLAQG-GRSIICTIHQPSaKLFELFDQLYVLSQGQ 291
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQ-EVLRLADRVVVLEDGR 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
74-273 |
1.32e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.52 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP------- 146
Cdd:PRK10584 7 VEVHHLKKSVGQG-----EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 --RDLRCfRKVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:PRK10584 81 arAKLRA-KHVG-FVFQSFMLIPTLNALENVELPALLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQP 273
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
93-271 |
1.54e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFRKVSCYIM---QDDMLLPHL 169
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSARAASRRVAsvpQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEA--MMVSAHL-KLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:PRK09536 93 DVRQVveMGRTPHRsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180
....*....|....*....|....*
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
74-298 |
2.55e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.70 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS--YSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL--- 145
Cdd:PRK11153 2 IELKNISkvFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 ---PRDLRCFRKVSCYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKR 221
Cdd:PRK11153 71 alsEKELRKARRQIGMIFQHFNLLSSRTVFDN--VALPLELAGTPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 222 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPSA-KlfELFDQLYVLSQGQCVYRGKV 298
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVvK--RICDRVAVIDAGRLVEQGTV 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
90-261 |
3.90e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPrdLRCFRKVSCYIMQDDMLLPHL 169
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAmmVSAHLKLQEKDEGRremvkEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 249
Cdd:PRK11247 97 KVIDN--VGLGLKGQWRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170
....*....|..
gi 46592978 250 FQVVSLMKGLAQ 261
Cdd:PRK11247 170 IEMQDLIESLWQ 181
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
74-296 |
4.58e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGL---PRDLR 150
Cdd:PRK13647 5 IEVEDLHFRYKDG--------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 228
Cdd:PRK13647 76 WVRSKVGLVFQDpdDQVFSSTVWDDVAFGPVNMGLDKDEVERR--VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 229 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 296
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
100-245 |
4.92e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.19 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 100 GISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVL-----INGLPrDLRCFRKVSCYIMQDDMLLPHLTVQE 173
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILlrgqhIEGLP-GHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSAHLKLQE-------KDEGRREMVKEILT-------ALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDE 239
Cdd:PRK11300 100 NLLVAQHQQLKTglfsgllKTPAFRRAESEALDraatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
....*.
gi 46592978 240 PTSGLD 245
Cdd:PRK11300 180 PAAGLN 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
98-245 |
5.01e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.97 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScyiM--QDDMLLPHL 169
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RDIA---MvfQNYALYPHM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 170 TVQEAMmvsAH-LKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK11650 92 SVRENM---AYgLKIRgmPKAE-IEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
101-245 |
5.60e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLprDLRC---FRKVSCYIMQDDMLLPHLTVQEAMMV 177
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGV--DLSHvppYQRPINMMFQSYALFPHMTVEQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 178 SAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK11607 115 GLKQDKLPKAE-IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
98-246 |
5.99e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.85 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNS-------------GELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING--------LPRDLrcfrkvs 156
Cdd:PRK11432 9 LKNITKRFGSntvidnlnltikqGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDGedvthrsiQQRDI------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 157 CYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPV 234
Cdd:PRK11432 81 CMVFQSYALFPHMSLGEN--VGYGLKMLgvPKEE-RKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|..
gi 46592978 235 MFFDEPTSGLDS 246
Cdd:PRK11432 158 LLFDEPLSNLDA 169
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
65-291 |
6.93e-17 |
|
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: 84.41 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 65 SLPRRAAvNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLIN 143
Cdd:COG4618 323 PLPRPKG-RLSVENLTVVPPGSK-------RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvWPPTA--GSVRLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GlpRDLRCFRKVSC-----YIMQDDMLLPHlTVQE----------------AMMVSAHlklqekdegrrEMvkeILT-AL 201
Cdd:COG4618 393 G--ADLSQWDREELgrhigYLPQDVELFDG-TIAEniarfgdadpekvvaaAKLAGVH-----------EM---ILRlPD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 202 GLlscaNTRTGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSakL 277
Cdd:COG4618 456 GY----DTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--L 529
|
250
....*....|....
gi 46592978 278 FELFDQLYVLSQGQ 291
Cdd:COG4618 530 LAAVDKLLVLRDGR 543
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
108-271 |
7.26e-17 |
|
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: 79.89 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRdlRCFRKVSCYIMQDDML---LPhLTVQEAMMVS-----A 179
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGrtghiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 180 HLKLQEKDEGRreMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL 259
Cdd:TIGR03771 82 WLRRPCVADFA--AVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170
....*....|..
gi 46592978 260 AQGGRSIICTIH 271
Cdd:TIGR03771 160 AGAGTAILMTTH 171
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
98-267 |
2.09e-16 |
|
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: 79.02 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMN-ILAGYRETGmkGAVLI---NGL-------PRD---LRcfRKVSCYIMQdd 163
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVrhdGGWvdlaqasPREilaLR--RRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 mllpHLTV---QEAMMVSAH--LKLQEKDEGRREMVKEILTALGL------LSCANtrtgsLSGGQRKRLAIALELVNNP 232
Cdd:COG4778 101 ----FLRViprVSALDVVAEplLERGVDREEARARARELLARLNLperlwdLPPAT-----FSGGEQQRVNIARGFIADP 171
|
170 180 190
....*....|....*....|....*....|....*
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSII 267
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
93-291 |
2.14e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 82.78 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING--LPR-DLRCFRKVSCYIMQDDMLLPHL 169
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP-TSGSVRLDGadLKQwDRETFGKHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQ---------EAMMVSAHLKLQekdeGRREMvkeIL-------TALGllscanTRTGSLSGGQRKRLAIALELVNNPP 233
Cdd:TIGR01842 408 VAEniarfgenaDPEKIIEAAKLA----GVHEL---ILrlpdgydTVIG------PGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 234 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSakLFELFDQLYVLSQGQ 291
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
56-247 |
2.60e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.70 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 56 NLTEAQRFSSLprraavnIEFRDLSYSVPegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA-GYRET 134
Cdd:PRK13657 324 GAIDLGRVKGA-------VEFDDVSFSYD--------NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 135 GmkGAVLINGLP-RD--LRCFRKVSCYIMQDDMLLphltvqeAMMVSAHLKLQEKDEGRREMVK--EILTALGLL----S 205
Cdd:PRK13657 389 S--GRILIDGTDiRTvtRASLRRNIAVVFQDAGLF-------NRSIEDNIRVGRPDATDEEMRAaaERAQAHDFIerkpD 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46592978 206 CANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 247
Cdd:PRK13657 460 GYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
98-298 |
3.19e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDlRCFRKVSC-----YIMQDDMLLPHLTVQ 172
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVSAHLKlqEKDEG--------RREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 244
Cdd:PRK09700 99 ENLYIGRHLT--KKVCGvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46592978 245 DSASCFQVVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCVYRGKV 298
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
98-267 |
3.65e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPRDLRCFRK-VSCYI-M--QDDMLLPHLTVQ 172
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGlYQPD--SGEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 E----AMMVSAHLKLQEKDEgrREMVKEILTALGL---LscaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL- 244
Cdd:COG3845 99 EnivlGLEPTKGGRLDRKAA--RARIRELSERYGLdvdP---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLt 173
|
170 180
....*....|....*....|....*
gi 46592978 245 --DSASCFQVvslMKGLAQGGRSII 267
Cdd:COG3845 174 pqEADELFEI---LRRLAAEGKSII 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
74-291 |
3.98e-16 |
|
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: 77.51 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRKKgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETG-MKGAVLINGlprdlrcf 152
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF----TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPG-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 153 rKVScyimqddmllphLTVQEAMMVSAHLK-----LQEKDEgrrEMVKEILTAlgllsCA------------NTRTG--- 212
Cdd:cd03250 67 -SIA------------YVSQEPWIQNGTIRenilfGKPFDE---ERYEKVIKA-----CAlepdleilpdgdLTEIGekg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 213 -SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA-------SCFQvvslmkGLAQGGRSIICTIHQPSakLFELFDQL 284
Cdd:cd03250 126 iNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvgrhifeNCIL------GLLLNNKTRILVTHQLQ--LLPHADQI 197
|
....*..
gi 46592978 285 YVLSQGQ 291
Cdd:cd03250 198 VVLDNGR 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
74-245 |
4.44e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS--YSVPEGP----------WWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagyreTGM----K 137
Cdd:COG4586 2 IEVENLSktYRVYEKEpglkgalkglFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML-----TGIlvptS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 138 GAVLINGL-P-RDLRCFRK---VscyIM-QDDMLLPHLTVQEAMMVSAHL-KLQEKD-EGRREMVKEILTALGLLscaNT 209
Cdd:COG4586 77 GEVRVLGYvPfKRRKEFARrigV---VFgQRSQLWWDLPAIDSFRLLKAIyRIPDAEyKKRLDELVELLDLGELL---DT 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 46592978 210 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
92-273 |
7.41e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.77 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 92 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG--YRETGmkgAVLINGLP-RDLR-CFRKVSCYIMQDDMLLP 167
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRdEYHQDLLYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTVQEAMMVSAHLKlqekDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 247
Cdd:PRK13538 88 ELTALENLRFYQRLH----GPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....*.
gi 46592978 248 SCFQVVSLMKGLAQGGRSIICTIHQP 273
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
96-296 |
1.57e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 96 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY---------------RETGMKGAVLINGLPRDLRCF---RKVSC 157
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyiGDKKNNHELITNPYSKKIKNFkelRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 158 YIMQ-DDMLLPHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLSCANTRTG-SLSGGQRKRLAIALELVNNPPVM 235
Cdd:PRK13631 120 MVFQfPEYQLFKDTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 236 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCVYRG 296
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
74-271 |
1.69e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLM---NIL----------AGYR---ETGMK 137
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKG----LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALlkpssgtitiAGYHitpETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 138 GAvlinglpRDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGL-LSCANTRTGSLSG 216
Cdd:PRK13641 79 NL-------KKLR--KKVSLVFQFPEAQLFENTVLKDVEFGP-KNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 217 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
69-296 |
2.23e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 69 RAAVNIEFRDLSYSVP--EGPwwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLp 146
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPgkEVP---------ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI-DEGEILLDGH- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 rDLRcfrkvscyimqdDMLLPHLTVQEAMmVSAHLKL-----------QEKDEGRREmvkEILTAlGLLSCA-------- 207
Cdd:PRK11176 406 -DLR------------DYTLASLRNQVAL-VSQNVHLfndtianniayARTEQYSRE---QIEEA-ARMAYAmdfinkmd 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 208 ---NTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIICTIHQPSAklFEL 280
Cdd:PRK11176 468 nglDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEK 544
|
250
....*....|....*.
gi 46592978 281 FDQLYVLSQGQCVYRG 296
Cdd:PRK11176 545 ADEILVVEDGEIVERG 560
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
73-248 |
2.83e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 75.22 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLS--YSvPEGPWwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---- 146
Cdd:cd03244 2 DIEFKNVSlrYR-PNLPP--------VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-SSGSILIDGVDiski 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 --RDLRcfRKVSCyIMQDDMLL---------PHLTVQEAMMVSA----HLKlqekdegrrEMVKEILTALGLLSCANtrT 211
Cdd:cd03244 72 glHDLR--SRISI-IPQDPVLFsgtirsnldPFGEYSDEELWQAlervGLK---------EFVESLPGGLDTVVEEG--G 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 46592978 212 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 248
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
112-248 |
3.10e-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: 77.83 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 112 AIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLRCF-----RKVScYIMQDDMLLPHLTVQEammvsaHLKL 183
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------NLLY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 184 QEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 248
Cdd:COG4148 101 GRKRAPRAERrisFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
93-271 |
3.25e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------LPRDLRCFRKVSCYIMQDDMLL 166
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
95-296 |
3.67e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET-----GMKGAVLING---LPRDLRCFRKVSCYIMQDDMLL 166
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskiKVDGKVLYFGkdiFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQE--AMMVSAHlKLQEKDEGRReMVKEILTALGLLSCANTRTGS----LSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:PRK14246 103 PHLSIYDniAYPLKSH-GIKEKREIKK-IVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 241 TSGLDSASCFQVVSLMKGLaQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQ-QVARVADYVAFLYNGELVEWG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
98-293 |
6.03e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLINGlpRDL------RCFRKVSCYIMQDDMLLPHLT 170
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpRAT--SGRIVFDG--KDItdwqtaKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 171 VQEAMMVSAHLKLQEKDEGRREMVKEILTALglLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592978 251 QVVSLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQCV 293
Cdd:PRK11614 175 QIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
74-313 |
8.51e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 8.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGMKGAVLINGLPR---- 147
Cdd:PRK13640 6 VEFKHVSFTYPDSK-------KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGITLtakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 --DLRcfRKVSCYIMQDDMLLPHLTVQEAMMvsahLKLQEKDEGRREMVK---EILTALGLLSCANTRTGSLSGGQRKRL 222
Cdd:PRK13640 79 vwDIR--EKVGIVFQNPDNQFVGATVGDDVA----FGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 223 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSAKlfELFDQLYVLSQGQCVYRG---KV 298
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGspvEI 230
|
250
....*....|....*
gi 46592978 299 CNLVPYLRDLGLNCP 313
Cdd:PRK13640 231 FSKVEMLKEIGLDIP 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
98-297 |
9.73e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPrdlrCFR-------KVSCYIM-QDDMLLPHL 169
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNP----CARltpakahQLGIYLVpQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAMMvsahLKLQeKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 249
Cdd:PRK15439 102 SVKENIL----FGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592978 250 FQVVSLMKGLAQGGRSIICTIHqpsaKLFE---LFDQLYVLSQGQCVYRGK 297
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISH----KLPEirqLADRISVMRDGTIALSGK 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
63-296 |
1.42e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 63 FSSLPRRAavnieFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLI 142
Cdd:PRK10070 14 FGEHPQRA-----FKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 143 NGLP---------RDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGS 213
Cdd:PRK10070 88 DGVDiakisdaelREVR--RKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEE-RREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQC 292
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEV 243
|
....
gi 46592978 293 VYRG 296
Cdd:PRK10070 244 VQVG 247
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
74-326 |
2.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRkkgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLR 150
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQD-DMLLPHLTVQ-------EAMMVSaHLKLQEKdegrremVKEILTALGLLSCANTRTGSLSGGQRKRL 222
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVKydvafglENHAVP-YDEMHRR-------VSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 223 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELfDQLYVLSQGQCVYRGK---VC 299
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTpteIF 230
|
250 260
....*....|....*....|....*..
gi 46592978 300 NLVPYLRDLGLNCPtyhnpadFVMEVA 326
Cdd:PRK13648 231 DHAEELTRIGLDLP-------FPIKIN 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
74-315 |
3.82e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.54 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP------- 146
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKA----LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGVDitdkkvk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 -RDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVS-AHLKLQEKDEGRRemVKEILTALGLlSCANTRTGS---LSGGQRKR 221
Cdd:PRK13637 78 lSDIR--KKVGLVFQYPEYQLFEETIEKDIAFGpINLGLSEEEIENR--VKRAMNIVGL-DYEDYKDKSpfeLSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 222 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGK---V 298
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTpreV 232
|
250
....*....|....*....
gi 46592978 299 CNLVPYLRDLGLNCP--TY 315
Cdd:PRK13637 233 FKEVETLESIGLAVPqvTY 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
96-271 |
4.07e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 96 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFRKVSCYIMQD---DMLLPHLTVQ 172
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVS-AHLKLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:PRK15056 100 VVMMGRyGHMGWLRRAKKRdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|.
gi 46592978 251 QVVSLMKGLAQGGRSIICTIH 271
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTH 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
101-297 |
4.24e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYreTGMKGAVLINGLP------RDLRCFRkvsCYIMQDDMLLPHLTVQEA 174
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGSGSIQFAGQPleawsaAELARHR---AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 175 MMVSAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSA 247
Cdd:PRK03695 90 LTLHQPDKTRTEAV--ASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592978 248 scfQVV---SLMKGLAQGGRSIICTIHQPSAKLFELfDQLYVLSQGQCVYRGK 297
Cdd:PRK03695 168 ---QQAaldRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGR 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
73-296 |
6.28e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 75.16 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 73 NIEFRDLSYSVpegpwwrkkGY-KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPR---D 148
Cdd:TIGR01193 473 DIVINDVSYSY---------GYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRCFRKVSCYIMQDDMLLPHlTVQEAMMVSAHLKLQEKDEGRREMVKEILT-----ALGLLSCANTRTGSLSGGQRKRLA 223
Cdd:TIGR01193 543 RHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDdienmPLGYQTELSEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 224 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQggRSIICTIHQPSakLFELFDQLYVLSQGQCVYRG 296
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQG 690
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
95-269 |
8.32e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNIL-------AGYRETGmkgAVLINGLP----RDLRCFRKVSCYIMQDD 163
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 MLLPHLTVQEAMM-VSAHlKLQEKDEgRREMVKEILTALGLLSCANTRTGS----LSGGQRKRLAIALELVNNPPVMFFD 238
Cdd:PRK14271 111 NPFPMSIMDNVLAgVRAH-KLVPRKE-FRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190
....*....|....*....|....*....|.
gi 46592978 239 EPTSGLDSASCFQVVSLMKGLAQGGRSIICT 269
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
93-290 |
1.30e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.81 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScYIMQDDMLL 166
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQEAmmVSAHLKLQEKDEgR------REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:PRK10851 87 RHMTVFDN--IAFGLTVLPRRE-RpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 241 TSGLDSascfQV-VSLMKGLAQGGR-----SIICTIHQPSAklFELFDQLYVLSQG 290
Cdd:PRK10851 164 FGALDA----QVrKELRRWLRQLHEelkftSVFVTHDQEEA--MEVADRVVVMSQG 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
93-274 |
1.72e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMN----ILAGYRETGMKGAVLINGL--------PRDLRcfRKVScYIM 160
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGRniyspdvdPIEVR--REVG-MVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 161 QDDMLLPHLTVQEAmmVSAHLKLQEKDEGRREMVKEILTALGLLSC-------ANTRTGSLSGGQRKRLAIALELVNNPP 233
Cdd:PRK14267 92 QYPNPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46592978 234 VMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPS 274
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
98-291 |
1.91e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLP------RDLRcfRKVSCYIMQDDMLLPHLT 170
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEElqasniRDTE--RAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 171 VQEAMMVSAhlklqEKDEGRR----EMV---KEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:PRK13549 99 VLENIFLGN-----EITPGGImdydAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592978 244 LDSASCFQVVSLMKGLAQGGRSIICTIHqpsaKLFELF---DQLYVLSQGQ 291
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHGIACIYISH----KLNEVKaisDTICVIRDGR 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
99-291 |
2.22e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 99 KGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL---PRD-LRCFRKVSCYIMQ---DDMLLPHLTV 171
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRSpLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSAHLKL----------QEKDEGR-REMVKEILTalglLSCA--NTRTGSLSGGQRKRLAIALELVNNPPVMFFD 238
Cdd:PRK09700 359 AQNMAISRSLKDggykgamglfHEVDEQRtAENQRELLA----LKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 239 EPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFELF---DQLYVLSQGQ 291
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
98-261 |
3.98e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTL------MNILagYRETGMKGAVLINGL--------PRDLRcfRKVScYIMQDD 163
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDL--IPGARVEGEILLDGEdiydpdvdVVELR--RRVG-MVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 MLLPHlTVQEAmmVSAHLKLQE-KDegRREM---VKEILTALGL-------LscaNTRTGSLSGGQRKRLAIALELVNNP 232
Cdd:COG1117 102 NPFPK-SIYDN--VAYGLRLHGiKS--KSELdeiVEESLRKAALwdevkdrL---KKSALGLSGGQQQRLCIARALAVEP 173
|
170 180
....*....|....*....|....*....
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLAQ 261
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKK 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
74-291 |
4.57e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.10 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS--YSVPEGPWWRKK-----------GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGA 139
Cdd:cd03220 1 IELENVSksYPTYKGGSSSLKklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 140 VLINGlprdlrcfrKVSCYIMQDDMLLPHLTVQE-AMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQ 218
Cdd:cd03220 79 VTVRG---------RVSSLLGLGGGFNPELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 219 RKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQ 291
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGK 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
54-291 |
4.96e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 54 DNNLTEAQRFSSLPRRAAVN----IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA 129
Cdd:COG4178 339 EEALEAADALPEAASRIETSedgaLALEDLTLRTPDG--------RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 130 GYRETGmKGAVLingLPRDLRCfrkvscyimqddMLLPhltvQEAMMVSAHLKLQ-----EKDEGRREMVKEILTALGL- 203
Cdd:COG4178 411 GLWPYG-SGRIA---RPAGARV------------LFLP----QRPYLPLGTLREAllypaTAEAFSDAELREALEAVGLg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 204 -----LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGrSIICTIHQPSakLF 278
Cdd:COG4178 471 hlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRST--LA 547
|
250
....*....|...
gi 46592978 279 ELFDQLYVLSQGQ 291
Cdd:COG4178 548 AFHDRVLELTGDG 560
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
87-271 |
8.57e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 87 PWWRKKGYKTLlKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMK----GAVLINGLPRDLRCFRKVSCYIMQ 161
Cdd:PRK15079 27 FWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEvawlGKDLLGMKDDEWRAVRSDIQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 162 DDM--LLPHLTVQEAM---MVSAHLKLQeKDEgRREMVKEILTALGLL-SCANTRTGSLSGGQRKRLAIALELVNNPPVM 235
Cdd:PRK15079 106 DPLasLNPRMTIGEIIaepLRTYHPKLS-RQE-VKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 46592978 236 FFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIH 271
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAH 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
96-293 |
9.14e-13 |
|
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: 71.01 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 96 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLP------RDLRcfRKVSCYIMQDDMLLPH 168
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPlkasniRDTE--RAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQEAMMVSAHLKLQEKDEGRREMV---KEILTALGLLSCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 244
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAYNAMYlraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46592978 245 DSASCFQVVSLMKGLAQGGRSIICTIHqpsaKLFE---LFDQLYVLSQGQCV 293
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
74-297 |
1.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEG-PWWRKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLP------ 146
Cdd:PRK13649 3 INLQNVSYTYQAGtPFEGRA-----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDTLitstsk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 -RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRreMVKEILTALGLLSCANTRTG-SLSGGQRKRL 222
Cdd:PRK13649 77 nKDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEA--LAREKLALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 223 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGK 297
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
74-245 |
1.28e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSvpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING-----LPRD 148
Cdd:PRK11831 8 VDMRGVSFT---------RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipaMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 -LRCFRKVSCYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDEGRREMVKeiLTALGLLSCANTRTGSLSGGQRKRLAIA 225
Cdd:PRK11831 78 rLYTVRKRMSMLFQSGALFTDMNVFDnvAYPLREHTQLPAPLLHSTVMMK--LEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180
....*....|....*....|
gi 46592978 226 LELVNNPPVMFFDEPTSGLD 245
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQD 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
101-291 |
1.48e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLR----CFRKVSCYIMQD---DMLLPHLTVQE 173
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnpaqAIRAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSA---HLKLQEKDEGRREmvKEILTALGLLSCANTR----TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:TIGR02633 359 NITLSVlksFCFKMRIDAAAEL--QIIGSAIQRLKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQ 291
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
447-661 |
1.51e-12 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 66.76 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 447 MLFLMFAALMPTVLTF--PLEMGVFlrEHLNYW-YSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFA 523
Cdd:COG0842 11 AMSLLFTALMLTALSIarEREQGTL--ERLLVTpVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 524 ALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGldr 603
Cdd:COG0842 89 LVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG--- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 604 edlhcdidetchfqkseailrelDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRA 661
Cdd:COG0842 166 -----------------------GAGLADVWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
98-291 |
1.58e-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: 66.30 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDLRCFRKVS----CYIMQD---DMLLPHLT 170
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDAIragiAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 171 VQEAMMVSAHLklqekdegrremvkeiltalgllscantrtgslSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:cd03215 95 VAENIALSSLL---------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 251 QVVSLMKGLAQGGRSIICTihqpSAKLFELF---DQLYVLSQGQ 291
Cdd:cd03215 142 EIYRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEGR 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
107-271 |
1.81e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 67.78 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 107 SGELVAIMGPSGAGKSTLMNILAG--------------YRE--TGMKGAVLINGLPR----DLRCFRKVscyimQDDMLL 166
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdWDEilDEFRGSELQNYFTKllegDVKVIVKP-----QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PhltvqEAMMVSAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:cd03236 100 P-----KAVKGKVGELLKKKDE--RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
74-296 |
1.93e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFR 153
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 KVSC---YIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLL-SCANTRTGSLSGGQRKRLAIALE 227
Cdd:PRK15112 84 YRSQrirMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592978 228 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIICTIHQPSAKlfELFDQLYVLSQGQCVYRG 296
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
93-318 |
2.10e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLPRDLRCFRKVSCYI---MQDDMLLPHL 169
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIgllAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 TVQEAMMVSAH------LKLQEKDEgrrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:PRK10253 97 TVQELVARGRYphqplfTRWRKEDE---EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 244 LDSASCFQVVSLMKGL-AQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGKVCNLV-PYL--RDLGLNCPTYHNP 318
Cdd:PRK10253 174 LDISHQIDLLELLSELnREKGYTLAAVLHDLN-QACRYASHLIALREGKIVAQGAPKEIVtAELieRIYGLRCMIIDDP 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
74-313 |
2.17e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP------- 146
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQA----IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP-TTGTVTVDDITithktkd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKL---QEKDEGRRemvkeILTALGLlsCANTRTGS---LSGGQ 218
Cdd:PRK13646 78 KYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnldEVKNYAHR-----LLMDLGF--SRDVMSQSpfqMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 219 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGK 297
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTS 229
|
250
....*....|....*....
gi 46592978 298 VCNLV---PYLRDLGLNCP 313
Cdd:PRK13646 230 PKELFkdkKKLADWHIGLP 248
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
74-298 |
2.31e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS--YSVPEGPWWR-----------KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGA 139
Cdd:COG1134 5 IEVENVSksYRLYHEPSRSlkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--SGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 140 VLINGlprdlrcfrKVSCyimqddmLL-------PHLTVQE-AMMVSAHLKLQEKDEgrREMVKEIL--TALGllSCANT 209
Cdd:COG1134 83 VEVNG---------RVSA-------LLelgagfhPELTGREnIYLNGRLLGLSRKEI--DEKFDEIVefAELG--DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 210 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVL 287
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWL 219
|
250
....*....|.
gi 46592978 288 SQGQCVYRGKV 298
Cdd:COG1134 220 EKGRLVMDGDP 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
98-271 |
2.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTL---MNIL----AGYRE-----------TGMKGAVLIN---GLPR--------D 148
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdTGTIEwifkdeknkkkTKEKEKVLEKlviQKTRfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRrEMVKEILTALGL-LSCANTRTGSLSGGQRKRLAIALE 227
Cdd:PRK13651 103 IR--RRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAK-KRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 228 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
74-296 |
2.52e-12 |
|
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: 69.85 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYsvpegpwwrkkGY---KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGlpRDL 149
Cdd:COG5265 358 VRFENVSF-----------GYdpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfYDVTS--GRILIDG--QDI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 R-----CFRKVSCYIMQDDMLL------------PHLT---VQEAMMvSAHL-----KLQEKDE---GRRemvkeiltal 201
Cdd:COG5265 423 RdvtqaSLRAAIGIVPQDTVLFndtiayniaygrPDASeeeVEAAAR-AAQIhdfieSLPDGYDtrvGER---------- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 202 GLlscantrtgSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIIctI-HQPS----Ak 276
Cdd:COG5265 492 GL---------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV--IaHRLStivdA- 559
|
250 260
....*....|....*....|
gi 46592978 277 lfelfDQLYVLSQGQCVYRG 296
Cdd:COG5265 560 -----DEILVLEAGRIVERG 574
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
77-261 |
3.38e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 77 RDL--SYSVPEGPWwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgYRETGMKGAVLINGLP-------- 146
Cdd:PRK11308 9 IDLkkHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPTGGELYYQGQDllkadpea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 -RDLRcfRKVScYIMQDDM--LLPHLTV----QEAMMVSAHLKLQEkdegRREMVKEILTALGLLSCANTRTGSL-SGGQ 218
Cdd:PRK11308 87 qKLLR--QKIQ-IVFQNPYgsLNPRKKVgqilEEPLLINTSLSAAE----RREKALAMMAKVGLRPEHYDRYPHMfSGGQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592978 219 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 261
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
93-261 |
4.34e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.72 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTL------MNILAgyRETGMKGAVLING----LPR-DLRCFRKVSCYIMQ 161
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGhniySPRtDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 162 DDMLLPhLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTG----SLSGGQRKRLAIALELVNNPPVMFF 237
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180
....*....|....*....|....
gi 46592978 238 DEPTSGLDSASCFQVVSLMKGLAQ 261
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKD 196
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
74-249 |
4.40e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.01 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLPRdlrcfr 153
Cdd:cd03221 1 IELENLSKTY---------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 kvSCYIMQddmllphltvqeammvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVNNPP 233
Cdd:cd03221 65 --IGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170
....*....|....*.
gi 46592978 234 VMFFDEPTSGLDSASC 249
Cdd:cd03221 91 LLLLDEPTNHLDLESI 106
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
107-267 |
4.62e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.04 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 107 SGELVAIMGPSGAGKSTLMNILAG---------------------YRETGMKG--AVLINGlprDLRCFRKVScYImqdD 163
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrFRGTELQDyfKKLANG---EIKVAHKPQ-YV---D 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 MLLPHL--TVQEammvsahlkLQEK-DEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:COG1245 171 LIPKVFkgTVRE---------LLEKvDE--RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180
....*....|....*....|....*..
gi 46592978 241 TSGLDSASCFQVVSLMKGLAQGGRSII 267
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
74-313 |
5.29e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.96 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPR----- 147
Cdd:PRK13635 6 IRVEHISFRYPDAA-------TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPE--AGTITVGGMVLseetv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 -DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREMVKEILTAL---GLLSCANTRTGSLSGGQRKRLA 223
Cdd:PRK13635 77 wDVR--RQVGMVFQNPDNQFVGATVQDDVAFG----LENIGVPREEMVERVDQALrqvGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 224 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIH--QPSAKLfelfDQLYVLSQGQCVYRG---K 297
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHdlDEAAQA----DRVIVMNKGEILEEGtpeE 226
|
250
....*....|....*.
gi 46592978 298 VCNLVPYLRDLGLNCP 313
Cdd:PRK13635 227 IFKSGHMLQEIGLDVP 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
74-298 |
6.27e-12 |
|
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: 68.56 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKS-TLMNI--LAGYRETGMKGAVLINGL----- 145
Cdd:COG4172 7 LSVEDLSVAFGQG-----GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 -PRDLRCFR--KVSCyIMQDDM--LLPHLTV--QEAMMVSAHLKLQEKDegRREMVKEILTALGLLScANTRTGS----L 214
Cdd:COG4172 82 sERELRRIRgnRIAM-IFQEPMtsLNPLHTIgkQIAEVLRLHRGLSGAA--ARARALELLERVGIPD-PERRLDAyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 215 SGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMKGL-AQGGRSIictihqpsakLF---------ELF 281
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDvtvQA---QILDLLKDLqRELGMAL----------LLithdlgvvrRFA 224
|
250
....*....|....*..
gi 46592978 282 DQLYVLSQGQCVYRGKV 298
Cdd:COG4172 225 DRVAVMRQGEIVEQGPT 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
74-340 |
8.88e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSV-PEGPWWRKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL------- 145
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASRA-----LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP-TEGKVTVGDIvvsstsk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 146 PRDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQeKDEGRReMVKEILTALGLLSCANTRTG-SLSGGQRKRL 222
Cdd:PRK13643 76 QKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIP-KEKAEK-IAAEKLEMVGLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 223 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGKVCNL- 301
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVf 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 46592978 302 --VPYLRDLGLNCPTYHNPADFVMEvaSGEYGDQNSRLVRA 340
Cdd:PRK13643 233 qeVDFLKAHELGVPKATHFADQLQK--TGAVTFEKLPITRA 271
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
95-245 |
1.71e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLPRDlrcfrkvscyimqddmllphltvQE 173
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVDVPDNQFG-----------------------RE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 174 AMMVSAHLKLQEKDEgrremVKEILTALGLLSCANTRT--GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:COG2401 100 ASLIDAIGRKGDFKD-----AVELLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
106-245 |
2.81e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 106 NSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLklqe 185
Cdd:PRK13543 35 DAGEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 186 kdEGRR--EMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK13543 110 --HGRRakQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
74-298 |
2.93e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMKGAVLING-----LPR 147
Cdd:CHL00131 8 LEIKNLHASVNE---------NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGesildLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRCFRKVsCYIMQDDMLLPHLTVQEAMMVS--AHLKLQEKDEGRR----EMVKEILTALGL----LScANTRTGsLSGG 217
Cdd:CHL00131 79 EERAHLGI-FLAFQYPIEIPGVSNADFLRLAynSKRKFQGLPELDPleflEIINEKLKLVGMdpsfLS-RNVNEG-FSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 218 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsaKLFELF--DQLYVLSQGQCVYR 295
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKT 233
|
...
gi 46592978 296 GKV 298
Cdd:CHL00131 234 GDA 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
98-267 |
3.01e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--REtgmKGAVLINGLPRDLRC----FRKVSCYIMQD---DMLLPH 168
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAlpRT---SGYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLSCANTRT-------GSLSGGQRKRLAIALELVNNPPVMFFDEPT 241
Cdd:PRK10762 345 MSVKENMSLTA-LRYFSRAGGSLKHADEQQAVSDFIRLFNIKTpsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180
....*....|....*....|....*.
gi 46592978 242 SGLDSASCFQVVSLMKGLAQGGRSII 267
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
108-296 |
3.56e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLinglprdlrcfrkvscYIMQDDMLLPHLTVQEA------------- 174
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSA-RLAPDAGEVH----------------YRMRDGQLRDLYALSEAerrrllrtewgfv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 175 ---------MMVSAhlklqekdeGRRemVKEILTALGLLSCANTRT--------------------GSLSGGQRKRLAIA 225
Cdd:PRK11701 95 hqhprdglrMQVSA---------GGN--IGERLMAVGARHYGDIRAtagdwlerveidaariddlpTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 226 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPS-AKLfeLFDQLYVLSQGQCVYRG 296
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAvARL--LAHRLLVMKQGRVVESG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
97-272 |
3.57e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 97 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQE 173
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERqsIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMMVSAHLKlqekdEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 253
Cdd:PRK13540 94 NCLYDIHFS-----PGAVG-ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 46592978 254 SLMKGLAQGGRSIICTIHQ 272
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQ 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
108-271 |
5.31e-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: 66.19 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQE 185
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGksILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 186 KDEGRReMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRS 265
Cdd:TIGR01257 2044 AEEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRA 2122
|
....*.
gi 46592978 266 IICTIH 271
Cdd:TIGR01257 2123 VVLTSH 2128
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
95-313 |
6.90e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.57 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILAgyreTGMKGAVLINGL----PRDLRCFRKVSCYIMQ--DDML 165
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL----IPSEGKVYVDGLdtsdEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 166 LPHLTVQEAMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK13633 99 VATIVEEDVAFGPENLGIPPEE--IRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592978 246 SASCFQVVSLMKGL-AQGGRSIICTIH--QPSAKLfelfDQLYVLSQGQCVYRG---KVCNLVPYLRDLGLNCP 313
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGtpkEIFKEVEMMKKIGLDVP 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
106-271 |
8.38e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 106 NSGELVAIMGPSGAGKS----TLMNILAGYRETGmkGAVLING-----LP-RDLRCFR--KVScYIMQDDM--LLPHLTV 171
Cdd:PRK09473 40 RAGETLGIVGESGSGKSqtafALMGLLAANGRIG--GSATFNGreilnLPeKELNKLRaeQIS-MIFQDPMtsLNPYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAMMVSAHL-KLQEKDEGRREMVKeILTALGLLScANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:PRK09473 117 GEQLMEVLMLhKGMSKAEAFEESVR-MLDAVKMPE-ARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180
....*....|....*....|....*.
gi 46592978 247 ASCFQVVSLMKGLAQG-GRSIICTIH 271
Cdd:PRK09473 195 TVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
97-298 |
9.76e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 97 LLKGISGKFNSGELVAIMGPSGAGKS----TLMNIL-AGYRETGmkGAVLING---LPRDLRCfRKVSCyIMQDdmllPH 168
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGkpvAPCALRG-RKIAT-IMQN----PR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQEAMMVSAHLK---LQEKDEGRREMVKEILTALGLlscANTRT------GSLSGGQRKRLAIALELVNNPPVMFFDE 239
Cdd:PRK10418 90 SAFNPLHTMHTHARetcLALGKPADDATLTAALEAVGL---ENAARvlklypFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 240 PTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 298
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDV 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
74-248 |
1.04e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 61.66 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLS--YSvPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLmnILAGYRET-GMKGAVLINGLP---- 146
Cdd:cd03369 7 IEVENLSvrYA-PDLP--------PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDisti 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 147 --RDLRcfRKVSCyIMQDDMLLphltvqeamMVSAHLKLQEKDEGRREmvkEILTALGLLSCANtrtgSLSGGQRKRLAI 224
Cdd:cd03369 76 plEDLR--SSLTI-IPQDPTLF---------SGTIRSNLDPFDEYSDE---EIYGALRVSEGGL----NLSQGQRQLLCL 136
|
170 180
....*....|....*....|....
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSAS 248
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYAT 160
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
176-301 |
1.95e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 176 MVSAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 255
Cdd:NF000106 109 MIGR*LDLSRKDA--RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 46592978 256 MKGLAQGGRSIICTIhQPSAKLFELFDQLYVLSQGQCVYRGKVCNL 301
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
74-288 |
1.98e-10 |
|
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: 59.86 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVlinGLPRDlrcfr 153
Cdd:cd03223 1 IELENLSLATPDG--------RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 154 kvscyimQDDMLLPhltvQEAMMVSAHLKLQekdegrremvkeILTALGLLscantrtgsLSGGQRKRLAIALELVNNPP 233
Cdd:cd03223 64 -------EDLLFLP----QRPYLPLGTLREQ------------LIYPWDDV---------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 234 VMFFDEPTSGLDSASCFQVVSLMKGLaqgGRSIICTIHQPSakLFELFDQLYVLS 288
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPS--LWKFHDRVLDLD 161
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
74-245 |
3.05e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSV-PEGPWWRKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLI-------NG 144
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRA-----LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPT--SGTVTIgervitaGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 145 LPRDLRCFRKVSCYIMQddmlLP-HLTVQEAMmvsahlklqEKD------------EGRREMVKEILTALGLLSCANTRT 211
Cdd:PRK13634 76 KNKKLKPLRKKVGIVFQ----FPeHQLFEETV---------EKDicfgpmnfgvseEDAKQKAREMIELVGLPEELLARS 142
|
170 180 190
....*....|....*....|....*....|....*
gi 46592978 212 G-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK13634 143 PfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
98-245 |
3.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPR------DLRcfRKVSCYIMQDDMLLPHLTV 171
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLtaenvwNLR--RKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 172 QEAMMvsahLKLQEKDEGRREMVK---EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK13642 100 EDDVA----FGMENQGIPREEMIKrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
107-277 |
3.25e-10 |
|
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: 58.92 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 107 SGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGlprdlrcfrkvscyimqddmllphltvqeammvsahlklqek 186
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 187 degrrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMKGLA 260
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 46592978 261 QGGRSIICTIHQPSAKL 277
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
108-262 |
3.39e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAG--------YRETGMKGAV---------------LINGlprDLRCFRKVScYImqdDm 164
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVlkrfrgtelqnyfkkLYNG---EIKVVHKPQ-YV---D- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 LLPHL---TVQEAmmvsahlkLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 241
Cdd:PRK13409 171 LIPKVfkgKVREL--------LKKVDE--RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180
....*....|....*....|.
gi 46592978 242 SGLDSASCFQVVSLMKGLAQG 262
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEG 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
98-293 |
3.65e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.73 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDLR----------CF----RKvscyimqD 162
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGaDPADS--GEIRLDGKPVRIRsprdairagiAYvpedRK-------G 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 DMLLPHLTVQEAMMVSAHLK------LQEKDEgrREMVKEILTALGL-LSCANTRTGSLSGG-QRKrLAIALELVNNPPV 234
Cdd:COG1129 339 EGLVLDLSIRENITLASLDRlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 235 MFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFELF---DQLYVLSQGQCV 293
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI----SSELPELLglsDRILVMREGRIV 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
95-248 |
3.95e-10 |
|
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: 62.65 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKG-AVLINGLprdlrcfrKVScYIMQDDMLLPHLTVQE 173
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGeARPQPGI--------KVG-YLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMM--VSAHLKLQEK---------------DEGRREMVK--EILTALGL-------------LSCA--NTRTGSLSGGQR 219
Cdd:TIGR03719 88 NVEegVAEIKDALDRfneisakyaepdadfDKLAAEQAElqEIIDAADAwdldsqleiamdaLRCPpwDADVTKLSGGER 167
|
170 180
....*....|....*....|....*....
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLDSAS 248
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
108-291 |
4.14e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLR-CFRKVS---CYIMQD---DMLLPHLTVQEAMMVSAH 180
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRnPQQAIAqgiAMVPEDrkrDGIVPVMGVGKNITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 181 LKL---------QEKDEGRREMVK-EILTALGLLscantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 250
Cdd:PRK13549 368 DRFtggsriddaAELKTILESIQRlKVKTASPEL-----AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 251 QVVSLMKGLAQGGRSIICTihqpSAKLFE---LFDQLYVLSQGQ 291
Cdd:PRK13549 443 EIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGK 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
108-245 |
4.52e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGyrETGM-KGAVLINglpRDLRCFR-----------KVSCYIM-----QDDML----- 165
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNG--EVLLdDGRIIYE---QDLIVARlqqdpprnvegTVYDFVAegieeQAEYLkryhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 166 LPHLTVQEAM--MVSAHLKLQEK-D-------EGRremVKEILTALGLlsCANTRTGSLSGGQRKRLAIALELVNNPPVM 235
Cdd:PRK11147 104 ISHLVETDPSekNLNELAKLQEQlDhhnlwqlENR---INEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170
....*....|
gi 46592978 236 FFDEPTSGLD 245
Cdd:PRK11147 179 LLDEPTNHLD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
108-301 |
5.47e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAG-Y-RETG----MKGAVLINGlPRDlrcfrkvS-----CYIMQDDMLLPHLTVQEAMM 176
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGiYtRDAGsilyLGKEVTFNG-PKS-------SqeagiGIIHQELNLIPQLTIAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 177 VsahlklqekdeGR-----------REMVKE---ILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 242
Cdd:PRK10762 102 L-----------GRefvnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 243 GL---DSASCFQVVSLMKglAQGgrsiiCTIHQPSAKLFELF---DQLYVLSQGQCVYRGKVCNL 301
Cdd:PRK10762 171 ALtdtETESLFRVIRELK--SQG-----RGIVYISHRLKEIFeicDDVTVFRDGQFIAEREVADL 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
112-245 |
7.10e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 112 AIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----------LPRDLRcfrKVScYIMQDDMLLPHLTVQeammvsAH 180
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGL-TRPQKGRIVLNGrvlfdaekgicLPPEKR---RIG-YVFQDARLFPHYKVR------GN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592978 181 LK--LQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK11144 97 LRygMAKSM---VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
108-256 |
7.16e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL------PRDLRCFRKVSCYIMQDDM--LLPHLTVQEAMM--V 177
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMepL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 178 SAHLKLQEKDEGRRemVKEILTALGLLSCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 256
Cdd:PRK10261 429 RVHGLLPGKAAAAR--VAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
67-245 |
7.84e-10 |
|
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: 61.87 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 67 PRRAAVNIEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING 144
Cdd:TIGR03719 316 PRLGDKVIEAENLT-----------KAFgdKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTIEIGE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 145 LPrdlrcfrKVSCYIMQDDMLLPHLTVQEAmmVSA---HLKLqekdeGRREMvkeilTALGLLSCAN-------TRTGSL 214
Cdd:TIGR03719 384 TV-------KLAYVDQSRDALDPNKTVWEE--ISGgldIIKL-----GKREI-----PSRAYVGRFNfkgsdqqKKVGQL 444
|
170 180 190
....*....|....*....|....*....|.
gi 46592978 215 SGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
95-320 |
8.48e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyRETGMKGAVLINGLPR-----------DLRCFRKVSCYIMQDD 163
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 MLLPhLTVQEAM-----MVSAHLKLQEKDegrreMVKEILTALGLLSCANTRTGS----LSGGQRKRLAIALELVNNPPV 234
Cdd:PRK14258 98 NLFP-MSVYDNVaygvkIVGWRPKLEIDD-----IVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 235 MFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQpsaklfelFDQLYVLSQGQCVYRGKVcNLVPYLRDLGLNCP 313
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKGNE-NRIGQLVEFGLTKK 242
|
....*..
gi 46592978 314 TYHNPAD 320
Cdd:PRK14258 243 IFNSPHD 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
95-308 |
1.12e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKS----TLMNILAGYRETGMKGAVLING---LPRDLRCFRKVS----CYIMQDD 163
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPSGDIRFHGeslLHASEQTLRGVRgnkiAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 ML----LPHLTVQEAMMVSAHLKLqekdegRREMVK-EILTAL---GLLSCANTRTG---SLSGGQRKRLAIALELVNNP 232
Cdd:PRK15134 102 MVslnpLHTLEKQLYEVLSLHRGM------RREAARgEILNCLdrvGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 233 PVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKVCNLV-----PYLR 306
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSI-VRKLADRVAVMQNGRCVEQNRAATLFsapthPYTQ 254
|
..
gi 46592978 307 DL 308
Cdd:PRK15134 255 KL 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
95-296 |
1.38e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.97 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRC-------FRKVSC---------- 157
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCgyverpsKVGEPCpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 158 ---YIMQDDMLLPHLTVQEAMMVSAHLKLQEKD-----------EGRREMVKEILTALGLLSCANTR------TGSLSGG 217
Cdd:TIGR03269 93 evdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDtvldnvlealeEIGYEGKEAVGRAVDLIEMVQLShrithiARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 218 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS-LMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRG 296
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEV-IEDLSDKAIWLENGEIKEEG 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-271 |
1.71e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 45 LLNGHLKKVDNNLTEAQRF---SSLPRRAAVN------IEFRDLS---YSVpegpwwrKKGYKTLLKGISGKFNSGELVA 112
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFmegVSEVEKECEVevgepiIKVRNVSkryISV-------DRGVVKAVDNVSLEVKEGEIFG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 113 IMGPSGAGKSTLMNILAGYRE-TGMKGAVLI-------NGLPRDLRcfRKVSCYI---MQDDMLLPHLTVQEAMMVSAHL 181
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEpTSGEVNVRVgdewvdmTKPGPDGR--GRAKRYIgilHQEYDLYPHRTVLDNLTEAIGL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 182 KLqEKDEGRREMVKeILTALGL-----LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SL 255
Cdd:TIGR03269 393 EL-PDELARMKAVI-TLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSI 470
|
250
....*....|....*.
gi 46592978 256 MKGLAQGGRSIICTIH 271
Cdd:TIGR03269 471 LKAREEMEQTFIIVSH 486
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
98-308 |
1.82e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKS----TLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQD----DM----- 164
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 -----LLPHLTVQEAMMVSAHLklqEKDEGRREMVKEILTALGLLSCANTRT------GSLSGGQRKRLAIALELVNNPP 233
Cdd:PRK10261 112 epmtsLNPVFTVGEQIAESIRL---HQGASREEAMVEAKRMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 234 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLV-----PYLRDL 308
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
74-297 |
2.34e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDL---R 150
Cdd:PRK10790 341 IDIDNVSFAYRDD--------NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL-TEGEIRLDGRPLSSlshS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CFRKVSCYIMQDDMLLphltvqeAMMVSAHLKLqekdeGR---REMVKEILTALGLLSCA-------NTRTG----SLSG 216
Cdd:PRK10790 412 VLRQGVAMVQQDPVVL-------ADTFLANVTL-----GRdisEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 217 GQRKRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVSLMKGLAQGGRSIICTIHQPSAkLFELfDQLYVLSQGQCVYRG 296
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGT-EQAIQQALAAVREHTTLVVIAHRLST-IVEA-DTILVLHRGQAVEQG 556
|
.
gi 46592978 297 K 297
Cdd:PRK10790 557 T 557
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
101-297 |
3.06e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKStlMNILAGYRETGMKGAVLINGLPRDLRCFRKVS------------CYIMQDDM--LL 166
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISekerrnlvgaevAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQEAMMVSahLKLQE--KDEGRREMVKEILTALGL---LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 241
Cdd:PRK11022 104 PCYTVGFQIMEA--IKVHQggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 242 SGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGK 297
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
103-246 |
3.35e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.80 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 103 GKFNSGELVAIMGPSGAGKSTLMNILAGyretGMKGAVLINGLPRDlrcfrKVScYIMQddmllpHLTVQEAMMVSAHLK 182
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAG----VLKPDEGDIEIELD-----TVS-YKPQ------YIKADYEGTVRDLLS 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 183 LQEKDEGRREMVK-EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:cd03237 84 SITKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
98-274 |
3.79e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNilagyretgmkgavlinglprdlRCFRKVSCYIMQDDmlLPHLTVQEAMMV 177
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------------EGLYASGKARLISF--LPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 178 SahlKLQEkdegrreMVKEILTALGLlscaNTRTGSLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSL 255
Cdd:cd03238 66 D---QLQF-------LIDVGLGYLTL----GQKLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEV 131
|
170
....*....|....*....
gi 46592978 256 MKGLAQGGRSIICTIHQPS 274
Cdd:cd03238 132 IKGLIDLGNTVILIEHNLD 150
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
74-239 |
4.56e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.43 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPE---------GPwwrkkgyktllkgISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLIN 143
Cdd:COG4615 328 LELRGVTYRYPGedgdegftlGP-------------IDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GLP---RDLRCFRKVSCYIMQDDMLLPHLtvqeammvsahlkLQEKDEGRREMVKEILTALGL---LSCANTR--TGSLS 215
Cdd:COG4615 393 GQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LGLDGEADPARARELLERLELdhkVSVEDGRfsTTDLS 459
|
170 180
....*....|....*....|....
gi 46592978 216 GGQRKRLAIALELVNNPPVMFFDE 239
Cdd:COG4615 460 QGQRKRLALLVALLEDRPILVFDE 483
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
75-291 |
4.59e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL------PRD 148
Cdd:COG3845 259 EVENLSVRDDRG--------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-SGSIRLDGEditglsPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 149 LRCfRKVScYIMQDDM---LLPHLTVQEAMMVSAH----------LKLQEKDEGRREMVKE--ILTAlGllscANTRTGS 213
Cdd:COG3845 330 RRR-LGVA-YIPEDRLgrgLVPDMSVAENLILGRYrrppfsrggfLDRKAIRAFAEELIEEfdVRTP-G----PDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICtIhqpSAKLFELF---DQLYVLSQG 290
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL-I---SEDLDEILalsDRIAVMYEG 478
|
.
gi 46592978 291 Q 291
Cdd:COG3845 479 R 479
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
74-239 |
4.93e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGpwwrkkGYKtlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP---RDL 149
Cdd:PRK10522 323 LELRNVTFAYQDN------GFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 150 RCFRKVSCYIMQDDMLLPHLTVQEAMMVS--------AHLKLQEK---DEGRremvkeiltalgllsCANTRtgsLSGGQ 218
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPEGKPANpalvekwlERLKMAHKlelEDGR---------------ISNLK---LSKGQ 454
|
170 180
....*....|....*....|.
gi 46592978 219 RKRLAIALELVNNPPVMFFDE 239
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDE 475
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
74-291 |
5.06e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---------YRETGMKGAVL--- 141
Cdd:PLN03073 509 ISFSDASFGYPGGP--------LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGelqpssgtvFRSAKVRMAVFsqh 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 142 -INGLprDL---------RCFRKVScyimqDDMLLPHLTvqeAMMVSAHLKLQEkdegrreMVkeiltalgllscantrt 211
Cdd:PLN03073 581 hVDGL--DLssnpllymmRCFPGVP-----EQKLRAHLG---SFGVTGNLALQP-------MY----------------- 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 212 gSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMKGLA--QGGrsiICTIHQPSAKLFELFDQLYVLSQ 289
Cdd:PLN03073 627 -TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSE 699
|
..
gi 46592978 290 GQ 291
Cdd:PLN03073 700 GK 701
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
74-296 |
6.27e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLINGlpRDLR 150
Cdd:PRK09580 2 LSIKDLHVSVED---------KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTG--GTVEFKG--KDLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 151 CF----RKVSCYIM--QDDMLLP----HLTVQEAmmVSAHLKLQEKDEGRR----EMVKEILTALGLLSCANTRTGSL-- 214
Cdd:PRK09580 69 ELspedRAGEGIFMafQYPVEIPgvsnQFFLQTA--LNAVRSYRGQEPLDRfdfqDLMEEKIALLKMPEDLLTRSVNVgf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 215 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVY 294
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
..
gi 46592978 295 RG 296
Cdd:PRK09580 227 SG 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
95-248 |
7.63e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKG-AVLINGLprdlrcfrKVScYIMQDDMLLPHLTVQE 173
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGeARPAPGI--------KVG-YLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 174 AMM--VSAHLKLQEK---------------DEGRREMVK--EILTALGL-------------LSC--ANTRTGSLSGGQR 219
Cdd:PRK11819 90 NVEegVAEVKAALDRfneiyaayaepdadfDALAAEQGElqEIIDAADAwdldsqleiamdaLRCppWDAKVTKLSGGER 169
|
170 180
....*....|....*....|....*....
gi 46592978 220 KRLAIALELVNNPPVMFFDEPTSGLDSAS 248
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
92-285 |
9.71e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 55.06 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 92 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMN--ILAgyreTGMKGAVLINGLPRDLRCFrkvSCYimqddmllphl 169
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiGLA----LGGAQSATRRRSGVKAGCI---VAA----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 170 tvqeammVSAHLklqekdegrremvkeILTALGLlscantrtgslSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLD 245
Cdd:cd03227 67 -------VSAEL---------------IFTRLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46592978 246 SASCFQVVSLMKGLAQGGRSIICTIHQPsaKLFELFDQLY 285
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
108-245 |
1.91e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILagyreTGM----KGAVLINGLP---RDLRCFRKVScYIMQDDMLLPHLTVQEAMMVSAH 180
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKML-----TGLlpasEGEAWLFGQPvdaGDIATRRRVG-YMSQAFSLYGELTVRQNLELHAR 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 181 L-KLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:NF033858 366 LfHLPAAEIAAR--VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
90-245 |
3.27e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 90 RKKGYKT----LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING-----LPRDLrcFRKVSCYIM 160
Cdd:PRK10247 11 QNVGYLAgdakILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP-TSGTLLFEGedistLKPEI--YRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 161 QDDMLLPHlTVQEAMMVSAHLKLQEKDEGRreMVKEiLTALGL-LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDE 239
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRNQQPDPAI--FLDD-LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
....*.
gi 46592978 240 PTSGLD 245
Cdd:PRK10247 164 ITSALD 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
102-246 |
3.42e-08 |
|
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: 56.72 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 102 SGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVlinglPRDLrcfrKVSC---YIMQD-DMllphlTVQEAMMV 177
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAG-VLKPDEGEV-----DEDL----KISYkpqYISPDyDG-----TVEEFLRS 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 178 SAHLKLQEKdegrreMVK-EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:COG1245 425 ANTDDFGSS------YYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
98-272 |
6.18e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.87 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDLRCF-------RKVSCYIMQDDMLLpHLT 170
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 171 VQEAMMVSAHLKLQekdegRREMVKEI--------LTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 242
Cdd:cd03290 95 VEENITFGSPFNKQ-----RYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|...
gi 46592978 243 GLD---SASCFQvVSLMKGLAQGGRSIICTIHQ 272
Cdd:cd03290 170 ALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
65-296 |
6.95e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.49 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 65 SLP-RRAAVNIEFRDLSYSVPEGPwwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLIN 143
Cdd:PRK10789 306 PVPeGRGELDVNIRQFTYPQTDHP---------ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 144 GLP-RDLRC--FRKVSCYIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltalgll 204
Cdd:PRK10789 376 DIPlTKLQLdsWRSRLAVVSQTPFLFsdtvannialgrPDATQQEiehvARLASVHDDILRLPQGYDTEVGE-------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 205 scantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVvslMKGLAQGG--RSIICTIHQPSAkLFELfD 282
Cdd:PRK10789 448 -----RGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI---LHNLRQWGegRTVIISAHRLSA-LTEA-S 517
|
250
....*....|....
gi 46592978 283 QLYVLSQGQCVYRG 296
Cdd:PRK10789 518 EILVMQHGHIAQRG 531
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
108-293 |
7.41e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAGYRETG-MKGAVLINGlprDLRCFRKVS-------CYIMQDDMLLPHLTVQEAMMVS- 178
Cdd:NF040905 27 GEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDG---EVCRFKDIRdsealgiVIIHQELALIPYLSIAENIFLGn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 179 --AHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAscfQVV 253
Cdd:NF040905 104 erAKRGVIDWNETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA---ALL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592978 254 SLMKGL-AQGGRSIIctIhqpSAKLFELF---DQLYVLSQGQCV 293
Cdd:NF040905 180 DLLLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
209-291 |
8.11e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 209 TRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLS 288
Cdd:PRK10982 387 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVMS 465
|
...
gi 46592978 289 QGQ 291
Cdd:PRK10982 466 NGL 468
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
93-245 |
8.90e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY---------RETGMKgavlINGLPRDLRCfrkvscyimqdD 163
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvapdegvikRNGKLR----IGYVPQKLYL-----------D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 MLLPhLTVQEAMMVSAHLKlqekdegrremVKEILTALGLLSCA---NTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:PRK09544 80 TTLP-LTVNRFLRLRPGTK-----------KEDILPALKRVQAGhliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
....*
gi 46592978 241 TSGLD 245
Cdd:PRK09544 148 TQGVD 152
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
89-290 |
1.02e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 89 WRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGlprdlrcfrkVSCYIMQDDMLLpH 168
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG----------SVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 169 LTVQEAMMVSAhlKLQEKDEGRREMVKEILTALGLLSCAN-----TRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:PLN03232 693 ATVRENILFGS--DFESERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46592978 244 LDSASCFQVV-SLMKGLAQGGRSIICT--IHqpsakLFELFDQLYVLSQG 290
Cdd:PLN03232 771 LDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
98-269 |
1.92e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.86 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLM-------NILAGYRetgMKGAVLINGL--------PRDLRcfRKVScYIMQD 162
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR---VEGKVTFHGKnlyapdvdPVEVR--RRIG-MVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 DMLLPHlTVQEAMMVSAHL--------KLQEK--------DEgrremVKEILTALGLlscantrtgSLSGGQRKRLAIAL 226
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARIngykgdmdELVERslrqaalwDE-----VKDKLKQSGL---------SLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592978 227 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICT 269
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
67-245 |
2.34e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 67 PRRAAVNIEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING 144
Cdd:PRK11819 318 PRLGDKVIEAENLS-----------KSFgdRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG-QEQPDSGTIKIGE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 145 LPrdlrcfrKVScYIMQD-DMLLPHLTVQEAmmVSA---HLKLqekdeGRREMvkeiltalgllscaNTR---------- 210
Cdd:PRK11819 386 TV-------KLA-YVDQSrDALDPNKTVWEE--ISGgldIIKV-----GNREI--------------PSRayvgrfnfkg 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46592978 211 ------TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK11819 437 gdqqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
74-291 |
2.52e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSYSvpegpwWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING--LPR---- 147
Cdd:PRK13650 5 IEVKNLTFK------YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGdlLTEenvw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 148 DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAI 224
Cdd:PRK13650 78 DIR--HKIGMVFQNPDNQFVGATVEDDVAFG----LENKGIPHEEMkerVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 225 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQpsakLFE--LFDQLYVLSQGQ 291
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
95-245 |
3.66e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTL-LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYR--ETGmKGAVLiNGLPRDLRcFRKVSC----YimqddM--- 164
Cdd:NF033858 13 KTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARkiQQG-RVEVL-GGDMADAR-HRRAVCpriaY-----Mpqg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 ----LLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:NF033858 85 lgknLYPTLSVFENLDFFGRLFGQDAAE-RRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
....*
gi 46592978 241 TSGLD 245
Cdd:NF033858 164 TTGVD 168
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
98-293 |
3.88e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTL-MNILAGYRETGMKGAVLINGLPRDLRCF--------------RKVSCYIMQD 162
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 DML----LPHL-TVQEAMMVSAHLKLQEKDEGRREMvkEILTalgllSCANTRTGSLSGGQRKRLAIALELVNNPPVMFF 237
Cdd:NF040905 356 DIKrnitLANLgKVSRRGVIDENEEIKVAEEYRKKM--NIKT-----PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 238 DEPTSGLDSASCFQVVSLMKGLAQGGRSIIcTIhqpSAKLFELF---DQLYVLSQGQCV 293
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPELLgmcDRIYVMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
102-245 |
5.04e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 102 SGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLInglprDLrcfrKVSC---YIMQDdmllPHLTVQEAMMvs 178
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAG-VLKPDEGEVDP-----EL----KISYkpqYIKPD----YDGTVEDLLR-- 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592978 179 ahlklQEKDEGRREMVK-EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK13409 423 -----SITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
98-296 |
6.13e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGmKGAVLINGLPRDLRCFRKVS--------CYIMQDDMLLP 167
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiiSETG-QTIVGDYAIPANLKKIKEVKrlrkeiglVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTVQEAMMVSAHLklqekDEGRREMVKEILTALGLLSC----ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:PRK13645 106 ETIEKDIAFGPVNL-----GENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46592978 244 LDSASCFQVVSLMKGLAQG-GRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 296
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-248 |
1.86e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRDLSY---SVPEGPwwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY------------------- 131
Cdd:PTZ00265 1166 IEIMDVNFryiSRPNVP---------IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndm 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 132 -----------RETGMK-----------------------GAVLINGL---PRDLRCFRKVSCYIMQDDMLLphltvqeA 174
Cdd:PTZ00265 1237 tneqdyqgdeeQNVGMKnvnefsltkeggsgedstvfknsGKILLDGVdicDYNLKDLRNLFSIVSQEPMLF-------N 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 175 MMVSAHLKLQeKDEGRREMVKEI--LTAL-----GLLSCANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSG 243
Cdd:PTZ00265 1310 MSIYENIKFG-KEDATREDVKRAckFAAIdefieSLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSS 1388
|
....*
gi 46592978 244 LDSAS 248
Cdd:PTZ00265 1389 LDSNS 1393
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
43-291 |
2.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 43 TDLLNGHLK---KVDNNLTEAQRFSS---LPRRAAVNIEFRDLSYSVPEGPWWR--------KKGYKTLLKGISGKFNSG 108
Cdd:PLN03232 1183 TTLLSGVLRqasKAENSLNSVERVGNyidLPSEATAIIENNRPVSGWPSRGSIKfedvhlryRPGLPPVLHGLSFFVSPS 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 109 ELVAIMGPSGAGKSTLMNILagYRETGM-KGAVLINGLprDLRCF-----RKVSCYIMQDDMLLPHLTVQEAMMVSAHLK 182
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNAL--FRIVELeKGRIMIDDC--DVAKFgltdlRRVLSIIPQSPVLFSGTVRFNIDPFSEHND 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 183 LQEKDEGRREMVKEIL--TALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDsascFQVVSLM-KGL 259
Cdd:PLN03232 1339 ADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIqRTI 1414
|
250 260 270
....*....|....*....|....*....|....
gi 46592978 260 AQGGRSiiCTIHQPSAKLFELF--DQLYVLSQGQ 291
Cdd:PLN03232 1415 REEFKS--CTMLVIAHRLNTIIdcDKILVLSSGQ 1446
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
95-245 |
2.16e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPR-------DLRcfRK---VSCYImqddm 164
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgsgetiwDIK--KHigyVSSSL----- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 165 llpHLTVQeammVSAHLK-------------LQEKDEGRREMVKEILTALGLLSC-ANTRTGSLSGGQRKRLAIALELVN 230
Cdd:PRK10938 346 ---HLDYR----VSTSVRnvilsgffdsigiYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVK 418
|
170
....*....|....*
gi 46592978 231 NPPVMFFDEPTSGLD 245
Cdd:PRK10938 419 HPTLLILDEPLQGLD 433
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
103-294 |
2.83e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 103 GKFNSGELVAIMGPSGAGKSTLMNILAGYREtgmkgavlinglPRDlrcfrkvscyimqDDMLLPHLTVQeammvsahLK 182
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV--------YK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 183 LQEKDegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG 262
Cdd:cd03222 67 PQYID--------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|..
gi 46592978 263 GRSIICTIHQPSAKLFELFDQLYVLSQGQCVY 294
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFEGEPGVY 152
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
438-584 |
4.34e-06 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 49.31 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 438 SNSGFLFFSMLFLMFAALMPTVLTFPLEMgVFLRE----HLNYWYSLK--AYYLAKTMADVPFQIMFPVAYCSIVYWMTS 511
Cdd:pfam12698 155 PQSGYAYYLVGLILMIIILIGAAIIAVSI-VEEKEsrikERLLVSGVSplQYWLGKILGDFLVGLLQLLIILLLLFGIGI 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592978 512 QPSDAVRFVLFAALGtmtSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYI 584
Cdd:pfam12698 234 PFGNLGLLLLLFLLY---GLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSI 303
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
95-274 |
9.38e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-------YRETGMKGAVLINGLP------RDLRCFRKVscyimq 161
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaPRGARVTGDVTLNGEPlaaidaPRLARLRAV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 162 ddmlLPHlTVQEAMMVSAH--LKLQEKDEGRREMVKEILTAlGLLSCANTRTG----------SLSGGQRKRLAIALELV 229
Cdd:PRK13547 88 ----LPQ-AAQPAFAFSAReiVLLGRYPHARRAGALTHRDG-EIAWQALALAGatalvgrdvtTLSGGELARVQFARVLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 230 N---------NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGR-SIICTIHQPS 274
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPN 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
92-248 |
1.06e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 92 KGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAV------LINGLPRDlrcfrkvSCYIMQDD 163
Cdd:PRK15064 327 KGFdnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGTVkwsenaNIGYYAQD-------HAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 164 MllphlTVQEAMMvsahlklQEKDEGRRE-MVKEILTALgLLSC--ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 240
Cdd:PRK15064 399 L-----TLFDWMS-------QWRQEGDDEqAVRGTLGRL-LFSQddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
....*...
gi 46592978 241 TSGLDSAS 248
Cdd:PRK15064 466 TNHMDMES 473
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
95-302 |
2.27e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.44 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 95 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMniLAGYRETGM-KGAVLING-----LPrdLRCFRKVSCYIMQDDMLL-- 166
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfDGKIVIDGidiskLP--LHTLRSRLSIILQDPILFsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 -------PHLTVQEAMMVSAHLKLQEKDegrreMVKEIltaLGLLSCANTRTG-SLSGGQRKRLAIALELVNNPPVMFFD 238
Cdd:cd03288 110 sirfnldPECKCTDDRLWEALEIAQLKN-----MVKSL---PGGLDAVVTEGGeNFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 239 EPTSGLDSAS--CFQVVsLMKGLAQggRSIICTIHQPSAKLFElfDQLYVLSQGQCVYRGKVCNLV 302
Cdd:cd03288 182 EATASIDMATenILQKV-VMTAFAD--RTVVTIAHRVSTILDA--DLVLVLSRGILVECDTPENLL 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
101-291 |
2.68e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING------------------LPRDlrcfRKVS------ 156
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGkeinalstaqrlarglvyLPED----RQSSglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 157 ------CYIMQDDMLLPHLTVQEAMMVsahlklqekDEGRRemvkeiltALGL-LSCANTRTGSLSGGQRKRLAIALELV 229
Cdd:PRK15439 357 plawnvCALTHNRRGFWIKPARENAVL---------ERYRR--------ALNIkFNHAEQAARTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 230 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFE---LFDQLYVLSQGQ 291
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
101-291 |
2.80e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 101 ISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGLPRDLRCFRK-VSCYIM------QDDMLLPHLTVQ 172
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGAtRRTA--GQVYLDGKPIDIRSPRDaIRAGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 173 EAMMVSA---HLK----LQEKDEgrREMVKEILTALgllscaNTRT-------GSLSGGQRKRLAIALELVNNPPVMFFD 238
Cdd:PRK11288 350 DNINISArrhHLRagclINNRWE--AENADRFIRSL------NIKTpsreqliMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592978 239 EPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFE---LFDQLYVLSQGQ 291
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFV----SSDLPEvlgVADRIVVMREGR 473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
75-245 |
4.80e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 75 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG----------------------YR 132
Cdd:PRK11147 321 EMENVNYQIDG---------KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqlqadsgrihcgtklevayfdqHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 133 E------TGM------KGAVLINGLPrdlrcfRKVSCYiMQDDMLLPhltvqeammvsahlklqekdegRREMvkeilta 200
Cdd:PRK11147 392 AeldpekTVMdnlaegKQEVMVNGRP------RHVLGY-LQDFLFHP----------------------KRAM------- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592978 201 lgllscanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK11147 436 --------TPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
88-274 |
6.35e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 88 WWRKKG-YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGlprdlrcfrkVSCYIMQDDMLL 166
Cdd:PRK13545 29 FRSKDGeYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKG----------SAALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 167 PHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 246
Cdd:PRK13545 98 GQLTGIENIELKG-LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180
....*....|....*....|....*...
gi 46592978 247 ASCFQVVSLMKGLAQGGRSIICTIHQPS 274
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLS 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
214-288 |
9.19e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 9.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIICTIHQPSAKLFELFDQLYVLS 288
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL-KGNENRITIIIAHRLSTIRYANTIFVLS 653
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
104-271 |
1.47e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 104 KFNSGeLVAIMGPSGAGKSTLMNIL--AGYRETGMKGavliNGLPRDLRCFRKVScyimqddmllphltvqeammVSAHL 181
Cdd:cd03240 19 EFFSP-LTLIVGQNGAGKTTIIEALkyALTGELPPNS----KGGAHDPKLIREGE--------------------VRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 182 KLQEKDEGRREMVkeILTALG-LLSCANTRTG-----------SLSGGQRK------RLAIALELVNNPPVMFFDEPTSG 243
Cdd:cd03240 74 KLAFENANGKKYT--ITRSLAiLENVIFCHQGesnwplldmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|
gi 46592978 244 LDSASC-FQVVSLMKG-LAQGGRSIICTIH 271
Cdd:cd03240 152 LDEENIeESLAEIIEErKSQKNFQLIVITH 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
104-263 |
1.84e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 104 KFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAvLINGLPRDLR-CFRKVSCYIMQD------DMLLPH-----LTV 171
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAG-ELPLLSGE-RQSQFSHITRlSFEQLQKLVSDEwqrnntDMLSPGeddtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 172 QEAmmvsahLKLQEKDEGRREMVKEILTALGLLScanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 251
Cdd:PRK10938 103 AEI------IQDEVKDPARCEQLAQQFGITALLD---RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|..
gi 46592978 252 VVSLMKGLAQGG 263
Cdd:PRK10938 174 LAELLASLHQSG 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-245 |
2.18e-04 |
|
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: 44.55 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 15 SYSAEMTEPKSVCVSVDEVVSSNMEATEtdllngHLKKVDNNLTEA-------QRFSSLPRRAAVniEFRDlsYSVPEGP 87
Cdd:TIGR00957 1227 SYSLQVTFYLNWLVRMSSEMETNIVAVE------RLKEYSETEKEApwqiqetAPPSGWPPRGRV--EFRN--YCLRYRE 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 88 wwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLprdlrcfrKVSCYIMQDdmLLP 167
Cdd:TIGR00957 1297 -----DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDGL--------NIAKIGLHD--LRF 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 168 HLTV--QEAMMVSAHLKL------QEKDEgrremvkEILTALGL---------------LSCANTRTgSLSGGQRKRLAI 224
Cdd:TIGR00957 1361 KITIipQDPVLFSGSLRMnldpfsQYSDE-------EVWWALELahlktfvsalpdkldHECAEGGE-NLSVGQRQLVCL 1432
|
250 260
....*....|....*....|.
gi 46592978 225 ALELVNNPPVMFFDEPTSGLD 245
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVD 1453
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
89-135 |
2.45e-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: 2.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 89 WRKKGYKTLLkgISGKFNSG--EL--------VAIMGPSGAGKSTLMNILAG--YRETG 135
Cdd:cd01854 58 YEKLGYPVLA--VSAKTGEGldELrellkgktSVLVGQSGVGKSTLLNALLPelVLATG 114
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
107-129 |
3.13e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.10 E-value: 3.13e-04
10 20
....*....|....*....|...
gi 46592978 107 SGELVAIMGPSGAGKSTLMNILA 129
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAAR 26
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
271-328 |
4.98e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 42.97 E-value: 4.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592978 271 HQPSAKLFELFDQLYVLSQ-GQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASG 328
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
213-271 |
8.90e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 8.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 213 SLSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
74-245 |
1.39e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 74 IEFRD--LSYSvPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLprDLRC 151
Cdd:PLN03130 1238 IKFEDvvLRYR-PELP--------PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-ERGRILIDGC--DISK 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 152 F-----RKVSCYIMQDDMLLPHlTVQ---------------EAMMvSAHLklqeKDEGRRemvkeilTALGLLSCANTRT 211
Cdd:PLN03130 1306 FglmdlRKVLGIIPQAPVLFSG-TVRfnldpfnehndadlwESLE-RAHL----KDVIRR-------NSLGLDAEVSEAG 1372
|
170 180 190
....*....|....*....|....*....|....
gi 46592978 212 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 245
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
98-128 |
2.00e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.00e-03
10 20 30
....*....|....*....|....*....|..
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMN-IL 128
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
93-245 |
2.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 93 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGmkGAVLINGLPR--DLRC-------FRKVSCYIMQD 162
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEpSA--GNVSLDPNERlgKLRQdqfafeeFTVLDTVIMGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 163 DML------------LPHLTVQEAMMVsAHLKLQ--EKD----EGRremVKEILTALGL-LSCANTRTGSLSGGQRKRLA 223
Cdd:PRK15064 90 TELwevkqerdriyaLPEMSEEDGMKV-ADLEVKfaEMDgytaEAR---AGELLLGVGIpEEQHYGLMSEVAPGWKLRVL 165
|
170 180
....*....|....*....|..
gi 46592978 224 IALELVNNPPVMFFDEPTSGLD 245
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
108-130 |
2.09e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.69 E-value: 2.09e-03
10 20
....*....|....*....|...
gi 46592978 108 GELVAIMGPSGAGKSTLMNILAG 130
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
214-293 |
2.15e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 214 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCV 293
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
98-128 |
2.60e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|..
gi 46592978 98 LKGISGKFNSGELVAIMGPSGAGKSTLMN-IL 128
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
107-130 |
3.03e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 3.03e-03
10 20
....*....|....*....|....
gi 46592978 107 SGELVAIMGPSGAGKSTLMNILAG 130
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
110-129 |
5.57e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 35.78 E-value: 5.57e-03
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
91-247 |
7.47e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 91 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGlpRD-----LRCFRKVSCYIMQDDML 165
Cdd:PTZ00243 1319 REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-CGGEIRVNG--REigaygLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592978 166 L---------PHLTVQEAmMVSAHLKLQekdeGRREMVKEilTALGLLSCANTRTGSLSGGQRKRLAIALELVN-NPPVM 235
Cdd:PTZ00243 1396 FdgtvrqnvdPFLEASSA-EVWAALELV----GLRERVAS--ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFI 1468
|
170
....*....|..
gi 46592978 236 FFDEPTSGLDSA 247
Cdd:PTZ00243 1469 LMDEATANIDPA 1480
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
213-271 |
7.72e-03 |
|
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: 39.61 E-value: 7.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592978 213 SLSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 271
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
111-132 |
8.44e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.44 E-value: 8.44e-03
|
| |
