|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
62-668 |
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: 776.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 62 LTEAQRFSSLPRRAAVNIEfRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM 141
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 142 KGA--VLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEK--DEGRREMVKEILTALGLLSCANTRTG 217
Cdd:TIGR00955 80 KGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 218 ------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYV 291
Cdd:TIGR00955 160 vpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 292 LSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSrlVRAVREGMCDSDHKRDLGGDAEVNPFLWH 371
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENE--SRERIEKICDSFAVSDIGRDMLVNTNLWS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 372 RPS---EEDSSSMEGCHsFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFL 448
Cdd:TIGR00955 318 GKAgglVKDSENMEGIG-YNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 449 FFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFA 528
Cdd:TIGR00955 397 FLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 529 ALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDR 608
Cdd:TIGR00955 477 FLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVD 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 609 --EDLHCDIDETCHFQKsEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER 668
Cdd:TIGR00955 557 niECTSANTTGPCPSSG-EVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
76-301 |
1.98e-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: 307.56 E-value: 1.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 76 AVNIEFRDLSYSVPEGPWwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET-GMKGAVLINGLPRDL 154
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPS---KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqekdegrremvkeiltalgllscantrtgSLSGGQRKRLAIALELV 234
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 235 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
100-661 |
2.61e-78 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 262.51 E-value: 2.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLPRDLRCFRKVScYIMQDDMLLPHLTVQE 178
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSAHLKLQE---KDEGRReMVKEILTALGLLSCANTRTGS-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PLN03211 160 TLVFCSLLRLPKsltKQEKIL-VAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 251 SASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEV 330
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 331 ASGE------------------YGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSeeDSSSMegchsfsASCL 392
Cdd:PLN03211 319 ANGVcqtdgvserekpnvkqslVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSS--DRISI-------STWF 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 393 TQFCILFKRTfLSIMRDSVLTHLRITShiGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMG 472
Cdd:PLN03211 390 NQFSILLQRS-LKERKHESFNTLRVFQ--VIAAALLAGLMWWHSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERA 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 473 VFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSL 552
Cdd:PLN03211 467 IFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDA 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 553 QVATFVGPVTAIPVLLFSGFFVsfDTIPTYLQWMSYISYVRYGFEGVILSIYGLDRED---LHCDIDE-----TCHFQKS 624
Cdd:PLN03211 547 KKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRIsslLGCSLPHgsdraSCKFVEE 624
|
570 580 590
....*....|....*....|....*....|....*..
gi 46592964 625 EAIlreldvENAKLYLDFIVLGIFFISLRLIAYFVLR 661
Cdd:PLN03211 625 DVA------GQISPATSVSVLIFMFVGYRLLAYLALR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
80-619 |
1.48e-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: 1.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM--KGAVLINGLPRDlRCF 157
Cdd:TIGR00956 761 HWRNLTYEVK-----IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 158 RKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEK--DEGRREMVKEILTALGLLSCANTRTG----SLSGGQRKRLAIAL 231
Cdd:TIGR00956 835 QRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSvsKSEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 232 ELVNNPP-VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQG-QCVY---RGKVCN- 305
Cdd:TIGR00956 915 ELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYfgdLGENSHt 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 306 LVPYLRDLGL-NCPTYHNPADFVMEV---ASGEYGDQ-------NSRLVRAVREgmcdsdhkrdlggdaEVNPFLWHRPS 374
Cdd:TIGR00956 995 IINYFEKHGApKCPEDANPAEWMLEVigaAPGAHANQdyhevwrNSSEYQAVKN---------------ELDRLEAELSK 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 375 EEDSSSMEGCHSFSASCLTQFCILFKRTFLSIMR--DSVLTHLRITshigiglligllylgigneakkvLSNS---GFLF 449
Cdd:TIGR00956 1060 AEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRtpDYLYSKFFLT-----------------------IFAAlfiGFTF 1116
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 450 F----SMLFL---MFAALMPTVLTFPLEMG-----------VFLREHLNYWYSLKAYYLAKTMADVPFQIMF-PVAYCSI 510
Cdd:TIGR00956 1117 FkvgtSLQGLqnqMFAVFMATVLFNPLIQQylppfvaqrdlYEVRERPSRTFSWLAFIAAQITVEIPYNLVAgTIFFFIW 1196
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 511 VYWM----TSQPSDAV--RFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQ 584
Cdd:TIGR00956 1197 YYPVgfywNASKTGQVheRGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWI 1276
|
570 580 590
....*....|....*....|....*....|....*
gi 46592964 585 WMSYISYVRYGFEGVILSIYGldredlhcDIDETC 619
Cdd:TIGR00956 1277 FMYRCSPFTYLVQALLSTGLA--------DVPVTC 1303
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
91-301 |
2.92e-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: 217.14 E-value: 2.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 91 GPWWR-------KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMK-GAVLINGLPRDLRCFRKVS 161
Cdd:cd03234 4 LPWWDvglkaknWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTsGQILFNGQPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 162 CYIMQDDMLLPHLTVQEAMMVSAHLKLQE-KDEGRREMVKEI--LTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPP 238
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRkSSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 239 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
79-301 |
2.27e-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: 213.64 E-value: 2.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETG-MKGAVLINGLPRDlRCF 157
Cdd:cd03232 4 LTWKNLNYTVPV-----KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 158 RKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqekdegrremvkeiltalgllscantrtgSLSGGQRKRLAIALELVNNP 237
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFSALLR------------------------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQ-GQCVYRG 301
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-610 |
3.50e-58 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 213.17 E-value: 3.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 16 QNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQrfSSLPRRAAV------NIEFRDLSYSVP 89
Cdd:PLN03140 801 ETAEEMEGEEDSIPRSLSSADGNNTREVAIQRMSNPEGLSKNRDSSLEAAN--GVAPKRGMVlpftplAMSFDDVNYFVD 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 90 EGPWWRKKGYK----TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETG--MKGAVLINGLPRDLRCFRKVSCY 163
Cdd:PLN03140 879 MPAEMKEQGVTedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGgyIEGDIRISGFPKKQETFARISGY 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 164 IMQDDMLLPHLTVQEAMMVSAHLKLqEKDEGRRE---MVKEILTALGLLSCANTRTG-----SLSGGQRKRLAIALELVN 235
Cdd:PLN03140 958 CEQNDIHSPQVTVRESLIYSAFLRL-PKEVSKEEkmmFVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVA 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 236 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQ-GQCVYRGKV----CNLVPYL 310
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYF 1116
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 311 RDL-GL-NCPTYHNPADFVMEVASgeygdqnsrLVRAVREGM-------CDSDHKRDlggDAEVNPFLWHRPSEEDsssM 381
Cdd:PLN03140 1117 EAIpGVpKIKEKYNPATWMLEVSS---------LAAEVKLGIdfaehykSSSLYQRN---KALVKELSTPPPGASD---L 1181
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 382 EGCHSFSASCLTQFCILFKRTFLSIMR--DSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNS-GFLFFSMLFLMFA 458
Cdd:PLN03140 1182 YFATQYSQSTWGQFKSCLWKQWWTYWRspDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMViGAMYAAVLFVGIN 1261
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 459 ALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVA 538
Cdd:PLN03140 1262 NCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYF 1341
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 539 QSLGLLIGAASTSLQVAT-FVGPVTAIpVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGlDRED 610
Cdd:PLN03140 1342 TYYGMMTVSLTPNQQVAAiFAAAFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG-DVED 1412
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
95-600 |
3.18e-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: 3.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE---TGMKGAVLINGLPRD--LRCFRKVSCYIMQDDM 169
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhIGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 LLPHLTVQEAMMVSAHLK-------LQEKDEGRREMVKEILTALGLLSCANTRTGS-----LSGGQRKRLAIALELVNNP 237
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLN 316
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 317 CPTYHNPADFVMEVAS-------GEYGDQNSRLVRAVREGMCDSDHKRDLggDAEVNPFLWHRPSEEDSSSMEGCH---- 385
Cdd:TIGR00956 309 CPDRQTTADFLTSLTSpaerqikPGYEKKVPRTPQEFETYWRNSPEYAQL--MKEIDEYLDRCSESDTKEAYRESHvakq 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 386 --------SFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMF 457
Cdd:TIGR00956 387 skrtrpssPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAF 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 458 AALMPTVLTFplEMGVFLREHLNY-WYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSL 536
Cdd:TIGR00956 467 SSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTL 544
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 537 VAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVI 600
Cdd:TIGR00956 545 AMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
79-306 |
7.29e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 7.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP--RD 153
Cdd:COG1131 1 IEVRGLT-----------KRYgdKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRPTS--GEVRVLGEDvaRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 233
Cdd:COG1131 68 PAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKE-ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKVCNL 306
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
80-296 |
7.86e-48 |
|
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: 167.26 E-value: 7.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---RDLRC 156
Cdd:cd03225 1 ELKNLSFSYP-------DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 157 FRKVSCYIMQ--DDMLLpHLTVQEAMMVSA-HLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 233
Cdd:cd03225 73 LRRKVGLVFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQ 296
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
398-600 |
3.24e-47 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 165.52 E-value: 3.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 398 LFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKkVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLRE 477
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 478 HLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATF 557
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592964 558 VGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVI 600
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
79-298 |
2.80e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 163.68 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP------R 152
Cdd:COG1136 5 LELRNLTKSYGTG-----EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVLIDGQDisslseR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSC-YIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 231
Cdd:COG1136 79 ELARLRRRHIgFVFQFFNLLPELTALENVALPLLLAGVSRKE-RRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 232 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHqpSAKLFELFDQLYVLSQGQCV 298
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTH--DPELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
79-296 |
8.48e-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: 8.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP------R 152
Cdd:cd03255 1 IELKNLSKTYGGG-----GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFR--KVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:cd03255 75 ELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLLLA-GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
79-302 |
1.10e-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: 162.12 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP---RDL 154
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQ--DDMLLpHLTVQEAMMVS-AHLKLqEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 231
Cdd:COG1122 71 RELRRKVGLVFQnpDDQLF-APTVEEDVAFGpENLGL-PREE-IRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 232 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGK 302
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGT 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
79-301 |
1.53e-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: 148.47 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYsvpegpwwrKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP--RDLRC 156
Cdd:COG4555 2 IEVENLSK---------KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-LKPDSGSILIDGEDvrKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 157 FRKVSCYIMQDDMLLPHLTVQEammvsaHLKL-----QEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 231
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLTVRE------NIRYfaelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 232 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
103-247 |
1.67e-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: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP---RDLRCFRKVSCYIMQDDMLLPHLTVQEA 179
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 180 MMVSAHLKLQEKDEGRREMvKEILTALGLLSCANTR----TGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 247
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA-EEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
96-296 |
4.49e-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: 143.41 E-value: 4.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 96 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETGM-KGAVLING--LPRDLRCFRKVSCYIMQDDMLLP 172
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG--ELRPtSGTAYINGysIRTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 252
Cdd:cd03263 89 ELTVREHLRFYARLKGLPKSEIKEE-VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 253 SCFQVVSLMKGLaQGGRSIICTIHqpSAKLFELF-DQLYVLSQGQ 296
Cdd:cd03263 168 SRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGK 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
79-301 |
4.68e-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: 143.80 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPR----- 152
Cdd:cd03261 1 IELRGLTKSF---------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 -DLRCFRKVSCYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSEEE--IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIICTiHQPSAkLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
79-302 |
9.01e-39 |
|
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: 143.48 E-value: 9.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PR 152
Cdd:cd03256 1 IEVENLSKTYPNG--------KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGTdinklkGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSA------------HLKLQEKDEGRremvkEILTALGLLSCANTRTGSLS 220
Cdd:cd03256 72 ALRQLRRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrslfgLFPKEEKQRAL-----AALERVGLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 221 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLFelFDQLYVLSQGQCV 298
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIV 224
|
....
gi 46592964 299 YRGK 302
Cdd:cd03256 225 FDGP 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
79-299 |
1.35e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.92 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDlRCFR 158
Cdd:COG1121 7 IELENLTVSY---------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPR-RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 KVScYIMQD---DMLLPhLTVQE--AMMVSAHLKLQEK-DEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALE 232
Cdd:COG1121 76 RIG-YVPQRaevDWDFP-ITVRDvvLMGRYGRRGLFRRpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 233 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVY 299
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLVAH 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
79-301 |
1.60e-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: 140.18 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP------R 152
Cdd:COG1120 2 LEAENLSVGYGG---------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRcfRKVScYIMQDDMLLPHLTVQEAMMV--SAHLK----LQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKR 226
Cdd:COG1120 72 ELA--RRIA-YVPQEPPAPFGLTVRELVALgrYPHLGlfgrPSAED---REAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 227 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLFelFDQLYVLSQGQCVYRG 301
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
79-294 |
2.48e-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: 138.00 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSvpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLPRDLRC-- 156
Cdd:COG4133 3 LEAENLSCR---------RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-LLPPSAGEVLWNGEPIRDARed 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 157 FRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqeKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNN 236
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 237 PPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsakLFELFDQLYVLSQ 294
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
96-599 |
1.69e-36 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 147.30 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 96 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMK--GAVLINGLPRDLRCFRKVSCYIMQDDMLLPH 173
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGYRLNEFVPRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQEAMMVSA-------------HLKLQEKDEG--------------RREMVKE------ILTALGLLSCANTRTGS-- 218
Cdd:PLN03140 254 MTVKETLDFSArcqgvgtrydllsELARREKDAGifpeaevdlfmkatAMEGVKSslitdyTLKILGLDICKDTIVGDem 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 ---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSAKLFELFDQLYVLSQ 294
Cdd:PLN03140 334 irgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 295 GQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASG----EYGDQNSRLVRAVREGMCDSDHKR-----DLGGDAEV 365
Cdd:PLN03140 414 GQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKkdqeQYWADRNKPYRYISVSEFAERFKSfhvgmQLENELSV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 366 nPFlwHRPSEEDSSSMEGCHSFSASCLTQFCilFKRTFLSIMRDSVL----THLRITSHIGIGLLIGLLYLGIGNEAKKV 441
Cdd:PLN03140 494 -PF--DKSQSHKAALVFSKYSVPKMELLKAC--WDKEWLLMKRNAFVyvfkTVQIIIVAAIASTVFLRTEMHTRNEEDGA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 442 LSnSGFLFFSMLFLMF---AALMPTVLTFPlemgVFLRE-----HLNYWYSLKAYYLAktmadVPFQIMFPVAYCSIVYW 513
Cdd:PLN03140 569 LY-IGALLFSMIINMFngfAELALMIQRLP----VFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVVWVVITYY 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 514 MTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVR 593
Cdd:PLN03140 639 SIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLS 718
|
....*.
gi 46592964 594 YGFEGV 599
Cdd:PLN03140 719 YGFNAL 724
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
79-306 |
1.76e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.11 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGL------PR 152
Cdd:COG3638 3 LELRNLSKRYPGG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGQdvtalrGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMV---------SAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQ 223
Cdd:COG3638 74 ALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgrtstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 224 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPS-AKlfELFDQLYVLSQGQCVYRG 301
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDlAR--RYADRIIGLRDGRVVFDG 229
|
....*
gi 46592964 302 KVCNL 306
Cdd:COG3638 230 PPAEL 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
79-296 |
3.02e-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: 134.06 E-value: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGYKTL--LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TgmKGAVLINGLP--RD 153
Cdd:cd03230 1 IEVRNLS-----------KRYGKKtaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpD--SGEIKVLGKDikKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRCFRKVSCYIMQDDMLLPHLTVQEammvsaHLKlqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALEL 233
Cdd:cd03230 68 PEEVKRRIGYLPEEPSLYENLTVRE------NLK-------------------------------LSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQ 296
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
95-301 |
4.36e-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: 134.70 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET--GMKGAVLINGLPRD--LRCFRKVSCYIMQDDML 170
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPYKefAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 171 LPHLTVQEAMMVSAHLKlqekdegRREMVKEIltalgllscantrtgslSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:cd03233 95 FPTLTVRETLDFALRCK-------GNEFVRGI-----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46592964 251 SASCFQVVSLMKGLAQG-GRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
110-301 |
1.81e-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: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 110 FNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScYIMQDDMLLPHLTVQE--AMM 181
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 182 VSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 261
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46592964 262 KGL-AQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 301
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 ... |
79-250 |
3.16e-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: 132.60 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDlRCF 157
Cdd:cd03293 1 LEVRNVSKTYGGG-----GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEPVT-GPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 158 RKVScYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNP 237
Cdd:cd03293 73 PDRG-YVFQQDALLPWLTVLDNVALGLELQGVPKAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170
....*....|...
gi 46592964 238 PVMFFDEPTSGLD 250
Cdd:cd03293 151 DVLLLDEPFSALD 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
79-303 |
3.51e-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: 140.04 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP------ 151
Cdd:COG1123 261 LEVRNLSKRYPV----RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRCFRKVSCYIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGL-LSCANTRTGSLSGGQRKRLA 228
Cdd:COG1123 335 RSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 229 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIictihqpsakLF---------ELFDQLYVLSQGQCV 298
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTY----------LFishdlavvrYIADRVAVMYDGRIV 484
|
....*
gi 46592964 299 YRGKV 303
Cdd:COG1123 485 EDGPT 489
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
64-301 |
2.31e-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: 139.58 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 64 EAQRFSSLPRRAAvNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmK 142
Cdd:COG2274 460 EGRSKLSLPRLKG-DIELENVSFRYPGDS-------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPT--S 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 143 GAVLINGL------PRDLRcfRKVScYIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGrremvk 200
Cdd:COG2274 530 GRILIDGIdlrqidPASLR--RQIG-VVLQDVFLFsgtirenitlgdPDATDEEiieaARLAGLHDFIEALPMG------ 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 201 eILTALGllscanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSa 280
Cdd:COG2274 601 -YDTVVG------EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS- 671
|
250 260
....*....|....*....|.
gi 46592964 281 kLFELFDQLYVLSQGQCVYRG 301
Cdd:COG2274 672 -TIRLADRIIVLDKGRIVEDG 691
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
79-301 |
5.13e-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: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING-----LPRD 153
Cdd:cd03257 2 LEVKNLSVSFP-----TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP-TSGSIIFDGkdllkLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LR--CFRKVScYIMQDDM--LLPHLTVQEAMM--VSAHLKLQEKDEgRREMVKEILTALGLLS-CANTRTGSLSGGQRKR 226
Cdd:cd03257 76 LRkiRRKEIQ-MVFQDPMssLNPRMTIGEQIAepLRIHGKLSKKEA-RKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 227 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
100-301 |
5.13e-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: 128.85 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGeLVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQ 177
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGqdVLKQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVSAHLK-LQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 256
Cdd:cd03264 91 EFLDYIAWLKgIPSKEVKAR--VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 257 VVSLMKGLAQgGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03264 169 FRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
79-296 |
5.79e-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: 5.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRD---- 153
Cdd:COG4619 1 LELEGLSFRV---------GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTS--GEIYLDGKPLSampp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 --LRcfRKVScYIMQDdmllPHL---TVQEAMMVSAHLKLQEKDegrREMVKEILTALGL-LSCANTRTGSLSGGQRKRL 227
Cdd:COG4619 70 peWR--RQVA-YVPQE----PALwggTVRDNLPFPFQLRERKFD---RERALELLERLGLpPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 228 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPsAKLFELFDQLYVLSQGQ 296
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
103-301 |
5.90e-34 |
|
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: 129.48 E-value: 5.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVL-----INGLPRDLRC-------FRKVScyimqddm 169
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLfdgedITGLPPHEIArlgigrtFQIPR-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 LLPHLTVQEAMMVSAHLKLQE---------KDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVM 240
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 241 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
79-250 |
6.55e-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: 130.21 E-value: 6.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPRDlRCFR 158
Cdd:COG1116 8 LELRGVSKRFP-----TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPVT-GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 KVScYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPP 238
Cdd:COG1116 81 DRG-VVFQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170
....*....|..
gi 46592964 239 VMFFDEPTSGLD 250
Cdd:COG1116 159 VLLMDEPFGALD 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
69-307 |
7.90e-34 |
|
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: 136.43 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 69 SSLPRRAAVNIEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYREtGMKGAVLIN 148
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGG--------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-PYSGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 GLPR---DLRCFRKVSCYIMQDDMLlPHLTVQEammvsaHLKLQEKDEGRREM--------VKEILTAL--GLlscaNTR 215
Cdd:COG4988 398 GVDLsdlDPASWRRQIAWVPQNPYL-FAGTIRE------NLRLGRPDASDEELeaaleaagLDEFVAALpdGL----DTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 216 TGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTiHQPSakLFELFDQLYV 291
Cdd:COG4988 467 LGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILV 543
|
250
....*....|....*.
gi 46592964 292 LSQGQCVYRGKVCNLV 307
Cdd:COG4988 544 LDDGRIVEQGTHEELL 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
79-296 |
7.90e-34 |
|
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: 127.11 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPR---DL 154
Cdd:cd03228 1 IEFKNVSFSYPGRP-------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlYDPT--SGEILIDGVDLrdlDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQDDMLLpHLTVQEAMmvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELV 234
Cdd:cd03228 72 ESLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 235 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
80-296 |
1.05e-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: 126.21 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP---RDLR 155
Cdd:cd00267 1 EIENLSFRYGG---------RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGlLKPT--SGEILIDGKDiakLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQddmllphltvqeammvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVN 235
Cdd:cd00267 70 ELRRRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 236 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQ 296
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 ... |
98-296 |
1.81e-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: 127.64 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGlpRDLRCF----RKVScYIMQDDMLLPH 173
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDG--RDVTGVpperRNIG-MVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQEAmmVSAHLKLQEKDEG-RREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 252
Cdd:cd03259 87 LTVAEN--IAFGLKLRGVPKAeIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46592964 253 SCFQVVSLMKGL-AQGGRSIICTIHQPS-AklFELFDQLYVLSQGQ 296
Cdd:cd03259 165 LREELREELKELqRELGITTIYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
79-312 |
2.88e-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: 127.79 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----L 150
Cdd:COG1127 6 IEVRNLT-----------KSFgdRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGqditgL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 PRD----LRcfRKVScYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQR 224
Cdd:COG1127 73 SEKelyeLR--RRIG-MLFQGGALFDSLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIICTiHQ-PSAklFELFDQLYVLSQGQCVYRG 301
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEG 224
|
250
....*....|....*
gi 46592964 302 KVCNLV----PYLRD 312
Cdd:COG1127 225 TPEELLasddPWVRQ 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
80-301 |
2.94e-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: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGlpRDLrcfrk 159
Cdd:cd03214 1 EVENLSVGYGG---------RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDG--KDL----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 160 vscyimqddmllphltvqeammvsAHLKLQEKdegRREM--VKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNP 237
Cdd:cd03214 64 ------------------------ASLSPKEL---ARKIayVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPS-AKLFelFDQLYVLSQGQCVYRG 301
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
79-302 |
3.47e-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: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP------R 152
Cdd:TIGR02315 2 LEVENLSKVYPNG--------KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-VEPSSGSILLEGTDitklrgK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQDDMLLPHLTVQEAMM---VSAHLKLQ-------EKDegrREMVKEILTALGLLSCANTRTGSLSGG 222
Cdd:TIGR02315 73 KLRKLRRRIGMIFQHYNLIERLTVLENVLhgrLGYKPTWRsllgrfsEED---KERALSALERVGLADKAYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 223 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLFElfDQLYVLSQGQCVYR 300
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFD 227
|
..
gi 46592964 301 GK 302
Cdd:TIGR02315 228 GA 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
79-296 |
2.15e-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: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----LPR 152
Cdd:COG2884 2 IRFENVSKRYPGG--------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 D----LRcfRKVScYIMQDDMLLPHLTVQE----AMMVsahLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQR 224
Cdd:COG2884 72 ReipyLR--RRIG-VVFQDFRLLPDRTVYEnvalPLRV---TGKSRKEIRRR--VREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsaklfELFDQL----YVLSQGQ 296
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL-----ELVDRMpkrvLELEDGR 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
78-301 |
2.38e-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: 124.62 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGL------ 150
Cdd:cd03245 2 RIEFRNVSFSYPNQE-------IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTS--GSVLLDGTdirqld 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 PRDLRcfRKVScYIMQDdmllPHL---TVQEAMMvsahLKLQEKDEgrrEMVKEILTALGLLSCANT-----------RT 216
Cdd:cd03245 73 PADLR--RNIG-YVPQD----VTLfygTLRDNIT----LGAPLADD---ERILRAAELAGVTDFVNKhpngldlqigeRG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 217 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAqGGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGR 215
|
....*
gi 46592964 297 CVYRG 301
Cdd:cd03245 216 IVADG 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
79-277 |
2.65e-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: 124.18 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGYKTL--LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGLP-- 151
Cdd:cd03262 1 IEIKNLH-----------KSFGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGLKlt 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 ---RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVsAHLKLQ--EKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKR 226
Cdd:cd03262 66 ddkKNINELRQKVGMVFQQFNLFPHLTVLENITL-APIKVKgmSKAEAE-ERALELLEKVGLADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592964 227 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQ 277
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
79-347 |
2.78e-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: 131.18 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGMKGAVLING-----LP 151
Cdd:COG1123 5 LEVRDLSVRYPGGD-------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGrdlleLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRCfRKVScYIMQDDM--LLPhLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:COG1123 78 EALRG-RRIG-MVFQDPMtqLNP-VTVGDQIAEALENLGLSRAE-ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPsAKLFELFDQLYVLSQGQCVYRGKVCNL-- 306
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIla 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 46592964 307 -------VPYLRDLGLNCPTYHNPADFVMEVA--SGEYGDQNSRLVRAVR 347
Cdd:COG1123 233 apqalaaVPRLGAARGRAAPAAAAAEPLLEVRnlSKRYPVRGKGGVRAVD 282
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
79-276 |
5.36e-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: 5.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP------R 152
Cdd:cd03292 1 IEFINVTKTYPNG--------TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:cd03292 72 AIPYLRRKIGVVFQDFRLLPDRNVYENVAFA----LEVTGVPPREIrkrVPAALELVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
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 ... |
83-276 |
1.20e-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: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 83 DLSYSVPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPRDLRCFRKVS 161
Cdd:cd03226 4 NISFSYKKGT--------EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 162 CYIMQD-DMLLPHLTVQEAMMVSahLKLQEKDEGRREmvkEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVM 240
Cdd:cd03226 74 GYVMQDvDYQLFTDSVREELLLG--LKELDAGNEQAE---TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 46592964 241 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
79-296 |
1.26e-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: 121.14 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPRD 153
Cdd:cd03229 1 LELKNVSKRYGQ---------KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGedltdLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRCFRKVSCYIMQDDMLLPHLTVQEammvsahlklqekdegrremvkeiltalgllscaNTRTGsLSGGQRKRLAIALEL 233
Cdd:cd03229 71 LPPLRRRIGMVFQDFALFPHLTVLE----------------------------------NIALG-LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPsAKLFELFDQLYVLSQGQ 296
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
79-301 |
4.39e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP-----R 152
Cdd:PRK13639 2 LETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT--SGEVLIKGEPikydkK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:PRK13639 72 SLLEVRKTVGIVFQnpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpsAKLFELF-DQLYVLSQGQCVYRG 301
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
80-295 |
1.22e-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: 119.56 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLINGLPrdLRCFR 158
Cdd:cd03235 1 EVEDLTVSY---------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLlKPT--SGSIRVFGKP--LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 KVSCYIMQD---DMLLPhLTVQEAMM------VSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:cd03235 68 KRIGYVPQRrsiDRDFP-ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQG 295
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
79-278 |
1.63e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 127.15 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNIL-------AG-YRETGMKGAVLINGL 150
Cdd:PRK10535 5 LELKDIRRSYPSG-----EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 PRDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:PRK10535 80 LAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQP 278
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
79-313 |
1.65e-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: 120.29 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLR 155
Cdd:COG1124 2 LEVRNLSVSYGQGGRRV-----PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQDDM--LLPHLTVQEAmmVSAHLKLQEKDEgRREMVKEILTALGL-LSCANTRTGSLSGGQRKRLAIALE 232
Cdd:COG1124 76 AFRRRVQMVFQDPYasLHPRHTVDRI--LAEPLRIHGLPD-REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 233 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPSAKLFeLFDQLYVLSQGQCV---YRGKVCNLV- 307
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGRIVeelTVADLLAGPk 231
|
....*..
gi 46592964 308 -PYLRDL 313
Cdd:COG1124 232 hPYTREL 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
69-313 |
2.43e-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: 126.03 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 69 SSLPRRAAVNIEFRDLSYSVPEGPWWrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLIN 148
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRP-------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 GLP-RDLR--CFRKVSCYIMQDdmllPHL---TVQEammvsaHLKLQEKDEGRREMVkEILTALGLLSCA-------NTR 215
Cdd:COG4987 396 GVDlRDLDedDLRRRIAVVPQR----PHLfdtTLRE------NLRLARPDATDEELW-AALERVGLGDWLaalpdglDTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 216 TGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYV 291
Cdd:COG4987 465 LGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILV 541
|
250 260
....*....|....*....|....*
gi 46592964 292 LSQGQCVYRGKVCNLV---PYLRDL 313
Cdd:COG4987 542 LEDGRIVEQGTHEELLaqnGRYRQL 566
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
103-302 |
2.54e-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: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 178
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSAHLKLQEKDEGRREMVKEILTALGLLScaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 258
Cdd:cd03224 95 NLLLGAYARRRAKRKARLERVYELFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 259 SLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQCVYRGK 302
Cdd:cd03224 173 EAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
103-276 |
3.11e-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: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP-----RDLRCFRKVSCYIMQ--DDMLLPHL 174
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQ--SGAVLIDGEPldysrKGLLERRQRVGLVFQdpDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 254
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERR--VREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|..
gi 46592964 255 FQVVSLMKGLAQGGRSIICTIH 276
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTH 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
78-303 |
4.17e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLSYSvpegpwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPR 152
Cdd:COG3840 1 MLRLDDLTYR-----------YGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGF-LPPDSGRILWNGqdltaLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLrcfRKVScYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:COG3840 69 AE---RPVS-MLFQENNLFPHLTVAQniGLGLRPGLKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPS-AKLfeLFDQLYVLSQGQCVYRGKV 303
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAAR--IADRVLLVADGRIAADGPT 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
79-277 |
7.64e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.27 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLM---NILagyrETGMKGAVLINGL----P 151
Cdd:PRK09493 2 IEFKNVS---------KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVDGLkvndP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 R-DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSA-HLKLQEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:PRK09493 69 KvDERLIRQEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAE-KQARELLAKVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQ 277
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
103-296 |
8.42e-30 |
|
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: 118.60 E-value: 8.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGlpRDL--------------RCFRKVScyimqd 167
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDG--RDItglpphriarlgiaRTFQNPR------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 dmLLPHLTVQEAMMVSAHLKLQE-------------KDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 233
Cdd:COG0411 90 --LFPELTVLENVLVAAHARLGRgllaallrlprarREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQ 296
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 ... |
64-298 |
1.74e-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: 124.21 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 64 EAQRFSSLPRRAAvNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmK 142
Cdd:TIGR03375 450 EGTRFLHRPRLQG-EIEFRNVSFAYPGQE-------TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGlYQPT--E 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 143 GAVLINGL------PRDLRcfRKVScYIMQDDMLLpHLTVQEAMMVSAhlkLQEKDEgrrEMVkEILTALGLLSCANT-- 214
Cdd:TIGR03375 520 GSVLLDGVdirqidPADLR--RNIG-YVPQDPRLF-YGTLRDNIALGA---PYADDE---EIL-RAAELAGVTEFVRRhp 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 215 ---------RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAqGGRSIICTIHQPSakLFEL 285
Cdd:TIGR03375 589 dgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS--LLDL 665
|
250
....*....|...
gi 46592964 286 FDQLYVLSQGQCV 298
Cdd:TIGR03375 666 VDRIIVMDNGRIV 678
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
79-276 |
2.22e-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: 116.63 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGYKTL--LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGLP-- 151
Cdd:COG1126 2 IEIENLH-----------KSFGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDlt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 ---RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVS-AHLKLQEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRL 227
Cdd:COG1126 67 dskKDINKLRRKVGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46592964 228 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
79-303 |
6.46e-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: 6.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PR 152
Cdd:cd03258 2 IELKNVSKVFGDT-----GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALE 232
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAE-IEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 233 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 303
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTV 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
98-301 |
9.88e-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: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLPRDLRCFRKVSCyIMQDDMLLPHLTV 176
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDSGEITFDGKSYQKNIEALRRIGA-LIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSAHLKLqekdeGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 256
Cdd:cd03268 90 RENLRLLARLLG-----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 257 VVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03268 165 LRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
79-301 |
1.58e-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: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGL------PR 152
Cdd:COG4559 2 LEAENLSVRL---------GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGEL-TPSSGEVRLNGRplaawsPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVscyimqddmlLP-------HLTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGG- 222
Cdd:COG4559 72 ELARRRAV----------LPqhsslafPFTVEEvvALGRAPHGSSAAQD---RQIVREALALVGLAHLAGRSYQTLSGGe 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 223 -QRKRLAIAL----ELVNNPP-VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPS-AKLFElfDQLYVLSQG 295
Cdd:COG4559 139 qQRVQLARVLaqlwEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYA--DRILLLHQG 216
|
....*.
gi 46592964 296 QCVYRG 301
Cdd:COG4559 217 RLVAQG 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
99-302 |
1.84e-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: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 99 YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPR-DLRCFRKVSCYIMQDDMLLPHLTVQ 177
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-IEPASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVSAH--LKLQEKdegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:TIGR01277 89 QNIGLGLHpgLKLNAE---QQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46592964 256 QVVSLMKGLA-QGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGK 302
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGKIKVVSD 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
79-266 |
3.02e-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: 113.30 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPRD 153
Cdd:COG4181 9 IELRGLTKTVGTG-----AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGqdlfaLDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRC-FR--KVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:COG4181 83 ARArLRarHVG-FVFQSFQLLPTLTALENVMLPLELA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 266
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
79-303 |
8.24e-28 |
|
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: 112.49 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSvpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-----YRET----GMK-GAVLIn 148
Cdd:COG1119 4 LELRNVTVR---------RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptYGNDvrlfGERrGGEDV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 glpRDLRcfRK---VSCYIMQDdmLLPHLTVQEaMMVSA-------HLKLQEKDEGRremVKEILTALGLLSCANTRTGS 218
Cdd:COG1119 74 ---WELR--KRiglVSPALQLR--FPRDETVLD-VVLSGffdsiglYREPTDEQRER---ARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSAkLFELFDQLYVLSQGQC 297
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRV 221
|
....*.
gi 46592964 298 VYRGKV 303
Cdd:COG1119 222 VAAGPK 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
98-278 |
1.27e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 110.73 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQ 177
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVSAHLKlqekdEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 257
Cdd:PRK13539 92 ENLEFWAAFL-----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|..
gi 46592964 258 VSLMKG-LAQGGRSIICTiHQP 278
Cdd:PRK13539 167 AELIRAhLAQGGIVIAAT-HIP 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
96-301 |
1.29e-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: 111.48 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 96 KKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----LPRDLRCfRKVSCYIMQD 167
Cdd:cd03218 7 SKRYgkRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGKILLDGqditkLPMHKRA-RLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 DMLLPHLTVQEAMMvsAHLKLQEKD-EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 246
Cdd:cd03218 84 ASIFRKLTVEENIL--AVLEIRGLSkKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 247 SGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 301
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEG 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
79-250 |
1.78e-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: 114.04 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LP 151
Cdd:COG3842 6 LELENVS-----------KRYgdVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGrdvtgLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 ---RDLrcfrkvsCYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKR 226
Cdd:COG3842 74 pekRNV-------GMVFQDYALFPHLTVAEN--VAFGLRMRgvPKAE-IRARVAELLELVGLEGLADRYPHQLSGGQQQR 143
|
170 180
....*....|....*....|....
gi 46592964 227 LAIALELVNNPPVMFFDEPTSGLD 250
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALD 167
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
95-306 |
3.08e-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: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGLP--RDLRCFRKVSCYIMQDDMLL 171
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQEAMMVsaHLKLQE-KDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:cd03265 86 DELTGWENLYI--HARLYGvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 251 SASCFQVVSLMKGL-AQGGRSIICTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVCNL 306
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
103-250 |
5.27e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.86 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------LPRDlrcfRKVScyiM--QDDMLLPHL 174
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL-EDPTSGEILIGGrdvtdlPPKD----RNIA---MvfQSYALYPHM 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 175 TVQEAMmvSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:COG3839 91 TVYENI--AFPLKLRkvPKAE-IDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
98-250 |
5.49e-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: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP-RDLRCFRKVSCYIMQDDMLLPHLTV 176
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 177 QEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
112-301 |
1.27e-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: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 112 SGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------------PRDlrcfRKVScYIMQDDMLLPHLTVQEA 179
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 180 MMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 259
Cdd:cd03297 96 LAFGLKRKRNRED---RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 260 LMKGLAQ--GGRSIICTiHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03297 173 ELKQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
101-251 |
1.72e-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: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 101 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-------LPRDlrcfRKVScYIMQDDMLLPH 173
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGrdlftnlPPRE----RRVG-FVFQHYALFPH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 174 LTVQEAmmVSAHLKLQEKDEG-RREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:COG1118 90 MTVAEN--IAFGLRVRPPSKAeIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
100-252 |
5.79e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.03 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETG--MKGAVLINGlpRDLRCF----RKVScYIMQDDMLLPH 173
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNG--RRLTALpaeqRRIG-ILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQE--AMMVSAHLKLQEkdegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:COG4136 91 LSVGEnlAFALPPTIGRAQ----RRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 46592964 252 A 252
Cdd:COG4136 167 A 167
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
71-292 |
7.85e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 111.99 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 71 LPRRAAVNIEFRDLSYSVPegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL 150
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYP--------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 PR---DLRCFRKVSCYIMQddmlLPHLTvqeAMMVSAHLKLQEKDeGRREMVKEILTALGLLSCA-------NTRTGS-- 218
Cdd:TIGR02857 385 PLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRLARPD-ASDAEIREALERAGLDEFVaalpqglDTPIGEgg 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 219 --LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPsaKLFELFDQLYVL 292
Cdd:TIGR02857 457 agLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
100-301 |
9.59e-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: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNIL----AGYRETG---MKGAVLINGLPRDLRCFRKVSCYIMQDDM 169
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLeqpeAGTIRVGditIDTARSLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 LLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 249
Cdd:PRK11264 96 LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592964 250 DSASCFQVVSLMKGLAQGGRSIICTIHQPS-AKlfELFDQLYVLSQGQCVYRG 301
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQG 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
78-301 |
9.97e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 9.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLSYSVPEGPWwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP------ 151
Cdd:COG1132 339 EIEFENVSFSYPGDRP--------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDirdltl 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRcfRKVScYIMQDDMLLpHLTVQE-----------------AMMVSAHLKLQEKDEGRREMVKEiltalgllscant 214
Cdd:COG1132 410 ESLR--RQIG-VVPQDTFLF-SGTIREnirygrpdatdeeveeaAKAAQAHEFIEALPDGYDTVVGE------------- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 215 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIIctI-HQPSAklFELFDQLYVLS 293
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV--IaHRLST--IRNADRILVLD 548
|
....*...
gi 46592964 294 QGQCVYRG 301
Cdd:COG1132 549 DGRIVEQG 556
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
113-252 |
1.34e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.82 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGlpRDLRCF----RKVScYIMQDDMLLPHLTVQEAMMVSAH--L 186
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFL-TPASGSLTLNG--QDHTTTppsrRPVS-MLFQENNLFSHLTVAQNIGLGLNpgL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 187 KLqekDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 252
Cdd:PRK10771 101 KL---NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
97-278 |
6.04e-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: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 97 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP----RDLRcfRKVSCYIMQDDMLLP 172
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPlaeqRDEP--HENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTVQEAMMVSAHLKlqekdEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 252
Cdd:TIGR01189 87 ELSALENLHFWAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 46592964 253 SCFQVVSLMKGLAQGGRSIICTIHQP 278
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
79-296 |
1.05e-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: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP---RDLR 155
Cdd:cd03246 1 LEVENVSFRYPGAEPP-------VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADisqWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQDDMLLPHlTVQEAMmvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVN 235
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 236 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-262 |
2.22e-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: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING-----LPRDLRCFrkvsCYIMQDDMLLPHLTVQ 177
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGkditnLPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 257
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
....*
gi 46592964 258 VSLMK 262
Cdd:cd03299 169 REELK 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
79-266 |
3.62e-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: 101.49 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMK----GAVLING----- 149
Cdd:cd03260 1 IELRDLNVYY---------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGkdiyd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 150 ---LPRDLRcfRKVScYIMQDDMLLPhLTVQEAmmVSAHLKLQE--KDEGRREMVKEILTALGLLSCANTRTG--SLSGG 222
Cdd:cd03260 72 ldvDVLELR--RRVG-MVFQKPNPFP-GSIYDN--VAYGLRLHGikLKEELDERVEEALRKAALWDEVKDRLHalGLSGG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 223 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 266
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
97-278 |
5.44e-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: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 97 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRD-LRCFRKVSC-YIMQDDMLLPHL 174
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPLDfQRDSIARGLlYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAMMVSAhlklqekDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 254
Cdd:cd03231 89 SVLENLRFWH-------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 46592964 255 FQVVSLMKGLAQGGRSIICTIHQP 278
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
78-301 |
6.00e-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: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---RDL 154
Cdd:cd03254 2 EIEFENVNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQDDMLLPHlTVQEAMMVSahlklqeKDEGRREMVKEILTAL-----------GLLSCANTRTGSLSGGQ 223
Cdd:cd03254 73 KSLRSMIGVVLQDTFLFSG-TIMENIRLG-------RPNATDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 224 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTiHQPSAKLFElfDQLYVLSQGQCVYRG 301
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
101-278 |
1.01e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 101 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYREtgmkgavlinglPRDLRCFRKVSC---YIMQ---DDMLLPhL 174
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------------PTSGTVRRAGGArvaYVPQrseVPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAMMVS--AHLKLQEK-DEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:NF040873 73 TVRDLVAMGrwARRGLWRRlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIHQP 278
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
103-268 |
1.50e-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: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL---------PRDLRCFRKVSCYIMQDDML 170
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 171 LPHLTVQEAMmVSAHLKL--QEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:COG4161 94 WPHLTVMENL-IEAPCKVlgLSKEQAR-EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|
gi 46592964 249 LDSASCFQVVSLMKGLAQGG 268
Cdd:COG4161 172 LDPEITAQVVEIIRELSQTG 191
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
103-306 |
1.76e-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: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGL-----PRDLR-----CFRKVSCYimqDDmll 171
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGYdvvrePRKVRrsigiVPQYASVD---ED--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 phLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:TIGR01188 81 --LTGRENLEMMGRLYGLPKDE-AEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIHQpsakLFE---LFDQLYVLSQGQCVYRGKVCNL 306
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
79-298 |
1.81e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL------PR 152
Cdd:PRK13548 3 LEARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVscyimqddmlLPH-------LTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLSCANTRTGSLSGG- 222
Cdd:PRK13548 73 ELARRRAV----------LPQhsslsfpFTVEEvvAMGRAPHGLSRAED---DALVAAALAQVDLAHLAGRDYPQLSGGe 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 223 -QRKRLAIAL----ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHqpSAKLFELF-DQLYVLSQG 295
Cdd:PRK13548 140 qQRVQLARVLaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQG 217
|
...
gi 46592964 296 QCV 298
Cdd:PRK13548 218 RLV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
79-301 |
2.39e-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: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRkkgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP-RD--LR 155
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV-------LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDGHDvRDytLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKvSCYIMQDDMLLPHLTVQE-----------------AMMVSAHLKLQEKDEGRREMVKEiltalgllscantRTGS 218
Cdd:cd03251 73 SLRR-QIGLVSQDVFLFNDTVAEniaygrpgatreeveeaARAANAHEFIMELPEGYDTVIGE-------------RGVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYVLSQGQCV 298
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIV 215
|
...
gi 46592964 299 YRG 301
Cdd:cd03251 216 ERG 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
79-298 |
4.11e-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: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL------PR 152
Cdd:cd03295 1 IEFENVTKRYGGG--------KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRcfRKVScYIMQDDMLLPHLTVQEAmmVSAHLKLQE-KDEGRREMVKEILTALGL--LSCANTRTGSLSGGQRKRLAI 229
Cdd:cd03295 72 ELR--RKIG-YVIQQIGLFPHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSaKLFELFDQLYVLSQGQCV 298
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDID-EAFRLADRIAIMKNGEIV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
98-301 |
4.93e-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: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPRDLRCFRKVScYIMQDDMLLPHLTV 176
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPD--SGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 256
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 257 VVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
102-250 |
1.25e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 102 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---------RDLRCfRKVScYIMQDDMLLP 172
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTVQE--AM-MVSAHLKLQEKDEGRREMvkeiLTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 249
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
.
gi 46592964 250 D 250
Cdd:PRK11629 177 D 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
79-251 |
1.54e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.63 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP-----RD 153
Cdd:COG4525 4 LTVRHVSVRYPGG-----GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 lrcfRKVscyIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 231
Cdd:COG4525 78 ----RGV---VFQKDALLPWLNVLDN--VAFGLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180
....*....|....*....|
gi 46592964 232 ELVNNPPVMFFDEPTSGLDS 251
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDA 167
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
79-302 |
1.58e-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: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGlpRDLR--- 155
Cdd:cd03253 1 IEFENVTFAYDPG--------RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDG--QDIRevt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 --CFRKVSCYIMQDDMLL----------PHLTVQEAMMVSA------HLKLQEKDEGRREMVKEiltalgllscantRTG 217
Cdd:cd03253 70 ldSLRRAIGVVPQDTVLFndtigyniryGRPDATDEEVIEAakaaqiHDKIMRFPDGYDTIVGE-------------RGL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 218 SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPS----AklfelfDQLYVLS 293
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLStivnA------DKIIVLK 209
|
....*....
gi 46592964 294 QGQCVYRGK 302
Cdd:cd03253 210 DGRIVERGT 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
76-278 |
1.91e-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: 101.67 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 76 AVNIEFRDLSYSVPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---R 152
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAP--------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVSCYIMQDdmllPHL---TVQEAMMVSahlklqeKDEGRREMVKEILTALGLL-------SCANTRTG----S 218
Cdd:TIGR02868 403 DQDEVRRRVSVCAQD----AHLfdtTVRENLRLA-------RPDATDEELWAALERVGLAdwlralpDGLDTVLGeggaR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGlAQGGRSIICTIHQP 278
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
103-301 |
2.01e-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: 95.90 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL-----PRDLRcfRKVScyIMQDDM-LLPHLTV 176
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFdvvkePAEAR--RRLG--FVSDSTgLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSAHLKLQEKDE--GRremVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 254
Cdd:cd03266 96 RENLEYFAGLYGLKGDEltAR---LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46592964 255 FQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
111-268 |
3.03e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 111 NSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLINGL---------PRDLRCFRKVSCYIMQDDMLLPHLTVQEAMm 181
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 182 VSAHLKLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 260
Cdd:PRK11124 104 IEAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
....*...
gi 46592964 261 MKGLAQGG 268
Cdd:PRK11124 184 IRELAETG 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
94-296 |
3.18e-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: 95.40 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 94 WRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LP---RDLrcfrkvsCYIM 165
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGrdvtdLPpkdRDI-------AMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 166 QDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592964 246 TSGLDSASCFQVVSLMKGLAQG-GRSIICTIH-QPSAklFELFDQLYVLSQGQ 296
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
79-250 |
3.69e-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: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS--YSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL--- 150
Cdd:COG1135 2 IELENLSktFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 ---PRDLRCFR-KVScYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQR 224
Cdd:COG1135 71 alsERELRAARrKIG-MIFQHFNLLSSRTVAEN--VALPLEIAgvPKAE-IRKRVAELLELVGLSDKADAYPSQLSGGQK 146
|
170 180
....*....|....*....|....*.
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALD 172
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
103-301 |
3.69e-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: 95.82 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGlpRD---LRCFRKVS---CYIMQDDMLLPHLTV 176
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL-LPPRSGSIRFDG--EDitgLPPHRIARlgiGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSAHL-KLQEKDEGRREMVKEILTALGLLscANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL-----D 250
Cdd:COG0410 96 EENLLLGAYArRDRAEVRADLERVYELFPRLKER--RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592964 251 sascfQVVSLMKGLAQGGRSIICtIHQPSAKLFELFDQLYVLSQGQCVYRG 301
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 ... |
103-251 |
5.37e-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: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScYIMQDDMLLPHLTV 176
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEdatdvpVQE----RNVG-FVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAmmVSAHLKLQEKDEGR-----REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:cd03296 92 FDN--VAFGLRVKPRSERPpeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
80-301 |
5.63e-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: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLING-----LP 151
Cdd:COG0396 2 EIKNLHVSVEG---------KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGedileLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRC----FrkvscYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGR--REMVKEILTALGL----LS-CANtrtGSLS 220
Cdd:COG0396 71 PDERAragiF-----LAFQYPVEIPGVSVSNFLRTALNARRGEELSARefLKLLKEKMKELGLdedfLDrYVN---EGFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 221 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVS-LMKGLAQGGRSIICTIHQPsaKLFELF--DQLYVLSQGQC 297
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRI 219
|
....
gi 46592964 298 VYRG 301
Cdd:COG0396 220 VKSG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
103-272 |
7.22e-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: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDLRCFRK-----VSCyIMQDDMLLPHLTV 176
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagIAI-IHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSahlklQEKDEG----RREMVK---EILTALGL-LScANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:COG1129 97 AENIFLG-----REPRRGglidWRAMRRrarELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180
....*....|....*....|....
gi 46592964 249 LDSASCFQVVSLMKGLAQGGRSII 272
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
79-302 |
7.86e-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: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSV-PEGPWwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLPR---DL 154
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--------ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-VPENGRVLVDGHDLalaDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQDDMLLP----------------HLTVQEAMMVSAHLKLQEKDEGRREMVKEiltalgllscantRTGS 218
Cdd:cd03252 72 AWLRRQVGVVLQENVLFNrsirdnialadpgmsmERVIEAAKLAGAHDFISELPEGYDTIVGE-------------QGAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYVLSQGQCV 298
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIV 215
|
....
gi 46592964 299 YRGK 302
Cdd:cd03252 216 EQGS 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
81-250 |
8.71e-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: 8.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 81 FRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLInglPRDLRcfrkV 160
Cdd:COG0488 1 LENLSKSFGG---------RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVSI---PKGLR----I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 161 ScYIMQDDMLLPHLTV-QEAMMVSAHLK--LQEKDEGRREM----------------------------VKEILTALGLL 209
Cdd:COG0488 64 G-YLPQEPPLDDDLTVlDTVLDGDAELRalEAELEELEAKLaepdedlerlaelqeefealggweaearAEEILSGLGFP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46592964 210 SC-ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:COG0488 143 EEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
79-250 |
1.01e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LP 151
Cdd:PRK09452 15 VELRGIS-----------KSFdgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDGqdithVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRCFRKVscyiMQDDMLLPHLTVQEAmmVSAHLKLQE--KDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:PRK09452 83 AENRHVNTV----FQSYALFPHMTVFEN--VAFGLRMQKtpAAE-ITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 46592964 230 ALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
95-277 |
1.05e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.04 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLING----LPRD------------LRCFR 158
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGqtinLVRDkdgqlkvadknqLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 KVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGS-LSGGQRKRLAIALELVNNP 237
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQ 277
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
98-301 |
1.31e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyR-ETGMKGAVLINGLPRDLRCFRKVSCYIMqddmLLP-HLT 175
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RlLTPQSGTVFLGDKPISMLSSRQLARRLA----LLPqHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 176 VQEAMMV--------SAHL----KLQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFD 243
Cdd:PRK11231 87 TPEGITVrelvaygrSPWLslwgRLSAED---NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 244 EPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH---QPSaklfELFDQLYVLSQGQCVYRG 301
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
79-301 |
1.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRD----- 153
Cdd:PRK13636 6 LKVEELNYNYSDG--------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPIDysrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 231
Cdd:PRK13636 77 LMKLRESVGMVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKR--VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 232 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHqpSAKLFELF-DQLYVLSQGQCVYRG 301
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQG 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
103-276 |
1.84e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 94.48 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL----------------PRDLRCFRKVSCY 163
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 164 IMQDDMLLPHLTVQE-AMMVSAHLKLQEKDEGRrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFF 242
Cdd:COG4598 100 VFQSFNLWSHMTVLEnVIEAPVHVLGRPKAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190
....*....|....*....|....*....|....
gi 46592964 243 DEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
79-318 |
2.37e-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: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGL------- 150
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKA----LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 --PRDLRcfRKVScYIMQddmlLPH-----LTVQEAMMVSAH-LKLQEKDEGRRemVKEILTALGL------LSCAntrt 216
Cdd:TIGR04521 75 kkLKDLR--KKVG-LVFQ----FPEhqlfeETVYKDIAFGPKnLGLSEEEAEER--VKEALELVGLdeeyleRSPF---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 217 gSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIICTIHQPSaKLFELFDQLYVLSQG 295
Cdd:TIGR04521 142 -ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKG 219
|
250 260
....*....|....*....|....*.
gi 46592964 296 QCVYRGK---VCNLVPYLRDLGLNCP 318
Cdd:TIGR04521 220 KIVLDGTpreVFSDVDELEKIGLDVP 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
82-298 |
5.67e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 82 RDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP------RDLR 155
Cdd:PRK10419 7 SGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQDDM--LLPHLTV----QEAMMvsaHLkLQEKDEGRREMVKEILTALGL-LSCANTRTGSLSGGQRKRLA 228
Cdd:PRK10419 86 AFRRDIQMVFQDSIsaVNPRKTVreiiREPLR---HL-LSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 229 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHqpSAKLFELFDQ-LYVLSQGQCV 298
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITH--DLRLVERFCQrVMVMDNGQIV 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
97-301 |
9.15e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 97 KGYK--TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGmkgAVLING-----LPRDLRCFRKVScYIMQD 167
Cdd:PRK10895 11 KAYKgrRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDedislLPLHARARRGIG-YLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 247
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46592964 248 GLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 301
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
103-311 |
1.01e-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: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPRDLRCFRKVscYIMQDDMLLPHLTVQE--AM 180
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 181 MVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS- 259
Cdd:TIGR01184 78 AVDRVLPDLSKSE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEe 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46592964 260 LMKGLAQGGRSIICTIHQPSAKLFeLFDQLYVLSQGQCVYRGKVCNlVPYLR 311
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE-VPFPR 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
79-266 |
1.22e-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: 93.19 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPegpwwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL----MNILAGYRETGmkGAVLINGL---- 150
Cdd:COG0444 2 LEVRNLKVYFP-----TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGITS--GEILFDGEdllk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 --PRDLRCFR--KVScYIMQDDM--LLPHLTVQEAMM--VSAHLKLQEKDegRREMVKEILTALGLlSCANTRTGS---- 218
Cdd:COG0444 75 lsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQIAepLRIHGGLSKAE--ARERAIELLERVGL-PDPERRLDRyphe 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMKGLAQ 266
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiQA---QILNLLKDLQR 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
96-250 |
1.39e-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: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 96 KKGYK--TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagyreTGM----KGAVLING-----LPRDLRC-------- 156
Cdd:COG1137 10 VKSYGkrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI-----VGLvkpdSGRIFLDGedithLPMHKRArlgigylp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 157 -----FRKvscyimqddmllphLTVQEAMMvsAHLKLQEKD-EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:COG1137 85 qeasiFRK--------------LTVEDNIL--AVLELRKLSkKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180
....*....|....*....|
gi 46592964 231 LELVNNPPVMFFDEPTSGLD 250
Cdd:COG1137 149 RALATNPKFILLDEPFAGVD 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
103-301 |
1.39e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.00 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY----RETGMKGAVLING------LPRDLRCFRKVSCYIMQDDMLLP 172
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTvqregrLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTVQEAMMVSA-------HLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:PRK09984 100 RLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 246 TSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 301
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
104-327 |
1.53e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 104 KGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE--TG--MKGAVLINGLPRDLRCFRKVscyiMQDDMLLPHLTVQEA 179
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGVGMV----FQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 180 MmvSAHLKLQEKDEG----RREMVKEILTALGLLscaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:PRK11000 96 M--SFGLKLAGAKKEeinqRVNQVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 256 Q----VVSLMKGLaqgGRSIICTIH-QPSAklFELFDQLYVLSQGQCVYRGKVCNLvpylrdlglncptYHNPAD-FV 327
Cdd:PRK11000 171 QmrieISRLHKRL---GRTMIYVTHdQVEA--MTLADKIVVLDAGRVAQVGKPLEL-------------YHYPANrFV 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
79-302 |
1.93e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLsysvpegpwwRKK-GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING--LPRDLR 155
Cdd:PRK13537 8 IDFRNV----------EKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGepVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQDDMLLPHLTVQEAMMV-SAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELV 234
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLLVfGRYFGLSAAAA--RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 235 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH-QPSAKlfELFDQLYVLSQGQCVYRGK 302
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHfMEEAE--RLCDRLCVIEEGRKIAEGA 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
78-302 |
2.47e-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: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLSYSVPEGPwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP-RDLR 155
Cdd:TIGR00958 478 LIEFQDVSFSYPNRP------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlYQPTG--GQVLLDGVPlVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 C---FRKVScyIMQDDMLLPHLTVQEAM----------MVSAHLKLQEKDEGRREMVKEILTALGllscantRTGS-LSG 221
Cdd:TIGR00958 550 HhylHRQVA--LVGQEPVLFSGSVRENIaygltdtpdeEIMAAAKAANAHDFIMEFPNGYDTEVG-------EKGSqLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 222 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKglaQGGRSIICTIHQPSakLFELFDQLYVLSQGQCVYRG 301
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKGSVVEMG 695
|
.
gi 46592964 302 K 302
Cdd:TIGR00958 696 T 696
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
93-302 |
2.51e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 93 WWRKKGyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP-----RDLRCFRKVSCYIMQD 167
Cdd:PRK13638 8 WFRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-QKGAVLWQGKPldyskRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 -DMLLPHLTVQEAMMVS-AHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:PRK13638 86 pEQQIFYTDIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 246 TSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGK 302
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGA 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
70-301 |
2.67e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.30 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 70 SLPRRAAVNIEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRetgmkGAVL 146
Cdd:PRK11174 341 ELASNDPVTIEAEDLEILSPDG--------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 147 INGLPR---DLRCFRKVSCYIMQDDmLLPHLTVQEAMMVSAHlklQEKDEG-----RREMVKEILTAL--GLLSCANTRT 216
Cdd:PRK11174 408 INGIELrelDPESWRKHLSWVGQNP-QLPHGTLRDNVLLGNP---DASDEQlqqalENAWVSEFLPLLpqGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 217 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTiHQpsakLFEL--FDQLYVLSQ 294
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ----LEDLaqWDQIWVMQD 558
|
....*..
gi 46592964 295 GQCVYRG 301
Cdd:PRK11174 559 GQIVQQG 565
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
79-301 |
2.85e-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: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDL--RC 156
Cdd:cd03247 1 LSINNVSFSYPEQE-------QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 157 FRKVSCYIMQDdmllPHL---TVQEAMmvsahlklqekdeGRRemvkeiltalgllscantrtgsLSGGQRKRLAIALEL 233
Cdd:cd03247 73 LSSLISVLNQR----PYLfdtTLRNNL-------------GRR----------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELFDQLYVLSQGQCVYRG 301
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
98-334 |
3.41e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM-KGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTV 176
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgKITVLGVPVPARARLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMV-SAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:PRK13536 132 RENLLVfGRYFGMSTRE--IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 256 QVVSLMKGLAQGGRSIICTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVCNLVpylrDLGLNCPtyhnpadfVMEVASGE 334
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTHfMEEAE--RLCDRLCVLEAGRKIAEGRPHALI----DEHIGCQ--------VIEIYGGD 275
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
71-301 |
3.98e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 71 LPRRAAVNIEFRDLSYSVP--EGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTlmNILAGYRETGMKGAVLIN 148
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPirKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 GLP------RDLRCFRKVSCYIMQD--DMLLPHLTVQEamMVSAHLKLQEKD---EGRREMVKEILTALGLLSCANTR-T 216
Cdd:PRK15134 346 GQPlhnlnrRQLLPVRHRIQVVFQDpnSSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 217 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQ 296
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
....*
gi 46592964 297 CVYRG 301
Cdd:PRK15134 504 VVEQG 508
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
103-298 |
6.12e-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: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGlprdlrcfRKVScyimqddmllpHLTVQEAM- 180
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlYKPDS--GEILVDG--------KEVS-----------FASPRDARr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 181 ----MVSahlklQekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 256
Cdd:cd03216 75 agiaMVY-----Q-----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 257 VVSLMKGLAQGGRSIICTIHqpsaKLFELF---DQLYVLSQGQCV 298
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
79-302 |
6.19e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGL---PRDL 154
Cdd:PRK13632 8 IKVENVSFSYPNS-------ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGItisKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQD-DMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:PRK13632 79 KEIRKKIGIIFQNpDNQFIGATVEDDIAFG----LENKKVPPKKMkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSAKLfeLFDQLYVLSQGQCVYRGK 302
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQGK 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
79-302 |
6.31e-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: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP-RDL--R 155
Cdd:cd03249 1 IEFKNVSFRYPSRP------DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGVDiRDLnlR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQDDMLL------------PHLTVQEAM----MVSAHLKLQEKDEGRREMVKEiltalgllscantRTGSL 219
Cdd:cd03249 74 WLRSQIGLVSQEPVLFdgtiaenirygkPDATDEEVEeaakKANIHDFIMSLPDGYDTLVGE-------------RGSQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 220 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVvslMKGL--AQGGRSIICTIHQPS----AklfelfDQLYVLS 293
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV---QEALdrAMKGRTTIVIAHRLStirnA------DLIAVLQ 211
|
....*....
gi 46592964 294 QGQCVYRGK 302
Cdd:cd03249 212 NGQVVEQGT 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
100-295 |
7.58e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLP-RDLRCFRKVscyIMQDDMLLPHLTVQE 178
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPvEGPGAERGV---VFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 258
Cdd:PRK11248 90 NVAFGLQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 46592964 259 SLMKGLAQG-GRSIICTIHQPSAKLFeLFDQLYVLSQG 295
Cdd:PRK11248 169 TLLLKLWQEtGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
106-250 |
9.39e-20 |
|
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: 89.63 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGmkGAVLINGLP---------RDLRcfRKVSCYIMQDDMLLPHLT 175
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTS--GKVLIDGQDiaamsrkelRELR--RKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 176 VQEAmmVSAHLKLQ-EKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:cd03294 119 VLEN--VAFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
71-301 |
1.10e-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: 92.83 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 71 LPRRAAVNIEFRDLS--YSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL-MNILagyRETGMKGAVLI 147
Cdd:COG4172 268 VPPDAPPLLEARDLKvwFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL---RLIPSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 148 NGLP------RDLRCFRK---VscyIMQDDM--LLPHLTV----QEAMMVsahLKLQEKDEGRREMVKEILTALGLLscA 212
Cdd:COG4172 345 DGQDldglsrRALRPLRRrmqV---VFQDPFgsLSPRMTVgqiiAEGLRV---HGPGLSAAERRARVAEALEEVGLD--P 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 213 NTRT---GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIictihqpsAKLF------ 283
Cdd:COG4172 417 AARHrypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHGL--------AYLFishdla 487
|
250 260
....*....|....*....|.
gi 46592964 284 ---ELFDQLYVLSQGQCVYRG 301
Cdd:COG4172 488 vvrALAHRVMVMKDGKVVEQG 508
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
103-302 |
1.24e-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: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETGMKGAVLINGLP------RDLRCFRkvsCYIMQDDMLLPhltv 176
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 qeAMMVSAHLKLQEKDEGRREMVK----EILTALGLLSCANTRTGSLSGG--QRKRLAIALELV---NNPP--VMFFDEP 245
Cdd:COG4138 83 --AMPVFQYLALHQPAGASSEAVEqllaQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 246 TSGLDSAScfQVV--SLMKGLAQGGRSIICTIHQPSAKLFELfDQLYVLSQGQCVYRGK 302
Cdd:COG4138 161 MNSLDVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGE 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
82-276 |
1.80e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 82 RDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLINGLPR---DLRCF- 157
Cdd:PRK10575 15 RNVSFRVPG---------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLeswSSKAFa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 158 RKVScYIMQDdmlLPH---LTVQEAMMVSA---HLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIAL 231
Cdd:PRK10575 85 RKVA-YLPQQ---LPAaegMTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46592964 232 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIH 276
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
79-303 |
1.81e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLP---RDLR 155
Cdd:PRK13652 4 IETRDLCYSY--------SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL-KPTSGSVLIRGEPitkENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 233
Cdd:PRK13652 75 EVRKFVGLVFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 303
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
79-303 |
1.92e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG----YRETGMKGAVLING---LP 151
Cdd:PRK14247 4 IEIRDLKVSF---------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGqdiFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRCFRKVSCYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEGRREM---VKEILTALGLLSCANTR----TGSLSGGQR 224
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNLSIFEN--VALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPsAKLFELFDQLYVLSQGQCVYRGKV 303
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGPT 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
110-296 |
2.11e-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: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 110 FNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLK 187
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGkdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 188 LQEKDEGRREMvKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG 267
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180
....*....|....*....|....*....
gi 46592964 268 GRSIICTIHQPSAKLfeLFDQLYVLSQGQ 296
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGR 1137
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
79-301 |
2.55e-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: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS-----YSVPEG-------PWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAV 145
Cdd:cd03267 1 IEVSNLSksyrvYSKEPGligslksLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 146 LINGL-P--RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGG 222
Cdd:cd03267 79 RVAGLvPwkRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKR-LDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 223 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIH--QPSAKlfeLFDQLYVLSQGQCVY 299
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEA---LARRVLVIDKGRLLY 234
|
..
gi 46592964 300 RG 301
Cdd:cd03267 235 DG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
60-302 |
2.67e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 60 NNLTEAQ---RFS--SLPRRAAVNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA 134
Cdd:PRK11160 315 NEITEQKpevTFPttSTAAADQVSLTLNNVSFTYPDQP-------QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 135 GYRETGmKGAVLINGLPrdLRCFRkvscyimqDDMLLPHLTV--QEAMMVSAHLK---LQEKDEGRREMVKEILTALGLL 209
Cdd:PRK11160 388 RAWDPQ-QGEILLNGQP--IADYS--------EAALRQAISVvsQRVHLFSATLRdnlLLAAPNASDEALIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 210 SCANTRTG----------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQps 279
Cdd:PRK11160 457 KLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR-- 533
|
250 260
....*....|....*....|...
gi 46592964 280 AKLFELFDQLYVLSQGQCVYRGK 302
Cdd:PRK11160 534 LTGLEQFDRICVMDNGQIIEQGT 556
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
79-276 |
3.27e-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: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyRETGM-KGAVLINGLP------ 151
Cdd:COG4604 2 IEIKNVSKRY---------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGLDvattps 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRcfRKVScyIM-QDDMLLPHLTVQEamMVS----AHLK--LQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQR 224
Cdd:COG4604 71 RELA--KRLA--ILrQENHINSRLTVRE--LVAfgrfPYSKgrLTAED---REIIDEAIAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIH 276
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
100-250 |
3.38e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.83 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLING-----LPRDLRcfrkvSCYI---MQDDML 170
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGkdvtkLPEYKR-----AKYIgrvFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 171 --LPHLTVQEAMMVSAH------LKLQEKDEgRREMVKEILTALGL-----LscaNTRTGSLSGGQRKRLAIALELVNNP 237
Cdd:COG1101 92 gtAPSMTIEENLALAYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLMATLTKP 167
|
170
....*....|...
gi 46592964 238 PVMFFDEPTSGLD 250
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
79-296 |
5.12e-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: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLP---RDL 154
Cdd:cd03248 12 VKFQNVTFAYPTRP------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfYQPQG--GQVLLDGKPisqYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQDDMLLPH---------LTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGllscanTRTGSLSGGQRK 225
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVG------EKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 226 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
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 ... |
103-301 |
7.85e-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: 86.04 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 178
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDiTKLPPHERARagiAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSahlkLQEKDEGRREMVKEILTALGLL-SCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL------DS 251
Cdd:TIGR03410 95 NLLTG----LAALPRRSRKIPDEIYELFPVLkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsiikDI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46592964 252 AscfQVVSLMKglAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQCVYRG 301
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 ... |
70-302 |
1.27e-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: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 70 SLPRRAAvNIEFRDLSYSV-PEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLIN 148
Cdd:TIGR01846 448 ALPELRG-AITFENIRFRYaPDSP--------EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVD 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 GL------PRDLRcfRKVSCyIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltal 206
Cdd:TIGR01846 518 GVdlaiadPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAPFEHvihaAKLAGAHDFISELPQGYNTEVGE----- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 207 gllscantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPSAklFELF 286
Cdd:TIGR01846 590 --------KGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLST--VRAC 658
|
250
....*....|....*.
gi 46592964 287 DQLYVLSQGQCVYRGK 302
Cdd:TIGR01846 659 DRIIVLEKGQIAESGR 674
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
79-301 |
1.69e-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: 84.12 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETgmKGAVLING-----L 150
Cdd:cd03217 1 LEIKDLHVSVGG---------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGeditdL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 PRDLRcFRKVSCYIMQDDMLLPHLTVQEAmmvsahlkLQEKDEGrremvkeiltalgllscantrtgsLSGGQRKRLAIA 230
Cdd:cd03217 70 PPEER-ARLGIFLAFQYPPEIPGVKNADF--------LRYVNEG------------------------FSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpsAKLFELF--DQLYVLSQGQCVYRG 301
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
103-250 |
1.88e-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: 89.63 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLRCFRKVSCYIMQDDMLLP------- 172
Cdd:TIGR03797 469 LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDlagLDVQAVRRQLGVVLQNGRLMSgsifeni 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 ----HLTVQEAMMVSAHLKLqekDEGRREMvkeiltALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:TIGR03797 548 aggaPLTLDEAWEAARMAGL---AEDIRAM------PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
..
gi 46592964 249 LD 250
Cdd:TIGR03797 619 LD 620
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
79-319 |
3.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL----PRDL 154
Cdd:PRK13644 2 IRLENVSYSYPDG--------TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGIdtgdFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQD-DMLLPHLTVQEAMMVSAHLKLQEKDEGRReMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 233
Cdd:PRK13644 73 QGIRKLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpsakLFELF--DQLYVLSQGQCVYRGKVCNLV--PY 309
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN----LEELHdaDRIIVMDRGKIVLEGEPENVLsdVS 227
|
250
....*....|
gi 46592964 310 LRDLGLNCPT 319
Cdd:PRK13644 228 LQTLGLTPPS 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
79-250 |
5.67e-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: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLIN-GLprdlrcf 157
Cdd:COG0488 316 LELEGLSKSYGD---------KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVKLGeTV------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 158 rKVScYIMQD-DMLLPHLTVQEAMMvsahlklQEKDEGRREMVKEILTALgLLS--CANTRTGSLSGGQRKRLAIALELV 234
Cdd:COG0488 379 -KIG-YFDQHqEELDPDKTVLDELR-------DGAPGGTEQEVRGYLGRF-LFSgdDAFKPVGVLSGGEKARLALAKLLL 448
|
170
....*....|....*.
gi 46592964 235 NNPPVMFFDEPTSGLD 250
Cdd:COG0488 449 SPPNVLLLDEPTNHLD 464
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
118-250 |
5.84e-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: 85.62 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 118 IMGPSGAGKSTLMNILAGYrETGMKGAVLING-----LPRDLRCFRKVscyiMQDDMLLPHLTVQEAmmVSAHLKLQEKD 192
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMRKVP 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 193 -EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:TIGR01187 74 rAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
95-303 |
6.39e-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: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDLRCFRKVScYimqddM---- 169
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPDS--GEVLWDGEPLDPEDRRRIG-Y-----Lpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 -LLPHLTVQEAMMVSAHLKLQEKDEGRREMvKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:COG4152 81 gLYPKMKVGEQLVYLARLKGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 249 LDSAScfqvVSLMKG----LAQGGRSIICTIHQ-PSAKlfELFDQLYVLSQGQCVYRGKV 303
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 ... |
100-303 |
6.80e-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: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLING-----LPRDLRCfRKVSCYIMQDDMLL 171
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsYEVTS--GTILFKGqdlleLEPDERA-RAGLFLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQEAMMVSAHLKLQEKDEGR------REMVKEILTALGL---LSCANTRTGsLSGGQRKRLAIALELVNNPPVMFF 242
Cdd:TIGR01978 90 PGVSNLEFLRSALNARRSARGEEPldlldfEKLLKEKLALLDMdeeFLNRSVNEG-FSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 243 DEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsaKLFELF--DQLYVLSQGQCVYRGKV 303
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSGDV 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
103-298 |
1.28e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDlrcFRKVS-------CYIMQDDMLLPHL 174
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMR---FASTTaalaagvAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAMMVsAHL--KLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:PRK11288 95 TVAENLYL-GQLphKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCV 298
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGRYV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
114-296 |
1.29e-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: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 114 ELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGlprdlRCF-------------RKVScYIMQDDMLLPHLTVQEam 180
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNG-----RTLfdsrkgiflppekRRIG-YVFQEARLFPHLSVRG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 181 mvsaHLKLQEKD---EGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 257
Cdd:TIGR02142 95 ----NLRYGMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46592964 258 VSLMKGLAQG-GRSIICTIHQPSaKLFELFDQLYVLSQGQ 296
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQ-EVLRLADRVVVLEDGR 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
79-278 |
1.33e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.52 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP------- 151
Cdd:PRK10584 7 VEVHHLKKSVGQG-----EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 --RDLRCfRKVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:PRK10584 81 arAKLRA-KHVG-FVFQSFMLIPTLNALENVELPALLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQP 278
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
98-276 |
1.55e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFRKVSCYIM---QDDMLLPHL 174
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSARAASRRVAsvpQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEA--MMVSAHL-KLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:PRK09536 93 DVRQVveMGRTPHRsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180
....*....|....*....|....*
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
79-303 |
1.98e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS--YSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGL--- 150
Cdd:PRK11153 2 IELKNISkvFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 ---PRDLRCFRKVSCYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKR 226
Cdd:PRK11153 71 alsEKELRKARRQIGMIFQHFNLLSSRTVFDN--VALPLELAGTPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 227 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPSA-KlfELFDQLYVLSQGQCVYRGKV 303
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVvK--RICDRVAVIDAGRLVEQGTV 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
103-250 |
3.68e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.35 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScyiM--QDDMLLPHL 174
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RDIA---MvfQNYALYPHM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 175 TVQEAMmvsAH-LKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK11650 92 SVRENM---AYgLKIRgmPKAE-IEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
95-266 |
3.94e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPrdLRCFRKVSCYIMQDDMLLPHL 174
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAmmVSAHLKLQEKDEGRremvkEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 254
Cdd:PRK11247 97 KVIDN--VGLGLKGQWRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170
....*....|..
gi 46592964 255 FQVVSLMKGLAQ 266
Cdd:PRK11247 170 IEMQDLIESLWQ 181
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
53-296 |
4.58e-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: 84.80 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 53 GHLKKVDNNLTEAQRFSSLPRRAAvNIEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNI 132
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPRPKG-RLSVENLTVVPPGSK-------RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 133 LAG-YRETGmkGAVLINGlpRDLRCFRKVSC-----YIMQDDMLLPHlTVQE----------------AMMVSAHlklqe 190
Cdd:COG4618 378 LVGvWPPTA--GSVRLDG--ADLSQWDREELgrhigYLPQDVELFDG-TIAEniarfgdadpekvvaaAKLAGVH----- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 191 kdegrrEMvkeILT-ALGLlscaNTRTGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA 265
Cdd:COG4618 448 ------EM---ILRlPDGY----DTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK 514
|
250 260 270
....*....|....*....|....*....|.
gi 46592964 266 QGGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
Cdd:COG4618 515 ARGATVVVITHRPS--LLAAVDKLLVLRDGR 543
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
79-301 |
4.63e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGL---PRDLR 155
Cdd:PRK13647 5 IEVEDLHFRYKDG--------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALEL 233
Cdd:PRK13647 76 WVRSKVGLVFQDpdDQVFSSTVWDDVAFGPVNMGLDKDEVERR--VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 234 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQCVYRG 301
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
105-250 |
4.97e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.19 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 105 GISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVL-----INGLPrDLRCFRKVSCYIMQDDMLLPHLTVQE 178
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILlrgqhIEGLP-GHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSAHLKLQE-------KDEGRREMVKEILT-------ALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDE 244
Cdd:PRK11300 100 NLLVAQHQQLKTglfsgllKTPAFRRAESEALDraatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
....*.
gi 46592964 245 PTSGLD 250
Cdd:PRK11300 180 PAAGLN 185
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
106-250 |
5.66e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLprDLRC---FRKVSCYIMQDDMLLPHLTVQEAMMV 182
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGV--DLSHvppYQRPINMMFQSYALFPHMTVEQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 183 SAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK11607 115 GLKQDKLPKAE-IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
103-251 |
6.06e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.85 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNS-------------GELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING--------LPRDLrcfrkvs 161
Cdd:PRK11432 9 LKNITKRFGSntvidnlnltikqGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDGedvthrsiQQRDI------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 162 CYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPV 239
Cdd:PRK11432 81 CMVFQSYALFPHMSLGEN--VGYGLKMLgvPKEE-RKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|..
gi 46592964 240 MFFDEPTSGLDS 251
Cdd:PRK11432 158 LLFDEPLSNLDA 169
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
113-276 |
7.33e-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: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRdlRCFRKVSCYIMQDDML---LPhLTVQEAMMVS-----A 184
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGrtghiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 185 HLKLQEKDEGRreMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL 264
Cdd:TIGR03771 82 WLRRPCVADFA--AVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170
....*....|..
gi 46592964 265 AQGGRSIICTIH 276
Cdd:TIGR03771 160 AGAGTAILMTTH 171
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
103-272 |
1.68e-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: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMN-ILAGYRETGmkGAVLI---NGL-------PRD---LRcfRKVSCYIMQdd 168
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVrhdGGWvdlaqasPREilaLR--RRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 mllpHLTV---QEAMMVSAH--LKLQEKDEGRREMVKEILTALGL------LSCANtrtgsLSGGQRKRLAIALELVNNP 237
Cdd:COG4778 101 ----FLRViprVSALDVVAEplLERGVDREEARARARELLARLNLperlwdLPPAT-----FSGGEQQRVNIARGFIADP 171
|
170 180 190
....*....|....*....|....*....|....*
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSII 272
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
61-252 |
1.80e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.09 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 61 NLTEAQRFSSLprraavnIEFRDLSYSVPegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA-GYRET 139
Cdd:PRK13657 324 GAIDLGRVKGA-------VEFDDVSFSYD--------NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 140 GmkGAVLINGLP-RD--LRCFRKVSCYIMQDDMLLphltvqeAMMVSAHLKLQEKDEGRREMVK--EILTALGLL----S 210
Cdd:PRK13657 389 S--GRILIDGTDiRTvtRASLRRNIAVVFQDAGLF-------NRSIEDNIRVGRPDATDEEMRAaaERAQAHDFIerkpD 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46592964 211 CANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 252
Cdd:PRK13657 460 GYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
98-296 |
1.86e-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: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING--LPR-DLRCFRKVSCYIMQDDMLLPHL 174
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP-TSGSVRLDGadLKQwDRETFGKHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQ---------EAMMVSAHLKLQekdeGRREMvkeIL-------TALGllscanTRTGSLSGGQRKRLAIALELVNNPP 238
Cdd:TIGR01842 408 VAEniarfgenaDPEKIIEAAKLA----GVHEL---ILrlpdgydTVIG------PGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 239 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSakLFELFDQLYVLSQGQ 296
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
103-303 |
3.24e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDlRCFRKVSC-----YIMQDDMLLPHLTVQ 177
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVSAHLKlqEKDEG--------RREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 249
Cdd:PRK09700 99 ENLYIGRHLT--KKVCGvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46592964 250 DSASCFQVVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCVYRGKV 303
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
103-272 |
3.70e-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: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPRDLRCFRK-VSCYI-M--QDDMLLPHLTVQ 177
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGlYQPD--SGEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 E----AMMVSAHLKLQEKDEgrREMVKEILTALGL---LscaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL- 249
Cdd:COG3845 99 EnivlGLEPTKGGRLDRKAA--RARIRELSERYGLdvdP---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLt 173
|
170 180
....*....|....*....|....*
gi 46592964 250 --DSASCFQVvslMKGLAQGGRSII 272
Cdd:COG3845 174 pqEADELFEI---LRRLAAEGKSII 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
79-296 |
3.73e-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: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRKKgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETG-MKGAVLINGlprdlrcf 157
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF----TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPG-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 158 rKVScyimqddmllphLTVQEAMMVSAHLK-----LQEKDEgrrEMVKEILTAlgllsCA------------NTRTG--- 217
Cdd:cd03250 67 -SIA------------YVSQEPWIQNGTIRenilfGKPFDE---ERYEKVIKA-----CAlepdleilpdgdLTEIGekg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 218 -SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA-------SCFQvvslmkGLAQGGRSIICTIHQPSakLFELFDQL 289
Cdd:cd03250 126 iNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvgrhifeNCIL------GLLLNNKTRILVTHQLQ--LLPHADQI 197
|
....*..
gi 46592964 290 YVLSQGQ 296
Cdd:cd03250 198 VVLDNGR 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
79-250 |
4.32e-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: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS--YSVPEGP----------WWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagyreTGM----K 142
Cdd:COG4586 2 IEVENLSktYRVYEKEpglkgalkglFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML-----TGIlvptS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 143 GAVLINGL-P-RDLRCFRK---VscyIM-QDDMLLPHLTVQEAMMVSAHL-KLQEKD-EGRREMVKEILTALGLLscaNT 214
Cdd:COG4586 77 GEVRVLGYvPfKRRKEFARrigV---VFgQRSQLWWDLPAIDSFRLLKAIyRIPDAEyKKRLDELVELLDLGELL---DT 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 46592964 215 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
97-278 |
7.48e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.77 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 97 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG--YRETGmkgAVLINGLP-RDLR-CFRKVSCYIMQDDMLLP 172
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRdEYHQDLLYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTVQEAMMVSAHLKlqekDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 252
Cdd:PRK13538 88 ELTALENLRFYQRLH----GPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....*.
gi 46592964 253 SCFQVVSLMKGLAQGGRSIICTIHQP 278
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
101-301 |
1.59e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 101 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY---------------RETGMKGAVLINGLPRDLRCF---RKVSC 162
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyiGDKKNNHELITNPYSKKIKNFkelRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 163 YIMQ-DDMLLPHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLSCANTRTG-SLSGGQRKRLAIALELVNNPPVM 240
Cdd:PRK13631 120 MVFQfPEYQLFKDTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 241 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQpSAKLFELFDQLYVLSQGQCVYRG 301
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
74-301 |
1.60e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.06 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 74 RAAVNIEFRDLSYSVP--EGPwwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLp 151
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPgkEVP---------ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI-DEGEILLDGH- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 rDLRcfrkvscyimqdDMLLPHLTVQEAMmVSAHLKL-----------QEKDEGRREmvkEILTAlGLLSCA-------- 212
Cdd:PRK11176 406 -DLR------------DYTLASLRNQVAL-VSQNVHLfndtianniayARTEQYSRE---QIEEA-ARMAYAmdfinkmd 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 213 ---NTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIICTIHQPSAklFEL 285
Cdd:PRK11176 468 nglDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEK 544
|
250
....*....|....*.
gi 46592964 286 FDQLYVLSQGQCVYRG 301
Cdd:PRK11176 545 ADEILVVEDGEIVERG 560
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
79-276 |
1.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLM---NIL----------AGYR---ETGMK 142
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKG----LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALlkpssgtitiAGYHitpETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 143 GAvlinglpRDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGL-LSCANTRTGSLSG 221
Cdd:PRK13641 79 NL-------KKLR--KKVSLVFQFPEAQLFENTVLKDVEFGP-KNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 222 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
78-253 |
2.39e-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: 75.61 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLS--YSvPEGPWwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP---- 151
Cdd:cd03244 2 DIEFKNVSlrYR-PNLPP--------VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-SSGSILIDGVDiski 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 --RDLRcfRKVSCyIMQDDMLL---------PHLTVQEAMMVSA----HLKlqekdegrrEMVKEILTALGLLSCANtrT 216
Cdd:cd03244 72 glHDLR--SRISI-IPQDPVLFsgtirsnldPFGEYSDEELWQAlervGLK---------EFVESLPGGLDTVVEEG--G 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 46592964 217 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 253
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
117-253 |
2.57e-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: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 117 AIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLRCF-----RKVScYIMQDDMLLPHLTVQEammvsaHLKL 188
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------NLLY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 189 QEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 253
Cdd:COG4148 101 GRKRAPRAERrisFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
98-276 |
3.28e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------LPRDLRCFRKVSCYIMQDDMLL 171
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-301 |
3.70e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET-----GMKGAVLING---LPRDLRCFRKVSCYIMQDDMLL 171
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskiKVDGKVLYFGkdiFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQE--AMMVSAHlKLQEKDEGRReMVKEILTALGLLSCANTRTGS----LSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:PRK14246 103 PHLSIYDniAYPLKSH-GIKEKREIKK-IVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 246 TSGLDSASCFQVVSLMKGLaQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQ-QVARVADYVAFLYNGELVEWG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
103-298 |
6.09e-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: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLINGlpRDL------RCFRKVSCYIMQDDMLLPHLT 175
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpRAT--SGRIVFDG--KDItdwqtaKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 176 VQEAMMVSAHLKLQEKDEGRREMVKEILTALglLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592964 256 QVVSLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQCV 298
Cdd:PRK11614 175 QIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
79-318 |
8.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGMKGAVLINGLPR---- 152
Cdd:PRK13640 6 VEFKHVSFTYPDSK-------KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGITLtakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 --DLRcfRKVSCYIMQDDMLLPHLTVQEAMMvsahLKLQEKDEGRREMVK---EILTALGLLSCANTRTGSLSGGQRKRL 227
Cdd:PRK13640 79 vwDIR--EKVGIVFQNPDNQFVGATVGDDVA----FGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 228 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSAKlfELFDQLYVLSQGQCVYRG---KV 303
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGspvEI 230
|
250
....*....|....*
gi 46592964 304 CNLVPYLRDLGLNCP 318
Cdd:PRK13640 231 FSKVEMLKEIGLDIP 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
103-302 |
9.86e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLPrdlrCFR-------KVSCYIM-QDDMLLPHL 174
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNP----CARltpakahQLGIYLVpQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAMMvsahLKLQeKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 254
Cdd:PRK15439 102 SVKENIL----FGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592964 255 FQVVSLMKGLAQGGRSIICTIHqpsaKLFE---LFDQLYVLSQGQCVYRGK 302
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISH----KLPEirqLADRISVMRDGTIALSGK 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
68-301 |
1.32e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 68 FSSLPRRAavnieFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLI 147
Cdd:PRK10070 14 FGEHPQRA-----FKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 148 NGLP---------RDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGS 218
Cdd:PRK10070 88 DGVDiakisdaelREVR--RKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEE-RREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKGLAQGGRSIICTIHQPSAKLfELFDQLYVLSQGQC 297
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEV 243
|
....
gi 46592964 298 VYRG 301
Cdd:PRK10070 244 VQVG 247
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
79-331 |
2.29e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRkkgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGLP---RDLR 155
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQD-DMLLPHLTVQ-------EAMMVSaHLKLQEKdegrremVKEILTALGLLSCANTRTGSLSGGQRKRL 227
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVKydvafglENHAVP-YDEMHRR-------VSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 228 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELfDQLYVLSQGQCVYRGK---VC 304
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTpteIF 230
|
250 260
....*....|....*....|....*..
gi 46592964 305 NLVPYLRDLGLNCPtyhnpadFVMEVA 331
Cdd:PRK13648 231 DHAEELTRIGLDLP-------FPIKIN 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
101-276 |
3.81e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 101 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFRKVSCYIMQD---DMLLPHLTVQ 177
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVS-AHLKLQEKDEGR-REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:PRK15056 100 VVMMGRyGHMGWLRRAKKRdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|.
gi 46592964 256 QVVSLMKGLAQGGRSIICTIH 276
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTH 200
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
79-320 |
3.86e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.54 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP------- 151
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKA----LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGVDitdkkvk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 -RDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVS-AHLKLQEKDEGRRemVKEILTALGLlSCANTRTGS---LSGGQRKR 226
Cdd:PRK13637 78 lSDIR--KKVGLVFQYPEYQLFEETIEKDIAFGpINLGLSEEEIENR--VKRAMNIVGL-DYEDYKDKSpfeLSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 227 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGK---V 303
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTpreV 232
|
250
....*....|....*....
gi 46592964 304 CNLVPYLRDLGLNCP--TY 320
Cdd:PRK13637 233 FKEVETLESIGLAVPqvTY 251
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
106-302 |
3.97e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYreTGMKGAVLINGLP------RDLRCFRkvsCYIMQDDMLLPHLTVQEA 179
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGSGSIQFAGQPleawsaAELARHR---AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 180 MMVSAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSA 252
Cdd:PRK03695 90 LTLHQPDKTRTEAV--ASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46592964 253 scfQVV---SLMKGLAQGGRSIICTIHQPSAKLFELfDQLYVLSQGQCVYRGK 302
Cdd:PRK03695 168 ---QQAaldRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGR 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
78-301 |
5.04e-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: 75.55 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 78 NIEFRDLSYSVpegpwwrkkGY-KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPR---D 153
Cdd:TIGR01193 473 DIVINDVSYSY---------GYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRCFRKVSCYIMQDDMLLPHlTVQEAMMVSAHLKLQEKDEGRREMVKEILT-----ALGLLSCANTRTGSLSGGQRKRLA 228
Cdd:TIGR01193 543 RHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDdienmPLGYQTELSEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 229 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQggRSIICTIHQPSakLFELFDQLYVLSQGQCVYRG 301
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQG 690
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-274 |
8.41e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNIL-------AGYRETGmkgAVLINGLP----RDLRCFRKVSCYIMQDD 168
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 MLLPHLTVQEAMM-VSAHlKLQEKDEgRREMVKEILTALGLLSCANTRTGS----LSGGQRKRLAIALELVNNPPVMFFD 243
Cdd:PRK14271 111 NPFPMSIMDNVLAgVRAH-KLVPRKE-FRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190
....*....|....*....|....*....|.
gi 46592964 244 EPTSGLDSASCFQVVSLMKGLAQGGRSIICT 274
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
98-295 |
1.31e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.81 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL------PRDlrcfRKVScYIMQDDMLL 171
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQEAmmVSAHLKLQEKDEgR------REMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:PRK10851 87 RHMTVFDN--IAFGLTVLPRRE-RpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 246 TSGLDSascfQV-VSLMKGLAQGGR-----SIICTIHQPSAklFELFDQLYVLSQG 295
Cdd:PRK10851 164 FGALDA----QVrKELRRWLRQLHEelkftSVFVTHDQEEA--MEVADRVVVMSQG 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
98-279 |
1.74e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMN----ILAGYRETGMKGAVLINGL--------PRDLRcfRKVScYIM 165
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGRniyspdvdPIEVR--REVG-MVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 166 QDDMLLPHLTVQEAmmVSAHLKLQEKDEGRREMVKEILTALGLLSC-------ANTRTGSLSGGQRKRLAIALELVNNPP 238
Cdd:PRK14267 92 QYPNPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46592964 239 VMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIICTIHQPS 279
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
103-296 |
1.93e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLP------RDLRcfRKVSCYIMQDDMLLPHLT 175
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEElqasniRDTE--RAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 176 VQEAMMVSAhlklqEKDEGRR----EMV---KEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:PRK13549 99 VLENIFLGN-----EITPGGImdydAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46592964 249 LDSASCFQVVSLMKGLAQGGRSIICTIHqpsaKLFELF---DQLYVLSQGQ 296
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHGIACIYISH----KLNEVKaisDTICVIRDGR 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
104-296 |
2.25e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 104 KGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGL---PRD-LRCFRKVSCYIMQ---DDMLLPHLTV 176
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRSpLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSAHLKL----------QEKDEGR-REMVKEILTalglLSCA--NTRTGSLSGGQRKRLAIALELVNNPPVMFFD 243
Cdd:PRK09700 359 AQNMAISRSLKDggykgamglfHEVDEQRtAENQRELLA----LKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 244 EPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFELF---DQLYVLSQGQ 296
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
79-296 |
3.65e-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: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS--YSVPEGPWWRKK-----------GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGA 144
Cdd:cd03220 1 IELENVSksYPTYKGGSSSLKklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 145 VLINGlprdlrcfrKVSCYIMQDDMLLPHLTVQE-AMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQ 223
Cdd:cd03220 79 VTVRG---------RVSSLLGLGGGFNPELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 224 RKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQ 296
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGK 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
103-266 |
4.02e-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: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTL------MNILagYRETGMKGAVLINGL--------PRDLRcfRKVScYIMQDD 168
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDL--IPGARVEGEILLDGEdiydpdvdVVELR--RRVG-MVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 MLLPHlTVQEAmmVSAHLKLQE-KDegRREM---VKEILTALGL-------LscaNTRTGSLSGGQRKRLAIALELVNNP 237
Cdd:COG1117 102 NPFPK-SIYDN--VAYGLRLHGiKS--KSELdeiVEESLRKAALwdevkdrL---KKSALGLSGGQQQRLCIARALAVEP 173
|
170 180
....*....|....*....|....*....
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLAQ 266
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKK 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
59-296 |
4.41e-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: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 59 DNNLTEAQRFSSLPRRAAVN----IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA 134
Cdd:COG4178 339 EEALEAADALPEAASRIETSedgaLALEDLTLRTPDG--------RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 135 GYRETGmKGAVLingLPRDLRCfrkvscyimqddMLLPhltvQEAMMVSAHLKLQ-----EKDEGRREMVKEILTALGL- 208
Cdd:COG4178 411 GLWPYG-SGRIA---RPAGARV------------LFLP----QRPYLPLGTLREAllypaTAEAFSDAELREALEAVGLg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 209 -----LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGrSIICTIHQPSakLF 283
Cdd:COG4178 471 hlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRST--LA 547
|
250
....*....|...
gi 46592964 284 ELFDQLYVLSQGQ 296
Cdd:COG4178 548 AFHDRVLELTGDG 560
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
452-666 |
7.62e-13 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 67.92 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 452 MLFLMFAALMPTVLTF--PLEMGVFlrEHLNYW-YSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFA 528
Cdd:COG0842 11 AMSLLFTALMLTALSIarEREQGTL--ERLLVTpVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 529 ALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGldr 608
Cdd:COG0842 89 LVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG--- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 609 edlhcdidetchfqkseailrelDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRA 666
Cdd:COG0842 166 -----------------------GAGLADVWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
92-276 |
8.66e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 92 PWWRKKGYKTLlKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMK----GAVLINGLPRDLRCFRKVSCYIMQ 166
Cdd:PRK15079 27 FWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEvawlGKDLLGMKDDEWRAVRSDIQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 167 DDM--LLPHLTVQEAM---MVSAHLKLQeKDEgRREMVKEILTALGLL-SCANTRTGSLSGGQRKRLAIALELVNNPPVM 240
Cdd:PRK15079 106 DPLasLNPRMTIGEIIaepLRTYHPKLS-RQE-VKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 46592964 241 FFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIH 276
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAH 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
79-302 |
9.11e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEG-PWWRKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLP------ 151
Cdd:PRK13649 3 INLQNVSYTYQAGtPFEGRA-----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDTLitstsk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 -RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRreMVKEILTALGLLSCANTRTG-SLSGGQRKRL 227
Cdd:PRK13649 77 nKDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEA--LAREKLALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 228 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGK 302
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGK 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
101-298 |
9.26e-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: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 101 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLP------RDLRcfRKVSCYIMQDDMLLPH 173
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPlkasniRDTE--RAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQEAMMVSAHLKLQEKDEGRREMV---KEILTALGLLSCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 249
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAYNAMYlraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46592964 250 DSASCFQVVSLMKGLAQGGRSIICTIHqpsaKLFE---LFDQLYVLSQGQCV 298
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
79-250 |
1.12e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSvpegpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING-----LPRD 153
Cdd:PRK11831 8 VDMRGVSFT---------RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipaMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 -LRCFRKVSCYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDEGRREMVKeiLTALGLLSCANTRTGSLSGGQRKRLAIA 230
Cdd:PRK11831 78 rLYTVRKRMSMLFQSGALFTDMNVFDnvAYPLREHTQLPAPLLHSTVMMK--LEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180
....*....|....*....|
gi 46592964 231 LELVNNPPVMFFDEPTSGLD 250
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQD 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
106-296 |
1.50e-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: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLR----CFRKVSCYIMQD---DMLLPHLTVQE 178
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnpaqAIRAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSA---HLKLQEKDEGRREmvKEILTALGLLSCANTR----TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:TIGR02633 359 NITLSVlksFCFKMRIDAAAEL--QIIGSAIQRLKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLSQGQ 296
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
79-301 |
1.51e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFR 158
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 KVSC---YIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLL-SCANTRTGSLSGGQRKRLAIALE 232
Cdd:PRK15112 84 YRSQrirMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46592964 233 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIICTIHQPSAKlfELFDQLYVLSQGQCVYRG 301
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
103-296 |
1.59e-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: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDLRCFRKVS----CYIMQD---DMLLPHLT 175
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDAIragiAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 176 VQEAMMVSAHLklqekdegrremvkeiltalgllscantrtgslSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:cd03215 95 VAENIALSSLL---------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 256 QVVSLMKGLAQGGRSIICTihqpSAKLFELF---DQLYVLSQGQ 296
Cdd:cd03215 142 EIYRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEGR 181
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
79-303 |
1.61e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.80 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS--YSVPEGPWWR-----------KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGA 144
Cdd:COG1134 5 IEVENVSksYRLYHEPSRSlkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--SGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 145 VLINGlprdlrcfrKVSCyimqddmLL-------PHLTVQE-AMMVSAHLKLQEKDEgrREMVKEIL--TALGllSCANT 214
Cdd:COG1134 83 VEVNG---------RVSA-------LLelgagfhPELTGREnIYLNGRLLGLSRKEI--DEKFDEIVefAELG--DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 215 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSLMKGLAQGGRSIICTIHQPSAkLFELFDQLYVL 292
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWL 219
|
250
....*....|.
gi 46592964 293 SQGQCVYRGKV 303
Cdd:COG1134 220 EKGRLVMDGDP 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
79-301 |
1.76e-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: 70.23 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYsvpegpwwrkkGY---KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGlpRDL 154
Cdd:COG5265 358 VRFENVSF-----------GYdpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfYDVTS--GRILIDG--QDI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 R-----CFRKVSCYIMQDDMLL------------PHLT---VQEAMMvSAHL-----KLQEKDE---GRRemvkeiltal 206
Cdd:COG5265 423 RdvtqaSLRAAIGIVPQDTVLFndtiayniaygrPDASeeeVEAAAR-AAQIhdfieSLPDGYDtrvGER---------- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 207 GLlscantrtgSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIIctI-HQPS----Ak 281
Cdd:COG5265 492 GL---------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV--IaHRLStivdA- 559
|
250 260
....*....|....*....|
gi 46592964 282 lfelfDQLYVLSQGQCVYRG 301
Cdd:COG5265 560 -----DEILVLEAGRIVERG 574
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
112-276 |
1.83e-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: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 112 SGELVAIMGPSGAGKSTLMNILAG--------------YRE--TGMKGAVLINGLPR----DLRCFRKVscyimQDDMLL 171
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdWDEilDEFRGSELQNYFTKllegDVKVIVKP-----QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PhltvqEAMMVSAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:cd03236 100 P-----KAVKGKVGELLKKKDE--RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
98-323 |
2.13e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGLPRDLRCFRKVSCYI---MQDDMLLPHL 174
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIgllAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 TVQEAMMVSAH------LKLQEKDEgrrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:PRK10253 97 TVQELVARGRYphqplfTRWRKEDE---EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 249 LDSASCFQVVSLMKGL-AQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGKVCNLV-PYL--RDLGLNCPTYHNP 323
Cdd:PRK10253 174 LDISHQIDLLELLSELnREKGYTLAAVLHDLN-QACRYASHLIALREGKIVAQGAPKEIVtAELieRIYGLRCMIIDDP 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
79-318 |
2.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPWWRKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLP------- 151
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQA----IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP-TTGTVTVDDITithktkd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKL---QEKDEGRRemvkeILTALGLlsCANTRTGS---LSGGQ 223
Cdd:PRK13646 78 KYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnldEVKNYAHR-----LLMDLGF--SRDVMSQSpfqMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 224 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGK 302
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTS 229
|
250
....*....|....*....
gi 46592964 303 VCNLV---PYLRDLGLNCP 318
Cdd:PRK13646 230 PKELFkdkKKLADWHIGLP 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-276 |
2.50e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTL---MNIL----AGYRE-----------TGMKGAVLIN---GLPR--------D 153
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdTGTIEwifkdeknkkkTKEKEKVLEKlviQKTRfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRrEMVKEILTALGL-LSCANTRTGSLSGGQRKRLAIALE 232
Cdd:PRK13651 103 IR--RRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAK-KRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 233 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
82-266 |
3.41e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 82 RDL--SYSVPEGPWwRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgYRETGMKGAVLINGLP-------- 151
Cdd:PRK11308 9 IDLkkHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPTGGELYYQGQDllkadpea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 -RDLRcfRKVScYIMQDDM--LLPHLTV----QEAMMVSAHLKLQEkdegRREMVKEILTALGLLSCANTRTGSL-SGGQ 223
Cdd:PRK11308 87 qKLLR--QKIQ-IVFQNPYgsLNPRKKVgqilEEPLLINTSLSAAE----RREKALAMMAKVGLRPEHYDRYPHMfSGGQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592964 224 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 266
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
79-254 |
3.52e-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: 64.39 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVpegpwwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGLPRdlrcfr 158
Cdd:cd03221 1 IELENLSKTY---------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 kvSCYIMQddmllphltvqeammvsahlklqekdegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVNNPP 238
Cdd:cd03221 65 --IGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170
....*....|....*.
gi 46592964 239 VMFFDEPTSGLDSASC 254
Cdd:cd03221 91 LLLLDEPTNHLDLESI 106
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
98-266 |
4.38e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.72 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTL------MNILAgyRETGMKGAVLING----LPR-DLRCFRKVSCYIMQ 166
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGhniySPRtDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 167 DDMLLPhLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTG----SLSGGQRKRLAIALELVNNPPVMFF 242
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180
....*....|....*....|....
gi 46592964 243 DEPTSGLDSASCFQVVSLMKGLAQ 266
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKD 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
79-303 |
4.52e-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: 68.94 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkKGYKTLLKGISGKFNSGELVAIMGPSGAGKS-TLMNI--LAGYRETGMKGAVLINGL----- 150
Cdd:COG4172 7 LSVEDLSVAFGQG-----GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 -PRDLRCFR--KVSCyIMQDDM--LLPHLTV--QEAMMVSAHLKLQEKDegRREMVKEILTALGLLScANTRTGS----L 219
Cdd:COG4172 82 sERELRRIRgnRIAM-IFQEPMtsLNPLHTIgkQIAEVLRLHRGLSGAA--ARARALELLERVGIPD-PERRLDAyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 220 SGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMKGL-AQGGRSIictihqpsakLF---------ELF 286
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDvtvQA---QILDLLKDLqRELGMAL----------LLithdlgvvrRFA 224
|
250
....*....|....*..
gi 46592964 287 DQLYVLSQGQCVYRGKV 303
Cdd:COG4172 225 DRVAVMRQGEIVEQGPT 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
112-272 |
4.68e-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: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 112 SGELVAIMGPSGAGKSTLMNILAG---------------------YRETGMKG--AVLINGlprDLRCFRKVScYImqdD 168
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrFRGTELQDyfKKLANG---EIKVAHKPQ-YV---D 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 MLLPHL--TVQEammvsahlkLQEK-DEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:COG1245 171 LIPKVFkgTVRE---------LLEKvDE--RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180
....*....|....*....|....*..
gi 46592964 246 TSGLDSASCFQVVSLMKGLAQGGRSII 272
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
79-318 |
5.34e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.96 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLPR----- 152
Cdd:PRK13635 6 IRVEHISFRYPDAA-------TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPE--AGTITVGGMVLseetv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 -DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREMVKEILTAL---GLLSCANTRTGSLSGGQRKRLA 228
Cdd:PRK13635 77 wDVR--RQVGMVFQNPDNQFVGATVQDDVAFG----LENIGVPREEMVERVDQALrqvGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 229 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIH--QPSAKLfelfDQLYVLSQGQCVYRG---K 302
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHdlDEAAQA----DRVIVMNKGEILEEGtpeE 226
|
250
....*....|....*.
gi 46592964 303 VCNLVPYLRDLGLNCP 318
Cdd:PRK13635 227 IFKSGHMLQEIGLDVP 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
79-345 |
8.97e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSV-PEGPWWRKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL------- 150
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASRA-----LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP-TEGKVTVGDIvvsstsk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 151 PRDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQeKDEGRReMVKEILTALGLLSCANTRTG-SLSGGQRKRL 227
Cdd:PRK13643 76 QKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIP-KEKAEK-IAAEKLEMVGLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 228 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRGKVCNL- 306
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVf 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 46592964 307 --VPYLRDLGLNCPTYHNPADFVMEvaSGEYGDQNSRLVRA 345
Cdd:PRK13643 233 qeVDFLKAHELGVPKATHFADQLQK--TGAVTFEKLPITRA 271
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
100-250 |
1.51e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGLPRDlrcfrkvscyimqddmllphltvQE 178
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVDVPDNQFG-----------------------RE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 179 AMMVSAHLKLQEKDEgrremVKEILTALGLLSCANTRT--GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:COG2401 100 ASLIDAIGRKGDFKD-----AVELLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
111-250 |
2.84e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 111 NSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLklqe 190
Cdd:PRK13543 35 DAGEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 191 kdEGRR--EMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK13543 110 --HGRRakQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
113-301 |
2.88e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLinglprdlrcfrkvscYIMQDDMLLPHLTVQEA------------- 179
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSA-RLAPDAGEVH----------------YRMRDGQLRDLYALSEAerrrllrtewgfv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 180 ---------MMVSAhlklqekdeGRRemVKEILTALGLLSCANTRT--------------------GSLSGGQRKRLAIA 230
Cdd:PRK11701 95 hqhprdglrMQVSA---------GGN--IGERLMAVGARHYGDIRAtagdwlerveidaariddlpTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 231 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIICTIHQPS-AKLfeLFDQLYVLSQGQCVYRG 301
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAvARL--LAHRLLVMKQGRVVESG 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
79-303 |
2.96e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMKGAVLING-----LPR 152
Cdd:CHL00131 8 LEIKNLHASVNE---------NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGesildLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRCFRKVsCYIMQDDMLLPHLTVQEAMMVS--AHLKLQEKDEGRR----EMVKEILTALGL----LScANTRTGsLSGG 222
Cdd:CHL00131 79 EERAHLGI-FLAFQYPIEIPGVSNADFLRLAynSKRKFQGLPELDPleflEIINEKLKLVGMdpsfLS-RNVNEG-FSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 223 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPsaKLFELF--DQLYVLSQGQCVYR 300
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKT 233
|
...
gi 46592964 301 GKV 303
Cdd:CHL00131 234 GDA 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
103-272 |
3.04e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--REtgmKGAVLINGLPRDLRC----FRKVSCYIMQD---DMLLPH 173
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAlpRT---SGYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLSCANTRT-------GSLSGGQRKRLAIALELVNNPPVMFFDEPT 246
Cdd:PRK10762 345 MSVKENMSLTA-LRYFSRAGGSLKHADEQQAVSDFIRLFNIKTpsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180
....*....|....*....|....*.
gi 46592964 247 SGLDSASCFQVVSLMKGLAQGGRSII 272
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
102-277 |
3.60e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 102 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQE 178
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERqsIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMMVSAHLKlqekdEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 258
Cdd:PRK13540 94 NCLYDIHFS-----PGAVG-ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 46592964 259 SLMKGLAQGGRSIICTIHQ 277
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQ 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
113-276 |
5.38e-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: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING--LPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQE 190
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGksILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 191 KDEGRReMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRS 270
Cdd:TIGR01257 2044 AEEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRA 2122
|
....*.
gi 46592964 271 IICTIH 276
Cdd:TIGR01257 2123 VVLTSH 2128
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
102-303 |
5.97e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 102 LLKGISGKFNSGELVAIMGPSGAGKS----TLMNIL-AGYRETGmkGAVLING---LPRDLRCfRKVSCyIMQDdmllPH 173
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGkpvAPCALRG-RKIAT-IMQN----PR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQEAMMVSAHLK---LQEKDEGRREMVKEILTALGLlscANTRT------GSLSGGQRKRLAIALELVNNPPVMFFDE 244
Cdd:PRK10418 90 SAFNPLHTMHTHARetcLALGKPADDATLTAALEAVGL---ENAARvlklypFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 245 PTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 303
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDV 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
100-318 |
6.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.57 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILAgyreTGMKGAVLINGL----PRDLRCFRKVSCYIMQ--DDML 170
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL----IPSEGKVYVDGLdtsdEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 171 LPHLTVQEAMMVSAHLKLQEKDegRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK13633 99 VATIVEEDVAFGPENLGIPPEE--IRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46592964 251 SASCFQVVSLMKGL-AQGGRSIICTIH--QPSAKLfelfDQLYVLSQGQCVYRG---KVCNLVPYLRDLGLNCP 318
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGtpkEIFKEVEMMKKIGLDVP 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
111-276 |
8.47e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 111 NSGELVAIMGPSGAGKS----TLMNILAGYRETGmkGAVLING-----LP-RDLRCFR--KVScYIMQDDM--LLPHLTV 176
Cdd:PRK09473 40 RAGETLGIVGESGSGKSqtafALMGLLAANGRIG--GSATFNGreilnLPeKELNKLRaeQIS-MIFQDPMtsLNPYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAMMVSAHL-KLQEKDEGRREMVKeILTALGLLScANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:PRK09473 117 GEQLMEVLMLhKGMSKAEAFEESVR-MLDAVKMPE-ARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180
....*....|....*....|....*.
gi 46592964 252 ASCFQVVSLMKGLAQG-GRSIICTIH 276
Cdd:PRK09473 195 TVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
79-253 |
1.05e-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: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLS--YSvPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLmnILAGYRET-GMKGAVLINGLP---- 151
Cdd:cd03369 7 IEVENLSvrYA-PDLP--------PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDisti 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 152 --RDLRcfRKVSCyIMQDDMLLphltvqeamMVSAHLKLQEKDEGRREmvkEILTALGLLSCANtrtgSLSGGQRKRLAI 229
Cdd:cd03369 76 plEDLR--SSLTI-IPQDPTLF---------SGTIRSNLDPFDEYSDE---EIYGALRVSEGGL----NLSQGQRQLLCL 136
|
170 180
....*....|....*....|....
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSAS 253
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYAT 160
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
79-293 |
1.73e-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: 60.25 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVlinGLPRDlrcfr 158
Cdd:cd03223 1 IELENLSLATPDG--------RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 159 kvscyimQDDMLLPhltvQEAMMVSAHLKLQekdegrremvkeILTALGLLscantrtgsLSGGQRKRLAIALELVNNPP 238
Cdd:cd03223 64 -------EDLLFLP----QRPYLPLGTLREQ------------LIYPWDDV---------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 239 VMFFDEPTSGLDSASCFQVVSLMKGLaqgGRSIICTIHQPSakLFELFDQLYVLS 293
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPS--LWKFHDRVLDLD 161
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
181-306 |
1.97e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 181 MVSAHLKLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 260
Cdd:NF000106 109 MIGR*LDLSRKDA--RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 46592964 261 MKGLAQGGRSIICTIhQPSAKLFELFDQLYVLSQGQCVYRGKVCNL 306
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
112-282 |
2.11e-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: 59.31 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 112 SGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGlprdlrcfrkvscyimqddmllphltvqeammvsahlklqek 191
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 192 degrrEMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMKGLA 265
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 46592964 266 QGGRSIICTIHQPSAKL 282
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
79-250 |
3.08e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSV-PEGPWWRKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLI-------NG 149
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRA-----LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPT--SGTVTIgervitaGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 150 LPRDLRCFRKVSCYIMQddmlLP-HLTVQEAMmvsahlklqEKD------------EGRREMVKEILTALGLLSCANTRT 216
Cdd:PRK13634 76 KNKKLKPLRKKVGIVFQ----FPeHQLFEETV---------EKDicfgpmnfgvseEDAKQKAREMIELVGLPEELLARS 142
|
170 180 190
....*....|....*....|....*....|....*
gi 46592964 217 G-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK13634 143 PfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
103-250 |
3.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPR------DLRcfRKVSCYIMQDDMLLPHLTV 176
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLtaenvwNLR--RKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 177 QEAMMvsahLKLQEKDEGRREMVK---EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK13642 100 EDDVA----FGMENQGIPREEMIKrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
113-267 |
3.43e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAG--------YRETGMKGAV---------------LINGlprDLRCFRKVScYImqdDm 169
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVlkrfrgtelqnyfkkLYNG---EIKVVHKPQ-YV---D- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 LLPHL---TVQEAmmvsahlkLQEKDEgrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 246
Cdd:PRK13409 171 LIPKVfkgKVREL--------LKKVDE--RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180
....*....|....*....|.
gi 46592964 247 SGLDSASCFQVVSLMKGLAQG 267
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEG 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
103-298 |
3.70e-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: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGLPRDLR----------CF----RKvscyimqD 167
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGaDPADS--GEIRLDGKPVRIRsprdairagiAYvpedRK-------G 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 DMLLPHLTVQEAMMVSAHLK------LQEKDEgrREMVKEILTALGL-LSCANTRTGSLSGG-QRKrLAIALELVNNPPV 239
Cdd:COG1129 339 EGLVLDLSIRENITLASLDRlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 240 MFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFELF---DQLYVLSQGQCV 298
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 ... |
100-253 |
4.00e-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: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKG-AVLINGLprdlrcfrKVScYIMQDDMLLPHLTVQE 178
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGeARPQPGI--------KVG-YLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMM--VSAHLKLQEK---------------DEGRREMVK--EILTALGL-------------LSCA--NTRTGSLSGGQR 224
Cdd:TIGR03719 88 NVEegVAEIKDALDRfneisakyaepdadfDKLAAEQAElqEIIDAADAwdldsqleiamdaLRCPpwDADVTKLSGGER 167
|
170 180
....*....|....*....|....*....
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLDSAS 253
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
113-296 |
4.19e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLR-CFRKVS---CYIMQD---DMLLPHLTVQEAMMVSAH 185
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRnPQQAIAqgiAMVPEDrkrDGIVPVMGVGKNITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 186 LKL---------QEKDEGRREMVK-EILTALGLLscantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 255
Cdd:PRK13549 368 DRFtggsriddaAELKTILESIQRlKVKTASPEL-----AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 256 QVVSLMKGLAQGGRSIICTihqpSAKLFE---LFDQLYVLSQGQ 296
Cdd:PRK13549 443 EIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGK 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
113-250 |
4.58e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGyrETGM-KGAVLINglpRDLRCFR-----------KVSCYIM-----QDDML----- 170
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNG--EVLLdDGRIIYE---QDLIVARlqqdpprnvegTVYDFVAegieeQAEYLkryhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 171 LPHLTVQEAM--MVSAHLKLQEK-D-------EGRremVKEILTALGLlsCANTRTGSLSGGQRKRLAIALELVNNPPVM 240
Cdd:PRK11147 104 ISHLVETDPSekNLNELAKLQEQlDhhnlwqlENR---INEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170
....*....|
gi 46592964 241 FFDEPTSGLD 250
Cdd:PRK11147 179 LLDEPTNHLD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
113-306 |
5.54e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAG-Y-RETG----MKGAVLINGlPRDlrcfrkvS-----CYIMQDDMLLPHLTVQEAMM 181
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGiYtRDAGsilyLGKEVTFNG-PKS-------SqeagiGIIHQELNLIPQLTIAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 182 VsahlklqekdeGR-----------REMVKE---ILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 247
Cdd:PRK10762 102 L-----------GRefvnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 248 GL---DSASCFQVVSLMKglAQGgrsiiCTIHQPSAKLFELF---DQLYVLSQGQCVYRGKVCNL 306
Cdd:PRK10762 171 ALtdtETESLFRVIRELK--SQG-----RGIVYISHRLKEIFeicDDVTVFRDGQFIAEREVADL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
113-261 |
5.79e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGL------PRDLRCFRKVSCYIMQDDM--LLPHLTVQEAMM--V 182
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMepL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 183 SAHLKLQEKDEGRRemVKEILTALGLLSCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 261
Cdd:PRK10261 429 RVHGLLPGKAAAAR--VAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
117-250 |
6.22e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.43 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 117 AIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----------LPRDLRcfrKVScYIMQDDMLLPHLTVQeammvsAH 185
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGL-TRPQKGRIVLNGrvlfdaekgicLPPEKR---RIG-YVFQDARLFPHYKVR------GN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46592964 186 LK--LQEKDegrREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK11144 97 LRygMAKSM---VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
72-250 |
7.93e-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: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 72 PRRAAVNIEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING 149
Cdd:TIGR03719 316 PRLGDKVIEAENLT-----------KAFgdKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTIEIGE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 150 LPrdlrcfrKVSCYIMQDDMLLPHLTVQEAmmVSA---HLKLqekdeGRREMvkeilTALGLLSCAN-------TRTGSL 219
Cdd:TIGR03719 384 TV-------KLAYVDQSRDALDPNKTVWEE--ISGgldIIKL-----GKREI-----PSRAYVGRFNfkgsdqqKKVGQL 444
|
170 180 190
....*....|....*....|....*....|.
gi 46592964 220 SGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-325 |
8.56e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyRETGMKGAVLINGLPR-----------DLRCFRKVSCYIMQDD 168
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 MLLPhLTVQEAM-----MVSAHLKLQEKDegrreMVKEILTALGLLSCANTRTGS----LSGGQRKRLAIALELVNNPPV 239
Cdd:PRK14258 98 NLFP-MSVYDNVaygvkIVGWRPKLEIDD-----IVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 240 MFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIICTIHQpsaklfelFDQLYVLSQGQCVYRGKVcNLVPYLRDLGLNCP 318
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKGNE-NRIGQLVEFGLTKK 242
|
....*..
gi 46592964 319 TYHNPAD 325
Cdd:PRK14258 243 IFNSPHD 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
100-313 |
9.56e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKS----TLMNILAGYRETGMKGAVLING---LPRDLRCFRKVS----CYIMQDD 168
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPSGDIRFHGeslLHASEQTLRGVRgnkiAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 ML----LPHLTVQEAMMVSAHLKLqekdegRREMVK-EILTAL---GLLSCANTRTG---SLSGGQRKRLAIALELVNNP 237
Cdd:PRK15134 102 MVslnpLHTLEKQLYEVLSLHRGM------RREAARgEILNCLdrvGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 238 PVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRGKVCNLV-----PYLR 311
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSI-VRKLADRVAVMQNGRCVEQNRAATLFsapthPYTQ 254
|
..
gi 46592964 312 DL 313
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 ... |
100-301 |
1.39e-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: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRC-------FRKVSC---------- 162
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCgyverpsKVGEPCpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 163 ---YIMQDDMLLPHLTVQEAMMVSAHLKLQEKD-----------EGRREMVKEILTALGLLSCANTR------TGSLSGG 222
Cdd:TIGR03269 93 evdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDtvldnvlealeEIGYEGKEAVGRAVDLIEMVQLShrithiARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 223 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS-LMKGLAQGGRSIICTIHQPSAkLFELFDQLYVLSQGQCVYRG 301
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEV-IEDLSDKAIWLENGEIKEEG 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
103-313 |
1.45e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKS----TLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQD----DM----- 169
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 -----LLPHLTVQEAMMVSAHLklqEKDEGRREMVKEILTALGLLSCANTRT------GSLSGGQRKRLAIALELVNNPP 238
Cdd:PRK10261 112 epmtsLNPVFTVGEQIAESIRL---HQGASREEAMVEAKRMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 239 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLV-----PYLRDL 313
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
50-276 |
1.73e-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: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 50 LLNGHLKKVDNNLTEAQRF---SSLPRRAAVN------IEFRDLS---YSVpegpwwrKKGYKTLLKGISGKFNSGELVA 117
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFmegVSEVEKECEVevgepiIKVRNVSkryISV-------DRGVVKAVDNVSLEVKEGEIFG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 118 IMGPSGAGKSTLMNILAGYRE-TGMKGAVLI-------NGLPRDLRcfRKVSCYI---MQDDMLLPHLTVQEAMMVSAHL 186
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEpTSGEVNVRVgdewvdmTKPGPDGR--GRAKRYIgilHQEYDLYPHRTVLDNLTEAIGL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 187 KLqEKDEGRREMVKeILTALGL-----LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SL 260
Cdd:TIGR03269 393 EL-PDELARMKAVI-TLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSI 470
|
250
....*....|....*.
gi 46592964 261 MKGLAQGGRSIICTIH 276
Cdd:TIGR03269 471 LKAREEMEQTFIIVSH 486
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
79-302 |
2.17e-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: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDL---R 155
Cdd:PRK10790 341 IDIDNVSFAYRDD--------NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL-TEGEIRLDGRPLSSlshS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CFRKVSCYIMQDDMLLphltvqeAMMVSAHLKLqekdeGR---REMVKEILTALGLLSCA-------NTRTG----SLSG 221
Cdd:PRK10790 412 VLRQGVAMVQQDPVVL-------ADTFLANVTL-----GRdisEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 222 GQRKRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVSLMKGLAQGGRSIICTIHQPSAkLFELfDQLYVLSQGQCVYRG 301
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGT-EQAIQQALAAVREHTTLVVIAHRLST-IVEA-DTILVLHRGQAVEQG 556
|
.
gi 46592964 302 K 302
Cdd:PRK10790 557 T 557
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
106-302 |
2.59e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKStlMNILAGYRETGMKGAVLINGLPRDLRCFRKVS------------CYIMQDDM--LL 171
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISekerrnlvgaevAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQEAMMVSahLKLQE--KDEGRREMVKEILTALGL---LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 246
Cdd:PRK11022 104 PCYTVGFQIMEA--IKVHQggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 247 SGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGK 302
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
103-303 |
3.16e-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: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNilagyretgmkgavlinglprdlRCFRKVSCYIMQDDmlLPHLTVQEAMMV 182
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------------EGLYASGKARLISF--LPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 183 SahlKLQEkdegrreMVKEILTALGLlscaNTRTGSLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSL 260
Cdd:cd03238 66 D---QLQF-------LIDVGLGYLTL----GQKLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592964 261 MKGLAQGGRSIICTIHQPsaKLFELFDQLYVLSQGQCVYRGKV 303
Cdd:cd03238 132 IKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGSGKSGGKV 172
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
79-244 |
3.23e-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: 59.81 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPE---------GPwwrkkgyktllkgISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLIN 148
Cdd:COG4615 328 LELRGVTYRYPGedgdegftlGP-------------IDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 GLP---RDLRCFRKVSCYIMQDDMLLPHLtvqeammvsahlkLQEKDEGRREMVKEILTALGL---LSCANTR--TGSLS 220
Cdd:COG4615 393 GQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LGLDGEADPARARELLERLELdhkVSVEDGRfsTTDLS 459
|
170 180
....*....|....*....|....
gi 46592964 221 GGQRKRLAIALELVNNPPVMFFDE 244
Cdd:COG4615 460 QGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
108-251 |
3.38e-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: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 108 GKFNSGELVAIMGPSGAGKSTLMNILAGyretGMKGAVLINGLPRDlrcfrKVScYIMQddmllpHLTVQEAMMVSAHLK 187
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAG----VLKPDEGDIEIELD-----TVS-YKPQ------YIKADYEGTVRDLLS 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 188 LQEKDEGRREMVK-EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:cd03237 84 SITKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
79-244 |
4.61e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGpwwrkkGYKtlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGLP---RDL 154
Cdd:PRK10522 323 LELRNVTFAYQDN------GFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 155 RCFRKVSCYIMQDDMLLPHLTVQEAMMVS--------AHLKLQEK---DEGRremvkeiltalgllsCANTRtgsLSGGQ 223
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPEGKPANpalvekwlERLKMAHKlelEDGR---------------ISNLK---LSKGQ 454
|
170 180
....*....|....*....|.
gi 46592964 224 RKRLAIALELVNNPPVMFFDE 244
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDE 475
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
80-296 |
4.64e-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: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPEGpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGL------PRD 153
Cdd:COG3845 259 EVENLSVRDDRG--------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-SGSIRLDGEditglsPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 154 LRCfRKVScYIMQDDM---LLPHLTVQEAMMVSAH----------LKLQEKDEGRREMVKE--ILTAlGllscANTRTGS 218
Cdd:COG3845 330 RRR-LGVA-YIPEDRLgrgLVPDMSVAENLILGRYrrppfsrggfLDRKAIRAFAEELIEEfdVRTP-G----PDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICtIhqpSAKLFELF---DQLYVLSQG 295
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL-I---SEDLDEILalsDRIAVMYEG 478
|
.
gi 46592964 296 Q 296
Cdd:COG3845 479 R 479
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
79-296 |
4.95e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---------YRETGMKGAVL--- 146
Cdd:PLN03073 509 ISFSDASFGYPGGP--------LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGelqpssgtvFRSAKVRMAVFsqh 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 147 -INGLprDL---------RCFRKVScyimqDDMLLPHLTvqeAMMVSAHLKLQEkdegrreMVkeiltalgllscantrt 216
Cdd:PLN03073 581 hVDGL--DLssnpllymmRCFPGVP-----EQKLRAHLG---SFGVTGNLALQP-------MY----------------- 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 217 gSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMKGLA--QGGrsiICTIHQPSAKLFELFDQLYVLSQ 294
Cdd:PLN03073 627 -TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSE 699
|
..
gi 46592964 295 GQ 296
Cdd:PLN03073 700 GK 701
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
79-301 |
5.93e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLINGlpRDLR 155
Cdd:PRK09580 2 LSIKDLHVSVED---------KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTG--GTVEFKG--KDLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 156 CF----RKVSCYIM--QDDMLLP----HLTVQEAmmVSAHLKLQEKDEGRR----EMVKEILTALGLLSCANTRTGSL-- 219
Cdd:PRK09580 69 ELspedRAGEGIFMafQYPVEIPgvsnQFFLQTA--LNAVRSYRGQEPLDRfdfqDLMEEKIALLKMPEDLLTRSVNVgf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 220 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVY 299
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
..
gi 46592964 300 RG 301
Cdd:PRK09580 227 SG 228
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
97-290 |
6.56e-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: 55.44 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 97 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMN--ILAgyreTGMKGAVLINGLPRDLRCFrkvSCYimqddmllphl 174
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiGLA----LGGAQSATRRRSGVKAGCI---VAA----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 175 tvqeammVSAHLklqekdegrremvkeILTALGLlscantrtgslSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLD 250
Cdd:cd03227 67 -------VSAEL---------------IFTRLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46592964 251 SASCFQVVSLMKGLAQGGRSIICTIHQPsaKLFELFDQLY 290
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
100-253 |
7.72e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKG-AVLINGLprdlrcfrKVScYIMQDDMLLPHLTVQE 178
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGeARPAPGI--------KVG-YLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 179 AMM--VSAHLKLQEK---------------DEGRREMVK--EILTALGL-------------LSC--ANTRTGSLSGGQR 224
Cdd:PRK11819 90 NVEegVAEVKAALDRfneiyaayaepdadfDALAAEQGElqEIIDAADAwdldsqleiamdaLRCppWDAKVTKLSGGER 169
|
170 180
....*....|....*....|....*....
gi 46592964 225 KRLAIALELVNNPPVMFFDEPTSGLDSAS 253
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
113-250 |
1.76e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILagyreTGM----KGAVLINGLP---RDLRCFRKVScYIMQDDMLLPHLTVQEAMMVSAH 185
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKML-----TGLlpasEGEAWLFGQPvdaGDIATRRRVG-YMSQAFSLYGELTVRQNLELHAR 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 186 L-KLQEKDEGRRemVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:NF033858 366 LfHLPAAEIAAR--VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
95-250 |
3.30e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 95 RKKGYKT----LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING-----LPRDLrcFRKVSCYIM 165
Cdd:PRK10247 11 QNVGYLAgdakILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP-TSGTLLFEGedistLKPEI--YRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 166 QDDMLLPHlTVQEAMMVSAHLKLQEKDEGRreMVKEiLTALGL-LSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDE 244
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRNQQPDPAI--FLDD-LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
....*.
gi 46592964 245 PTSGLD 250
Cdd:PRK10247 164 ITSALD 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
107-251 |
3.46e-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: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 107 SGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVlinglPRDLrcfrKVSC---YIMQD-DMllphlTVQEAMMV 182
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAG-VLKPDEGEV-----DEDL----KISYkpqYISPDyDG-----TVEEFLRS 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 183 SAHLKLQEKdegrreMVK-EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:COG1245 425 ANTDDFGSS------YYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
70-301 |
6.12e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 70 SLP-RRAAVNIEFRDLSYSVPEGPwwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLIN 148
Cdd:PRK10789 306 PVPeGRGELDVNIRQFTYPQTDHP---------ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 149 GLP-RDLRC--FRKVSCYIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltalgll 209
Cdd:PRK10789 376 DIPlTKLQLdsWRSRLAVVSQTPFLFsdtvannialgrPDATQQEiehvARLASVHDDILRLPQGYDTEVGE-------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 210 scantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVvslMKGLAQGG--RSIICTIHQPSAkLFELfD 287
Cdd:PRK10789 448 -----RGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI---LHNLRQWGegRTVIISAHRLSA-LTEA-S 517
|
250
....*....|....
gi 46592964 288 QLYVLSQGQCVYRG 301
Cdd:PRK10789 518 EILVMQHGHIAQRG 531
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
103-277 |
6.24e-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: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLPRDLRCF-------RKVSCYIMQDDMLLpHLT 175
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 176 VQEAMMVSAHLKLQekdegRREMVKEI--------LTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 247
Cdd:cd03290 95 VEENITFGSPFNKQ-----RYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|...
gi 46592964 248 GLD---SASCFQvVSLMKGLAQGGRSIICTIHQ 277
Cdd:cd03290 170 ALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
98-250 |
7.48e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY---------RETGMKgavlINGLPRDLRCfrkvscyimqdD 168
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvapdegvikRNGKLR----IGYVPQKLYL-----------D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 MLLPhLTVQEAMMVSAHLKlqekdegrremVKEILTALGLLSCA---NTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:PRK09544 80 TTLP-LTVNRFLRLRPGTK-----------KEDILPALKRVQAGhliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
....*
gi 46592964 246 TSGLD 250
Cdd:PRK09544 148 TQGVD 152
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
113-298 |
7.49e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAGYRETG-MKGAVLINGlprDLRCFRKVS-------CYIMQDDMLLPHLTVQEAMMVS- 183
Cdd:NF040905 27 GEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDG---EVCRFKDIRdsealgiVIIHQELALIPYLSIAENIFLGn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 184 --AHLKLQEKDEGRREmVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAscfQVV 258
Cdd:NF040905 104 erAKRGVIDWNETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA---ALL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46592964 259 SLMKGL-AQGGRSIIctIhqpSAKLFELF---DQLYVLSQGQCV 298
Cdd:NF040905 180 DLLLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
214-296 |
7.85e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 214 TRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIIcTIHQPSAKLFELFDQLYVLS 293
Cdd:PRK10982 387 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVMS 465
|
...
gi 46592964 294 QGQ 296
Cdd:PRK10982 466 NGL 468
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
94-295 |
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 46592964 94 WRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGlprdlrcfrkVSCYIMQDDMLLpH 173
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG----------SVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 174 LTVQEAMMVSAhlKLQEKDEGRREMVKEILTALGLLSCAN-----TRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:PLN03232 693 ATVRENILFGS--DFESERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46592964 249 LDSASCFQVV-SLMKGLAQGGRSIICT--IHqpsakLFELFDQLYVLSQG 295
Cdd:PLN03232 771 LDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
103-274 |
1.94e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.86 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLM-------NILAGYRetgMKGAVLINGL--------PRDLRcfRKVScYIMQD 167
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR---VEGKVTFHGKnlyapdvdPVEVR--RRIG-MVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 DMLLPHlTVQEAMMVSAHL--------KLQEK--------DEgrremVKEILTALGLlscantrtgSLSGGQRKRLAIAL 231
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARIngykgdmdELVERslrqaalwDE-----VKDKLKQSGL---------SLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46592964 232 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICT 274
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
72-250 |
2.37e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 72 PRRAAVNIEFRDLSysvpegpwwrkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING 149
Cdd:PRK11819 318 PRLGDKVIEAENLS-----------KSFgdRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG-QEQPDSGTIKIGE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 150 LPrdlrcfrKVScYIMQD-DMLLPHLTVQEAmmVSA---HLKLqekdeGRREMvkeiltalgllscaNTR---------- 215
Cdd:PRK11819 386 TV-------KLA-YVDQSrDALDPNKTVWEE--ISGgldIIKV-----GNREI--------------PSRayvgrfnfkg 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46592964 216 ------TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK11819 437 gdqqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
79-296 |
2.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSYSvpegpwWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING--LPR---- 152
Cdd:PRK13650 5 IEVKNLTFK------YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGdlLTEenvw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 153 DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLSCANTRTGSLSGGQRKRLAI 229
Cdd:PRK13650 78 DIR--HKIGMVFQNPDNQFVGATVEDDVAFG----LENKGIPHEEMkerVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 230 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIICTIHQpsakLFE--LFDQLYVLSQGQ 296
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
100-250 |
3.15e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTL-LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYR--ETGmKGAVLiNGLPRDLRcFRKVSC----YimqddM--- 169
Cdd:NF033858 13 KTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARkiQQG-RVEVL-GGDMADAR-HRRAVCpriaY-----Mpqg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 ----LLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:NF033858 85 lgknLYPTLSVFENLDFFGRLFGQDAAE-RRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
....*
gi 46592964 246 TSGLD 250
Cdd:NF033858 164 TTGVD 168
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
103-298 |
3.92e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTL-MNILAGYRETGMKGAVLINGLPRDLRCF--------------RKVSCYIMQD 167
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 DML----LPHL-TVQEAMMVSAHLKLQEKDEGRREMvkEILTalgllSCANTRTGSLSGGQRKRLAIALELVNNPPVMFF 242
Cdd:NF040905 356 DIKrnitLANLgKVSRRGVIDENEEIKVAEEYRKKM--NIKT-----PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 243 DEPTSGLDSASCFQVVSLMKGLAQGGRSIIcTIhqpSAKLFELF---DQLYVLSQGQCV 298
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPELLgmcDRIYVMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
107-250 |
5.10e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 107 SGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLInglprDLrcfrKVSC---YIMQDdmllPHLTVQEAMMvs 183
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAG-VLKPDEGEVDP-----EL----KISYkpqYIKPD----YDGTVEDLLR-- 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46592964 184 ahlklQEKDEGRREMVK-EILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK13409 423 -----SITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
103-301 |
6.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGmKGAVLINGLPRDLRCFRKVS--------CYIMQDDMLLP 172
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiiSETG-QTIVGDYAIPANLKKIKEVKrlrkeiglVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTVQEAMMVSAHLklqekDEGRREMVKEILTALGLLSC----ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:PRK13645 106 ETIEKDIAFGPVNL-----GENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46592964 249 LDSASCFQVVSLMKGLAQG-GRSIICTIHQPSaKLFELFDQLYVLSQGQCVYRG 301
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-253 |
1.88e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRDLSY---SVPEGPwwrkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY------------------- 136
Cdd:PTZ00265 1166 IEIMDVNFryiSRPNVP---------IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndm 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 137 -----------RETGMK-----------------------GAVLINGL---PRDLRCFRKVSCYIMQDDMLLphltvqeA 179
Cdd:PTZ00265 1237 tneqdyqgdeeQNVGMKnvnefsltkeggsgedstvfknsGKILLDGVdicDYNLKDLRNLFSIVSQEPMLF-------N 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 180 MMVSAHLKLQeKDEGRREMVKEI--LTAL-----GLLSCANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSG 248
Cdd:PTZ00265 1310 MSIYENIKFG-KEDATREDVKRAckFAAIdefieSLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSS 1388
|
....*
gi 46592964 249 LDSAS 253
Cdd:PTZ00265 1389 LDSNS 1393
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-296 |
2.01e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 48 TDLLNGHLK---KVDNNLTEAQRFSS---LPRRAAVNIEFRDLSYSVPEGPWWR--------KKGYKTLLKGISGKFNSG 113
Cdd:PLN03232 1183 TTLLSGVLRqasKAENSLNSVERVGNyidLPSEATAIIENNRPVSGWPSRGSIKfedvhlryRPGLPPVLHGLSFFVSPS 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 114 ELVAIMGPSGAGKSTLMNILagYRETGM-KGAVLINGLprDLRCF-----RKVSCYIMQDDMLLPHLTVQEAMMVSAHLK 187
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNAL--FRIVELeKGRIMIDDC--DVAKFgltdlRRVLSIIPQSPVLFSGTVRFNIDPFSEHND 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 188 LQEKDEGRREMVKEIL--TALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDsascFQVVSLM-KGL 264
Cdd:PLN03232 1339 ADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIqRTI 1414
|
250 260 270
....*....|....*....|....*....|....
gi 46592964 265 AQGGRSiiCTIHQPSAKLFELF--DQLYVLSQGQ 296
Cdd:PLN03232 1415 REEFKS--CTMLVIAHRLNTIIdcDKILVLSSGQ 1446
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
100-250 |
2.19e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPR-------DLRcfRK---VSCYImqddm 169
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgsgetiwDIK--KHigyVSSSL----- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 170 llpHLTVQeammVSAHLK-------------LQEKDEGRREMVKEILTALGLLSC-ANTRTGSLSGGQRKRLAIALELVN 235
Cdd:PRK10938 346 ---HLDYR----VSTSVRnvilsgffdsigiYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVK 418
|
170
....*....|....*
gi 46592964 236 NPPVMFFDEPTSGLD 250
Cdd:PRK10938 419 HPTLLILDEPLQGLD 433
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
443-589 |
2.52e-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: 50.08 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 443 SNSGFLFFSMLFLMFAALMPTVLTFPLEMgVFLRE----HLNYWYSLK--AYYLAKTMADVPFQIMFPVAYCSIVYWMTS 516
Cdd:pfam12698 155 PQSGYAYYLVGLILMIIILIGAAIIAVSI-VEEKEsrikERLLVSGVSplQYWLGKILGDFLVGLLQLLIILLLLFGIGI 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46592964 517 QPSDAVRFVLFAALGtmtSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYI 589
Cdd:pfam12698 234 PFGNLGLLLLLFLLY---GLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSI 303
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
108-299 |
2.86e-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: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 108 GKFNSGELVAIMGPSGAGKSTLMNILAGYREtgmkgavlinglPRDlrcfrkvscyimqDDMLLPHLTVQeammvsahLK 187
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV--------YK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 188 LQEKDegrremvkeiltalgllscantrtgsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG 267
Cdd:cd03222 67 PQYID--------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|..
gi 46592964 268 GRSIICTIHQPSAKLFELFDQLYVLSQGQCVY 299
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFEGEPGVY 152
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
100-279 |
9.47e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-------YRETGMKGAVLINGLP------RDLRCFRKVscyimq 166
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaPRGARVTGDVTLNGEPlaaidaPRLARLRAV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 167 ddmlLPHlTVQEAMMVSAH--LKLQEKDEGRREMVKEILTAlGLLSCANTRTG----------SLSGGQRKRLAIALELV 234
Cdd:PRK13547 88 ----LPQ-AAQPAFAFSAReiVLLGRYPHARRAGALTHRDG-EIAWQALALAGatalvgrdvtTLSGGELARVQFARVLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 235 N---------NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGR-SIICTIHQPS 279
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPN 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
97-250 |
9.86e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 97 KGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAV------LINGLPRDlrcfrkvSCYIMQDD 168
Cdd:PRK15064 327 KGFdnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGTVkwsenaNIGYYAQD-------HAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 169 MllphlTVQEAMMvsahlklQEKDEGRRE-MVKEILTALgLLSC--ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 245
Cdd:PRK15064 399 L-----TLFDWMS-------QWRQEGDDEqAVRGTLGRL-LFSQddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
....*
gi 46592964 246 TSGLD 250
Cdd:PRK15064 466 TNHMD 470
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
100-307 |
2.29e-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: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 100 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMniLAGYRETGM-KGAVLING-----LPrdLRCFRKVSCYIMQDDMLL-- 171
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfDGKIVIDGidiskLP--LHTLRSRLSIILQDPILFsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 -------PHLTVQEAMMVSAHLKLQEKDegrreMVKEIltaLGLLSCANTRTG-SLSGGQRKRLAIALELVNNPPVMFFD 243
Cdd:cd03288 110 sirfnldPECKCTDDRLWEALEIAQLKN-----MVKSL---PGGLDAVVTEGGeNFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 244 EPTSGLDSAS--CFQVVsLMKGLAQggRSIICTIHQPSAKLFElfDQLYVLSQGQCVYRGKVCNLV 307
Cdd:cd03288 182 EATASIDMATenILQKV-VMTAFAD--RTVVTIAHRVSTILDA--DLVLVLSRGILVECDTPENLL 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
106-296 |
2.70e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING------------------LPRDlrcfRKVS------ 161
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGkeinalstaqrlarglvyLPED----RQSSglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 162 ------CYIMQDDMLLPHLTVQEAMMVsahlklqekDEGRRemvkeiltALGL-LSCANTRTGSLSGGQRKRLAIALELV 234
Cdd:PRK15439 357 plawnvCALTHNRRGFWIKPARENAVL---------ERYRR--------ALNIkFNHAEQAARTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 235 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFE---LFDQLYVLSQGQ 296
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
106-296 |
2.83e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 106 ISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGLPRDLRCFRK-VSCYIM------QDDMLLPHLTVQ 177
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGAtRRTA--GQVYLDGKPIDIRSPRDaIRAGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 178 EAMMVSA---HLK----LQEKDEgrREMVKEILTALgllscaNTRT-------GSLSGGQRKRLAIALELVNNPPVMFFD 243
Cdd:PRK11288 350 DNINISArrhHLRagclINNRWE--AENADRFIRSL------NIKTpsreqliMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46592964 244 EPTSGLDSASCFQVVSLMKGLAQGGRSIICTihqpSAKLFE---LFDQLYVLSQGQ 296
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFV----SSDLPEvlgVADRIVVMREGR 473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
80-250 |
4.84e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 80 EFRDLSYSVPEgpwwrkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG----------------------YR 137
Cdd:PRK11147 321 EMENVNYQIDG---------KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqlqadsgrihcgtklevayfdqHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 138 E------TGM------KGAVLINGLPrdlrcfRKVSCYiMQDDMLLPhltvqeammvsahlklqekdegRREMvkeilta 205
Cdd:PRK11147 392 AeldpekTVMdnlaegKQEVMVNGRP------RHVLGY-LQDFLFHP----------------------KRAM------- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46592964 206 lgllscanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK11147 436 --------TPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
93-279 |
6.42e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 93 WWRKKG-YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGlprdlrcfrkVSCYIMQDDMLL 171
Cdd:PRK13545 29 FRSKDGeYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKG----------SAALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 172 PHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 251
Cdd:PRK13545 98 GQLTGIENIELKG-LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180
....*....|....*....|....*...
gi 46592964 252 ASCFQVVSLMKGLAQGGRSIICTIHQPS 279
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLS 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
219-293 |
9.28e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 9.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIICTIHQPSAKLFELFDQLYVLS 293
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL-KGNENRITIIIAHRLSTIRYANTIFVLS 653
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
109-276 |
1.21e-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: 43.75 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 109 KFNSGeLVAIMGPSGAGKSTLMNIL--AGYRETGMKGavliNGLPRDLRCFRKVScyimqddmllphltvqeammVSAHL 186
Cdd:cd03240 19 EFFSP-LTLIVGQNGAGKTTIIEALkyALTGELPPNS----KGGAHDPKLIREGE--------------------VRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 187 KLQEKDEGRREMVkeILTALG-LLSCANTRTG-----------SLSGGQRK------RLAIALELVNNPPVMFFDEPTSG 248
Cdd:cd03240 74 KLAFENANGKKYT--ITRSLAiLENVIFCHQGesnwplldmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|
gi 46592964 249 LDSASC-FQVVSLMKG-LAQGGRSIICTIH 276
Cdd:cd03240 152 LDEENIeESLAEIIEErKSQKNFQLIVITH 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
109-268 |
1.86e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 109 KFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAvLINGLPRDLR-CFRKVSCYIMQD------DMLLPH-----LTV 176
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAG-ELPLLSGE-RQSQFSHITRlSFEQLQKLVSDEwqrnntDMLSPGeddtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 177 QEAmmvsahLKLQEKDEGRREMVKEILTALGLLScanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 256
Cdd:PRK10938 103 AEI------IQDEVKDPARCEQLAQQFGITALLD---RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|..
gi 46592964 257 VVSLMKGLAQGG 268
Cdd:PRK10938 174 LAELLASLHQSG 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-250 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 20 SYSAEMTEPKSVCVSVDEVVSSNMEATEtdllngHLKKVDNNLTEA-------QRFSSLPRRAAVniEFRDlsYSVPEGP 92
Cdd:TIGR00957 1227 SYSLQVTFYLNWLVRMSSEMETNIVAVE------RLKEYSETEKEApwqiqetAPPSGWPPRGRV--EFRN--YCLRYRE 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 93 wwrkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGLprdlrcfrKVSCYIMQDdmLLP 172
Cdd:TIGR00957 1297 -----DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDGL--------NIAKIGLHD--LRF 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 173 HLTV--QEAMMVSAHLKL------QEKDEgrremvkEILTALGL---------------LSCANTRTgSLSGGQRKRLAI 229
Cdd:TIGR00957 1361 KITIipQDPVLFSGSLRMnldpfsQYSDE-------EVWWALELahlktfvsalpdkldHECAEGGE-NLSVGQRQLVCL 1432
|
250 260
....*....|....*....|.
gi 46592964 230 ALELVNNPPVMFFDEPTSGLD 250
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVD 1453
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
94-140 |
2.28e-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: 2.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 94 WRKKGYKTLLkgISGKFNSG--EL--------VAIMGPSGAGKSTLMNILAG--YRETG 140
Cdd:cd01854 58 YEKLGYPVLA--VSAKTGEGldELrellkgktSVLVGQSGVGKSTLLNALLPelVLATG 114
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
112-134 |
3.15e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.10 E-value: 3.15e-04
10 20
....*....|....*....|...
gi 46592964 112 SGELVAIMGPSGAGKSTLMNILA 134
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAAR 26
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
276-333 |
4.65e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 42.97 E-value: 4.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 46592964 276 HQPSAKLFELFDQLYVLSQ-GQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASG 333
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
218-276 |
8.99e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 8.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 218 SLSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
79-250 |
1.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 79 IEFRD--LSYSvPEGPwwrkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGLprDLRC 156
Cdd:PLN03130 1238 IKFEDvvLRYR-PELP--------PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-ERGRILIDGC--DISK 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 157 F-----RKVSCYIMQDDMLLPHlTVQ---------------EAMMvSAHLklqeKDEGRRemvkeilTALGLLSCANTRT 216
Cdd:PLN03130 1306 FglmdlRKVLGIIPQAPVLFSG-TVRfnldpfnehndadlwESLE-RAHL----KDVIRR-------NSLGLDAEVSEAG 1372
|
170 180 190
....*....|....*....|....*....|....
gi 46592964 217 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 250
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
98-250 |
1.93e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 98 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGmkGAVLINGLPR--DLRC-------FRKVSCYIMQD 167
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEpSA--GNVSLDPNERlgKLRQdqfafeeFTVLDTVIMGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 168 DML------------LPHLTVQEAMMVsAHLKLQ--EKD----EGRremVKEILTALGL-LSCANTRTGSLSGGQRKRLA 228
Cdd:PRK15064 90 TELwevkqerdriyaLPEMSEEDGMKV-ADLEVKfaEMDgytaEAR---AGELLLGVGIpEEQHYGLMSEVAPGWKLRVL 165
|
170 180
....*....|....*....|..
gi 46592964 229 IALELVNNPPVMFFDEPTSGLD 250
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLD 187
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
103-133 |
2.02e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.02e-03
10 20 30
....*....|....*....|....*....|..
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMN-IL 133
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
113-135 |
2.11e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.69 E-value: 2.11e-03
10 20
....*....|....*....|...
gi 46592964 113 GELVAIMGPSGAGKSTLMNILAG 135
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
219-298 |
2.17e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 219 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCV 298
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
103-133 |
2.63e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.63e-03
10 20 30
....*....|....*....|....*....|..
gi 46592964 103 LKGISGKFNSGELVAIMGPSGAGKSTLMN-IL 133
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
112-135 |
3.05e-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: 3.05e-03
10 20
....*....|....*....|....
gi 46592964 112 SGELVAIMGPSGAGKSTLMNILAG 135
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
115-134 |
4.99e-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: 36.16 E-value: 4.99e-03
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
96-252 |
6.81e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 96 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGlpRD-----LRCFRKVSCYIMQDDML 170
Cdd:PTZ00243 1319 REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-CGGEIRVNG--REigaygLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46592964 171 L---------PHLTVQEAmMVSAHLKLQekdeGRREMVKEilTALGLLSCANTRTGSLSGGQRKRLAIALELVN-NPPVM 240
Cdd:PTZ00243 1396 FdgtvrqnvdPFLEASSA-EVWAALELV----GLRERVAS--ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFI 1468
|
170
....*....|..
gi 46592964 241 FFDEPTSGLDSA 252
Cdd:PTZ00243 1469 LMDEATANIDPA 1480
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
218-276 |
7.79e-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: 7.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46592964 218 SLSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIH 276
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
116-137 |
8.51e-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: 8.51e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
218-279 |
8.77e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 8.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46592964 218 SLSGGQRK---RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPS 279
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| |
