|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
60-666 |
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: 783.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 60 FTEAQRFSSLPRRAAVNIEfKDLSYSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM 139
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 140 KGA--VLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEK--DEGRREMVKEILTALGLLPCANTRTG 215
Cdd:TIGR00955 80 KGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 216 ------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYV 289
Cdd:TIGR00955 160 vpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 290 LSQGQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSrlVRAVREGMCDADYKRDLGGDTDVNPFLWH 369
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENE--SRERIEKICDSFAVSDIGRDMLVNTNLWS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 370 RPA---EEDSASMEGCHsFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFL 446
Cdd:TIGR00955 318 GKAgglVKDSENMEGIG-YNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 447 FFSMLFLMFAALMPTVLTFPLEMSVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFA 526
Cdd:TIGR00955 397 FLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 527 ALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVILSIYGLDR 606
Cdd:TIGR00955 477 FLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVD 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 607 --EDLHCDIAETCHFQKsEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER 666
Cdd:TIGR00955 557 niECTSANTTGPCPSSG-EVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
74-299 |
1.76e-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: 307.94 E-value: 1.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 74 AVNIEFKDLSYSVPEGPWwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET-GMKGAVLINGMPRDL 152
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPS---KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqekdegrremvkeiltalgllpcantrtgSLSGGQRKRLAIALELV 232
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 233 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
98-659 |
6.04e-80 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 267.13 E-value: 6.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGMPRDLRCFRKVScYIMQDDMLLPHLTVQE 176
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHLKLQE---KDEGRReMVKEILTALGLLPCANTRTGS-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PLN03211 160 TLVFCSLLRLPKsltKQEKIL-VAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 249 SASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEV 328
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 329 ASG--EYGDQNSRLVRAVREGMCdADYKRDLGGDTDVNPFLWHRPAEED----SASMEGCHSFSASCLT----QFCILFK 398
Cdd:PLN03211 319 ANGvcQTDGVSEREKPNVKQSLV-ASYNTLLAPKVKAAIEMSHFPQANArfvgSASTKEHRSSDRISIStwfnQFSILLQ 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 399 RTfLSIMRDSVLTHLRITShiGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMSVFLREHLN 478
Cdd:PLN03211 398 RS-LKERKHESFNTLRVFQ--VIAAALLAGLMWWHSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERAS 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 479 YWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGP 558
Cdd:PLN03211 475 GMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVT 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 559 VTAIPVLLFSGFFVsfDTIPAYLQWMSYISYVRYGFEGVILSIYGLDRED---LHCDIAE-----TCHFQKSEAIlreld 630
Cdd:PLN03211 555 VTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRIsslLGCSLPHgsdraSCKFVEEDVA----- 627
|
570 580
....*....|....*....|....*....
gi 13487145 631 vENAKLYLDFIVLGIFFISLRLIAYFVLR 659
Cdd:PLN03211 628 -GQISPATSVSVLIFMFVGYRLLAYLALR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-603 |
1.66e-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: 1.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 34 DEVVSSNVDEVETDLLNGHLKKVDNnFTEAQRFSSLPRRAAVNI-EFKDLSYSVPegpwwKKKGYKTLLKGISGKFNSGE 112
Cdd:TIGR00956 717 GETSASNKNDIEAGEVLGSTDLTDE-SDDVNDEKDMEKESGEDIfHWRNLTYEVK-----IKKEKRVILNNVDGWVKPGT 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 113 LVAIMGPSGAGKSTLMNILAGYRETGM--KGAVLINGMPRDlRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEK- 189
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSv 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 190 -DEGRREMVKEILTALGLLPCANTRTG----SLSGGQRKRLAIALELVNNPP-VMFFDEPTSGLDSASCFQVVSLMKGLA 263
Cdd:TIGR00956 870 sKSEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLA 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 264 QGGRSIVCTIHQPSAKLFELFDQLYVLSQG-QCVYRGKV----SNLVPYLRDLGL-NCPTYHNPADFVMEV---ASGEYG 334
Cdd:TIGR00956 950 DHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLgensHTIINYFEKHGApKCPEDANPAEWMLEVigaAPGAHA 1029
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 335 DQ-------NSRLVRAVREGMcdADYKRDLGGdtdvnpflwhrpAEEDSASmEGCHSFSASCLTQFCILFKRTFLSIMR- 406
Cdd:TIGR00956 1030 NQdyhevwrNSSEYQAVKNEL--DRLEAELSK------------AEDDNDP-DALSKYAASLWYQFKLVLWRTFQQYWRt 1094
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 407 -DSVLTHLRITshigiglligllylgigneakkvLSNS---GFLFF----SMLFL---MFAALMPTVLTFPL-------- 467
Cdd:TIGR00956 1095 pDYLYSKFFLT-----------------------IFAAlfiGFTFFkvgtSLQGLqnqMFAVFMATVLFNPLiqqylppf 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 468 ---EMSVFLREHLNYWYSLKAYYLAKTMADVPFQIMF-PVAYCSIVYWM----TSQPSDAV--RFVLFAALGTMTSLVAQ 537
Cdd:TIGR00956 1152 vaqRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAgTIFFFIWYYPVgfywNASKTGQVheRGVLFWLLSTMFFLYFS 1231
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 538 SLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVILSIYG 603
Cdd:TIGR00956 1232 TLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
89-299 |
3.56e-67 |
|
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: 219.45 E-value: 3.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 89 GPWW-------KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMK-GAVLINGMPRDLRCFRKVS 159
Cdd:cd03234 4 LPWWdvglkakNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTsGQILFNGQPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 160 CYIMQDDMLLPHLTVQEAMMVSAHLKLQE-KDEGRREMVKEI--LTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPP 236
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRkSSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 237 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
77-299 |
1.09e-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: 214.41 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETG-MKGAVLINGMPRDlRCF 155
Cdd:cd03232 4 LTWKNLNYTVPV-----KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 156 RKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqekdegrremvkeiltalgllpcantrtgSLSGGQRKRLAIALELVNNP 235
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFSALLR------------------------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 236 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQ-GQCVYRG 299
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
50-608 |
8.81e-57 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 208.93 E-value: 8.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 50 NGHLKKVDNNFTEAQrfSSLPRRAAV------NIEFKDLSYSVPEGPWWKKKGYK----TLLKGISGKFNSGELVAIMGP 119
Cdd:PLN03140 837 EGLSKNRDSSLEAAN--GVAPKRGMVlpftplAMSFDDVNYFVDMPAEMKEQGVTedrlQLLREVTGAFRPGVLTALMGV 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 120 SGAGKSTLMNILAGyRETG--MKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLqEKDEGRREMV 197
Cdd:PLN03140 915 SGAGKTTLMDVLAG-RKTGgyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRL-PKEVSKEEKM 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 198 KEILTALGLLPCANTR---------TGsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRS 268
Cdd:PLN03140 993 MFVDEVMELVELDNLKdaivglpgvTG-LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRT 1071
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 269 IVCTIHQPSAKLFELFDQLYVLSQ-GQCVYRGKVS----NLVPYLRDL-GL-NCPTYHNPADFVMEVASgeygdqnsrLV 341
Cdd:PLN03140 1072 VVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGrnshKIIEYFEAIpGVpKIKEKYNPATWMLEVSS---------LA 1142
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 342 RAVREGMCDADYKRdlggdtdvNPFLWHRP---AEEDSASMEGCHS------FSASCLTQFCILFKRTFLSIMR--DSVL 410
Cdd:PLN03140 1143 AEVKLGIDFAEHYK--------SSSLYQRNkalVKELSTPPPGASDlyfatqYSQSTWGQFKSCLWKQWWTYWRspDYNL 1214
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 411 THLRITSHIGIGLLIGLLYLGIGNEAKKVLSNS-GFLFFSMLFLMFAALMPTVLTFPLEMSVFLREHLNYWYSLKAYYLA 489
Cdd:PLN03140 1215 VRFFFTLAAALMVGTIFWKVGTKRSNANDLTMViGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIA 1294
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 490 KTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVAT-FVGPVTAIpVLLFS 568
Cdd:PLN03140 1295 QVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAiFAAAFYGL-FNLFS 1373
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 13487145 569 GFFVSFDTIPAYLQWMSYISYVRYGFEGVILSIYGlDRED 608
Cdd:PLN03140 1374 GFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG-DVED 1412
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
93-598 |
9.92e-52 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 193.79 E-value: 9.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE---TGMKGAVLINGMPRD--LRCFRKVSCYIMQDDM 167
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhIGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHLTVQEAMMVSAHLK-------LQEKDEGRREMVKEILTALGLLPCANTRTGS-----LSGGQRKRLAIALELVNNP 235
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 236 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIV-CTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLVPYLRDLGLN 314
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPlVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 315 CPTYHNPADFVMEVAS-------GEYGDQ-------------NSRLVRAVREGMcDADYKRDLGGDTDVNPFLWHRPAEE 374
Cdd:TIGR00956 309 CPDRQTTADFLTSLTSpaerqikPGYEKKvprtpqefetywrNSPEYAQLMKEI-DEYLDRCSESDTKEAYRESHVAKQS 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 375 DSASMEGCHSFSASCLTQFCIlfKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLM 454
Cdd:TIGR00956 388 KRTRPSSPYTVSFSMQVKYCL--ARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 455 FAALMPTVLTFplEMSVFLREHLNY-WYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTS 533
Cdd:TIGR00956 466 FSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICT 543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 534 LVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVI 598
Cdd:TIGR00956 544 LAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
77-304 |
1.73e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 1.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMP--RDLR 153
Cdd:COG1131 1 IEVRGLT---------KRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRPTS--GEVRVLGEDvaRDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVN 233
Cdd:COG1131 70 EVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKE-ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 234 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
78-294 |
8.96e-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: 8.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVPegpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP---RDLRC 154
Cdd:cd03225 1 ELKNLSFSYP-------DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 FRKVSCYIMQ--DDMLLpHLTVQEAMMVSA-HLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALEL 231
Cdd:cd03225 73 LRRKVGLVFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQ 294
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
77-296 |
2.24e-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: 2.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMP------R 150
Cdd:COG1136 5 LELRNLTKSYGTG-----EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVLIDGQDisslseR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSC-YIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:COG1136 79 ELARLRRRHIgFVFQFFNLLPELTALENVALPLLLAGVSRKE-RRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHqpSAKLFELFDQLYVLSQGQCV 296
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTH--DPELAARADRVIRLRDGRIV 223
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
396-598 |
1.43e-45 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 160.90 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 396 LFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKkVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMSVFLRE 475
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 476 HLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATF 555
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13487145 556 VGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVI 598
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
77-311 |
1.47e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 161.73 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMP---RDL 152
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQ--DDMLLpHLTVQEAMMVS-AHLKLqEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:COG1122 71 RELRRKVGLVFQnpDDQLF-APTVEEDVAFGpENLGL-PREE-IRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGKVSNLVPYLR 309
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
..
gi 13487145 310 DL 311
Cdd:COG1122 227 LL 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
77-294 |
1.67e-45 |
|
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: 161.12 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMP------R 150
Cdd:cd03255 1 IELKNLSKTYGGG-----GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFR--KVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:cd03255 75 ELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLLLA-GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHQPSakLFELFDQLYVLSQGQ 294
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
77-304 |
1.66e-41 |
|
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: 151.16 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP--RDLRC 154
Cdd:COG4555 2 IEVENLS---------KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-LKPDSGSILIDGEDvrKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 FRKVSCYIMQDDMLLPHLTVQEammvsaHLKL-----QEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLTVRE------NIRYfaelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
101-245 |
2.57e-40 |
|
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: 144.33 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMP---RDLRCFRKVSCYIMQDDMLLPHLTVQEA 177
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 178 MMVSAHLKLQEKDEGRREMvKEILTALGLLPCANTR----TGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA-EEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
77-310 |
6.56e-40 |
|
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: 146.49 E-value: 6.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPR----- 150
Cdd:cd03261 1 IELRGLTKSF---------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 -DLRCFRKVSCYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSEEE--IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIVCTiHQPSAkLFELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEGTPEELR 225
|
....*....
gi 13487145 306 ----PYLRD 310
Cdd:cd03261 226 asddPLVRQ 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
94-304 |
1.24e-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: 144.96 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 94 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETGM-KGAVLING--MPRDLRCFRKVSCYIMQDDMLLP 170
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG--ELRPtSGTAYINGysIRTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 HLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 250
Cdd:cd03263 89 ELTVREHLRFYARLKGLPKSEIKEE-VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 251 SCFQVVSLMKGLaQGGRSIVCTIHqpSAKLFELF-DQLYVLSQGQCVYRGKVSNL 304
Cdd:cd03263 168 SRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
77-304 |
3.13e-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: 144.63 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PR 150
Cdd:cd03256 1 IEVENLSKTYPNG--------KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGTdinklkGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSA------------HLKLQEKDEGRremvkEILTALGLLPCANTRTGSLS 218
Cdd:cd03256 72 ALRQLRRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrslfgLFPKEEKQRAL-----AALERVGLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 219 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPS-AKLFelFDQLYVLSQGQCV 296
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIV 224
|
....*...
gi 13487145 297 YRGKVSNL 304
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
77-297 |
2.49e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDlRCFR 156
Cdd:COG1121 7 IELENLTVSY---------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPR-RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 KVScYIMQD---DMLLPhLTVQE--AMMVSAHLKLQEK-DEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALE 230
Cdd:COG1121 76 RIG-YVPQRaevDWDFP-ITVRDvvLMGRYGRRGLFRRpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 231 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQCVY 297
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLVAH 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
77-292 |
1.26e-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: 138.77 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMPRDLRC-- 154
Cdd:COG4133 3 LEAENLS---------CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-LLPPSAGEVLWNGEPIRDARed 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 FRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKlqeKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNN 234
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 235 PPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPsakLFELFDQLYVLSQ 292
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
77-299 |
3.41e-37 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 139.41 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGmpRDLRCF- 155
Cdd:COG1120 2 LEAENLSVGYGG---------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDG--RDLASLs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 156 -----RKVScYIMQDDMLLPHLTVQEAMMV--SAHLK----LQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKR 224
Cdd:COG1120 70 rrelaRRIA-YVPQEPPAPFGLTVRELVALgrYPHLGlfgrPSAED---REAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 225 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPS-AKLFelFDQLYVLSQGQCVYRG 299
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQG 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
77-304 |
3.47e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGM------PR 150
Cdd:COG3638 3 LELRNLSKRYPGG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGQdvtalrGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMV---------SAHLKLQEKDEgrREMVKEILTALGLLPCANTRTGSLSGGQ 221
Cdd:COG3638 74 ALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgrtstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 222 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIVCTIHQPS-AKlfELFDQLYVLSQGQCVYRG 299
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDlAR--RYADRIIGLRDGRVVFDG 229
|
....*
gi 13487145 300 KVSNL 304
Cdd:COG3638 230 PPAEL 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
94-597 |
4.14e-37 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 149.23 E-value: 4.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 94 KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMK--GAVLINGMPRDLRCFRKVSCYIMQDDMLLPH 171
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGYRLNEFVPRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSA-------------HLKLQEKDEG--------------RREMVKE------ILTALGLLPCANTRTGS-- 216
Cdd:PLN03140 254 MTVKETLDFSArcqgvgtrydllsELARREKDAGifpeaevdlfmkatAMEGVKSslitdyTLKILGLDICKDTIVGDem 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 ---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIVCTIHQPSAKLFELFDQLYVLSQ 292
Cdd:PLN03140 334 irgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 293 GQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASG----EYGDQNSRLVRAVREGMCDADYKR-----DLGGDTDV 363
Cdd:PLN03140 414 GQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKkdqeQYWADRNKPYRYISVSEFAERFKSfhvgmQLENELSV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 364 nPFlwHRPAEEDSASMEGCHSFSASCLTQFCilFKRTFLSIMRDSVL----THLRITSHIGIGLLIGLLYLGIGNEAKKV 439
Cdd:PLN03140 494 -PF--DKSQSHKAALVFSKYSVPKMELLKAC--WDKEWLLMKRNAFVyvfkTVQIIIVAAIASTVFLRTEMHTRNEEDGA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 440 LSnSGFLFFSMLFLMFAALMPTVLTFPlEMSVFLRE-----HLNYWYSLKAYYLAktmadVPFQIMFPVAYCSIVYWMTS 514
Cdd:PLN03140 569 LY-IGALLFSMIINMFNGFAELALMIQ-RLPVFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVVWVVITYYSIG 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 515 QPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGF 594
Cdd:PLN03140 642 FAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGF 721
|
...
gi 13487145 595 EGV 597
Cdd:PLN03140 722 NAL 724
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
93-299 |
2.16e-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: 135.47 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET--GMKGAVLINGMPRD--LRCFRKVSCYIMQDDML 168
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPYKefAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 169 LPHLTVQEAMMVSAHLKlqekdegRREMVKEIltalgllpcantrtgslSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:cd03233 95 FPTLTVRETLDFALRCK-------GNEFVRGI-----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13487145 249 SASCFQVVSLMKGLAQG-GRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
77-294 |
3.23e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 133.68 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TgmKGAVLING--MPRDLR 153
Cdd:cd03230 1 IEVRNLS---------KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpD--SGEIKVLGkdIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDDMLLPHLTVQEammvsaHLKlqekdegrremvkeiltalgllpcantrtgsLSGGQRKRLAIALELVN 233
Cdd:cd03230 70 EVKRRIGYLPEEPSLYENLTVRE------NLK-------------------------------LSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 234 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQ 294
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
77-311 |
1.60e-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: 140.81 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMP------ 149
Cdd:COG1123 261 LEVRNLSKRYPV----RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRCFRKVSCYIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLP-CANTRTGSLSGGQRKRLA 226
Cdd:COG1123 335 RSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIvctihqpsakLF---------ELFDQLYVLSQGQCV 296
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTY----------LFishdlavvrYIADRVAVMYDGRIV 484
|
250 260
....*....|....*....|
gi 13487145 297 YRGKVSNLV-----PYLRDL 311
Cdd:COG1123 485 EDGPTEEVFanpqhPYTRAL 504
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
108-299 |
6.90e-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: 131.46 E-value: 6.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 108 FNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PRDlrcfRKVScYIMQDDMLLPHLTVQE--AMM 179
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 180 VSAHLKLQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 259
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13487145 260 KGL-AQGGRSIVCTIHQPSAKLfELFDQLYVLSQGQCVYRG 299
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
77-294 |
7.03e-35 |
|
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: 131.49 E-value: 7.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------MPR 150
Cdd:cd03259 1 LELKGLS---------KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDGrdvtgvPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DlrcfRKVScYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEG-RREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:cd03259 71 R----RNIG-MVFQDYALFPHLTVAEN--IAFGLKLRGVPKAeIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIVCTIHQPSAklFELFDQLYVLSQGQ 294
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEA--LALADRIAVMNEGR 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
77-248 |
8.29e-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: 131.44 E-value: 8.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRDlRCF 155
Cdd:cd03293 1 LEVRNVSKTYGGG-----GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEPVT-GPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 156 RKVScYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNP 235
Cdd:cd03293 73 PDRG-YVFQQDALLPWLTVLDNVALGLELQGVPKAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170
....*....|...
gi 13487145 236 PVMFFDEPTSGLD 248
Cdd:cd03293 151 DVLLLDEPFSALD 163
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
101-299 |
2.75e-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: 130.63 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVL-----INGMPRDLRC-------FRKVScyimqddm 167
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLfdgedITGLPPHEIArlgigrtFQIPR-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHLTVQEAMMVSAHLKLQE---------KDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVM 238
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 239 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
77-299 |
3.78e-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: 129.93 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING------MPR 150
Cdd:cd03257 2 LEVKNLSVSFPTG-----GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP-TSGSIIFDGkdllklSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDDM--LLPHLTVQEAMM--VSAHLKLQEKDEgRREMVKEILTALGLLP-CANTRTGSLSGGQRKRL 225
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMssLNPRMTIGEQIAepLRIHGKLSKKEA-RKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 226 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
98-299 |
6.76e-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: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGeLVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING--MPRDLRCFRKVSCYIMQDDMLLPHLTVQ 175
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGqdVLKQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVSAHLK-LQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 254
Cdd:cd03264 91 EFLDYIAWLKgIPSKEVKAR--VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13487145 255 VVSLMKGLAQgGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03264 169 FRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
62-299 |
8.78e-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: 137.66 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 62 EAQRFSSLPRRAAvNIEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmK 140
Cdd:COG2274 460 EGRSKLSLPRLKG-DIELENVSFRYPGDS-------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPT--S 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 141 GAVLINGM------PRDLRcfRKVScYIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGrremvk 198
Cdd:COG2274 530 GRILIDGIdlrqidPASLR--RQIG-VVLQDVFLFsgtirenitlgdPDATDEEiieaARLAGLHDFIEALPMG------ 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 199 eILTALGllpcanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPSa 278
Cdd:COG2274 601 -YDTVVG------EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS- 671
|
250 260
....*....|....*....|.
gi 13487145 279 kLFELFDQLYVLSQGQCVYRG 299
Cdd:COG2274 672 -TIRLADRIIVLDKGRIVEDG 691
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
77-304 |
9.18e-34 |
|
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: 129.34 E-value: 9.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP------R 150
Cdd:TIGR02315 2 LEVENLSKVYPNG--------KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-VEPSSGSILLEGTDitklrgK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDDMLLPHLTVQEAMM---VSAHLKLQ-------EKDegrREMVKEILTALGLLPCANTRTGSLSGG 220
Cdd:TIGR02315 73 KLRKLRRRIGMIFQHYNLIERLTVLENVLhgrLGYKPTWRsllgrfsEED---KERALSALERVGLADKAYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 221 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPS-AKLFElfDQLYVLSQGQCVYR 298
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFD 227
|
....*.
gi 13487145 299 GKVSNL 304
Cdd:TIGR02315 228 GAPSEL 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
77-248 |
1.08e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.82 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMPRDlRC 154
Cdd:COG1116 8 LELRGVSkrFPTGGGG-------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPVT-GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 FRKVScYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNN 234
Cdd:COG1116 79 GPDRG-VVFQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170
....*....|....
gi 13487145 235 PPVMFFDEPTSGLD 248
Cdd:COG1116 157 PEVLLMDEPFGALD 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
77-294 |
1.27e-33 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 126.34 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPR---DL 152
Cdd:cd03228 1 IEFKNVSFSYPGRP-------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlYDPT--SGEILIDGVDLrdlDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQDDMLLpHLTVQEAMmvsahlklqekdegrremvkeiltalgllpcantrtgsLSGGQRKRLAIALELV 232
Cdd:cd03228 72 ESLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 233 NNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTiHQPSakLFELFDQLYVLSQGQ 294
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGKTVIVIA-HRLS--TIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
67-305 |
1.51e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 135.66 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 67 SSLPRRAAVNIEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYREtGMKGAVLIN 146
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGG--------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-PYSGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 GMPR---DLRCFRKVSCYIMQDDMLlPHLTVQEammvsaHLKLQEKDEGRREM--------VKEILTAL--GLlpcaNTR 213
Cdd:COG4988 398 GVDLsdlDPASWRRQIAWVPQNPYL-FAGTIRE------NLRLGRPDASDEELeaaleaagLDEFVAALpdGL----DTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 214 TGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTiHQPSakLFELFDQLYV 289
Cdd:COG4988 467 LGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILV 543
|
250
....*....|....*.
gi 13487145 290 LSQGQCVYRGKVSNLV 305
Cdd:COG4988 544 LDDGRIVEQGTHEELL 559
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
77-294 |
1.58e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.62 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRD---- 151
Cdd:COG4619 1 LELEGLSFRV---------GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTS--GEIYLDGKPLSampp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 152 --LRcfRKVScYIMQDdmllPHL---TVQEAMMVSAHLKLQEKDegrREMVKEILTALGLLP-CANTRTGSLSGGQRKRL 225
Cdd:COG4619 70 peWR--RQVA-YVPQE----PALwggTVRDNLPFPFQLRERKFD---RERALELLERLGLPPdILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 226 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHQPsAKLFELFDQLYVLSQGQ 294
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
78-299 |
2.54e-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: 126.01 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMP---RDLRC 154
Cdd:cd03214 1 EVENLSVGYGG---------RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDlasLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 FRKVSCYIMQddmllphltvqeammvsahlklqekdegrremvkeILTALGLLPCANTRTGSLSGGQRKRLAIALELVNN 234
Cdd:cd03214 71 LARKIAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 235 PPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHQPS-AKLFelFDQLYVLSQGQCVYRG 299
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
78-294 |
3.05e-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: 125.05 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPRdlrcfr 156
Cdd:cd00267 1 EIENLSFRYGG---------RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGlLKPT--SGEILIDGKDI------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 kvscyimqddmllphltvqeammvsahlklqekdegRREMVKEILTALGLLPCantrtgsLSGGQRKRLAIALELVNNPP 236
Cdd:cd00267 64 ------------------------------------AKLPLEELRRRIGYVPQ-------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 237 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQ 294
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
77-310 |
3.57e-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: 127.40 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----MPR 150
Cdd:COG1127 6 IEVRNLT---------KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGqditgLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 D----LRcfRKVScYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegRREMVKEILTALGLLPCANTRTGSLSGGQRKR 224
Cdd:COG1127 75 KelyeLR--RRIG-MLFQGGALFDSLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 225 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIVCTiHQ-PSAklFELFDQLYVLSQGQCVYRGKV 301
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEGTP 226
|
250
....*....|...
gi 13487145 302 SNLV----PYLRD 310
Cdd:COG1127 227 EELLasddPWVRQ 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
77-275 |
5.95e-33 |
|
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: 126.11 E-value: 5.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGMP---- 149
Cdd:cd03262 1 IEIKNLH---------KSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGLKltdd 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 -RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVsAHLKLQ--EKDEGRrEMVKEILTALGLLPCANTRTGSLSGGQRKRLA 226
Cdd:cd03262 68 kKNINELRQKVGMVFQQFNLFPHLTVLENITL-APIKVKgmSKAEAE-ERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQ 275
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
77-294 |
3.50e-32 |
|
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: 122.68 E-value: 3.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP-----RD 151
Cdd:cd03229 1 LELKNVS---------KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEDltdleDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 152 LRCFRKVSCYIMQDDMLLPHLTVQEammvsahlklqekdegrremvkeiltalgllpcaNTRTGsLSGGQRKRLAIALEL 231
Cdd:cd03229 71 LPPLRRRIGMVFQDFALFPHLTVLE----------------------------------NIALG-LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHQPsAKLFELFDQLYVLSQGQ 294
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
76-299 |
4.96e-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: 123.85 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 76 NIEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGM------ 148
Cdd:cd03245 2 RIEFRNVSFSYPNQE-------IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTS--GSVLLDGTdirqld 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 PRDLRcfRKVScYIMQDdmllPHL---TVQEAMMvsahLKLQEKDEgrrEMVKEILTALGLLPCANT-----------RT 214
Cdd:cd03245 73 PADLR--RNIG-YVPQD----VTLfygTLRDNIT----LGAPLADD---ERILRAAELAGVTDFVNKhpngldlqigeRG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 215 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAqGGRSIVCTIHQPSakLFELFDQLYVLSQGQ 294
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGR 215
|
....*
gi 13487145 295 CVYRG 299
Cdd:cd03245 216 IVADG 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
77-294 |
6.61e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.24 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----MPR 150
Cdd:COG2884 2 IRFENVSKRYPGG--------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 D----LRcfRKVScYIMQDDMLLPHLTVQE----AMMVsahLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQR 222
Cdd:COG2884 72 ReipyLR--RRIG-VVFQDFRLLPDRTVYEnvalPLRV---TGKSRKEIRRR--VREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 223 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPsaklfELFDQL----YVLSQGQ 294
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL-----ELVDRMpkrvLELEDGR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
77-345 |
8.87e-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: 129.64 E-value: 8.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGMKGAVLING-----MP 149
Cdd:COG1123 5 LEVRDLSVRYPGGD-------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGrdlleLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRCfRKVScYIMQDDM--LLPhLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:COG1123 78 EALRG-RRIG-MVFQDPMtqLNP-VTVGDQIAEALENLGLSRAE-ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHQPsAKLFELFDQLYVLSQGQCVYRGKVSNL-- 304
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIla 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 13487145 305 -------VPYLRDLGLNCPTYHNPADFVMEVA--SGEYGDQNSRLVRAVR 345
Cdd:COG1123 233 apqalaaVPRLGAARGRAAPAAAAAEPLLEVRnlSKRYPVRGKGGVRAVD 282
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
80-274 |
9.74e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.37 E-value: 9.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 80 KDLSYSVPEGPwwkkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPRDLRCFRKV 158
Cdd:cd03226 3 ENISFSYKKGT--------EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 159 SCYIMQD-DMLLPHLTVQEAMMVSahLKLQEKDEGRREmvkEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPV 237
Cdd:cd03226 73 IGYVMQDvDYQLFTDSVREELLLG--LKELDAGNEQAE---TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 13487145 238 MFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
77-274 |
1.03e-31 |
|
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: 122.52 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMP------R 150
Cdd:cd03292 1 IEFINVTKTYPNG--------TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:cd03292 72 AIPYLRRKIGVVFQDFRLLPDRNVYENVAFA----LEVTGVPPREIrkrVPAALELVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
77-311 |
4.66e-31 |
|
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: 121.83 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP---RDLR 153
Cdd:COG1124 2 LEVRNLSVSYGQGGRRV-----PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDDM--LLPHLTVQEAmmVSAHLKLQEKDEgRREMVKEILTALGLLP-CANTRTGSLSGGQRKRLAIALE 230
Cdd:COG1124 76 AFRRRVQMVFQDPYasLHPRHTVDRI--LAEPLRIHGLPD-REERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 231 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHQPSAKLFeLFDQLYVLSQGQCVYRGKVSNLV---- 305
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGRIVEELTVADLLagpk 231
|
....*..
gi 13487145 306 -PYLRDL 311
Cdd:COG1124 232 hPYTREL 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
101-304 |
4.68e-31 |
|
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: 121.00 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 176
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHLKLQEKDEGRREMVKEILTALGLLpcANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 256
Cdd:cd03224 95 NLLLGAYARRRAKRKARLERVYELFPRLKER--RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 257 SLMKGLAQGGRSIVcTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:cd03224 173 EAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
78-293 |
9.88e-31 |
|
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: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLINGMPrdLRCFR 156
Cdd:cd03235 1 EVEDLTVSY---------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLlKPT--SGSIRVFGKP--LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 KVSCYIMQD---DMLLPhLTVQEAMM------VSAHLKLQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:cd03235 68 KRIGYVPQRrsiDRDFP-ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQG 293
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
77-275 |
1.16e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.58 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLM---NILagyrETGMKGAVLINGM----P 149
Cdd:PRK09493 2 IEFKNVS---------KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVDGLkvndP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 R-DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSA-HLKLQEKDEGRrEMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:PRK09493 69 KvDERLIRQEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAE-KQARELLAKVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQ 275
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
77-299 |
1.54e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMP-----R 150
Cdd:PRK13639 2 LETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT--SGEVLIKGEPikydkK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:PRK13639 72 SLLEVRKTVGIVFQnpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQpsAKLFELF-DQLYVLSQGQCVYRG 299
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
76-304 |
2.68e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 76 NIEFKDLSYSvpegpwwkkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGmpRDLRCF 155
Cdd:COG3840 1 MLRLDDLTYR-----------YGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGF-LPPDSGRILWNG--QDLTAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 156 ----RKVScYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:COG3840 67 ppaeRPVS-MLFQENNLFPHLTVAQniGLGLRPGLKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPS-AKLfeLFDQLYVLSQGQCVYRGKVSNL 304
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAAR--IADRVLLVADGRIAADGPTAAL 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
67-311 |
2.89e-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: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 67 SSLPRRAAVNIEFKDLSYSVPEGPWWkkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLIN 146
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRP-------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 GMP-RDLR--CFRKVSCYIMQDdmllPHL---TVQEammvsaHLKLQEKDEGRREMVkEILTALGLLPCA-------NTR 213
Cdd:COG4987 396 GVDlRDLDedDLRRRIAVVPQR----PHLfdtTLRE------NLRLARPDATDEELW-AALERVGLGDWLaalpdglDTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 214 TGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPSAklFELFDQLYV 289
Cdd:COG4987 465 LGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILV 541
|
250 260
....*....|....*....|....*
gi 13487145 290 LSQGQCVYRGKVSNLV---PYLRDL 311
Cdd:COG4987 542 LEDGRIVEQGTHEELLaqnGRYRQL 566
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
101-274 |
3.34e-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: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMP-----RDLRCFRKVSCYIMQ--DDMLLPHL 172
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQ--SGAVLIDGEPldysrKGLLERRQRVGLVFQdpDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 252
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERR--VREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|..
gi 13487145 253 FQVVSLMKGLAQGGRSIVCTIH 274
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
77-304 |
3.69e-30 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 118.84 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PR 150
Cdd:cd03258 2 IELKNVSKVFGDT-----GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALE 230
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAE-IEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 231 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
77-276 |
8.29e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.22 E-value: 8.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNIL-------AG-YRETGMKGAVLINGM 148
Cdd:PRK10535 5 LELKDIRRSYPSG-----EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 PRDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:PRK10535 80 LAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQP 276
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
101-294 |
8.36e-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: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGmpRDL--------------RCFRKVScyimqd 165
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDG--RDItglpphriarlgiaRTFQNPR------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 dmLLPHLTVQEAMMVSAHLKLQE-------------KDEGR-REMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALEL 231
Cdd:COG0411 90 --LFPELTVLENVLVAAHARLGRgllaallrlprarREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAkLFELFDQLYVLSQGQ 294
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL-VMGLADRIVVLDFGR 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
93-299 |
2.21e-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: 115.78 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGMPRDLRCFRKVSCyIMQDDMLLPH 171
Cdd:cd03268 8 KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDSGEITFDGKSYQKNIEALRRIGA-LIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSAHLKLqekdeGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:cd03268 87 LTARENLRLLARLLG-----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 252 CFQVVSLMKGLAQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
77-274 |
2.80e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.25 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGMP---- 149
Cdd:COG1126 2 IEIENLH---------KSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDltds 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 -RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVS-AHLKLQEKDEGRrEMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:COG1126 69 kKDINKLRRKVGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
93-305 |
5.20e-29 |
|
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: 115.33 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING-----MPRDLRCfRKVSCYIMQDD 166
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGKILLDGqditkLPMHKRA-RLGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 MLLPHLTVQEAMMvsAHLKLQEKD-EGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:cd03218 85 SIFRKLTVEENIL--AVLEIRGLSkKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 246 GLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLfELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
97-300 |
1.29e-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: 113.80 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 97 YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMPR-DLRCFRKVSCYIMQDDMLLPHLTVQ 175
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-IEPASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVSAH--LKLQEKdegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 253
Cdd:TIGR01277 89 QNIGLGLHpgLKLNAE---QQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 254 QVVSLMKGLA-QGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRGK 300
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGKIKVVSD 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
77-302 |
1.81e-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: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGM------PR 150
Cdd:COG4559 2 LEAENLSVRL---------GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGEL-TPSSGEVRLNGRplaawsPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVscyimqddmlLP-------HLTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLPCANTRTGSLSGG- 220
Cdd:COG4559 72 ELARRRAV----------LPqhsslafPFTVEEvvALGRAPHGSSAAQD---RQIVREALALVGLAHLAGRSYQTLSGGe 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 221 -QRKRLAIAL----ELVNNPP-VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPS-AKLFElfDQLYVLSQG 293
Cdd:COG4559 139 qQRVQLARVLaqlwEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYA--DRILLLHQG 216
|
....*....
gi 13487145 294 QCVYRGKVS 302
Cdd:COG4559 217 RLVAQGTPE 225
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
62-296 |
1.94e-28 |
|
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: 121.13 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 62 EAQRFSSLPRRAAvNIEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmK 140
Cdd:TIGR03375 450 EGTRFLHRPRLQG-EIEFRNVSFAYPGQE-------TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGlYQPT--E 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 141 GAVLINGM------PRDLRcfRKVScYIMQDDMLLpHLTVQEAMMVSAhlklQEKDEgrrEMVKEILTALGLLPCANT-- 212
Cdd:TIGR03375 520 GSVLLDGVdirqidPADLR--RNIG-YVPQDPRLF-YGTLRDNIALGA----PYADD---EEILRAAELAGVTEFVRRhp 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 213 ---------RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAqGGRSIVCTIHQPSakLFEL 283
Cdd:TIGR03375 589 dgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS--LLDL 665
|
250
....*....|...
gi 13487145 284 FDQLYVLSQGQCV 296
Cdd:TIGR03375 666 VDRIIVMDNGRIV 678
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
96-276 |
3.66e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 112.27 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQ 175
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVSAHLKlqekdEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 255
Cdd:PRK13539 92 ENLEFWAAFL-----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|..
gi 13487145 256 VSLMKG-LAQGGrSIVCTIHQP 276
Cdd:PRK13539 167 AELIRAhLAQGG-IVIAATHIP 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
77-248 |
9.48e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 9.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------MPR 150
Cdd:COG3839 4 LELENVS---------KSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL-EDPTSGEILIGGrdvtdlPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DlrcfRKVScyiM--QDDMLLPHLTVQEAMmvSAHLKLQ--EKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLA 226
Cdd:COG3839 74 D----RNIA---MvfQSYALYPHMTVYENI--AFPLKLRkvPKAE-IDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180
....*....|....*....|..
gi 13487145 227 IALELVNNPPVMFFDEPTSGLD 248
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLD 165
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
77-302 |
1.28e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 112.10 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSvpegpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-----YRET----GMK-GAVLIn 146
Cdd:COG1119 4 LELRNVTVR---------RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptYGNDvrlfGERrGGEDV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 gmpRDLRcfRK---VSCYIMQDdmLLPHLTVQEaMMVSA-------HLKLQEKDEGRremVKEILTALGLLPCANTRTGS 216
Cdd:COG1119 74 ---WELR--KRiglVSPALQLR--FPRDETVLD-VVLSGffdsiglYREPTDEQRER---ARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIVCTIHQPSAkLFELFDQLYVLSQGQC 295
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRV 221
|
....*..
gi 13487145 296 VYRGKVS 302
Cdd:COG1119 222 VAAGPKE 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
93-304 |
1.68e-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: 110.92 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGMP--RDLRCFRKVSCYIMQDDMLL 169
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 PHLTVQEAMMVsaHLKLQE-KDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:cd03265 86 DELTGWENLYI--HARLYGvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 249 SASCFQVVSLMKGL-AQGGRSIVCTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
77-248 |
1.96e-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: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGmpRDL---- 152
Cdd:COG3842 6 LELENVS---------KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDG--RDVtglp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 --RcfRKVScYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:COG3842 74 peK--RNVG-MVFQDYALFPHLTVAEN--VAFGLRMRgvPKAE-IRARVAELLELVGLEGLADRYPHQLSGGQQQRVALA 147
|
170 180
....*....|....*....|
gi 13487145 229 LELVNNPPVMFFDEPTSGLD 248
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALD 167
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
77-264 |
2.39e-27 |
|
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: 110.60 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----MPRD 151
Cdd:COG4181 9 IELRGLTKTVGTG-----AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGqdlfaLDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 152 LRC-FR--KVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:COG4181 83 ARArLRarHVG-FVFQSFQLLPTLTALENVMLPLELA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 264
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
93-248 |
3.54e-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: 110.02 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP-RDLRCFRKVSCYIMQDDMLLPH 171
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 172 LTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:cd03300 87 LTVFENIAFGLRLKKLPKAEIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
110-299 |
1.14e-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: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 110 SGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------------PRDlrcfRKVScYIMQDDMLLPHLTVQEA 177
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 178 MMVSAHLKLQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 257
Cdd:cd03297 96 LAFGLKRKRNRED---RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13487145 258 LMKGLAQ--GGRSIVCTiHQPSaKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03297 173 ELKQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
99-249 |
2.61e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.62 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 99 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGmpRDLrcFRKVSC------YIMQDDMLLPHL 172
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNG--RDL--FTNLPPrerrvgFVFQHYALFPHM 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 173 TVQEAmmVSAHLKLQEKDEG-RREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:COG1118 91 TVAEN--IAFGLRVRPPSKAeIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
98-304 |
2.91e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.91 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNIL----AGYRETG---MKGAVLINGMPRDLRCFRKVSCYIMQDDM 167
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLeqpeAGTIRVGditIDTARSLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 247
Cdd:PRK11264 96 LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 248 DSASCFQVVSLMKGLAQGGRSIVCTIHQPS-AKlfELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQGPAKAL 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
98-250 |
7.27e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 7.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETG--MKGAVLINGmpRDLRCF----RKVScYIMQDDMLLPH 171
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNG--RRLTALpaeqRRIG-ILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQE--AMMVSAHLKLQEkdegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:COG4136 91 LSVGEnlAFALPPTIGRAQ----RRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 13487145 250 A 250
Cdd:COG4136 167 A 167
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
111-250 |
1.68e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.43 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGmpRDLRCF----RKVScYIMQDDMLLPHLTVQEAMMVSAH--L 184
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFL-TPASGSLTLNG--QDHTTTppsrRPVS-MLFQENNLFSHLTVAQNIGLGLNpgL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 185 KLqekDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 250
Cdd:PRK10771 101 KL---NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
76-299 |
3.08e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.64 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 76 NIEFKDLSYSVPEGPWwkkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMP------ 149
Cdd:COG1132 339 EIEFENVSFSYPGDRP--------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDirdltl 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRcfRKVScYIMQDDMLLpHLTVQE-----------------AMMVSAHLKLQEKDEGRREMVKEiltalgllpcant 212
Cdd:COG1132 410 ESLR--RQIG-VVPQDTFLF-SGTIREnirygrpdatdeeveeaAKAAQAHEFIEALPDGYDTVVGE------------- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 213 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVctI-HQPSAklFELFDQLYVLS 291
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV--IaHRLST--IRNADRILVLD 548
|
....*...
gi 13487145 292 QGQCVYRG 299
Cdd:COG1132 549 DGRIVEQG 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
69-290 |
4.95e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 109.68 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 69 LPRRAAVNIEFKDLSYSVPegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGM 148
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYP--------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 PR---DLRCFRKVSCYIMQddmlLPHLTvqeAMMVSAHLKLQEKDeGRREMVKEILTALGLLPCA-------NTRTGS-- 216
Cdd:TIGR02857 385 PLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRLARPD-ASDAEIREALERAGLDEFVaalpqglDTPIGEgg 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 217 --LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPsaKLFELFDQLYVL 290
Cdd:TIGR02857 457 agLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
77-294 |
7.36e-25 |
|
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: 101.52 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWkkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMP---RDLR 153
Cdd:cd03246 1 LEVENVSFRYPGAEPP-------VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADisqWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDDMLLPHlTVQEAMmvsahlklqekdegrremvkeiltalgllpcantrtgsLSGGQRKRLAIALELVN 233
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 234 NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSakLFELFDQLYVLSQGQ 294
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
101-275 |
1.18e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGM---------PRDLRCFRKVSCYIMQDDML 168
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 169 LPHLTVQEAMmVSAHLKL--QEKDEGRrEMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:COG4161 94 WPHLTVMENL-IEAPCKVlgLSKEQAR-EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|....*....
gi 13487145 247 LDSASCFQVVSLMKGLAQGGRSIVCTIHQ 275
Cdd:COG4161 172 LDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
95-276 |
1.31e-24 |
|
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: 101.67 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 95 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP----RDLRcfRKVSCYIMQDDMLLP 170
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPlaeqRDEP--HENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 HLTVQEAMMVSAHLKlqekdEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 250
Cdd:TIGR01189 87 ELSALENLHFWAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 13487145 251 SCFQVVSLMKGLAQGGRSIVCTIHQP 276
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
77-264 |
2.03e-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: 102.26 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMK----GAVLINGM---- 148
Cdd:cd03260 1 IELRDLNVYY---------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGKdiyd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 ----PRDLRcfRKVScYIMQDDMLLPhLTVQEAmmVSAHLKLQE--KDEGRREMVKEILTALGLLPCANTRTG--SLSGG 220
Cdd:cd03260 72 ldvdVLELR--RRVG-MVFQKPNPFP-GSIYDN--VAYGLRLHGikLKEELDERVEEALRKAALWDEVKDRLHalGLSGG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13487145 221 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 264
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK 189
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
101-260 |
5.14e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 101.26 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING-----MPRDLRCFrkvsCYIMQDDMLLPHLTVQ 175
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGkditnLPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 255
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
....*
gi 13487145 256 VSLMK 260
Cdd:cd03299 169 REELK 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
76-299 |
5.17e-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: 101.15 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 76 NIEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP---RDL 152
Cdd:cd03254 2 EIEFENVNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQDDMLLPHlTVQEAMMVSahlklqeKDEGRREMVKEILTALGL------LP-----CANTRTGSLSGGQ 221
Cdd:cd03254 73 KSLRSMIGVVLQDTFLFSG-TIMENIRLG-------RPNATDEEVIEAAKEAGAhdfimkLPngydtVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 222 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTiHQPSAKLFElfDQLYVLSQGQCVYRG 299
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
99-276 |
6.06e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 99 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYREtgmkgavlingmPRDLRCFRKVSC---YIMQ---DDMLLPhL 172
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------------PTSGTVRRAGGArvaYVPQrseVPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAMMVS--AHLKLQEK-DEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:NF040873 73 TVRDLVAMGrwARRGLWRRlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 13487145 250 ASCFQVVSLMKGLAQGGRSIVCTIHQP 276
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
77-296 |
6.78e-24 |
|
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: 100.84 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGM------PR 150
Cdd:cd03295 1 IEFENVTKRYGGG--------KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRcfRKVScYIMQDDMLLPHLTVQEAmmVSAHLKLQE-KDEGRREMVKEILTALGLLPC--ANTRTGSLSGGQRKRLAI 227
Cdd:cd03295 72 ELR--RKIG-YVIQQIGLFPHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSaKLFELFDQLYVLSQGQCV 296
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDID-EAFRLADRIAIMKNGEIV 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
95-276 |
9.11e-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: 99.49 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 95 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRD-LRCFRKVSC-YIMQDDMLLPHL 172
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPLDfQRDSIARGLlYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAMMVSAhlklqekDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 252
Cdd:cd03231 89 SVLENLRFWH-------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 13487145 253 FQVVSLMKGLAQGGRSIVCTIHQP 276
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
93-304 |
1.34e-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: 101.70 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGMKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPH 171
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLlRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDE-AEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 252 CFQVVSLMKGLAQGGRSIVCTIHQpsakLFE---LFDQLYVLSQGQCVYRGKVSNL 304
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
93-299 |
2.13e-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: 98.51 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPRDLRCFRKVScYIMQDDMLLPH 171
Cdd:cd03269 8 KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPD--SGEVLFDGKPLDIAARNRIG-YLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:cd03269 85 MKVIDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 252 CFQVVSLMKGLAQGGRSIVCTIHQpSAKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
77-299 |
2.60e-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: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVP-EGPWwkkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGmpRDLRCF 155
Cdd:cd03251 1 VEFKNVTFRYPgDGPP--------VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDG--HDVRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 156 ------RKVScyIMQDDMLLPHLTVQE-----------------AMMVSAHLKLQEKDEGRREMVKEiltalgllpcant 212
Cdd:cd03251 70 tlaslrRQIG--LVSQDVFLFNDTVAEniaygrpgatreeveeaARAANAHEFIMELPEGYDTVIGE------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 213 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIV-----CTIHQPsaklfelfDQL 287
Cdd:cd03251 135 RGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFViahrlSTIENA--------DRI 206
|
250
....*....|..
gi 13487145 288 YVLSQGQCVYRG 299
Cdd:cd03251 207 VVLEDGKIVERG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
77-296 |
3.82e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.08 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGM------PR 150
Cdd:PRK13548 3 LEARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVscyimqddmlLPH-------LTVQE--AMMVSAHLKLQEKDegrREMVKEILTALGLLPCANTRTGSLSGG- 220
Cdd:PRK13548 73 ELARRRAV----------LPQhsslsfpFTVEEvvAMGRAPHGLSRAED---DALVAAALAQVDLAHLAGRDYPQLSGGe 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 221 -QRKRLAIAL----ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHqpSAKLFELF-DQLYVLSQG 293
Cdd:PRK13548 140 qQRVQLARVLaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQG 217
|
...
gi 13487145 294 QCV 296
Cdd:PRK13548 218 RLV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
100-272 |
4.17e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.35 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 100 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP---------RDLRCfRKVScYIMQDDMLLP 170
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 HLTVQE--AM-MVSAHLKLQEKDEGRREMvkeiLTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 247
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*..
gi 13487145 248 DSASCFQVVSLMKGL--AQGGRSIVCT 272
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVT 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
109-275 |
4.39e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 109 NSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLINGM---------PRDLRCFRKVSCYIMQDDMLLPHLTVQEAMm 179
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 180 VSAHLKLQEKDEGR-REMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 258
Cdd:PRK11124 104 IEAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
170
....*....|....*..
gi 13487145 259 MKGLAQGGRSIVCTIHQ 275
Cdd:PRK11124 184 IRELAETGITQVIVTHE 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
101-304 |
6.72e-23 |
|
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: 97.75 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 176
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL-LPPRSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHL-KLQEKDEGRREMVKEILTALGLLpcANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL-----Dsa 250
Cdd:COG0410 98 NLLLGAYArRDRAEVRADLERVYELFPRLKER--RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivE-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13487145 251 scfQVVSLMKGLAQGGRSIVCtIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:COG0410 174 ---EIFEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
77-304 |
1.04e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRD----- 151
Cdd:PRK13636 6 LKVEELNYNYSDG--------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPIDysrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 152 LRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:PRK13636 77 LMKLRESVGMVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKR--VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHqpSAKLFELF-DQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
93-299 |
1.30e-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: 96.67 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGM-----PRDLRcfRKVScyIMQDDM 167
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFdvvkePAEAR--RRLG--FVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 -LLPHLTVQEAMMVSAHLKLQEKDE--GRremVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 244
Cdd:cd03266 88 gLYDRLTARENLEYFAGLYGLKGDEltAR---LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 245 SGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRG 299
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
77-300 |
1.48e-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: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGmpRDLR--- 153
Cdd:cd03253 1 IEFENVTFAYDPG--------RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDG--QDIRevt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 --CFRKVSCYIMQDDMLL----------PHLTVQEAMMVSA------HLKLQEKDEGRREMVKEiltalgllpcantRTG 215
Cdd:cd03253 70 ldSLRRAIGVVPQDTVLFndtigyniryGRPDATDEEVIEAakaaqiHDKIMRFPDGYDTIVGE-------------RGL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 216 SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTiHQPS----AklfelfDQLYVLS 291
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLStivnA------DKIIVLK 209
|
....*....
gi 13487145 292 QGQCVYRGK 300
Cdd:cd03253 210 DGRIVERGT 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
77-304 |
1.54e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.38 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGM--- 148
Cdd:COG1135 2 IELENLSktFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 ---PRDLRCFR-KVScYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLPCANTRTGSLSGGQR 222
Cdd:COG1135 71 alsERELRAARrKIG-MIFQHFNLLSSRTVAEN--VALPLEIAgvPKAE-IRKRVAELLELVGLSDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 223 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK------GLaqggrSIVCTIHQPS-AKlfELFDQLYVLSQGQC 295
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKdinrelGL-----TIVLITHEMDvVR--RICDRVAVLENGRI 219
|
....*....
gi 13487145 296 VYRGKVSNL 304
Cdd:COG1135 220 VEQGPVLDV 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
93-275 |
1.69e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLING----MPRD------------LRCFR 156
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGqtinLVRDkdgqlkvadknqLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 KVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTGS-LSGGQRKRLAIALELVNNP 235
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13487145 236 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQ 275
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
92-294 |
1.90e-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: 95.78 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 92 WKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PRDlrcfRKVScYIMQD 165
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGRdvtdlpPKD----RDIA-MVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13487145 246 GLDSASCFQVVSLMKGLAQ--GGRSIVCTIHQPSAklFELFDQLYVLSQGQ 294
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEA--MTMADRIAVMNDGQ 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
78-312 |
2.00e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.67 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLING-----MP 149
Cdd:COG0396 2 EIKNLHVSVEG---------KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGedileLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRC----FrkvscYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGR--REMVKEILTALGLLPCANTRT--GSLSGGQ 221
Cdd:COG0396 71 PDERAragiF-----LAFQYPVEIPGVSVSNFLRTALNARRGEELSARefLKLLKEKMKELGLDEDFLDRYvnEGFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 222 RKRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVS-LMKGLAQGGRSIVCTIHQPsaKLFELF--DQLYVLSQGQCVYR 298
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVKS 222
|
250
....*....|....
gi 13487145 299 GKVSnLVPYLRDLG 312
Cdd:COG0396 223 GGKE-LALELEEEG 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
101-249 |
3.86e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP-----RDlrcfRKVscyIMQDDMLLPHLTVQ 175
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgAD----RGV---VFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 176 EAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:COG4525 95 DN--VAFGLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
79-248 |
4.16e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 79 FKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLIngmPRDLRcfrkV 158
Cdd:COG0488 1 LENLSKSFGG---------RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVSI---PKGLR----I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 159 ScYIMQDDMLLPHLTV-QEAMMVSAHLK--LQEKDEGRREM----------------------------VKEILTALGLL 207
Cdd:COG0488 64 G-YLPQEPPLDDDLTVlDTVLDGDAELRalEAELEELEAKLaepdedlerlaelqeefealggweaearAEEILSGLGFP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13487145 208 PC-ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:COG0488 143 EEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
101-304 |
4.58e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRDLRCFRK-----VSCyIMQDDMLLPHLTV 174
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagIAI-IHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 175 QEAMMVSahlklQEKDEG----RREMVK---EILTALGL-LPcANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:COG1129 97 AENIFLG-----REPRRGglidWRAMRRrarELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 247 LDSASCFQVVSLMKGLAQGGRSIVCTIHqpsaKLFELF---DQLYVLSQGQCVYRGKVSNL 304
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAIIYISH----RLDEVFeiaDRVTVLRDGRLVGTGPVAEL 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
77-316 |
9.70e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 95.60 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGM------- 148
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKA----LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 --PRDLRcfRKVScYIMQddmlLPH-----LTVQEAMMVSAH-LKLQEKDEGRRemVKEILTALGLLPCANTRTG-SLSG 219
Cdd:TIGR04521 75 kkLKDLR--KKVG-LVFQ----FPEhqlfeETVYKDIAFGPKnLGLSEEEAEER--VKEALELVGLDEEYLERSPfELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 220 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYR 298
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKGKIVLD 224
|
250 260
....*....|....*....|.
gi 13487145 299 GKVSNL---VPYLRDLGLNCP 316
Cdd:TIGR04521 225 GTPREVfsdVDELEKIGLDVP 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
74-276 |
1.01e-21 |
|
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: 99.36 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 74 AVNIEFKDLSYSVPEGPwwkkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP---R 150
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAP--------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVSCYIMQDdmllPHL---TVQEAMMVSahlklqeKDEGRREMVKEILTALGL------LP-CANTRTG----S 216
Cdd:TIGR02868 403 DQDEVRRRVSVCAQD----AHLfdtTVRENLRLA-------RPDATDEELWAALERVGLadwlraLPdGLDTVLGeggaR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGlAQGGRSIVCTIHQP 276
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
100-305 |
1.07e-21 |
|
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: 94.48 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 100 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGMPR---DLRCFRKVSCYIMQDDMLLP------ 170
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-VPENGRVLVDGHDLalaDPAWLRRQVGVVLQENVLFNrsirdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 ----------HLTVQEAMMVSAHLKLQEKDEGRREMVKEiltalgllpcantRTGSLSGGQRKRLAIALELVNNPPVMFF 240
Cdd:cd03252 96 ialadpgmsmERVIEAAKLAGAHDFISELPEGYDTIVGE-------------QGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 241 DEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPSAklFELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
96-299 |
1.38e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyR-ETGMKGAVLINGMPRDLRCFRKVSCYIMqddmLLP-HLT 173
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RlLTPQSGTVFLGDKPISMLSSRQLARRLA----LLPqHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 174 VQEAMMV--------SAHL----KLQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFD 241
Cdd:PRK11231 87 TPEGITVrelvaygrSPWLslwgRLSAED---NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 242 EPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH---QPSaklfELFDQLYVLSQGQCVYRG 299
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
77-249 |
1.48e-21 |
|
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: 93.94 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PR 150
Cdd:cd03296 3 IEVRNVS---------KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEdatdvpVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DlrcfRKVScYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEGR-----REMVKEILTALGLLPCANTRTGSLSGGQRKRL 225
Cdd:cd03296 73 E----RNVG-FVFQHYALFRHMTVFDN--VAFGLRVKPRSERPpeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRV 145
|
170 180
....*....|....*....|....
gi 13487145 226 AIALELVNNPPVMFFDEPTSGLDS 249
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDA 169
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
77-264 |
2.48e-21 |
|
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: 95.51 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL----MNILAGYRETGmkGAVLINGM---- 148
Cdd:COG0444 2 LEVRNLKVYFP-----TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGITS--GEILFDGEdllk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 --PRDLRCFR--KVScYIMQDDM--LLPHLTVQEAMM--VSAHLKLQEKDegRREMVKEILTALGLlPCANTRTGS---- 216
Cdd:COG0444 75 lsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQIAepLRIHGGLSKAE--ARERAIELLERVGL-PDPERRLDRyphe 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMKGLAQ 264
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiQA---QILNLLKDLQR 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
69-299 |
2.49e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 69 LPRRAAVNIEFKDLSYSVP--EGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTlmNILAGYRETGMKGAVLIN 146
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPirKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 GMP------RDLRCFRKVSCYIMQD--DMLLPHLTVQEamMVSAHLKLQEKD---EGRREMVKEILTALGLLPCANTR-T 214
Cdd:PRK15134 346 GQPlhnlnrRQLLPVRHRIQVVFQDpnSSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 215 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQ 294
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
....*
gi 13487145 295 CVYRG 299
Cdd:PRK15134 504 VVEQG 508
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
101-274 |
3.99e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.33 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGM----------------PRDLRCFRKVSCY 161
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 162 IMQDDMLLPHLTVQE-AMMVSAHLKLQEKDEGRrEMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFF 240
Cdd:COG4598 100 VFQSFNLWSHMTVLEnVIEAPVHVLGRPKAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190
....*....|....*....|....*....|....
gi 13487145 241 DEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
80-296 |
6.57e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 80 KDLSYSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP------RDLR 153
Cdd:PRK10419 7 SGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDDM--LLPHLTV----QEAMMvsaHLkLQEKDEGRREMVKEILTALGLLP-CANTRTGSLSGGQRKRLA 226
Cdd:PRK10419 86 AFRRDIQMVFQDSIsaVNPRKTVreiiREPLR---HL-LSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHqpSAKLFELFDQ-LYVLSQGQCV 296
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITH--DLRLVERFCQrVMVMDNGQIV 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
66-248 |
9.85e-21 |
|
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: 92.32 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 66 FSSLPRRAavnieFKDLSYSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGmkGAVL 144
Cdd:cd03294 10 FGKNPQKA-----FKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTS--GKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 145 INGMP---------RDLRcfRKVSCYIMQDDMLLPHLTVQEAmmVSAHLKLQ-EKDEGRREMVKEILTALGLLPCANTRT 214
Cdd:cd03294 83 IDGQDiaamsrkelRELR--RKKISMVFQSFALLPHRTVLEN--VAFGLEVQgVPRAEREERAAEALELVGLEGWEHKYP 158
|
170 180 190
....*....|....*....|....*....|....
gi 13487145 215 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
77-274 |
1.02e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.07 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyRETGM-KGAVLINGMP------ 149
Cdd:COG4604 2 IEIKNVS---------KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGLDvattps 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRcfRKVScyIM-QDDMLLPHLTVQEamMVS----AHLK--LQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQR 222
Cdd:COG4604 71 RELA--KRLA--ILrQENHINSRLTVRE--LVAfgrfPYSKgrLTAED---REIIDEAIAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13487145 223 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIH 274
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
94-248 |
1.26e-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: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 94 KKGYK--TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagyreTGM----KGAVLING-----MPRDLRC-------- 154
Cdd:COG1137 10 VKSYGkrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI-----VGLvkpdSGRIFLDGedithLPMHKRArlgigylp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 -----FRKvscyimqddmllphLTVQEAMMvsAHLKLQEKD-EGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:COG1137 85 qeasiFRK--------------LTVEDNIL--AVLELRKLSkKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180
....*....|....*....|
gi 13487145 229 LELVNNPPVMFFDEPTSGLD 248
Cdd:COG1137 149 RALATNPKFILLDEPFAGVD 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
94-248 |
1.39e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.24 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 94 KKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGmpRDLR----CFRKVSCyIMQDDM 167
Cdd:PRK09452 21 SKSFdgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDG--QDIThvpaENRHVNT-VFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHLTVQEAmmVSAHLKLQE--KDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:PRK09452 97 LFPHMTVFEN--VAFGLRMQKtpAAE-ITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
...
gi 13487145 246 GLD 248
Cdd:PRK09452 174 ALD 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
80-274 |
1.41e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.77 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 80 KDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILaGYRETGMKGAVLINGMPR---DLRCF- 155
Cdd:PRK10575 15 RNVSFRVPG---------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLeswSSKAFa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 156 RKVScYIMQDdmlLPH---LTVQEAMMVSA---HLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIAL 229
Cdd:PRK10575 85 RKVA-YLPQQ---LPAaegMTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIH 274
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
101-302 |
1.45e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETGMKGAVLINGMP------RDLRCFRkvsCYIMQDDMLLPhltv 174
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 175 qeAMMVSAHLKLQEKDEGRREMVK----EILTALGLLPCANTRTGSLSGG--QRKRLAIALELV---NNPP--VMFFDEP 243
Cdd:COG4138 83 --AMPVFQYLALHQPAGASSEAVEqllaQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 244 TSGLDSAScfQVV--SLMKGLAQGGRSIVCTIHQPSAKLFELfDQLYVLSQGQCVYRGKVS 302
Cdd:COG4138 161 MNSLDVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGETA 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
101-309 |
1.50e-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: 90.99 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMPRDLRCFRKVscYIMQDDMLLPHLTVQE--AM 178
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 179 MVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS- 257
Cdd:TIGR01184 78 AVDRVLPDLSKSE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEe 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13487145 258 LMKGLAQGGRSIVCTIHQPSAKLFeLFDQLYVLSQGQCVYRGKVSNlVPYLR 309
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE-VPFPR 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
93-305 |
1.90e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING--MPRDLRCFRKVSCYIMQDDMLLP 170
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGepVPSRARHARQRVGVVPQFDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 HLTVQEAMMV-SAHLKLQEKDEgrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:PRK13537 94 DFTVRENLLVfGRYFGLSAAAA--RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 250 ASCFQVVSLMKGLAQGGRSIVCTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:PRK13537 172 QARHLMWERLRSLLARGKTILLTTHfMEEAE--RLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
101-299 |
2.50e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.23 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY----RETGMKGAVLING------MPRDLRCFRKVSCYIMQDDMLLP 170
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTvqregrLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 HLTVQEAMMVSA-------HLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:PRK09984 100 RLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 244 TSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAKLfELFDQLYVLSQGQCVYRG 299
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
68-305 |
3.88e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.53 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 68 SLPRRAAVNIEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRetgmkGAVL 144
Cdd:PRK11174 341 ELASNDPVTIEAEDLEILSPDG--------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 145 INGMPR---DLRCFRKVSCYIMQDDmLLPHLTVQEAMMVSAHlklQEKDEG-----RREMVKEILTAL--GLlpcaNT-- 212
Cdd:PRK11174 408 INGIELrelDPESWRKHLSWVGQNP-QLPHGTLRDNVLLGNP---DASDEQlqqalENAWVSEFLPLLpqGL----DTpi 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 213 --RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTiHQpsakLFEL--FDQLY 288
Cdd:PRK11174 480 gdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ----LEDLaqWDQIW 554
|
250
....*....|....*..
gi 13487145 289 VLSQGQCVYRGKVSNLV 305
Cdd:PRK11174 555 VMQDGQIVQQGDYAELS 571
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
69-299 |
3.91e-20 |
|
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: 94.37 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 69 LPRRAAVNIEFKDLS--YSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL-MNILagyRETGMKGAVLI 145
Cdd:COG4172 268 VPPDAPPLLEARDLKvwFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL---RLIPSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 146 NGMP------RDLRCFRK---VscyIMQDDM--LLPHLTV----QEAMMVsahLKLQEKDEGRREMVKEILTALGLLPCA 210
Cdd:COG4172 345 DGQDldglsrRALRPLRRrmqV---VFQDPFgsLSPRMTVgqiiAEGLRV---HGPGLSAAERRARVAEALEEVGLDPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 211 NTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIvctihqpsAKLF-------- 281
Cdd:COG4172 419 RHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHGL--------AYLFishdlavv 489
|
250
....*....|....*....
gi 13487145 282 -ELFDQLYVLSQGQCVYRG 299
Cdd:COG4172 490 rALAHRVMVMKDGKVVEQG 508
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
76-304 |
4.14e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 76 NIEFKDLSYSVPEGPwwkkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMP-RDLR 153
Cdd:TIGR00958 478 LIEFQDVSFSYPNRP------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlYQPTG--GQVLLDGVPlVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 C---FRKVScyIMQDDMLLPHLTVQEAM----------MVSAHLKLQEKDEGRREMVKEILTALGllpcantRTGS-LSG 219
Cdd:TIGR00958 550 HhylHRQVA--LVGQEPVLFSGSVRENIaygltdtpdeEIMAAAKAANAHDFIMEFPNGYDTEVG-------EKGSqLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 220 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKglaQGGRSIVCTIHQPSakLFELFDQLYVLSQGQCVYRG 299
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKGSVVEMG 695
|
....*
gi 13487145 300 KVSNL 304
Cdd:TIGR00958 696 THKQL 700
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
95-299 |
4.22e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.95 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 95 KGYK--TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGmkgAVLING-----MPRDLRCFRKVScYIMQD 165
Cdd:PRK10895 11 KAYKgrRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDedislLPLHARARRGIG-YLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13487145 246 GLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLfELFDQLYVLSQGQCVYRG 299
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
92-300 |
4.54e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 92 WKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP-----RDLRCFRKVSCYIMQD- 165
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-QKGAVLWQGKPldyskRGLLALRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHLTVQEAMMVS-AHLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 244
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 245 SGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGK 300
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGA 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
77-299 |
5.17e-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: 87.75 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDL--RC 154
Cdd:cd03247 1 LSINNVSFSYPEQE-------QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 FRKVSCYIMQDdmllPHL---TVQEAMmvsahlklqekdeGRRemvkeiltalgllpcantrtgsLSGGQRKRLAIALEL 231
Cdd:cd03247 73 LSSLISVLNQR----PYLfdtTLRNNL-------------GRR----------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPSAklFELFDQLYVLSQGQCVYRG 299
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
77-305 |
6.23e-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: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP-RDL--R 153
Cdd:cd03249 1 IEFKNVSFRYPSRPDVP------ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGVDiRDLnlR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDdmllPHL---TVQEAMMVSahlklqeKDEGRREMVKEILTALGL------LPCA-NTRTG----SLSG 219
Cdd:cd03249 74 WLRSQIGLVSQE----PVLfdgTIAENIRYG-------KPDATDEEVEEAAKKANIhdfimsLPDGyDTLVGergsQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 220 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIV-----CTIhQPSaklfelfDQLYVLSQGQ 294
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIViahrlSTI-RNA-------DLIAVLQNGQ 214
|
250
....*....|.
gi 13487145 295 CVYRGKVSNLV 305
Cdd:cd03249 215 VVEQGTHDELM 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
93-332 |
8.20e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGM-KGAVLINGMPRDLRCFRKVSCYIMQDDMLLPH 171
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgKITVLGVPVPARARLARARIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMV-SAHLKLQEKDegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 250
Cdd:PRK13536 129 FTVRENLLVfGRYFGMSTRE--IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 251 SCFQVVSLMKGLAQGGRSIVCTIH-QPSAKlfELFDQLYVLSQGQCVYRGKVSNLVpylrDLGLNCPtyhnpadfVMEVA 329
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHfMEEAE--RLCDRLCVLEAGRKIAEGRPHALI----DEHIGCQ--------VIEIY 272
|
...
gi 13487145 330 SGE 332
Cdd:PRK13536 273 GGD 275
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
101-296 |
8.71e-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: 86.71 E-value: 8.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRDLRcfrkvscyimqddmllphlTVQEAM- 178
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlYKPDS--GEILVDGKEVSFA-------------------SPRDARr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 179 ----MVSahlklQekdegrremvkeiltalgllpcantrtgsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 254
Cdd:cd03216 75 agiaMVY-----Q-----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13487145 255 VVSLMKGLAQGGRSIVCTIHqpsaKLFELF---DQLYVLSQGQCV 296
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
98-293 |
1.16e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMP-RDLRCFRKVscyIMQDDMLLPHLTVQE 176
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPvEGPGAERGV---VFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 256
Cdd:PRK11248 90 NVAFGLQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 13487145 257 SLMKGLAQG-GRSIVCTIHQPSAKLFeLFDQLYVLSQG 293
Cdd:PRK11248 169 TLLLKLWQEtGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
101-304 |
1.33e-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: 88.35 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMP-RDLRCFRKVS---CYIMQDDMLLPHLTVQE 176
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDiTKLPPHERARagiAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSahlkLQEKDEGRREMVKEILTalgLLPC----ANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL----- 247
Cdd:TIGR03410 95 NLLTG----LAALPRRSRKIPDEIYE---LFPVlkemLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsii 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 248 -DSAscfQVVSLMKglAQGGRSIVcTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:TIGR03410 168 kDIG---RVIRRLR--AEGGMAIL-LVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
102-250 |
1.62e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.86 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 102 KGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE--TG--MKGAVLINGMPRDLRCFRKVscyiMQDDMLLPHLTVQEA 177
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGVGMV----FQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 178 MmvSAHLKLQEKDEG----RREMVKEILTALGLLpcaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 250
Cdd:PRK11000 96 M--SFGLKLAGAKKEeinqRVNQVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
77-317 |
2.04e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGM----PRDL 152
Cdd:PRK13644 2 IRLENVSYSYPDG--------TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGIdtgdFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQD-DMLLPHLTVQEAMMVSAHLKLQEKDEGRReMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALEL 231
Cdd:PRK13644 73 QGIRKLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQpsakLFELF--DQLYVLSQGQCVYRGKVSNLV--PY 307
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN----LEELHdaDRIIVMDRGKIVLEGEPENVLsdVS 227
|
250
....*....|
gi 13487145 308 LRDLGLNCPT 317
Cdd:PRK13644 228 LQTLGLTPPS 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
98-248 |
2.92e-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: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLING-----MPRDLRcfrkvSCYI---MQDDML 168
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGkdvtkLPEYKR-----AKYIgrvFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 169 --LPHLTVQEAMMVSAH------LKLQEKDEgRREMVKEILTALGL-----LpcaNTRTGSLSGGQRKRLAIALELVNNP 235
Cdd:COG1101 92 gtAPSMTIEENLALAYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLMATLTKP 167
|
170
....*....|...
gi 13487145 236 PVMFFDEPTSGLD 248
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
96-301 |
3.98e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG----YRETGMKGAVLING---MPRDLRCFRKVSCYIMQDDML 168
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGqdiFKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 169 LPHLTVQEAmmVSAHLKLQEKDEGRREM---VKEILTALGLLPCANTR----TGSLSGGQRKRLAIALELVNNPPVMFFD 241
Cdd:PRK14247 94 IPNLSIFEN--VALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 242 EPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPsAKLFELFDQLYVLSQGQCVYRGKV 301
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGPT 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
108-294 |
3.99e-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: 92.77 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 108 FNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLING--MPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLK 185
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGkdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 186 LQEKDEGRREMvKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG 265
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180
....*....|....*....|....*....
gi 13487145 266 GRSIVCTIHQPSAKLfeLFDQLYVLSQGQ 294
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGR 1137
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
77-300 |
4.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.74 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING--MPRD-L 152
Cdd:PRK13632 8 IKVENVSFSYPNS-------ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGitISKEnL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQD-DMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:PRK13632 79 KEIRKKIGIIFQNpDNQFIGATVEDDIAFG----LENKKVPPKKMkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTI-HQPSAKLfeLFDQLYVLSQGQCVYRGK 300
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAI--LADKVIVFSEGKLIAQGK 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
68-305 |
5.15e-19 |
|
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: 91.34 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 68 SLPRRAAvNIEFKDLSYSV-PEGPwwkkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLIN 146
Cdd:TIGR01846 448 ALPELRG-AITFENIRFRYaPDSP--------EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVD 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 GM------PRDLRcfRKVSCyIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltal 204
Cdd:TIGR01846 518 GVdlaiadPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAPFEHvihaAKLAGAHDFISELPQGYNTEVGE----- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 205 gllpcantRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPSAklFELF 284
Cdd:TIGR01846 590 --------KGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLST--VRAC 658
|
250 260
....*....|....*....|.
gi 13487145 285 DQLYVLSQGQCVYRGKVSNLV 305
Cdd:TIGR01846 659 DRIIVLEKGQIAESGRHEELL 679
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
77-294 |
7.06e-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: 85.99 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMP---RDL 152
Cdd:cd03248 12 VKFQNVTFAYPTRP------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfYQPQG--GQVLLDGKPisqYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQDDMLLPH---------LTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGllpcanTRTGSLSGGQRK 223
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVG------EKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 224 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHqpsAKLFELFDQLYVLSQGQ 294
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR---LSTVERADQILVLDGGR 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
77-302 |
8.81e-19 |
|
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: 86.16 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETGmkGAVLING-----M 148
Cdd:TIGR01978 1 LKIKDLHVSVED---------KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsYEVTS--GTILFKGqdlleL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 PRDLRCfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGR------REMVKEILTALGLLPCANTR---TGsLSG 219
Cdd:TIGR01978 70 EPDERA-RAGLFLAFQYPEEIPGVSNLEFLRSALNARRSARGEEPldlldfEKLLKEKLALLDMDEEFLNRsvnEG-FSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 220 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPsaKLFELF--DQLYVLSQGQCVY 297
Cdd:TIGR01978 148 GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVK 225
|
....*
gi 13487145 298 RGKVS 302
Cdd:TIGR01978 226 SGDVE 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
77-301 |
1.00e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGMP---RDLR 153
Cdd:PRK13652 4 IETRDLCYSY--------SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL-KPTSGSVLIRGEPitkENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALEL 231
Cdd:PRK13652 75 EVRKFVGLVFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGKV 301
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
112-294 |
1.31e-18 |
|
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: 87.86 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 112 ELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGmprdlRCF-------------RKVScYIMQDDMLLPHLTVQEam 178
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNG-----RTLfdsrkgiflppekRRIG-YVFQEARLFPHLSVRG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 179 mvsaHLKLQEKD---EGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 255
Cdd:TIGR02142 95 ----NLRYGMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13487145 256 VSLMKGLAQG-GRSIVCTIHQPSaKLFELFDQLYVLSQGQ 294
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQ-EVLRLADRVVVLEDGR 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
77-303 |
1.79e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.16 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILagyrETGMKGAVLINGM--- 148
Cdd:PRK11153 2 IELKNISkvFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 ---PRDLRCFRKVSCYIMQDDMLLPHLTVQEAmmVSAHLKLQEKDEGR-REMVKEILTALGLLPCANTRTGSLSGGQRKR 224
Cdd:PRK11153 71 alsEKELRKARRQIGMIFQHFNLLSSRTVFDN--VALPLELAGTPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 225 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHQPSA-KlfELFDQLYVLSQGQCVYRGKVS 302
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVvK--RICDRVAVIDAGRLVEQGTVS 226
|
.
gi 13487145 303 N 303
Cdd:PRK11153 227 E 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
77-248 |
2.35e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINgmprdlrcfR 156
Cdd:COG0488 316 LELEGLSKSYGD---------KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVKLG---------E 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 KVSC-YIMQD-DMLLPHLTVQEAMMvsahlklQEKDEGRREMVKEILTALGLLP-CANTRTGSLSGGQRKRLAIALELVN 233
Cdd:COG0488 377 TVKIgYFDQHqEELDPDKTVLDELR-------DGAPGGTEQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLS 449
|
170
....*....|....*
gi 13487145 234 NPPVMFFDEPTSGLD 248
Cdd:COG0488 450 PPNVLLLDEPTNHLD 464
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
77-299 |
2.59e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.73 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETgmKGAVLING-----M 148
Cdd:cd03217 1 LEIKDLHVSVGG---------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGeditdL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 PRDLRcFRKVSCYIMQDDMLLPHLTVQEAmmvsahlkLQEKDEGrremvkeiltalgllpcantrtgsLSGGQRKRLAIA 228
Cdd:cd03217 70 PPEER-ARLGIFLAFQYPPEIPGVKNADF--------LRYVNEG------------------------FSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQpsAKLFELF--DQLYVLSQGQCVYRG 299
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
58-305 |
2.64e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 58 NNFTEAQ---RFS--SLPRRAAVNIEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA 132
Cdd:PRK11160 315 NEITEQKpevTFPttSTAAADQVSLTLNNVSFTYPDQP-------QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 133 GYRETGmKGAVLINGmpRDLRCFRkvscyimqDDMLLPHLTV--QEAMMVSAHLK---LQEKDEGRREMVKEILTALGLL 207
Cdd:PRK11160 388 RAWDPQ-QGEILLNG--QPIADYS--------EAALRQAISVvsQRVHLFSATLRdnlLLAAPNASDEALIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 208 PCANTRTG----------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTiHQps 277
Cdd:PRK11160 457 KLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HR-- 533
|
250 260
....*....|....*....|....*...
gi 13487145 278 AKLFELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:PRK11160 534 LTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
77-299 |
3.47e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 84.31 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEG-PWWK---------KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAV 143
Cdd:cd03267 1 IEVSNLSksYRVYSKePGLIgslkslfkrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 144 LING-MP--RDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGG 220
Cdd:cd03267 79 RVAGlVPwkRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKR-LDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 221 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIH--QPSAKlfeLFDQLYVLSQGQCVY 297
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEA---LARRVLVIDKGRLLY 234
|
..
gi 13487145 298 RG 299
Cdd:cd03267 235 DG 236
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
101-248 |
4.67e-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: 88.47 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP---RDLRCFRKVSCYIMQDDMLLP------- 170
Cdd:TIGR03797 469 LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDlagLDVQAVRRQLGVVLQNGRLMSgsifeni 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 ----HLTVQEAMMVSAHLKLqekDEGRREMvkeiltALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:TIGR03797 548 aggaPLTLDEAWEAARMAGL---AEDIRAM------PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
..
gi 13487145 247 LD 248
Cdd:TIGR03797 619 LD 620
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
93-304 |
5.18e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRDLRCFRKVScYimqddM---- 167
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPDS--GEVLWDGEPLDPEDRRRIG-Y-----Lpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 -LLPHLTVQEAMMVSAHLKLQEKDEGRREMvKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:COG4152 81 gLYPKMKVGEQLVYLARLKGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 247 LDSAScfqvVSLMKG----LAQGGRSIVCTIHQ-PSAKlfELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:COG4152 160 LDPVN----VELLKDvireLAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
101-248 |
6.84e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.67 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PRDlrcfRKVScyiM--QDDMLLPHL 172
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RDIA---MvfQNYALYPHM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 173 TVQEAMmvsAH-LKLQ--EKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK11650 92 SVRENM---AYgLKIRgmPKAE-IEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
77-274 |
7.03e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMPRDLRCFR 156
Cdd:PRK09536 4 IDVSDLSVEF---------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 KVSCYIM---QDDMLLPHLTVQEA--MMVSAHL-KLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALE 230
Cdd:PRK09536 74 AASRRVAsvpQDTSLSFEFDVRQVveMGRTPHRsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13487145 231 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
77-305 |
8.19e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.02 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGM---PRDLR 153
Cdd:PRK13647 5 IEVEDLHFRYKDG--------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQD--DMLLPHLTVQEAMMVSAHLKLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALEL 231
Cdd:PRK13647 76 WVRSKVGLVFQDpdDQVFSSTVWDDVAFGPVNMGLDKDEVERR--VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13487145 232 VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLfELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
116-248 |
9.59e-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: 84.85 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 116 IMGPSGAGKSTLMNILAGYrETGMKGAVLING-----MPRDLRCFRKVscyiMQDDMLLPHLTVQEAmmVSAHLKLQEKD 190
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMRKVP 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 191 -EGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:TIGR01187 74 rAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
93-264 |
1.22e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMPrdLRCFRKVSCYIMQDDMLLPHL 172
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAmmVSAHLKLQEKDEGRremvkEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 252
Cdd:PRK11247 97 KVIDN--VGLGLKGQWRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170
....*....|..
gi 13487145 253 FQVVSLMKGLAQ 264
Cdd:PRK11247 170 IEMQDLIESLWQ 181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
77-259 |
1.96e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP------- 149
Cdd:PRK10584 7 VEVHHLKKSVGQG-----EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 --RDLRCfRKVScYIMQDDMLLPHLTVQEAMMVSAHLKlQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:PRK10584 81 arAKLRA-KHVG-FVFQSFMLIPTLNALENVELPALLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190
....*....|....*....|....*....|..
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 259
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
51-294 |
3.32e-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: 85.18 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 51 GHLKKVDNNFTEAQRFSSLPRRAAvNIEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNI 130
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPRPKG-RLSVENLTVVPPGSK-------RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 131 LAG-YRETGmkGAVLINGMprDLRCFRKVSC-----YIMQDDMLLPHlTVQE----------------AMMVSAHlklqe 188
Cdd:COG4618 378 LVGvWPPTA--GSVRLDGA--DLSQWDREELgrhigYLPQDVELFDG-TIAEniarfgdadpekvvaaAKLAGVH----- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 189 kdegrrEMvkeILTalglLPCA-NTRTGS----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA 263
Cdd:COG4618 448 ------EM---ILR----LPDGyDTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK 514
|
250 260 270
....*....|....*....|....*....|.
gi 13487145 264 QGGRSIVCTIHQPSakLFELFDQLYVLSQGQ 294
Cdd:COG4618 515 ARGATVVVITHRPS--LLAAVDKLLVLRDGR 543
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
93-304 |
5.23e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDlRCFRKVSC-----YIMQDDM 167
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHLTVQEAMMVSAHLKlqEKDEG--------RREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMF 239
Cdd:PRK09700 91 VIDELTVLENLYIGRHLT--KKVCGvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 240 FDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQpSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
111-274 |
6.09e-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: 80.28 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMPRdlRCFRKVSCYIMQDDML---LPhLTVQEAMMVS-----A 182
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGrtghiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 183 HLKLQEKDEGRreMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL 262
Cdd:TIGR03771 82 WLRRPCVADFA--AVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170
....*....|..
gi 13487145 263 AQGGRSIVCTIH 274
Cdd:TIGR03771 160 AGAGTAILMTTH 171
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
101-249 |
6.31e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.85 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNS-------------GELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING--------MPRDLrcfrkvs 159
Cdd:PRK11432 9 LKNITKRFGSntvidnlnltikqGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDGedvthrsiQQRDI------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 160 CYIMQDDMLLPHLTVQEAmmVSAHLKLQ--EKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPV 237
Cdd:PRK11432 81 CMVFQSYALFPHMSLGEN--VGYGLKMLgvPKEE-RKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|..
gi 13487145 238 MFFDEPTSGLDS 249
Cdd:PRK11432 158 LLFDEPLSNLDA 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
101-296 |
7.08e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRDlrcFRKVS-------CYIMQDDMLLPHL 172
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMR---FASTTaalaagvAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAMMVsAHL--KLQEKDEGR-REMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:PRK11288 95 TVAENLYL-GQLphKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13487145 250 ASCFQVVSLMKGLAQGGRSIVCTIHQpSAKLFELFDQLYVLSQGQCV 296
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGRYV 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
96-294 |
7.61e-17 |
|
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: 83.94 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPR---DLRCFRKVSCYIMQDDMLLPHL 172
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP-TSGSVRLDGADLkqwDRETFGKHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQ---------EAMMVSAHLKLQekdeGRREMvkeIL-------TALGllpcanTRTGSLSGGQRKRLAIALELVNNPP 236
Cdd:TIGR01842 408 VAEniarfgenaDPEKIIEAAKLA----GVHEL---ILrlpdgydTVIG------PGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 237 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSakLFELFDQLYVLSQGQ 294
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
95-276 |
9.30e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 95 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG--YRETGmkgAVLINGMP-RDLR-CFRKVSCYIMQDDMLLP 170
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRdEYHQDLLYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 171 HLTVQEAMMVSAHLKlqekDEGRREMVKEILTALGL-----LPCantrtGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:PRK13538 88 ELTALENLRFYQRLH----GPGDDEALWEALAQVGLagfedVPV-----RQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|.
gi 13487145 246 GLDSASCFQVVSLMKGLAQGGRSIVCTIHQP 276
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
104-248 |
9.64e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 9.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 104 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMprDLRC---FRKVSCYIMQDDMLLPHLTVQEAMMV 180
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGV--DLSHvppYQRPINMMFQSYALFPHMTVEQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 181 SAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK11607 115 GLKQDKLPKAE-IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
101-270 |
1.01e-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: 79.79 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMN-ILAGYRETGmkGAVLI---NGM-------PRD---LRcfRKVSCYIMQdd 166
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVrhdGGWvdlaqasPREilaLR--RRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 mllpHLTV---QEAMMVSAH--LKLQEKDEGRREMVKEILTALGL------LPCANtrtgsLSGGQRKRLAIALELVNNP 235
Cdd:COG4778 101 ----FLRViprVSALDVVAEplLERGVDREEARARARELLARLNLperlwdLPPAT-----FSGGEQQRVNIARGFIADP 171
|
170 180 190
....*....|....*....|....*....|....*
gi 13487145 236 PVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIV 270
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
103-248 |
1.07e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.42 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 103 GISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVL-----INGMPrDLRCFRKVSCYIMQDDMLLPHLTVQE 176
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILlrgqhIEGLP-GHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHLKLQE-------KDEGRREMVKEILT-------ALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDE 242
Cdd:PRK11300 100 NLLVAQHQQLKTglfsgllKTPAFRRAESEALDraatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
....*.
gi 13487145 243 PTSGLD 248
Cdd:PRK11300 180 PAAGLN 185
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
115-251 |
2.10e-16 |
|
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: 81.30 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 115 AIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP---RDLRCF-----RKVScYIMQDDMLLPHLTVQEammvsaHLKL 186
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------NLLY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 187 QEKDEGRREM---VKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:COG4148 101 GRKRAPRAERrisFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
101-270 |
2.80e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPRDLRCFRK-VSCYI-M--QDDMLLPHLTVQ 175
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGlYQPD--SGEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 E----AMMVSAHLKLQEKDEgrREMVKEILTALGL-LPcANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL--- 247
Cdd:COG3845 99 EnivlGLEPTKGGRLDRKAA--RARIRELSERYGLdVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpq 175
|
170 180
....*....|....*....|...
gi 13487145 248 DSASCFQVvslMKGLAQGGRSIV 270
Cdd:COG3845 176 EADELFEI---LRRLAAEGKSII 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
77-250 |
3.21e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILA-GYRETGmkGAVLINGMP-RD--L 152
Cdd:PRK13657 335 VEFDDVSFSYD--------NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQS--GRILIDGTDiRTvtR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQDDMLL------------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltalgllpcantRTGS 216
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFnrsiednirvgrPDATDEEmraaAERAQAHDFIERKPDGYDTVVGE-------------RGRQ 471
|
170 180 190
....*....|....*....|....*....|....
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 250
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
77-294 |
4.12e-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: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSvpegpwWKKKGYKT--LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyrETG-MKGAVLINGmprdlr 153
Cdd:cd03250 1 ISVEDASFT------WDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPG------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 cfrKVScyimqddmllphLTVQEAMMVSAHLK-----LQEKDEgrrEMVKEILTAlgllpCA------------NTRTG- 215
Cdd:cd03250 67 ---SIA------------YVSQEPWIQNGTIRenilfGKPFDE---ERYEKVIKA-----CAlepdleilpdgdLTEIGe 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 216 ---SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA-------SCFQvvslmkGLAQGGRSIVCTIHQPSakLFELFD 285
Cdd:cd03250 124 kgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvgrhifeNCIL------GLLLNNKTRILVTHQLQ--LLPHAD 195
|
....*....
gi 13487145 286 QLYVLSQGQ 294
Cdd:cd03250 196 QIVVLDNGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
101-304 |
1.90e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMPrdlrCFR-------KVSCYIM-QDDMLLPHL 172
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNP----CARltpakahQLGIYLVpQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAMMvsahLKLQeKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 252
Cdd:PRK15439 102 SVKENIL----FGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 253 FQVVSLMKGLAQGGRSIVCTIHqpsaKLFE---LFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISH----KLPEirqLADRISVMRDGTIALSGKTADL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
98-299 |
3.45e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRET-----GMKGAVLING---MPRDLRCFRKVSCYIMQDDMLL 169
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskiKVDGKVLYFGkdiFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 PHLTVQE--AMMVSAHlKLQEKDEGRReMVKEILTALGLLPCANTRTGS----LSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:PRK14246 103 PHLSIYDniAYPLKSH-GIKEKREIKK-IVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 244 TSGLDSASCFQVVSLMKGLaQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRG 299
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQ-QVARVADYVAFLYNGELVEWG 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
77-248 |
3.49e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEGP----------WWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagyreTGM----K 140
Cdd:COG4586 2 IEVENLSktYRVYEKEpglkgalkglFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML-----TGIlvptS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 141 GAVLINGM-P-RDLRCFRK---VscyIM-QDDMLLPHLTVQEAMMVSAHL-KLQEKD-EGRREMVKEILTALGLLpcaNT 212
Cdd:COG4586 77 GEVRVLGYvPfKRRKEFARrigV---VFgQRSQLWWDLPAIDSFRLLKAIyRIPDAEyKKRLDELVELLDLGELL---DT 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 13487145 213 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
77-274 |
3.82e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLM---NIL----------AGYR---ETGMK 140
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKG----LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALlkpssgtitiAGYHitpETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 141 GAvlingmpRDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLP-CANTRTGSLSG 219
Cdd:PRK13641 79 NL-------KKLR--KKVSLVFQFPEAQLFENTVLKDVEFGP-KNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 220 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
96-274 |
4.43e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLING------MPRDLRCFRKVSCYIMQDDMLL 169
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 PHLTVQEAMMVSAHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*
gi 13487145 250 ASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
76-251 |
4.53e-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: 74.84 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 76 NIEFKDLS--YSvPEGPWwkkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP---- 149
Cdd:cd03244 2 DIEFKNVSlrYR-PNLPP--------VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-SSGSILIDGVDiski 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 --RDLRcfRKVSCyIMQDDMLL---------PHLTVQEAMMVSA----HLKlqekdegrrEMVKEILTALGLLPCANtrT 214
Cdd:cd03244 72 glHDLR--SRISI-IPQDPVLFsgtirsnldPFGEYSDEELWQAlervGLK---------EFVESLPGGLDTVVEEG--G 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 13487145 215 GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
72-299 |
6.29e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.14 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 72 RAAVNIEFKDLSYSVP--EGPwwkkkgyktLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGmp 149
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPgkEVP---------ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI-DEGEILLDG-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRcfrkvscyimqdDMLLPHLTVQEAMmVSAHLKL-----------QEKDEGRREmvkEILTAL-------------- 204
Cdd:PRK11176 405 HDLR------------DYTLASLRNQVAL-VSQNVHLfndtianniayARTEQYSRE---QIEEAArmayamdfinkmdn 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 205 GLlpcaNTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLaQGGRSIVCTIHQPSAkl 280
Cdd:PRK11176 469 GL----DTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST-- 541
|
250
....*....|....*....
gi 13487145 281 FELFDQLYVLSQGQCVYRG 299
Cdd:PRK11176 542 IEKADEILVVEDGEIVERG 560
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
77-316 |
6.42e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGMKGAVLINGMPR---- 150
Cdd:PRK13640 6 VEFKHVSFTYPDSK-------KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGITLtakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 --DLRcfRKVSCYIMQDDMLLPHLTVQEAMMvsahLKLQEKDEGRREMVK---EILTALGLLPCANTRTGSLSGGQRKRL 225
Cdd:PRK13640 79 vwDIR--EKVGIVFQNPDNQFVGATVGDDVA----FGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 226 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHQPSAKlfELFDQLYVLSQGQCVYRG---KV 301
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGspvEI 230
|
250
....*....|....*
gi 13487145 302 SNLVPYLRDLGLNCP 316
Cdd:PRK13640 231 FSKVEMLKEIGLDIP 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
66-299 |
7.55e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 66 FSSLPRRAavnieFKDLSYSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLI 145
Cdd:PRK10070 14 FGEHPQRA-----FKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 146 NGMP---------RDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGS 216
Cdd:PRK10070 88 DGVDiakisdaelREVR--RKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEE-RREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKGLAQGGRSIVCTIHQPSAKLfELFDQLYVLSQGQC 295
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEV 243
|
....
gi 13487145 296 VYRG 299
Cdd:PRK10070 244 VQVG 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
101-296 |
1.05e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLINGmpRDL------RCFRKVSCYIMQDDMLLPHLT 173
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpRAT--SGRIVFDG--KDItdwqtaKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 174 VQEAMMVSAHLKLQEKDEGRREMVKEILTALglLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 253
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13487145 254 QVVSLMKGLAQGGRSIVcTIHQPSAKLFELFDQLYVLSQGQCV 296
Cdd:PRK11614 175 QIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
77-262 |
1.11e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDL--SYSVPEG---PWWKKKGYKTLlKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMK----GAVLIN 146
Cdd:PRK15079 9 LEVADLkvHFDIKDGkqwFWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEvawlGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 GMPRDLRCFRKVSCYIMQDDM--LLPHLTVQEAM---MVSAHLKLQeKDEgRREMVKEILTALGLLP-CANTRTGSLSGG 220
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLasLNPRMTIGEIIaepLRTYHPKLS-RQE-VKDRVKAMMLKVGLLPnLINRYPHEFSGG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13487145 221 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL 262
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
99-274 |
1.98e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 99 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMPRDLRCFRKVSCYIMQD---DMLLPHLTVQ 175
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVS-AHLKLQEKDEGR-REMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 253
Cdd:PRK15056 100 VVMMGRyGHMGWLRRAKKRdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|.
gi 13487145 254 QVVSLMKGLAQGGRSIVCTIH 274
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTH 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
99-299 |
2.25e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 99 TLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY---------------RETGMKGAVLINGMPRDLRCF---RKVSC 160
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyiGDKKNNHELITNPYSKKIKNFkelRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 161 YIMQ-DDMLLPHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGL-LPCANTRTGSLSGGQRKRLAIALELVNNPPVM 238
Cdd:PRK13631 120 MVFQfPEYQLFKDTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 239 FFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQpSAKLFELFDQLYVLSQGQCVYRG 299
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
104-300 |
2.61e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 104 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYreTGMKGAVLINGmpRDLRCFR-----KVSCYIMQDDMLLPHLTVQEAM 178
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGSGSIQFAG--QPLEAWSaaelaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 179 MVSAHLKLQEKDEgrREMVKEILTALGLLPCANTRTGSLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSAs 251
Cdd:PRK03695 91 TLHQPDKTRTEAV--ASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVA- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13487145 252 cfQVV---SLMKGLAQGGRSIVCTIHQPSAKLFELfDQLYVLSQGQCVYRGK 300
Cdd:PRK03695 168 --QQAaldRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGR 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
98-304 |
2.87e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNIL-------AGYRETGmkgAVLINGMP----RDLRCFRKVSCYIMQDD 166
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 MLLPHLTVQEAMM-VSAHlKLQEKDEgRREMVKEILTALGLLPCANTRTGS----LSGGQRKRLAIALELVNNPPVMFFD 241
Cdd:PRK14271 111 NPFPMSIMDNVLAgVRAH-KLVPRKE-FRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 242 EPTSGLDSASCFQVVSLMKGLAQggRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
77-329 |
4.67e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKkkgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGMP---RDLR 153
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQD-DMLLPHLTVQ-------EAMMVSaHLKLQEKdegrremVKEILTALGLLPCANTRTGSLSGGQRKRL 225
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVKydvafglENHAVP-YDEMHRR-------VSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 226 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELfDQLYVLSQGQCVYRGK---VS 302
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTpteIF 230
|
250 260
....*....|....*....|....*..
gi 13487145 303 NLVPYLRDLGLNCPtyhnpadFVMEVA 329
Cdd:PRK13648 231 DHAEELTRIGLDLP-------FPIKIN 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
77-318 |
6.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP------- 149
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKA----LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGVDitdkkvk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 -RDLRcfRKVSCYIMQDDMLLPHLTVQEAMMVS-AHLKLQEKDEGRRemVKEILTALGLlPCANTRTGS---LSGGQRKR 224
Cdd:PRK13637 78 lSDIR--KKVGLVFQYPEYQLFEETIEKDIAFGpINLGLSEEEIENR--VKRAMNIVGL-DYEDYKDKSpfeLSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 225 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGK---V 301
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTpreV 232
|
250
....*....|....*....
gi 13487145 302 SNLVPYLRDLGLNCP--TY 318
Cdd:PRK13637 233 FKEVETLESIGLAVPqvTY 251
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
101-311 |
1.23e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.36 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMPRDLRCFRKVSC---YIMQD--DMLLPHLTVQ 175
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYSYRSQrirMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVSAHLKLQEKDEGRREMVKEILTALGLLP-CANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 254
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 255 VVSLMKGL--AQGGRSIVCTIHQPSAKlfELFDQLYVLSQGQCVYRGKVSN-LVPYLRDL 311
Cdd:PRK15112 188 LINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERGSTADvLASPLHEL 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-294 |
1.56e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGMP------RDLRcfRKVSCYIMQDDMLLPHLT 173
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEElqasniRDTE--RAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 174 VQEAMMVSAhlklqEKDEGRR----EMV---KEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:PRK13549 99 VLENIFLGN-----EITPGGImdydAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13487145 247 LDSASCFQVVSLMKGLAQGGrsIVCT-IhqpSAKLFELF---DQLYVLSQGQ 294
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHG--IACIyI---SHKLNEVKaisDTICVIRDGR 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
56-307 |
1.57e-13 |
|
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: 74.01 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 56 VDNNFTEAQRFSSLPRRAAvNIEFKDLSYSVpegpwwkkkGY-KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY 134
Cdd:TIGR01193 454 VDSEFINKKKRTELNNLNG-DIVINDVSYSY---------GYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 135 RETGmKGAVLINGMPR---DLRCFRKVSCYIMQDDMLLPHlTVQEAMMVSAHLKLQEKDEGRREMVKEILT-----ALGL 206
Cdd:TIGR01193 524 FQAR-SGEILLNGFSLkdiDRHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDdienmPLGY 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 207 LPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQggRSIVCTIHQPSakLFELFDQ 286
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDK 677
|
250 260
....*....|....*....|.
gi 13487145 287 LYVLSQGQCVYRGKVSNLVPY 307
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
96-277 |
1.68e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMN----ILAGYRETGMKGAVLINGM--------PRDLRcfRKVScYIM 163
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGRniyspdvdPIEVR--REVG-MVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 164 QDDMLLPHLTVQEAmmVSAHLKLQEKDEGRREMVKEILTALGLLPC-------ANTRTGSLSGGQRKRLAIALELVNNPP 236
Cdd:PRK14267 92 QYPNPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13487145 237 VMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIHQPS 277
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
96-293 |
1.70e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM------PRDlrcfRKVScYIMQDDMLL 169
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 PHLTVQEAmmVSAHLKLQEKDEgR------REMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:PRK10851 87 RHMTVFDN--IAFGLTVLPRRE-RpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 244 TSGLDSascfQV-VSLMKGLAQGGR-----SIVCTIHQPSAklFELFDQLYVLSQG 293
Cdd:PRK10851 164 FGALDA----QVrKELRRWLRQLHEelkftSVFVTHDQEEA--MEVADRVVVMSQG 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
77-300 |
1.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGMP------- 149
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDTLitstskn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDEGRreMVKEILTALGLLPCANTRTG-SLSGGQRKRLA 226
Cdd:PRK13649 78 KDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEA--LAREKLALVGISESLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRGK 300
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGK 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
77-252 |
3.46e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.09 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVpegpwwkkkGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgmkgavlINGMPRDLRCFR 156
Cdd:cd03221 1 IELENLSKTY---------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP-------DEGIVTWGSTVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 kvSCYIMQddmllphltvqeammvsahlklqekdegrremvkeiltalgllpcantrtgsLSGGQRKRLAIALELVNNPP 236
Cdd:cd03221 65 --IGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170
....*....|....*.
gi 13487145 237 VMFFDEPTSGLDSASC 252
Cdd:cd03221 91 LLLLDEPTNHLDLESI 106
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
101-264 |
4.04e-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: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTL------MNILagYRETGMKGAVLINGM--------PRDLRcfRKVScYIMQDD 166
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDL--IPGARVEGEILLDGEdiydpdvdVVELR--RRVG-MVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 MLLPHlTVQEAmmVSAHLKLQE-KDegRREM---VKEILTALGL-------LpcaNTRTGSLSGGQRKRLAIALELVNNP 235
Cdd:COG1117 102 NPFPK-SIYDN--VAYGLRLHGiKS--KSELdeiVEESLRKAALwdevkdrL---KKSALGLSGGQQQRLCIARALAVEP 173
|
170 180
....*....|....*....|....*....
gi 13487145 236 PVMFFDEPTSGLDSASCFQVVSLMKGLAQ 264
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKK 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
93-296 |
4.05e-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: 72.16 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLINGMP------RDLRcfRKVSCYIMQD 165
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPlkasniRDTE--RAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHLTVQEAMMVSAHLKLQEKDEGRREMV---KEILTALGLLPCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFD 241
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEITLPGGRMAYNAMYlraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 242 EPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHqpsaKLFE---LFDQLYVLSQGQCV 296
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
102-294 |
4.50e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 102 KGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKGAVLINGM---PRD-LRCFRKVSCYIMQ---DDMLLPHLTV 174
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRSpLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 175 QEAMMVSAHLKL----------QEKDEGR-REMVKEILTalglLPCA--NTRTGSLSGGQRKRLAIALELVNNPPVMFFD 241
Cdd:PRK09700 359 AQNMAISRSLKDggykgamglfHEVDEQRtAENQRELLA----LKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 242 EPTSGLDSASCFQVVSLMKGLAQGGRSIVCTihqpSAKLFELF---DQLYVLSQGQ 294
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
77-311 |
5.64e-13 |
|
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: 71.64 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKS-TLMNI--LAGYRETGMKGAVLINGM----- 148
Cdd:COG4172 7 LSVEDLSVAFGQG-----GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 -PRDLRCFR--KVSCyIMQDDM--LLPHLTV--QEAMMVSAHLKLQEKDegRREMVKEILTALGLlPCANTRTGS----L 217
Cdd:COG4172 82 sERELRRIRgnRIAM-IFQEPMtsLNPLHTIgkQIAEVLRLHRGLSGAA--ARARALELLERVGI-PDPERRLDAyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 218 SGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMKGL-AQGGRSIvctihqpsakLF---------ELF 284
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDvtvQA---QILDLLKDLqRELGMAL----------LLithdlgvvrRFA 224
|
250 260 270
....*....|....*....|....*....|..
gi 13487145 285 DQLYVLSQGQCVYRGKVSNLV-----PYLRDL 311
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFaapqhPYTRKL 256
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
77-316 |
6.05e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.66 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMPR----- 150
Cdd:PRK13635 6 IRVEHISFRYPDAA-------TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPE--AGTITVGGMVLseetv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 -DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREMVKEILTAL---GLLPCANTRTGSLSGGQRKRLA 226
Cdd:PRK13635 77 wDVR--RQVGMVFQNPDNQFVGATVQDDVAFG----LENIGVPREEMVERVDQALrqvGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTI-H--QPSAKLfelfDQLYVLSQGQCVYRG---K 300
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSItHdlDEAAQA----DRVIVMNKGEILEEGtpeE 226
|
250
....*....|....*.
gi 13487145 301 VSNLVPYLRDLGLNCP 316
Cdd:PRK13635 227 IFKSGHMLQEIGLDVP 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
84-264 |
6.79e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.38 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 84 YSVPEGPWwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgYRETGMKGAVLINGMP---------RDLRc 154
Cdd:PRK11308 15 YPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPTGGELYYQGQDllkadpeaqKLLR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 fRKVScYIMQDDM--LLPHLTV----QEAMMVSAHLKLQEkdegRREMVKEILTALGLLPCANTRTGSL-SGGQRKRLAI 227
Cdd:PRK11308 92 -QKIQ-IVFQNPYgsLNPRKKVgqilEEPLLINTSLSAAE----RREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAI 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 264
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
110-274 |
9.55e-13 |
|
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: 68.55 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 110 SGELVAIMGPSGAGKSTLMNILAGyretGMKGAVLINGMPRD----LRCFR--KVSCYI--MQDDMLLPHLTVQEAMMVS 181
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG----KLKPNLGKFDDPPDwdeiLDEFRgsELQNYFtkLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 182 AHLK------LQEKDEgrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 255
Cdd:cd03236 101 KAVKgkvgelLKKKDE--RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170
....*....|....*....
gi 13487145 256 VSLMKGLAQGGRSIVCTIH 274
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEH 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
96-321 |
1.03e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYReTGMKGAVLINGMPRDLRCFRKVSCYI---MQDDMLLPHL 172
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIgllAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 TVQEAMMVSAH------LKLQEKDEgrrEMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:PRK10253 97 TVQELVARGRYphqplfTRWRKEDE---EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 247 LDSASCFQVVSLMKGL-AQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRGKVSNLV-PYL--RDLGLNCPTYHNP 321
Cdd:PRK10253 174 LDISHQIDLLELLSELnREKGYTLAAVLHDLN-QACRYASHLIALREGKIVAQGAPKEIVtAELieRIYGLRCMIIDDP 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
77-343 |
1.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSV-PEGPWWKKKgyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE----TGMKGAVLINGMPR- 150
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASRA-----LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQptegKVTVGDIVVSSTSKq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 -DLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQeKDEGRReMVKEILTALGLLPCANTRTG-SLSGGQRKRLA 226
Cdd:PRK13643 77 kEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIP-KEKAEK-IAAEKLEMVGLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRGKVSNL-- 304
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVfq 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 13487145 305 -VPYLRDLGLNCPTYHNPADFVMEvaSGEYGDQNSRLVRA 343
Cdd:PRK13643 234 eVDFLKAHELGVPKATHFADQLQK--TGAVTFEKLPITRA 271
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
77-294 |
1.12e-12 |
|
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: 67.94 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEGPWWKKK-----------GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGA 142
Cdd:cd03220 1 IELENVSksYPTYKGGSSSLKklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 143 VLINGmprdlrcfrKVSCYIMQDDMLLPHLTVQE-AMMVSAHLKLQEKDegRREMVKEILTALGLLPCANTRTGSLSGGQ 221
Cdd:cd03220 79 VTVRG---------RVSSLLGLGGGFNPELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 222 RKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVLSQGQ 294
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGK 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
104-294 |
1.16e-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: 70.62 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 104 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLR----CFRKVSCYIMQD---DMLLPHLTVQE 176
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnpaqAIRAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHLKL---------QEKDEGRREMVK-EILTALGLLPcantrTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:TIGR02633 359 NITLSVLKSFcfkmridaaAELQIIGSAIQRlKVKTASPFLP-----IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13487145 247 LDSASCFQVVSLMKGLAQGGRSIVcTIHQPSAKLFELFDQLYVLSQGQ 294
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
77-294 |
1.27e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLingMPRDLRCfr 156
Cdd:COG4178 363 LALEDLTLRTPDG--------RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIA---RPAGARV-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 kvscyimqddMLLPhltvQEAMMVSAHLKLQ-----EKDEGRREMVKEILTALGLLPCAN--------TRTgsLSGGQRK 223
Cdd:COG4178 429 ----------LFLP----QRPYLPLGTLREAllypaTAEAFSDAELREALEAVGLGHLAErldeeadwDQV--LSLGEQQ 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 224 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGrSIVCTIHQPSakLFELFDQLYVLSQGQ 294
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRST--LAAFHDRVLELTGDG 560
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
101-294 |
1.53e-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: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDLRCFRKVscyIMQDDMLLPhltvqeammv 180
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDA---IRAGIAYVP---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 181 sahlklqekdEGRREMvkeiltalGLLPCANTR-----TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 255
Cdd:cd03215 82 ----------EDRKRE--------GLVLDLSVAenialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13487145 256 VSLMKGLAQGGRSIVCTihqpSAKLFELF---DQLYVLSQGQ 294
Cdd:cd03215 144 YRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEGR 181
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
77-299 |
1.59e-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: 70.62 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYsvpegpwwkkkGY---KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGmpRDL 152
Cdd:COG5265 358 VRFENVSF-----------GYdpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfYDVTS--GRILIDG--QDI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 R-----CFRKVSCYIMQDDMLL------------PHLT---VQEAMMvSAHL-----KLQEKDE---GRRemvkeiltal 204
Cdd:COG5265 423 RdvtqaSLRAAIGIVPQDTVLFndtiayniaygrPDASeeeVEAAAR-AAQIhdfieSLPDGYDtrvGER---------- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 205 GLlpcantrtgSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVctI-HQPS----Ak 279
Cdd:COG5265 492 GL---------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV--IaHRLStivdA- 559
|
250 260
....*....|....*....|
gi 13487145 280 lfelfDQLYVLSQGQCVYRG 299
Cdd:COG5265 560 -----DEILVLEAGRIVERG 574
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
77-316 |
1.64e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.65 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMP------- 149
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQA----IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP-TTGTVTVDDITithktkd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKL---QEKDEGRRemvkeILTALGLlpCANTRTGS---LSGGQ 221
Cdd:PRK13646 78 KYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnldEVKNYAHR-----LLMDLGF--SRDVMSQSpfqMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 222 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRGK 300
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTS 229
|
250
....*....|....*....
gi 13487145 301 VSNLV---PYLRDLGLNCP 316
Cdd:PRK13646 230 PKELFkdkKKLADWHIGLP 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
110-270 |
2.89e-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: 69.81 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 110 SGELVAIMGPSGAGKSTLMNILAG---------------------YRETGMKG--AVLINGmprDLRCFRKVScYImqdD 166
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrFRGTELQDyfKKLANG---EIKVAHKPQ-YV---D 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 MLLPHL--TVQEammvsahlkLQEK-DEgrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:COG1245 171 LIPKVFkgTVRE---------LLEKvDE--RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180
....*....|....*....|....*..
gi 13487145 244 TSGLDSASCFQVVSLMKGLAQGGRSIV 270
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
96-264 |
3.18e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.11 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTL------MNILAgyRETGMKGAVLINGM----PR-DLRCFRKVSCYIMQ 164
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGHniysPRtDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 165 DDMLLPhLTVQEAMMVSAHLKlQEKDEGRR--------------EMVKEIL--TALGLlpcantrtgslSGGQRKRLAIA 228
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLK-GIKDKQVLdeavekslkgasiwDEVKDRLhdSALGL-----------SGGQQQRVCIA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ 264
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
77-301 |
4.12e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.64 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSVPEGPW-----------WKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGA 142
Cdd:COG1134 5 IEVENVSksYRLYHEPSrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--SGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 143 VLINGmprdlrcfrKVSCyimqddmLL-------PHLTVQE-AMMVSAHLKLQEKDEgrREMVKEIL--TALGllPCANT 212
Cdd:COG1134 83 VEVNG---------RVSA-------LLelgagfhPELTGREnIYLNGRLLGLSRKEI--DEKFDEIVefAELG--DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 213 RTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSLMKGLAQGGRSIVCTIHQPSAkLFELFDQLYVL 290
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWL 219
|
250
....*....|.
gi 13487145 291 SQGQCVYRGKV 301
Cdd:COG1134 220 EKGRLVMDGDP 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
77-304 |
5.93e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSvpegpwwkkKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLING-----MPRD 151
Cdd:PRK11831 8 VDMRGVSFT---------RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipaMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 152 -LRCFRKVSCYIMQDDMLLPHLTVQE--AMMVSAHLKLQEKDEGRREMVKeiLTALGLLPCANTRTGSLSGGQRKRLAIA 228
Cdd:PRK11831 78 rLYTVRKRMSMLFQSGALFTDMNVFDnvAYPLREHTQLPAPLLHSTVMMK--LEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL--AQGGRSIVCTIHQPsaKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVP--EVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
77-291 |
6.25e-12 |
|
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: 64.10 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVlinGMPRDlrcfr 156
Cdd:cd03223 1 IELENLSLATPDG--------RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 157 kvscyimQDDMLLPhltvQEAMMVSAHLklqekdegrremvKEILtalgLLPCANTrtgsLSGGQRKRLAIALELVNNPP 236
Cdd:cd03223 64 -------EDLLFLP----QRPYLPLGTL-------------REQL----IYPWDDV----LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 237 VMFFDEPTSGLDSASCFQVVSLMKGLaqggRSIVCTI-HQPSakLFELFDQLYVLS 291
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL----GITVISVgHRPS--LWKFHDRVLDLD 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
77-302 |
6.77e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMKGAVLING-----MPR 150
Cdd:CHL00131 8 LEIKNLHASVNE---------NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGesildLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRCFRKVsCYIMQDDMLLPHLTVQEAMMVS--AHLKLQEKDEGRR----EMVKEILTALGLLPCANTR--TGSLSGGQR 222
Cdd:CHL00131 79 EERAHLGI-FLAFQYPIEIPGVSNADFLRLAynSKRKFQGLPELDPleflEIINEKLKLVGMDPSFLSRnvNEGFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 223 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPsaKLFELF--DQLYVLSQGQCVYRGK 300
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGD 235
|
..
gi 13487145 301 VS 302
Cdd:CHL00131 236 AE 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
77-274 |
1.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEG-PWwkkkgYKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNIL----AGYRE-----------T 137
Cdd:PRK13651 3 IKVKNIVKIFNKKlPT-----ELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdTGTIEwifkdeknkkkT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 138 GMKGAVLIN---GMPR--------DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRrEMVKEILTALGL 206
Cdd:PRK13651 78 KEKEKVLEKlviQKTRfkkikkikEIR--RRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAK-KRAAKYIELVGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 207 LPCANTRTG-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:PRK13651 155 DESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
77-316 |
1.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTL---MNILAgyreTGMKGAVLINGM----P 149
Cdd:PRK13633 5 IKCKNVSYKYESN---EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL----IPSEGKVYVDGLdtsdE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRCFRKVSCYIMQ--DDMLLPHLTVQEAMMVSAHLKLQEKDegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:PRK13633 78 ENLWDIRNKAGMVFQnpDNQIVATIVEEDVAFGPENLGIPPEE--IRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIH--QPSAKLfelfDQLYVLSQGQCVYRG---KV 301
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGtpkEI 231
|
250
....*....|....*
gi 13487145 302 SNLVPYLRDLGLNCP 316
Cdd:PRK13633 232 FKEVEMMKKIGLDVP 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
109-262 |
1.80e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 109 NSGELVAIMGPSGAGKS----TLMNILAGYRETGmkGAVLING-----MP-RDLRCFR--KVScYIMQDDM--LLPHLTV 174
Cdd:PRK09473 40 RAGETLGIVGESGSGKSqtafALMGLLAANGRIG--GSATFNGreilnLPeKELNKLRaeQIS-MIFQDPMtsLNPYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 175 QEAMMVSAHL-KLQEKDEGRREMVKeILTALGLlPCANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:PRK09473 117 GEQLMEVLMLhKGMSKAEAFEESVR-MLDAVKM-PEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170
....*....|...
gi 13487145 250 ASCFQVVSLMKGL 262
Cdd:PRK09473 195 TVQAQIMTLLNEL 207
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
450-664 |
1.85e-11 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 63.68 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 450 MLFLMFAALMPTVLTFplemsVFLREH--LNYWY----SLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFV 523
Cdd:COG0842 11 AMSLLFTALMLTALSI-----AREREQgtLERLLvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 524 LFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVILSIYG 603
Cdd:COG0842 86 LLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 604 ldredlhcdiaetchfqkseailrelDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRA 664
Cdd:COG0842 166 --------------------------GAGLADVWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
111-259 |
2.55e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGM------PRDLRCFRKVSCYIMQDDM--LLPHLTVQEAMM--V 180
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMepL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 181 SAHLKLQEKDEGRRemVKEILTALGLLPCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 259
Cdd:PRK10261 429 RVHGLLPGKAAAAR--VAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
77-317 |
2.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPWWKKKGyktlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETgmKGAVLI-------NGM 148
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRA----LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPT--SGTVTIgervitaGKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 149 PRDLRCFRKVSCYIMQddmlLP-HLTVQEAMmvsahlklqEKD------------EGRREMVKEILTALGLLPCANTRTG 215
Cdd:PRK13634 77 NKKLKPLRKKVGIVFQ----FPeHQLFEETV---------EKDicfgpmnfgvseEDAKQKAREMIELVGLPEELLARSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 216 -SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQ-GGRSIVCTIHQ--PSAKlfeLFDQLYVLS 291
Cdd:PRK13634 144 fELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSmeDAAR---YADQIVVMH 220
|
250 260
....*....|....*....|....*....
gi 13487145 292 QGQCVYRGKVSNL---VPYLRDLGLNCPT 317
Cdd:PRK13634 221 KGTVFLQGTPREIfadPDELEAIGLDLPE 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
109-248 |
3.23e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 109 NSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLklqe 188
Cdd:PRK13543 35 DAGEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 189 kdEGRR--EMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK13543 110 --HGRRakQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
101-270 |
3.48e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--REtgmKGAVLINGMPRDLRC----FRKVSCYIMQD---DMLLPH 171
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAlpRT---SGYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSA-------HLKLQEKDEgrREMVKEILTALGL-LPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:PRK10762 345 MSVKENMSLTAlryfsraGGSLKHADE--QQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180
....*....|....*....|....*..
gi 13487145 244 TSGLDSASCFQVVSLMKGLAQGGRSIV 270
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
100-275 |
3.76e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 100 LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLING--MPRDLRCFRKVSCYIMQDDMLLPHLTVQE 176
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERqsIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMMVSAHLklQEKDEGRREMVKeiLTALGLL---PCantrtGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 253
Cdd:PRK13540 94 NCLYDIHF--SPGAVGITELCR--LFSLEHLidyPC-----GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 13487145 254 QVVSLMKGLAQGGRSIVCTIHQ 275
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
100-304 |
4.06e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.95 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 100 LLKGISGKFNSGELVAIMGPSGAGKS----TLMNIL-AGYRETGmkGAVLINGMP---RDLRCfRKVSCyIMQDdmllPH 171
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGKPvapCALRG-RKIAT-IMQN----PR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSAHLK---LQEKDEGRREMVKEILTALGLlpcANTRT------GSLSGGQRKRLAIALELVNNPPVMFFDE 242
Cdd:PRK10418 90 SAFNPLHTMHTHARetcLALGKPADDATLTAALEAVGL---ENAARvlklypFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 243 PTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDVETL 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
111-299 |
4.19e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLingmprdlrcfrkvscYIMQDDMLLPHLTVQEA------------- 177
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSA-RLAPDAGEVH----------------YRMRDGQLRDLYALSEAerrrllrtewgfv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 178 ---------MMVSAhlklqekdeGRRemVKEILTALGLLPCANTRT--------------------GSLSGGQRKRLAIA 228
Cdd:PRK11701 95 hqhprdglrMQVSA---------GGN--IGERLMAVGARHYGDIRAtagdwlerveidaariddlpTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 229 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGL-AQGGRSIVCTIHQPS-AKLfeLFDQLYVLSQGQCVYRG 299
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAvARL--LAHRLLVMKQGRVVESG 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
111-274 |
4.28e-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: 66.58 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING--MPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQE 188
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGksILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 189 KDEGRReMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRS 268
Cdd:TIGR01257 2044 AEEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRA 2122
|
....*.
gi 13487145 269 IVCTIH 274
Cdd:TIGR01257 2123 VVLTSH 2128
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
77-251 |
4.66e-11 |
|
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: 62.81 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLS--YSvPEGPwwkkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLmnILAGYRET-GMKGAVLINGMP---- 149
Cdd:cd03369 7 IEVENLSvrYA-PDLP--------PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDisti 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 --RDLRcfRKVSCyIMQDDMLLphltvqeamMVSAHLKLQEKDEGRREmvkEILTALGLlpcanTRTGS-LSGGQRKRLA 226
Cdd:cd03369 76 plEDLR--SSLTI-IPQDPTLF---------SGTIRSNLDPFDEYSDE---EIYGALRV-----SEGGLnLSQGQRQLLC 135
|
170 180
....*....|....*....|....*
gi 13487145 227 IALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYAT 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
98-251 |
7.39e-11 |
|
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: 64.96 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYrETGMKG-AVLINGMprdlrcfrKVScYIMQDDMLLPHLTVQE 176
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGeARPQPGI--------KVG-YLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMM--VSAHLKLQEK---------------DEGRREMVK--EILTALGL---------------LPCANTRTGSLSGGQR 222
Cdd:TIGR03719 88 NVEegVAEIKDALDRfneisakyaepdadfDKLAAEQAElqEIIDAADAwdldsqleiamdalrCPPWDADVTKLSGGER 167
|
170 180
....*....|....*....|....*....
gi 13487145 223 KRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
111-304 |
7.90e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAG-Y-RETG----MKGAVLINGmPRDlrcfrkvS-----CYIMQDDMLLPHLTVQEAMM 179
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGiYtRDAGsilyLGKEVTFNG-PKS-------SqeagiGIIHQELNLIPQLTIAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 180 VsahlklqekdeGR-----------REMVKE---ILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:PRK10762 102 L-----------GRefvnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 246 GL---DSASCFQVVSLMKglAQgGRSIVCTIHQpSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK10762 171 ALtdtETESLFRVIRELK--SQ-GRGIVYISHR-LKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
92-320 |
8.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 92 WKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPR------DLRcfRKVSCYIMQD 165
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLtaenvwNLR--RKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHLTVQEAMMvsahLKLQEKDEGRREMVK---EILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDE 242
Cdd:PRK13642 91 DNQFVGATVEDDVA----FGMENQGIPREEMIKrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 243 PTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFElFDQLYVLSQGQCVYRGKVSNLVPYLRDL---GLNCPTYH 319
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMveiGLDVPFSS 245
|
.
gi 13487145 320 N 320
Cdd:PRK13642 246 N 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
70-248 |
1.20e-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: 64.57 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 70 PRRAAVNIEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGMP 149
Cdd:TIGR03719 316 PRLGDKVIEAENLT---------KAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTIEIGETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 rdlrcfrKVSCYIMQDDMLLPHLTVQEAmmVSA---HLKLqekdeGRREMvkeiltalgllpcaNTRT------------ 214
Cdd:TIGR03719 386 -------KLAYVDQSRDALDPNKTVWEE--ISGgldIIKL-----GKREI--------------PSRAyvgrfnfkgsdq 437
|
170 180 190
....*....|....*....|....*....|....*...
gi 13487145 215 ----GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:TIGR03719 438 qkkvGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
179-304 |
1.22e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.60 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 179 MVSAHLKLQEKDEgrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 258
Cdd:NF000106 109 MIGR*LDLSRKDA--RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 13487145 259 MKGLAQGGRSIVCTIhQPSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
111-265 |
1.59e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAG--------YRETGMKGAV---------------LINGmprDLRCFRKVScYImqdDm 167
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVlkrfrgtelqnyfkkLYNG---EIKVVHKPQ-YV---D- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHL---TVQEAmmvsahlkLQEKDEgrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 244
Cdd:PRK13409 171 LIPKVfkgKVREL--------LKKVDE--RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180
....*....|....*....|.
gi 13487145 245 SGLDSASCFQVVSLMKGLAQG 265
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEG 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
101-311 |
1.80e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKS----TLMNILAGYRETGMKGAVLINGMPRDLRCFRKVSCYIMQD----DM----- 167
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 -----LLPHLTVQEAMMVSAHLklqEKDEGRREMVKEILTALGL--LPCANTRTG----SLSGGQRKRLAIALELVNNPP 236
Cdd:PRK10261 112 epmtsLNPVFTVGEQIAESIRL---HQGASREEAMVEAKRMLDQvrIPEAQTILSryphQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 237 VMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLV-----PYLRDL 311
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
98-248 |
1.94e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGMKGAVLIngmpRDLRCFRKVScyimqddmLLPHLtvqe 176
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVDV----PDNQFGREAS--------LIDAI---- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13487145 177 ammvsahLKLQEKDEgrremVKEILTALGLLPCANTRT--GSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:COG2401 107 -------GRKGDFKD-----AVELLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
101-296 |
2.11e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLINGMPRDLR----------CF----RKvscyimqD 165
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGaDPADS--GEIRLDGKPVRIRsprdairagiAYvpedRK-------G 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHLTVQEAMMVSAHLK------LQEKDEgrREMVKEILTALGL-LPCANTRTGSLSGG-QRKrLAIALELVNNPPV 237
Cdd:COG1129 339 EGLVLDLSIRENITLASLDRlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 238 MFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTihqpSAKLFELF---DQLYVLSQGQCV 296
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI----SSELPELLglsDRILVMREGRIV 473
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-323 |
2.32e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSvpegpwwkkkgYKT--LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAgyRETGMKGAVLINGMPR---- 150
Cdd:PRK14258 8 IKVNNLSFY-----------YDTqkILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 -------DLRCFRKVSCYIMQDDMLLPhLTVQEAM-----MVSAHLKLQEKDegrreMVKEILTALGLLPCANTRTGS-- 216
Cdd:PRK14258 75 niyerrvNLNRLRRQVSMVHPKPNLFP-MSVYDNVaygvkIVGWRPKLEIDD-----IVESALKDADLWDEIKHKIHKsa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 --LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLA-QGGRSIVCTIHQpsaklfelFDQLYVLSQG 293
Cdd:PRK14258 149 ldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDF 220
|
250 260 270
....*....|....*....|....*....|
gi 13487145 294 QCVYRGKvSNLVPYLRDLGLNCPTYHNPAD 323
Cdd:PRK14258 221 TAFFKGN-ENRIGQLVEFGLTKKIFNSPHD 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
111-248 |
2.83e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAG---------YRETGMKGAVLINGMPRD-------------------LRCFRKVSCYI 162
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGevllddgriIYEQDLIVARLQQDPPRNvegtvydfvaegieeqaeyLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 163 MQD--DMLLPHL-TVQEammVSAHLKLQEKDEgrreMVKEILTALGLLPcaNTRTGSLSGGQRKRLAIALELVNNPPVMF 239
Cdd:PRK11147 109 ETDpsEKNLNELaKLQE---QLDHHNLWQLEN----RINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*....
gi 13487145 240 FDEPTSGLD 248
Cdd:PRK11147 180 LDEPTNHLD 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
77-305 |
3.31e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSysvpegpwwKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLRC-- 154
Cdd:TIGR03269 1 IEVKNLT---------KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCgy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 155 -----FRKVSC-------------YIMQDDMLLPHLTVQEAMMVSAHLKLQEKD-----------EGRREMVKEILTALG 205
Cdd:TIGR03269 72 verpsKVGEPCpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDtvldnvlealeEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 206 LLPCANTR------TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS-LMKGLAQGGRSIVCTIHQPSA 278
Cdd:TIGR03269 152 LIEMVQLShrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 13487145 279 kLFELFDQLYVLSQGQCVYRGKVSNLV 305
Cdd:TIGR03269 232 -IEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
115-248 |
3.31e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 115 AIMGPSGAGKSTLMNILAGYrETGMKGAVLING-----------MPRDLRcfrKVScYIMQDDMLLPHLTVQeammvsAH 183
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGL-TRPQKGRIVLNGrvlfdaekgicLPPEKR---RIG-YVFQDARLFPHYKVR------GN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13487145 184 LK--LQEKDegrREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK11144 97 LRygMAKSM---VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
111-294 |
3.69e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLR-CFRKVS---CYIMQD---DMLLPHLTVQEAMMVSAH 183
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRnPQQAIAqgiAMVPEDrkrDGIVPVMGVGKNITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 184 LKL---------QEKDEGRREMVK-EILTALGLLPcantrTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 253
Cdd:PRK13549 368 DRFtggsriddaAELKTILESIQRlKVKTASPELA-----IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13487145 254 QVVSLMKGLAQGGRSIVCTihqpSAKLFE---LFDQLYVLSQGQ 294
Cdd:PRK13549 443 EIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGK 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
110-280 |
4.20e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.54 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 110 SGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGmprdlrcfrkvscyimqddmllphltvqeammvsahlklqek 189
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 190 degrrEMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMKGLA 263
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 13487145 264 QGGRSIVCTIHQPSAKL 280
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
77-312 |
6.23e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---YRETG----MKGAVLINGMP 149
Cdd:PRK09580 2 LSIKDLHVSVED---------KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTGgtveFKGKDLLELSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDlrcfRKVSCYIM--QDDMLLP----HLTVQEAmmVSAHLKLQEKDEGRR----EMVKEILTALGLLPCANTRTGSL-- 217
Cdd:PRK09580 73 ED----RAGEGIFMafQYPVEIPgvsnQFFLQTA--LNAVRSYRGQEPLDRfdfqDLMEEKIALLKMPEDLLTRSVNVgf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 218 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVY 297
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
250
....*....|....*
gi 13487145 298 RGKVSnLVPYLRDLG 312
Cdd:PRK09580 227 SGDFT-LVKQLEEQG 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
98-311 |
7.59e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKS-TLMNIL-----------AGyrETGMKGAVLINGMPRDLRCFR--KVScYIM 163
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSG--DIRFHGESLLHASEQTLRGVRgnKIA-MIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 164 QDDML----LPHLTVQEAMMVSAHLKLqekdegRREMVK-EILTALgllpcanTRTG-------------SLSGGQRKRL 225
Cdd:PRK15134 99 QEPMVslnpLHTLEKQLYEVLSLHRGM------RREAARgEILNCL-------DRVGirqaakrltdyphQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 226 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG-GRSIVCTIHQPSAkLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSI-VRKLADRVAVMQNGRCVEQNRAATL 244
|
250
....*....|..
gi 13487145 305 V-----PYLRDL 311
Cdd:PRK15134 245 FsapthPYTQKL 256
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
77-300 |
1.29e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDL---R 153
Cdd:PRK10790 341 IDIDNVSFAYRDD--------NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL-TEGEIRLDGRPLSSlshS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 154 CFRKVSCYIMQDDMLLphltvqeAMMVSAHLKLqekdeGR---REMVKEILTALGLLPCA-------NTRTG----SLSG 219
Cdd:PRK10790 412 VLRQGVAMVQQDPVVL-------ADTFLANVTL-----GRdisEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 220 GQRKRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVSLMKGLAQGGRSIVCTIHQPSAkLFELfDQLYVLSQGQCVYRG 299
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGT-EQAIQQALAAVREHTTLVVIAHRLST-IVEA-DTILVLHRGQAVEQG 556
|
.
gi 13487145 300 K 300
Cdd:PRK10790 557 T 557
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
78-294 |
1.97e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVPEGpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGM------PRD 151
Cdd:COG3845 259 EVENLSVRDDRG--------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-SGSIRLDGEditglsPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 152 LRCfRKVScYIMQDDM---LLPHLTVQEAMMVSAH----------LKLQEKDEGRREMVKE--ILTalgllPCANTRTGS 216
Cdd:COG3845 330 RRR-LGVA-YIPEDRLgrgLVPDMSVAENLILGRYrrppfsrggfLDRKAIRAFAEELIEEfdVRT-----PGPDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCtIhqpSAKLFELF---DQLYVLSQG 293
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL-I---SEDLDEILalsDRIAVMYEG 478
|
.
gi 13487145 294 Q 294
Cdd:COG3845 479 R 479
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
104-304 |
2.15e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 104 ISGKFNSGELVAIMGPSGAGKS----TLMNiLAGYRETGMKGAVLINGmpRDLRCF-----RKVS----CYIMQDDM--L 168
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMG-LIDYPGRVMAEKLEFNG--QDLQRIsekerRNLVgaevAMIFQDPMtsL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 169 LPHLTVQEAMMVSahLKLQE--KDEGRREMVKEILTALGLlPCANTRTG----SLSGGQRKRLAIALELVNNPPVMFFDE 242
Cdd:PRK11022 103 NPCYTVGFQIMEA--IKVHQggNKKTRRQRAIDLLNQVGI-PDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 243 PTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
98-251 |
2.54e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKG-AVLINGMprdlrcfrKVScYIMQDDMLLPHLTVQE 176
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGeARPAPGI--------KVG-YLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 177 AMM--VSAHLKLQEK---------------DEGRREMVK--EILTALGL---------------LPCANTRTGSLSGGQR 222
Cdd:PRK11819 90 NVEegVAEVKAALDRfneiyaayaepdadfDALAAEQGElqEIIDAADAwdldsqleiamdalrCPPWDAKVTKLSGGER 169
|
170 180
....*....|....*....|....*....
gi 13487145 223 KRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
101-301 |
3.00e-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: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNilagyretgmkgavlingmprdlRCFRKVSCYIMQDDmlLPHLTVQEAMMV 180
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------------EGLYASGKARLISF--LPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 181 SahlKLQEkdegrreMVKeilTALGLLPcANTRTGSLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSL 258
Cdd:cd03238 66 D---QLQF-------LID---VGLGYLT-LGQKLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13487145 259 MKGLAQGGRSIVCTIHQPsaKLFELFDQLYVLSQGQCVYRGKV 301
Cdd:cd03238 132 IKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGSGKSGGKV 172
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
101-275 |
3.01e-09 |
|
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: 57.73 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMPRDLRCF-------RKVSCYIMQDDMLLpHLT 173
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 174 VQEAMMVSAHLKLQekdegRREMVKEILTA---LGLLPCAN-TRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTS 245
Cdd:cd03290 95 VEENITFGSPFNKQ-----RYKAVTDACSLqpdIDLLPFGDqTEIGergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|...
gi 13487145 246 GLD---SASCFQvVSLMKGLAQGGRSIVCTIHQ 275
Cdd:cd03290 170 ALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
77-242 |
4.21e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGpwwkkkGYKtlLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETgmKGAVLINGMP---RDL 152
Cdd:PRK10522 323 LELRNVTFAYQDN------GFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 153 RCFRKVSCYIMQDDMLLPHLTVQEAMMVS--------AHLKLQEK---DEGRremvkeiltalgllpCANTRtgsLSGGQ 221
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPEGKPANpalvekwlERLKMAHKlelEDGR---------------ISNLK---LSKGQ 454
|
170 180
....*....|....*....|.
gi 13487145 222 RKRLAIALELVNNPPVMFFDE 242
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDE 475
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
106-249 |
4.74e-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: 57.42 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 106 GKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLINGmprdlrcfRKVScYIMQddmllpHLTVQEAMMVSAHLK 185
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAG-VLKPDEGDIEIEL--------DTVS-YKPQ------YIKADYEGTVRDLLS 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13487145 186 LQEKDEGRREMVK-EILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:cd03237 84 SITKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
105-249 |
6.92e-09 |
|
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: 59.03 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 105 SGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVlingmPRDLrcfrKVSC---YIMQD-DMllphlTVQEAMMV 180
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAG-VLKPDEGEV-----DEDL----KISYkpqYISPDyDG-----TVEEFLRS 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 181 SAHLKLQEKdegrreMVK-EILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:COG1245 425 ANTDDFGSS------YYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
111-248 |
7.44e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILagyreTGM----KGAVLINGMP---RDLRCFRKVScYIMQDDMLLPHLTVQEAMMVSAH 183
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKML-----TGLlpasEGEAWLFGQPvdaGDIATRRRVG-YMSQAFSLYGELTVRQNLELHAR 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 184 L-KLQEKDEGRRemVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:NF033858 366 LfHLPAAEIAAR--VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-274 |
7.94e-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: 58.66 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 36 VVSSNVDEVETDLL-------NGHLKKVDNNFTEAQRF---SSLPRRAAVN------IEFKDLS---YSVpegpwwkKKG 96
Cdd:TIGR03269 223 VLTSHWPEVIEDLSdkaiwleNGEIKEEGTPDEVVAVFmegVSEVEKECEVevgepiIKVRNVSkryISV-------DRG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 97 YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGMKGAVLINGMPRDLRCFR-----KVSCYI---MQDDM 167
Cdd:TIGR03269 296 VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVRVGDEWVDMTKPGpdgrgRAKRYIgilHQEYD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 LLPHLTVQE--------------AMMVSAH-LKLQEKDEgrrEMVKEILtalgllpcaNTRTGSLSGGQRKRLAIALELV 232
Cdd:TIGR03269 376 LYPHRTVLDnlteaiglelpdelARMKAVItLKMVGFDE---EKAEEIL---------DKYPDELSEGERHRVALAQVLI 443
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13487145 233 NNPPVMFFDEPTSGLDSASCFQVV-SLMKGLAQGGRSIVCTIH 274
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSH 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
77-294 |
8.32e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPEGPwwkkkgykTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG---------YRETGMKGAVL--- 144
Cdd:PLN03073 509 ISFSDASFGYPGGP--------LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGelqpssgtvFRSAKVRMAVFsqh 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 145 -INGMprDL---------RCFRKVScyimqDDMLLPHLTvqeAMMVSAHLKLQEkdegrreMVkeiltalgllpcantrt 214
Cdd:PLN03073 581 hVDGL--DLssnpllymmRCFPGVP-----EQKLRAHLG---SFGVTGNLALQP-------MY----------------- 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 215 gSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMKGLA--QGGrsiVCTIHQPSAKLFELFDQLYVLSQ 292
Cdd:PLN03073 627 -TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSE 699
|
..
gi 13487145 293 GQ 294
Cdd:PLN03073 700 GK 701
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
92-304 |
1.25e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 92 WKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGmprdlrcfrkVSCYIMQDDMLLpH 171
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG----------SVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 172 LTVQEAMMVSAhlKLQEKDEGRREMVKEILTALGLLPCAN-----TRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSG 246
Cdd:PLN03232 693 ATVRENILFGS--DFESERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13487145 247 LDSASCFQVV-SLMKGLAQGGRSIVCT--IHqpsakLFELFDQLYVLSQGQCVYRGKVSNL 304
Cdd:PLN03232 771 LDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
101-307 |
1.94e-08 |
|
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: 58.03 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGMprdlrcfrkvSCYIMQDdMLLPHLTVQEAMMV 180
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK-VEGHVHMKGS----------VAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 181 SAHLklqekDEGRREMVKE---ILTALGLLPCAN-TRTG----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS--- 249
Cdd:TIGR00957 722 GKAL-----NEKYYQQVLEacaLLPDLEILPSGDrTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvg 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 250 ASCFQVVSLMKGLAQGGRSIVCTiHQPSakLFELFDQLYVLSQgqcvyrGKVSNLVPY 307
Cdd:TIGR00957 797 KHIFEHVIGPEGVLKNKTRILVT-HGIS--YLPQVDVIIVMSG------GKISEMGSY 845
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
77-242 |
2.42e-08 |
|
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: 57.12 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSVPE---------GPwwkkkgyktllkgISGKFNSGELVAIMGPSGAGKSTLMNILAG-YRETGmkGAVLIN 146
Cdd:COG4615 328 LELRGVTYRYPGedgdegftlGP-------------IDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 147 GMP---RDLRCFRKVSCYIMQDDMLLPHLtvqeammvsahlkLQEKDEGRREMVKEILTALGL---LPCANTR--TGSLS 218
Cdd:COG4615 393 GQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LGLDGEADPARARELLERLELdhkVSVEDGRfsTTDLS 459
|
170 180
....*....|....*....|....
gi 13487145 219 GGQRKRLAIALELVNNPPVMFFDE 242
Cdd:COG4615 460 QGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
98-248 |
2.85e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTL-LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYR--ETGmKGAVLINGMpRDLRcFRKVSC----YimqddM--- 167
Cdd:NF033858 13 KTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARkiQQG-RVEVLGGDM-ADAR-HRRAVCpriaY-----Mpqg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 ----LLPHLTVQEAMMVSAHLKLQEKDEgRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:NF033858 85 lgknLYPTLSVFENLDFFGRLFGQDAAE-RRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
....*
gi 13487145 244 TSGLD 248
Cdd:NF033858 164 TTGVD 168
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
93-248 |
4.35e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 93 KKKGYKT----LLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGM------PRDLRcfRKVScYI 162
Cdd:PRK10247 11 QNVGYLAgdakILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP-TSGTLLFEGEdistlkPEIYR--QQVS-YC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 163 MQ----------DDMLLP----HLTVQEAMMVsahlklqeKDEGRREMVKEILtalgllpcaNTRTGSLSGGQRKRLAIA 228
Cdd:PRK10247 87 AQtptlfgdtvyDNLIFPwqirNQQPDPAIFL--------DDLERFALPDTIL---------TKNIAELSGGEKQRISLI 149
|
170 180
....*....|....*....|
gi 13487145 229 LELVNNPPVMFFDEPTSGLD 248
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALD 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
95-288 |
6.42e-08 |
|
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: 52.36 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 95 KGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMN--ILAgyreTGMKGAVLINGMPRDLRCFrkvSCYImqddmllphl 172
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiGLA----LGGAQSATRRRSGVKAGCI---VAAV---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 173 tvqeammvsahlklqekdegrremvkeILTALGLLPCantrtgsLSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLD 248
Cdd:cd03227 68 ---------------------------SAELIFTRLQ-------LSGGEKELSALALILalasLKPRPLYILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13487145 249 SASCFQVVSLMKGLAQGGRSIVCTIHQPsaKLFELFDQLY 288
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
70-248 |
7.03e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 70 PRRAAVNIEFKDLSysvpegpwwkkKGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLING 147
Cdd:PRK11819 318 PRLGDKVIEAENLS-----------KSFgdRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG-QEQPDSGTIKIGE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 148 MPrdlrcfrKVScYIMQD-DMLLPHLTVQEAmmVSA---HLKLqekdeGRREMvkeiltalgllpcaNTR---------- 213
Cdd:PRK11819 386 TV-------KLA-YVDQSrDALDPNKTVWEE--ISGgldIIKV-----GNREI--------------PSRayvgrfnfkg 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13487145 214 ------TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK11819 437 gdqqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
77-294 |
7.60e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 77 IEFKDLSYSvpegpwWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMPR------ 150
Cdd:PRK13650 5 IEVKNLTFK------YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLteenvw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 151 DLRcfRKVSCYIMQDDMLLPHLTVQEAMMVSahlkLQEKDEGRREM---VKEILTALGLLPCANTRTGSLSGGQRKRLAI 227
Cdd:PRK13650 78 DIR--HKIGMVFQNPDNQFVGATVEDDVAFG----LENKGIPHEEMkerVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 228 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIhqpSAKLFE--LFDQLYVLSQGQ 294
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISI---THDLDEvaLSDRVLVMKNGQ 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
96-248 |
8.71e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY---------RETGMKgavlINGMPRDLRCfrkvscyimqdD 166
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvapdegvikRNGKLR----IGYVPQKLYL-----------D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 MLLPhLTVQEAMMVSAHLKlqekdegrremVKEILTALGLLPCA---NTRTGSLSGGQRKRLAIALELVNNPPVMFFDEP 243
Cdd:PRK09544 80 TTLP-LTVNRFLRLRPGTK-----------KEDILPALKRVQAGhliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
....*
gi 13487145 244 TSGLD 248
Cdd:PRK09544 148 TQGVD 152
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
208-294 |
9.54e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 208 PCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVcTIHQPSAKLFELFDQL 287
Cdd:PRK10982 383 PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRI 461
|
....*..
gi 13487145 288 YVLSQGQ 294
Cdd:PRK10982 462 LVMSNGL 468
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
101-296 |
1.23e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTL-MNILAGYRETGMKGAVLINGMPRDLRCF--------------RKVSCYIMQD 165
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DML----LPHL-TVQEAMMVSAHLKLQEKDEGRREMvkEILTalgllPCANTRTGSLSGGQRKRLAIALELVNNPPVMFF 240
Cdd:NF040905 356 DIKrnitLANLgKVSRRGVIDENEEIKVAEEYRKKM--NIKT-----PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 241 DEPTSGLDSASCFQVVSLMKGLAQGGRSIVcTIhqpSAKLFELF---DQLYVLSQGQCV 296
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPELLgmcDRIYVMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
105-248 |
1.37e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 105 SGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAVLIngmprDLrcfrKVSC---YIMQDdmllPHLTVQEAMMvs 181
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAG-VLKPDEGEVDP-----EL----KISYkpqYIKPD----YDGTVEDLLR-- 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13487145 182 ahlklQEKDEGRREMVK-EILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK13409 423 -----SITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
101-334 |
1.67e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.25 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLM-------NILAGYRetgMKGAVLINGM--------PRDLRcfRKVScYIMQD 165
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR---VEGKVTFHGKnlyapdvdPVEVR--RRIG-MVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DMLLPHlTVQEAMMVSAHL--------KLQEK--------DEgrremVKEILTALGLlpcantrtgSLSGGQRKRLAIAL 229
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARIngykgdmdELVERslrqaalwDE-----VKDKLKQSGL---------SLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 230 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQgGRSIVCTIH--QPSAKL--FELFDQLYVLSQGqcvyrGKVSNLV 305
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHnmQQAARVsdMTAFFNVELTEGG-----GRYGYLV 238
|
250 260 270
....*....|....*....|....*....|
gi 13487145 306 PYLR-DLGLNCPTYHNPADFVmevaSGEYG 334
Cdd:PRK14243 239 EFDRtEKIFNSPQQQATRDYV----SGRFG 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
98-305 |
2.04e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.95 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMP-RDLRC--FRKVSCYIMQDDMLL----- 169
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFHDIPlTKLQLdsWRSRLAVVSQTPFLFsdtva 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 -------PHLTVQE----AMMVSAHLKLQEKDEGRREMVKEiltalgllpcantRTGSLSGGQRKRLAIALELVNNPPVM 238
Cdd:PRK10789 407 nnialgrPDATQQEiehvARLASVHDDILRLPQGYDTEVGE-------------RGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 239 FFDEPTSGLDSASCFQVvslMKGLAQGG--RSIVCTIHQPSAkLFELfDQLYVLSQGQCVYRGKVSNLV 305
Cdd:PRK10789 474 ILDDALSAVDGRTEHQI---LHNLRQWGegRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRGNHDQLA 537
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
111-296 |
2.96e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 111 GELVAIMGPSGAGKSTLMNILAGYRETG-MKGAVLINGMPRDlrcFRKVS-------CYIMQDDMLLPHLTVQEAMMVS- 181
Cdd:NF040905 27 GEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCR---FKDIRdsealgiVIIHQELALIPYLSIAENIFLGn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 182 --AHLKLQEKDEGRREmVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAscfQVV 256
Cdd:NF040905 104 erAKRGVIDWNETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA---ALL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13487145 257 SLMKGL-AQGGRSIVctIhqpSAKLFELF---DQLYVLSQGQCV 296
Cdd:NF040905 180 DLLLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-251 |
6.30e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 46 TDLLNGHLKKVDNNFteaqRFSSLPRraaVNIeFKDLSYSVpegpwwkkkgyktllkgisgkfNSGELVAIMGPSGAGKS 125
Cdd:PTZ00265 1159 KNDIKGKIEIMDVNF----RYISRPN---VPI-YKDLTFSC----------------------DSKKTTAIVGETGSGKS 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 126 TLMNILAGY------------------------------RETGMK-----------------------GAVLINGM---P 149
Cdd:PTZ00265 1209 TVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeQNVGMKnvnefsltkeggsgedstvfknsGKILLDGVdicD 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 150 RDLRCFRKVSCYIMQDDMLLphltvqeAMMVSAHLKLQeKDEGRREMVKEILTALGL------LPCA-NTRTG----SLS 218
Cdd:PTZ00265 1289 YNLKDLRNLFSIVSQEPMLF-------NMSIYENIKFG-KEDATREDVKRACKFAAIdefiesLPNKyDTNVGpygkSLS 1360
|
250 260 270
....*....|....*....|....*....|...
gi 13487145 219 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-294 |
1.31e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 1 MACLMAAFSV---GTAMNASSYSAAMTEPKSVCVSVdevvssnvdeveTDLLNGHLK---KVDNNFTEAQRFSS---LPR 71
Cdd:PLN03232 1147 MIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNI------------TTLLSGVLRqasKAENSLNSVERVGNyidLPS 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 72 RAAVNIEFKDLSYSVPEGPWWK--------KKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILagYRETGM-KGA 142
Cdd:PLN03232 1215 EATAIIENNRPVSGWPSRGSIKfedvhlryRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAL--FRIVELeKGR 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 143 VLINGMprDLRCF-----RKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEIL--TALGLLPCANTRTG 215
Cdd:PLN03232 1293 IMIDDC--DVAKFgltdlRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIdrNPFGLDAEVSEGGE 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 216 SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDsascFQVVSLM-KGLAQGGRSivCTIHQPSAKLFELF--DQLYVLSQ 292
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIqRTIREEFKS--CTMLVIAHRLNTIIdcDKILVLSS 1444
|
..
gi 13487145 293 GQ 294
Cdd:PLN03232 1445 GQ 1446
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
98-305 |
1.34e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG-------YRETGMKGAVLINGMP------RDLRCFRKVSCYIMQ 164
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaPRGARVTGDVTLNGEPlaaidaPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 165 -------DDMLL----PHltVQEAMMVSAHlklqekdegRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVN 233
Cdd:PRK13547 94 pafafsaREIVLlgryPH--ARRAGALTHR---------DGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 234 ---------NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTI-HQPSAKLfELFDQLYVLSQGQCVYRGKVSN 303
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADGAIVAHGAPAD 241
|
..
gi 13487145 304 LV 305
Cdd:PRK13547 242 VL 243
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
106-297 |
1.35e-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: 49.11 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 106 GKFNSGELVAIMGPSGAGKSTLMNILAGYREtgmkgavlingmPRDlrcfrkvscyimqDDMLLPHLTVQeammvsahLK 185
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV--------YK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 186 LQEKDegrremvkeiltalgllpcantrtgsLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQG 265
Cdd:cd03222 67 PQYID--------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|..
gi 13487145 266 GRSIVCTIHQPSAKLFELFDQLYVLSQGQCVY 297
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFEGEPGVY 152
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
101-299 |
2.62e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMNILAGY--RETGmKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQ--- 175
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiiSETG-QTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 ---EAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTG-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 251
Cdd:PRK13645 106 etiEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13487145 252 CFQVVSLMKGLAQG-GRSIVCTIHQPSaKLFELFDQLYVLSQGQCVYRG 299
Cdd:PRK13645 186 EEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
98-248 |
2.87e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPR-------DLRcfRK---VSCYImqddm 167
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgsgetiwDIK--KHigyVSSSL----- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 168 llpHLTVQeammVSAHLK-------------LQEKDEGRREMVKEILTALGLlpcaNTRTG-----SLSGGQRKRLAIAL 229
Cdd:PRK10938 346 ---HLDYR----VSTSVRnvilsgffdsigiYQAVSDRQQKLAQQWLDILGI----DKRTAdapfhSLSWGQQRLALIVR 414
|
170
....*....|....*....
gi 13487145 230 ELVNNPPVMFFDEPTSGLD 248
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLD 433
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
104-294 |
3.10e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 104 ISGKFNSGELVAIMGPSGAGKSTLMNILAGY-RETGmkGAVLINGMPRDLRCFRK-VSCYIM------QDDMLLPHLTVQ 175
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGAtRRTA--GQVYLDGKPIDIRSPRDaIRAGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 176 EAMMVSA---HLKL-------QEKDEGRREMVK-EILTalgllPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPT 244
Cdd:PRK11288 350 DNINISArrhHLRAgclinnrWEAENADRFIRSlNIKT-----PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13487145 245 SGLDSASCFQVVSLMKGLAQGGRSIVCTihqpSAKLFE---LFDQLYVLSQGQ 294
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFV----SSDLPEvlgVADRIVVMREGR 473
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
98-305 |
1.18e-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: 47.21 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 98 KTLLKGISGKFNSGELVAIMGPSGAGKSTLMniLAGYRETGM-KGAVLING-----MPrdLRCFRKVSCYIMQDDMLL-- 169
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfDGKIVIDGidiskLP--LHTLRSRLSIILQDPILFsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 -------PHLTVQEAMMVSAHLKLQEKDegrreMVKEIltaLGLLPCANTRTG-SLSGGQRKRLAIALELVNNPPVMFFD 241
Cdd:cd03288 110 sirfnldPECKCTDDRLWEALEIAQLKN-----MVKSL---PGGLDAVVTEGGeNFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 242 EPTSGLDSAS--CFQVVsLMKGLAQggRSIVCTIHQPSAKLFElfDQLYVLSQGQCVYRGKVSNLV 305
Cdd:cd03288 182 EATASIDMATenILQKV-VMTAFAD--RTVVTIAHRVSTILDA--DLVLVLSRGILVECDTPENLL 242
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
441-587 |
1.33e-05 |
|
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: 47.77 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 441 SNSGFLFFSMLFLMFAALMPTVLTFPLEMsVFLRE----HLNYWYSLK--AYYLAKTMADVPFQIMFPVAYCSIVYWMTS 514
Cdd:pfam12698 155 PQSGYAYYLVGLILMIIILIGAAIIAVSI-VEEKEsrikERLLVSGVSplQYWLGKILGDFLVGLLQLLIILLLLFGIGI 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13487145 515 QPSDAVRFVLFAALGtmtSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYI 587
Cdd:pfam12698 234 PFGNLGLLLLLFLLY---GLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSI 303
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
78-248 |
1.89e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 78 EFKDLSYSVPEgpwwkkkgyKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAG----------------------YR 135
Cdd:PRK11147 321 EMENVNYQIDG---------KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqlqadsgrihcgtklevayfdqHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 136 E------TGM------KGAVLINGMPrdlrcfRKVSCYiMQDDMLLPhltvqeammvsahlklqekdegRREMvkeilta 203
Cdd:PRK11147 392 AeldpekTVMdnlaegKQEVMVNGRP------RHVLGY-LQDFLFHP----------------------KRAM------- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13487145 204 lgllpcanTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK11147 436 --------TPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
95-251 |
1.96e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 95 KGY--KTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAV------LINGMPRDlrcfrkvSCYIMQDD 166
Cdd:PRK15064 327 KGFdnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGTVkwsenaNIGYYAQD-------HAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 167 MllphlTVQEAMMvsahlklQEKDEGRREMVkeILTALG-LLPCANTRTGS---LSGGQRKRLAIALELVNNPPVMFFDE 242
Cdd:PRK15064 399 L-----TLFDWMS-------QWRQEGDDEQA--VRGTLGrLLFSQDDIKKSvkvLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
....*....
gi 13487145 243 PTSGLDSAS 251
Cdd:PRK15064 465 PTNHMDMES 473
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
274-331 |
9.52e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 45.28 E-value: 9.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 274 HQPSAKLFELFDQLYVLSQ-GQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASG 331
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
107-270 |
9.87e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 107 KFNSGELVAIMGPSGAGKSTLMNILAGyRETGMKGAvLINGMPRDLR-CFRKVSCYIMQD------DMLLPH-----LTV 174
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAG-ELPLLSGE-RQSQFSHITRlSFEQLQKLVSDEwqrnntDMLSPGeddtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 175 QEAmmvsahLKLQEKDEGRREMVKEILTALGLLpcaNTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 254
Cdd:PRK10938 103 AEI------IQDEVKDPARCEQLAQQFGITALL---DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*.
gi 13487145 255 VVSLMKGLAQGGRSIV 270
Cdd:PRK10938 174 LAELLASLHQSGITLV 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
217-291 |
1.30e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTI-HQPSAKLFElfDQLYVLS 291
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIaHRLSTIRYA--NTIFVLS 653
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
91-277 |
2.27e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 91 WWKKKG-YKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGmKGAVLINGMprdlrcfrkvSCYIMQDDMLL 169
Cdd:PRK13545 29 FRSKDGeYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKGS----------AALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 170 PHLTVQEAMMVSAhLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 249
Cdd:PRK13545 98 GQLTGIENIELKG-LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180
....*....|....*....|....*...
gi 13487145 250 ASCFQVVSLMKGLAQGGRSIVCTIHQPS 277
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLS 204
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
110-132 |
3.14e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.10 E-value: 3.14e-04
10 20
....*....|....*....|...
gi 13487145 110 SGELVAIMGPSGAGKSTLMNILA 132
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAAR 26
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
92-138 |
4.05e-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: 42.00 E-value: 4.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 13487145 92 WKKKGYKTLLkgISGKFNSG--EL--------VAIMGPSGAGKSTLMNILAG--YRETG 138
Cdd:cd01854 58 YEKLGYPVLA--VSAKTGEGldELrellkgktSVLVGQSGVGKSTLLNALLPelVLATG 114
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
104-294 |
4.49e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 104 ISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETgMKGAVLINGmpRDLRCfRKVSCYIMQDDMLLPHLTVQEAMMVSAH 183
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNG--KEINA-LSTAQRLARGLVYLPEDRQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 184 LK--------------LQEKDEGRRemVKEILTALGL-LPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK15439 358 LAwnvcalthnrrgfwIKPARENAV--LERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13487145 249 SASCFQVVSLMKGLAQGGRSIVCTihqpSAKLFE---LFDQLYVLSQGQ 294
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
107-274 |
4.78e-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: 41.82 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 107 KFNSGeLVAIMGPSGAGKSTLMNIL--AGYRETGMKGavliNGMPRDLRCFRKVScyimqddmllphltvqeammVSAHL 184
Cdd:cd03240 19 EFFSP-LTLIVGQNGAGKTTIIEALkyALTGELPPNS----KGGAHDPKLIREGE--------------------VRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 185 KLQEKDEGRREMV----------------KEILTALGLLPcantrtGSLSGGQRK------RLAIALELVNNPPVMFFDE 242
Cdd:cd03240 74 KLAFENANGKKYTitrslailenvifchqGESNWPLLDMR------GRCSGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190
....*....|....*....|....*....|....
gi 13487145 243 PTSGLDSASC-FQVVSLMKG-LAQGGRSIVCTIH 274
Cdd:cd03240 148 PTTNLDEENIeESLAEIIEErKSQKNFQLIVITH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
199-274 |
4.86e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 199 EILTALGL--LPCANTRTgSLSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTI 273
Cdd:PRK00635 791 HALCSLGLdyLPLGRPLS-SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
|
.
gi 13487145 274 H 274
Cdd:PRK00635 870 H 870
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
96-248 |
1.31e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 96 GYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRE-TGmkGAVLINGMPR--DLRC-------FRKVSCYIMQD 165
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEpSA--GNVSLDPNERlgKLRQdqfafeeFTVLDTVIMGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 166 DML------------LPHLTVQEAMMVsAHLKLQ--EKD----EGRremVKEILTALGlLPcANTRTGSLSG---GQRKR 224
Cdd:PRK15064 90 TELwevkqerdriyaLPEMSEEDGMKV-ADLEVKfaEMDgytaEAR---AGELLLGVG-IP-EEQHYGLMSEvapGWKLR 163
|
170 180
....*....|....*....|....
gi 13487145 225 LAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLD 187
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
101-131 |
2.01e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.01e-03
10 20 30
....*....|....*....|....*....|..
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMN-IL 131
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
111-133 |
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 13487145 111 GELVAIMGPSGAGKSTLMNILAG 133
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLG 217
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
101-131 |
2.62e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.62e-03
10 20 30
....*....|....*....|....*....|..
gi 13487145 101 LKGISGKFNSGELVAIMGPSGAGKSTLMN-IL 131
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
110-133 |
3.04e-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: 3.04e-03
10 20
....*....|....*....|....
gi 13487145 110 SGELVAIMGPSGAGKSTLMNILAG 133
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
216-274 |
4.77e-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: 40.38 E-value: 4.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13487145 216 SLSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIH 274
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
217-321 |
5.15e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13487145 217 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCV 296
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|
gi 13487145 297 YRGKVSNLV-----PYLRDLGLNCPTYHNP 321
Cdd:PRK15093 239 ETAPSKELVttphhPYTQALIRAIPDFGSA 268
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
113-132 |
6.55e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 35.78 E-value: 6.55e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
200-248 |
7.37e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 7.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 13487145 200 ILTALGLLPCANTR-TGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 248
Cdd:PLN03073 327 ILAGLSFTPEMQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
114-135 |
8.48e-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: 8.48e-03
|
| |
