|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-582 |
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: 605.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 15 SGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQ--ILVNGRPRELRTFRKMSCYIMQDDMLLPHL 92
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMMVSANLKLSEK--QEVKKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPT 164
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 165 SGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADF 244
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 245 IIEVASGEYGDLNPMlfRAVQNGLCAmAEKKSSPEKNEVPAPCPPCPPEVDPI------ESHTFATSTLTQFCILFKRTF 318
Cdd:TIGR00955 275 YVQVLAVIPGSENES--RERIEKICD-SFAVSDIGRDMLVNTNLWSGKAGGLVkdsenmEGIGYNASWWTQFYALLKRSW 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 319 LSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNYWY 398
Cdd:TIGR00955 352 LSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 399 SLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTA 478
Cdd:TIGR00955 432 RVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFV 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 479 IPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG-MERGDLTC--LEERCPFrEPQSILRALDVEDAKLYMD 555
Cdd:TIGR00955 512 IPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSdVDNIECTSanTTGPCPS-SGEVILETLSFRNADLYLD 590
|
570 580
....*....|....*....|....*..
gi 2462526932 556 FLVLGIFFLALRLLAYLVLRYRVKSER 582
Cdd:TIGR00955 591 LIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-219 |
3.59e-90 |
|
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: 275.97 E-value: 3.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 10 KRIVASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES-GMKGQILVNGRPRELRTFRKMSCYIMQDDML 88
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 LPHLTVLEAMMVSANLKlsekqevkkelvteiltalGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:cd03213 94 HPTLTVRETLMFAAKLR-------------------GL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 169 SASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-580 |
8.57e-82 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 269.44 E-value: 8.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELRTFRKMScYIMQDDMLLPHLTVLE 96
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSANLKL--SEKQEVKKELVTEILTALGLMSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PLN03211 160 TLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 170 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVA 249
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 250 SGeYGDLNPMLFRA---VQNGLCAMAEKKSSPEKNEVPAPCPPCPPEVDPIESHTFA----------TSTLTQFCILFKR 316
Cdd:PLN03211 320 NG-VCQTDGVSEREkpnVKQSLVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKehrssdrisiSTWFNQFSILLQR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 317 TfLSILRDTVLTHLRFMSHVVIGVLIGLLYLHigDDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNY 396
Cdd:PLN03211 399 S-LKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 397 WYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPV 476
Cdd:PLN03211 476 MYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTV 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 477 TAIPVLLFSGFFVSfkTIPTYLQWSSYLSYVRYGFEGVILTIYGMERGDLTCLEERCPFREPQSILRALDVE---DAKLY 553
Cdd:PLN03211 556 TMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLLGCSLPHGSDRASCKFVEEDvagQISPA 633
|
570 580
....*....|....*....|....*..
gi 2462526932 554 MDFLVLGIFFLALRLLAYLVLRyRVKS 580
Cdd:PLN03211 634 TSVSVLIFMFVGYRLLAYLALR-RIKH 659
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-520 |
4.01e-65 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 231.54 E-value: 4.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGM--KGQILVNGRPRElRTFRKMSCYIMQDDMLLP 90
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 91 HLTVLEAMMVSANLKLSEK--QEVKKELVTEILTALGLMSCSHTRTAL----LSGGQRKRLAIALELVNNPP-VMFFDEP 163
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSvsKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKlLLFLDEP 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 164 TSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQG-QCIFKGVV----TNLIPYLKGLGLH-CPT 237
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLgensHTIINYFEKHGAPkCPE 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 238 YHNPADFIIEVASGEYGD----------LNPMLFRAVQNGLCAM------AEKKSSPEKNevpapcppcppevdpiesHT 301
Cdd:TIGR00956 1010 DANPAEWMLEVIGAAPGAhanqdyhevwRNSSEYQAVKNELDRLeaelskAEDDNDPDAL------------------SK 1071
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 302 FATSTLTQFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFfsMLFLMFAALMPTVL- 380
Cdd:TIGR00956 1072 YAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVF--MATVLFNPLIQQYLp 1149
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 381 TF-PLEMAVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTG-------QPAETSRFLLFSALATATALV 452
Cdd:TIGR00956 1150 PFvAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGfywnaskTGQVHERGVLFWLLSTMFFLY 1229
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 453 AQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG 520
Cdd:TIGR00956 1230 FSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-219 |
3.61e-60 |
|
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: 199.42 E-value: 3.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 17 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG--MKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTV 94
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 LEAMMVSANLKLSEKQ---EVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03234 99 RETLTYTAILRLPRKSsdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 172 CFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-520 |
2.49e-54 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 199.69 E-value: 2.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 20 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAM 98
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSekQEVKKE----LVTEILTALGLMSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PLN03140 975 IYSAFLRLP--KEVSKEekmmFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 170 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKGVV----TNLIPYLKGL-GL-HCPTYHNPA 242
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYFEAIpGVpKIKEKYNPA 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 243 DFIIEVASgeygdlnpmLFRAVQNGLCAMAEKKSSP----EKNEVPAPCPPCPPEVDPIESHTFATSTLTQFCILFKRTF 318
Cdd:PLN03140 1133 TWMLEVSS---------LAAEVKLGIDFAEHYKSSSlyqrNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQW 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 319 LSILRDTVLTHLRFMSHVVIGVLIGLLYLHIG---DDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLN 395
Cdd:PLN03140 1204 WTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGtkrSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAA 1283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 396 YWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVAT-FVG 474
Cdd:PLN03140 1284 GMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAiFAA 1363
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2462526932 475 PVTAIpVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG 520
Cdd:PLN03140 1364 AFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG 1408
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-219 |
4.88e-54 |
|
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: 182.06 E-value: 4.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRElRTFRKMSCYIMQDDMLLPH 91
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMMVSANLKlsekqevkkelvteiltalGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03232 94 LTVREALRFSALLR-------------------GL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462526932 172 CFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKG 219
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-515 |
1.48e-51 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 191.09 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 3 GFSHAFQKRivASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES---GMKGQILVNGRPRE--LRTFRK 77
Cdd:TIGR00956 61 GFRKLKKFR--DTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhiGVEGVITYDGITPEeiKKHYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 78 MSCYIMQDDMLLPHLTVLEAMMVSANLK-------LSEKQEVKKELVTEILTALGLmscSHTRTAL--------LSGGQR 142
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGL---SHTRNTKvgndfvrgVSGGER 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 143 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVV 221
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 222 TNLIPYLKGLGLHCPTYHNPADFIIEVAS-------GEYGDLNPM-------LFRAVQNGLCAMAEKKSSPEKNEVPAPC 287
Cdd:TIGR00956 296 DKAKQYFEKMGFKCPDRQTTADFLTSLTSpaerqikPGYEKKVPRtpqefetYWRNSPEYAQLMKEIDEYLDRCSESDTK 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 288 PPCPPEVDPIES-HTFATSTLT-----QFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTG 361
Cdd:TIGR00956 376 EAYRESHVAKQSkRTRPSSPYTvsfsmQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 362 CLFFSMLFLMFAALMPTVLTFplEMAVFMREHLNY-WYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFL 440
Cdd:TIGR00956 456 ALFFAILFNAFSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFF 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 441 LFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVI 515
Cdd:TIGR00956 534 FYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
313-515 |
2.42e-46 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 161.67 E-value: 2.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 313 LFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASkVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMRE 392
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 393 HLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATF 472
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462526932 473 VGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVI 515
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
32-225 |
3.94e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.37 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK-LSE 108
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYgLPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 KQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 188
Cdd:COG1131 106 KE--ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462526932 189 IICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 225
Cdd:COG1131 184 VLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-214 |
1.62e-41 |
|
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: 148.77 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 15 SGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQ--DDMLL 89
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKELRRKVGLVFQnpDDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 pHLTVLEAMMVSA-NLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:cd03225 90 -GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 169 SASCFQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 214
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
30-214 |
2.47e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.34 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAgyresGM----KGQILVNGRP------RELRTFRKMSC-YIMQDDMLLPHLTVLEAM 98
Cdd:COG1136 33 AGEFVAIVGPSGSGKSTLLNILG-----GLdrptSGEVLIDGQDisslseRELARLRRRHIgFVFQFFNLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKlSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:COG1136 108 ALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462526932 179 MKSLA-QGGRTIICTIHqpSAKLFEMFDKLYILSQGQ 214
Cdd:COG1136 187 LRELNrELGTTIVMVTH--DPELAARADRVIRLRDGR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-219 |
9.65e-39 |
|
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: 142.09 E-value: 9.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRP---RELRTFRKMSCYIMQ--DDMLLpH 91
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNLRELRRKVGLVFQnpDDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMMVS-ANLKLSEKqEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:COG1122 91 PTVEEDVAFGpENLGLPRE-EIR-ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462526932 171 SCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:COG1122 169 GRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADG 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
32-214 |
3.71e-38 |
|
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: 139.93 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP------RELRTFR--KMScYIMQDDMLLPHLTVLEAMMVSAN 103
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseKELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 LKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:cd03255 109 LAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 2462526932 184 -QGGRTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:cd03255 188 kEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
32-221 |
4.09e-36 |
|
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: 135.37 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 109
Cdd:COG4555 28 EITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDvrKEPREARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 110 QEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 189
Cdd:COG4555 107 EELKKR-IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV 185
|
170 180 190
....*....|....*....|....*....|....
gi 2462526932 190 ICTIHQPS--AKLfemFDKLYILSQGQCIFKGVV 221
Cdd:COG4555 186 LFSSHIMQevEAL---CDRVVILHKGKVVAQGSL 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-216 |
1.38e-35 |
|
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: 133.01 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 15 SGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHL 92
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG-ELRPTSGTAYINGYSirTDRKAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMMVSANLK-LSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03263 91 TVREHLRFYARLKgLPKSEI--KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 172 CFQVVSLMKSLaQGGRTIICTIHqpSAKLFEMF-DKLYILSQGQ--CI 216
Cdd:cd03263 169 RRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKlrCI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-219 |
2.75e-35 |
|
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: 132.63 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR------ELRTFRKMSCYIMQDDML 88
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglseaELYRLRRRMGMLFQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 LPHLTVLE--AMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:cd03261 89 FDSLTVFEnvAFPLREHTRLSE--EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 167 LDSASCFQVVSLMKSL--AQGGRTIICTiHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03261 167 LDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-219 |
1.94e-34 |
|
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: 130.38 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 15 SGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYREsGMKGQILVNG------RPRELRTFRKMSCYIMQDDML 88
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 LPHLTVLEAMMV---------SANLKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMF 159
Cdd:cd03256 90 IERLSVLENVLSgrlgrrstwRSLFGLFPKEE--KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 160 FDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 219
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
1.32e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 125.07 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLTVLEA 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 98 MMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-514 |
5.63e-33 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 135.36 E-value: 5.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 19 TLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMK--GQILVNGRprELRTF--RKMSCYIMQDDMLLPHLTV 94
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGY--RLNEFvpRKTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 LEAMMVSAN--------------------------------LKLSEKQEVKKELVTE-ILTALGLMSCSHTRTAL----- 136
Cdd:PLN03140 257 KETLDFSARcqgvgtrydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDyTLKILGLDICKDTIVGDemirg 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQC 215
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 216 IFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGE-----YGDLN-PMLFRAV----------------QNGLCAMAE 273
Cdd:PLN03140 417 VYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKdqeqyWADRNkPYRYISVsefaerfksfhvgmqlENELSVPFD 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 274 KKSSPEknevpapcppcppEVDPIESHTFATSTLTQFCilFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHI---- 349
Cdd:PLN03140 497 KSQSHK-------------AALVFSKYSVPKMELLKAC--WDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTemht 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 350 ---GDDASKVfnntGCLFFSMLFLMFAALMPTVLTFPlEMAVFMRE-----HLNYWYSLKAYYLAktmadVPFQVVCPVV 421
Cdd:PLN03140 562 rneEDGALYI----GALLFSMIINMFNGFAELALMIQ-RLPVFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVV 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 422 YCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWS 501
Cdd:PLN03140 632 WVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWA 711
|
570
....*....|...
gi 2462526932 502 SYLSYVRYGFEGV 514
Cdd:PLN03140 712 YWVSPLSYGFNAL 724
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-214 |
5.82e-33 |
|
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: 124.05 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVL 95
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EammvsaNLKLSekqevkkelvteiltalglmscshtrtallsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:cd03230 92 E------NLKLS-------------------------------GGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462526932 176 VSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQ 214
Cdd:cd03230 135 WELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
33-219 |
4.30e-32 |
|
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: 123.07 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 33 LIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 110
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 111 EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTII 190
Cdd:cd03264 106 EVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVI 183
|
170 180
....*....|....*....|....*....
gi 2462526932 191 CTIHQPSaKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03264 184 LSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
16-214 |
5.64e-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: 121.53 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-----RELRTFRKMSCYIMQDDMLLP 90
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEDltdleDELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 91 HLTVLEammvsaNLklsekqevkkelvteiltALGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:cd03229 90 HLTVLE------NI------------------ALGL-----------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462526932 171 SCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 214
Cdd:cd03229 135 TRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-214 |
7.24e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 7.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRE---LRTFRKMSCYIMQDdmll 89
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-DPPTSGEIYLDGKPLSampPPEWRRQVAYVPQE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 phlTVLEAMMVSANLKLS---EKQEVKKELVTEILTALGL-MSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:COG4619 83 ---PALWGGTVRDNLPFPfqlRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462526932 166 GLDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 214
Cdd:COG4619 160 ALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
18-220 |
3.05e-31 |
|
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: 121.64 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPH 91
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLEGtditklRGKKLRKLRRRIGMIFQHYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMMVSA-------NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 164
Cdd:TIGR02315 94 LTVLENVLHGRlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 165 SGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFEmfDKLYILSQGQCIFKGV 220
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFDGA 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-194 |
4.92e-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: 120.21 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP------RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 103
Cdd:cd03292 26 AGEFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYENVAFALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 LKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:cd03292 105 VTGVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKIN 183
|
170
....*....|.
gi 2462526932 184 QGGRTIICTIH 194
Cdd:cd03292 184 KAGTTVVVATH 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-194 |
6.92e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.28 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPRELRTFRKMSCYIMQD-DMLLPHLTVL 95
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EAMMVSANLkLSEKQEVkkelVTEILTALGL--MSCSHTRTalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:cd03226 91 EELLLGLKE-LDAGNEQ----AETVLKDLDLyaLKERHPLS--LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180
....*....|....*....|.
gi 2462526932 174 QVVSLMKSLAQGGRTIICTIH 194
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITH 184
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
32-196 |
7.73e-31 |
|
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: 119.51 E-value: 7.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELR--TFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKlseK 109
Cdd:COG4133 29 EALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPELTVRENLRFWAALY---G 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 110 QEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 189
Cdd:COG4133 105 LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV 184
|
....*..
gi 2462526932 190 ICTIHQP 196
Cdd:COG4133 185 LLTTHQP 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-219 |
9.82e-31 |
|
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: 119.85 E-value: 9.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR------PREL------RTFRKMScyimqddmLLPHLTVLE 96
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLFDGEditglpPHEIarlgigRTFQIPR--------LFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSANLKLSE---------KQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:cd03219 95 NVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 168 DSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03219 175 NPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
32-224 |
1.57e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.78 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMV----- 100
Cdd:COG3638 30 EFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGqdvtalRGRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 ----SANLKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:COG3638 109 tstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462526932 177 SLMKSLAQ-GGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKGVVTNL 224
Cdd:COG3638 187 DLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-219 |
1.60e-30 |
|
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: 118.52 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES--GMKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLT 93
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPykEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEAMMVSANLKLSEKqeVKKelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:cd03233 100 VRETLDFALRCKGNEF--VRG----------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462526932 174 QVVSLMKSLAQG-GRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03233 156 EILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-214 |
3.50e-30 |
|
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: 115.80 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP---RELRTFRKMSCYIMQddmllphltv 94
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDGKDiakLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 leammvsanlklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 174
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 175 VVSLMKSLAQGGRTIICTIHQPS-AKLFemFDKLYILSQGQ 214
Cdd:cd00267 119 LLELLRELAEEGRTVIIVTHDPElAELA--ADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-222 |
7.13e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 118.22 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP------RELRtfRKMScYIMQDDMLLPH 91
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrRELA--RRIA-YVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMM------VSANLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:COG1120 90 LTVRELVAlgryphLGLFGRPSAEDR---EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462526932 166 GLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG----VVT 222
Cdd:COG1120 167 HLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQGppeeVLT 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
32-195 |
8.76e-30 |
|
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: 116.48 E-value: 8.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNG-----RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 103
Cdd:cd03262 27 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGlkltdDKKNINELRQKVGMVFQQFNLFPHLTVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 --LKLSEKQEVKKELvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 181
Cdd:cd03262 103 kvKGMSKAEAEERAL--ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD 180
|
170
....*....|....
gi 2462526932 182 LAQGGRTIICTIHQ 195
Cdd:cd03262 181 LAEEGMTMVVVTHE 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-215 |
2.40e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRtfRKMSCYIMQD---DMLLPhL 92
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA--RRRIGYVPQRaevDWDFP-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMM------VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:COG1121 93 TVRDVVLmgrygrRGLFRRPSRAD---REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462526932 167 LDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQC 215
Cdd:COG1121 170 VDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLV 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
30-223 |
1.72e-28 |
|
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: 113.34 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPreLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSE 108
Cdd:cd03293 29 EGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEP--VTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 KQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV-VSLMKSLAQGGR 187
Cdd:cd03293 105 KAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGK 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462526932 188 TIICTIHQPSAKLFeMFDKLYILSQGQCIFKGVVTN 223
Cdd:cd03293 184 TVLLVTHDIDEAVF-LADRVVVLSARPGRIVAEVEV 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-219 |
2.10e-28 |
|
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: 112.59 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 28 FCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLE--AMM 99
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 179
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 180 KSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-219 |
4.14e-28 |
|
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: 112.77 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFR-KMScYIMQDDMLLP 90
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP-DSGEILVDGQditglsEKELYELRrRIG-MLFQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 91 HLTVLE--AMMVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:COG1127 96 SLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 169 SASCFQVVSLMKSL--AQGGRTIICTiHQ-PSAklFEMFDKLYILSQGQCIFKG 219
Cdd:COG1127 174 PITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEG 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-219 |
9.17e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 9.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMqddmLLPhlTVLEA 97
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDLASLSPKELARKIA----YVP--QALEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVSAnlkLSEKQevkkelVTEiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:cd03214 85 LGLAH---LADRP------FNE-----------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 178 LMKSLA-QGGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 219
Cdd:cd03214 139 LLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-214 |
2.24e-27 |
|
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: 108.24 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 15 SGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP-REL--RTFRKMSCYIMQDDMLLpH 91
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDGVDlRDLdlESLRKNIAYVPQDPFLF-S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEammvsaNLklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03228 90 GTIRE------NI--------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462526932 172 CFQVVSLMKSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:cd03228 132 EALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-194 |
5.23e-27 |
|
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: 107.89 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHLTV 94
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRP-QSGAVLIDGEPldysrKGLLERRQRVGLVFQDpDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 LEAMMVSA-NLKLSEkQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:TIGR01166 87 DQDVAFGPlNLGLSE-AEVE-RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|.
gi 2462526932 174 QVVSLMKSLAQGGRTIICTIH 194
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTH 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-190 |
5.55e-27 |
|
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: 114.62 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRP------RELRTFRKMSCYIMQD--DMLLPHLTVLEAMMV 100
Cdd:COG1123 290 RGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsrRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 SA-NLKLSEKQEVKkELVTEILTALGLM-SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:COG1123 368 PLrLHGLLSRAERR-ERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL 446
|
170
....*....|...
gi 2462526932 179 MKSL-AQGGRTII 190
Cdd:COG1123 447 LRDLqRELGLTYL 459
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
30-219 |
6.30e-27 |
|
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: 109.74 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR------PREL------RTFrkmscyimQDDMLLPHLTVLE 96
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDGRditglpPHRIarlgiaRTF--------QNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSA-------------NLKLSEKQEVK-KELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 162
Cdd:COG0411 99 NVLVAAharlgrgllaallRLPRARREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 163 PTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL-VMGLADRIVVLDFGRVIAEG 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
32-214 |
7.06e-27 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 108.38 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTFrkmsCYIMQDDMLLPHLTVLEAMMVSANLKL 106
Cdd:cd03259 27 EFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDGRdvtgvPPERRNI----GMVFQDYALFPHLTVAENIAFGLKLRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQG 185
Cdd:cd03259 102 VPKAEIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqREL 180
|
170 180 190
....*....|....*....|....*....|
gi 2462526932 186 GRTIICTIHQPS-AklFEMFDKLYILSQGQ 214
Cdd:cd03259 181 GITTIYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
36-194 |
8.80e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 108.22 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAG-YRESgmKGQILVNG------RPRE---LRtfRKMScYIMQDDMLLPHLTVLEammvsaNLK 105
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrlKRREipyLR--RRIG-VVFQDFRLLPDRTVYE------NVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LS------EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 179
Cdd:COG2884 102 LPlrvtgkSRKEIRRR-VREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL 180
|
170
....*....|....*
gi 2462526932 180 KSLAQGGRTIICTIH 194
Cdd:COG2884 181 EEINRRGTTVLIATH 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-216 |
9.24e-27 |
|
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: 108.36 E-value: 9.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTFRKMSCYIMQDDM--LLPHLTV----LEA 97
Cdd:cd03257 30 KGETLGLVGESGSGKSTLARAILGL-LKPTSGSIIFDGKDllklsrRLRKIRRKEIQMVFQDPMssLNPRMTIgeqiAEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVsanLKLSEKQEVKKELVTEILTALGLmscshTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03257 109 LRI---HGKLSKKEARKEAVLLLLVGVGL-----PEEVLnrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 172 CFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCI 216
Cdd:cd03257 181 QAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-195 |
1.24e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.64 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFM---NILagyrESGMKGQILV-----NGRPRELRTFRKMSCYIMQDDM 87
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVdglkvNDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 88 LLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:PRK09493 88 LFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 2462526932 168 DSASCFQVVSLMKSLAQGGRTIICTIHQ 195
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
32-196 |
2.01e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLE--AMMVSAN 103
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPP-DSGRILWNGQdltalpPAE----RPVS-MLFQENNLFPHLTVAQniGLGLRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 LKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:COG3840 100 LKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170
....*....|....
gi 2462526932 184 QG-GRTIICTIHQP 196
Cdd:COG3840 177 RErGLTVLMVTHDP 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-214 |
2.57e-26 |
|
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: 113.78 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLS 107
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGlYEPT--SGRILIDGIDLrqiDPASLRRQIGVVLQDVFLF-SGTIRE------NITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 eKQEVKKELVTEILTALGLMS--CSH---------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:COG2274 573 -DPDATDEEIIEAARLAGLHDfiEALpmgydtvvgEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462526932 177 SLMKSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:COG2274 652 ENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGR 686
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-213 |
6.84e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 105.69 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG----YResgmkGQILVNGRPreLRTFRKMSCYIMQD--- 85
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllkpTS-----GSIRVFGKP--LEKERKRIGYVPQRrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 86 DMLLPhLTVLEAMM------VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMF 159
Cdd:cd03235 80 DRDFP-ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 160 FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQG 213
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
32-225 |
7.97e-26 |
|
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: 106.13 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 105
Cdd:cd03258 32 EIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:cd03258 111 GVPKAEIEER-VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 186 -GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 225
Cdd:cd03258 190 lGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-225 |
1.25e-25 |
|
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: 111.00 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-REL--RTFRKMSCYIMQDDMLlPHLTV 94
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSILINGVDlSDLdpASWRRQIAWVPQNPYL-FAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 LEammvsaNLKLSE----KQEVKKEL----VTEILTAL--GLmscsHTRT----ALLSGGQRKRLAIALELVNNPPVMFF 160
Cdd:COG4988 428 RE------NLRLGRpdasDEELEAALeaagLDEFVAALpdGL----DTPLgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 161 DEPTSGLDSASCFQVVSLMKSLAQGGRTIICTiHQPSakLFEMFDKLYILSQGQCIFKGVVTNLI 225
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-219 |
1.36e-25 |
|
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: 104.61 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR--PRELRTFRKMSCyIMQDDMLLPHL 92
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDS--GEITFDGKsyQKNIEALRRIGA-LIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 172
Cdd:cd03268 88 TARENLRLLARLLGIRKKRID-----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462526932 173 FQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-219 |
2.24e-25 |
|
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: 104.30 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------------PRElrtfRKMScYIMQDDMLLPHLTVLEAMM 99
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 VSANLKlseKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 179
Cdd:cd03297 98 FGLKRK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462526932 180 KSLAQ--GGRTIICTiHQPSaKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03297 175 KQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-214 |
2.53e-25 |
|
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: 104.89 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 3 GFSHAFQKRIVAsgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTFRKMS 79
Cdd:COG1124 6 NLSVSYGQGGRR---VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 80 CYIMQDDM--LLPHLTVLEAmmVSANLKLSEKQEVKKElVTEILTALGLmscshTRTAL------LSGGQRKRLAIALEL 151
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRI--LAEPLRIHGLPDREER-IAELLEQVGL-----PPSFLdryphqLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 152 VNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPSAKLFeMFDKLYILSQGQ 214
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGR 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-168 |
3.29e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.79 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 5 SHAFQKRivaSGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRElRTFRKMScYIMQ 84
Cdd:COG1116 14 SKRFPTG---GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPVT-GPGPDRG-VVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 85 DDMLLPHLTVLEAMMVSANLKLSEKQEvKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFD 161
Cdd:COG1116 88 EPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGL---AGFEDAYphqLSGGMRQRVAIARALANDPEVLLMD 163
|
....*..
gi 2462526932 162 EPTSGLD 168
Cdd:COG1116 164 EPFGALD 170
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
17-214 |
9.31e-25 |
|
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: 102.25 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 17 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPR-ELRTFRKMSCYIMQDDMLLPHLTVL 95
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 E--AMMVSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:TIGR01277 89 QniGLGLHPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462526932 174 QVVSLMKSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 214
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGK 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
30-224 |
1.72e-24 |
|
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: 101.68 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGY-RESGmkGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKl 106
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLY- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQG 185
Cdd:cd03265 102 GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462526932 186 GRTIICTIH-QPSAKlfEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:cd03265 182 GMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-219 |
1.99e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKST-FMNILAGYRESgmKGQILVNGRP-----RELRTFRKMSCYIMQ--DDMLL-Ph 91
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTlFLHFNGILKPT--SGEVLIKGEPikydkKSLLEVRKTVGIVFQnpDDQLFaP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 lTVLEAMMVSA-NLKLSeKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:PRK13639 95 -TVEEDVAFGPlNLGLS-KEEVEKR-VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462526932 171 SCFQVVSLMKSLAQGGRTIICTIHQpsAKLFEMF-DKLYILSQGQCIFKG 219
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
32-203 |
2.00e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGRP-----RELRTFRKMSCYIMQDDMLLPHLTVLE----AMM 99
Cdd:COG1126 28 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDltdskKDINKLRRKVGMVFQQFNLFPHLTVLEnvtlAPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 VSanLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 179
Cdd:COG1126 104 KV--KKMS-KAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVM 179
|
170 180
....*....|....*....|....
gi 2462526932 180 KSLAQGGRTIICTIHqpsaklfEM 203
Cdd:COG1126 180 RDLAKEGMTMVVVTH-------EM 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-219 |
3.76e-24 |
|
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: 106.14 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 14 ASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGY--RESGMKGQILVNGR-----PRELRtfRKMSCYIMQDD 86
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRdllelSEALR--GRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 87 M--LLPhLTVLEAMM-VSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEP 163
Cdd:COG1123 93 MtqLNP-VTVGDQIAeALENLGLSRAE--ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 164 TSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG 219
Cdd:COG1123 170 TTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDG 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-168 |
4.32e-24 |
|
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: 101.16 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 110
Cdd:cd03300 27 EFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 111 EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:cd03300 106 EIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-219 |
4.94e-24 |
|
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: 106.00 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELR--TFRKMSCYIMQDdmllPHL---TVLEammvsaNLK 105
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLGGVDlRDLDedDLRRRIAVVPQR----PHLfdtTLRE------NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSeKQEVKKELVTEILTALGL--MSCS-----HTRT----ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 174
Cdd:COG4987 431 LA-RPDATDEELWAALERVGLgdWLAAlpdglDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462526932 175 VVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 219
Cdd:COG4987 510 LLADLLEALA-GRTVLLITHRLAG--LERMDRILVLEDGRIVEQG 551
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
32-219 |
5.07e-24 |
|
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: 100.36 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG------RPRELRtfRKMScYIMQDdmllPHL---TVLEammvsa 102
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGLYKP-TSGSVLLDGtdirqlDPADLR--RNIG-YVPQD----VTLfygTLRD------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSeKQEVKKELVTEILTALGLMSCSHT-----------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03245 97 NITLG-APLADDERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 172 CFQVVSLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03245 176 EERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-196 |
1.20e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.19 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNIL-------AG-YRESGMKGQILVNGRPRELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSAN 103
Cdd:PRK10535 35 EMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADALAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 LKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:PRK10535 113 YAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR 191
|
170
....*....|...
gi 2462526932 184 QGGRTIICTIHQP 196
Cdd:PRK10535 192 DRGHTVIIVTHDP 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-219 |
2.29e-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: 98.12 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMScYIMQDDMLLPHLTVL 95
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:cd03269 89 DQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 176 VSLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03269 168 KDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
30-219 |
3.63e-23 |
|
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: 97.89 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLK 105
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKELVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:cd03224 104 RRAKRKARLERVYELFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 2462526932 186 GRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03224 182 GVTIL-LVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-213 |
4.87e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.28 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILV-----------NGRPRELRTFRKMSCYIMQDDMLLPHLTVLEA 97
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLlrcINLL----EQPEAGTIRVgditidtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:PRK11264 106 IIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 178 LMKSLAQGGRTIICTIHQPS-----AKLFEMFDKLYILSQG 213
Cdd:PRK11264 186 TIRQLAQEKRTMVIVTHEMSfardvADRAIFMDQGRIVEQG 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-195 |
5.80e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGkfcrrELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR---------PRELRTFRKMSCYIMQDDML 88
Cdd:COG4161 23 LECPSG-----ETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 LPHLTVLEAMmVSAN---LKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:COG4161 94 WPHLTVMENL-IEAPckvLGLSKEQAREK--AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 2462526932 166 GLDSASCFQVVSLMKSLAQGGRTIICTIHQ 195
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-180 |
1.45e-22 |
|
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: 96.64 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR-----PRELRTFrkmsCYIMQDDMLLPHLTVL 95
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGKditnlPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
....*
gi 2462526932 176 VSLMK 180
Cdd:cd03299 169 REELK 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
30-197 |
2.58e-22 |
|
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: 95.96 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTFRKMSC-YIMQDDMLLPHLTVLEAMMVSA 102
Cdd:COG4181 37 AGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGQDlfaldeDARARLRARHVgFVFQSFQLLPTLTALENVMLPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKlSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:COG4181 116 ELA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFEL 192
|
170
....*....|....*.
gi 2462526932 183 -AQGGRTIICTIHQPS 197
Cdd:COG4181 193 nRERGTTLVLVTHDPA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
16-214 |
7.04e-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: 94.24 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLL 89
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGRdvtdlpPKD----RDIA-MVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 PHLTVLEAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462526932 170 ASCFQVVSLMKSLAQG-GRTIICTIH-QPSAklFEMFDKLYILSQGQ 214
Cdd:cd03301 164 KLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
32-219 |
9.54e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGY----RESGMKGQILVN-----GR-PRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVS 101
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRtvqreGRlARDIRKSRANTGYIFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 102 A-------NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 174
Cdd:PRK09984 111 AlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 175 VVSLMKSLAQG-GRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:PRK09984 191 VMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
32-168 |
9.84e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 96.71 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLEammvsaN-- 103
Cdd:COG3842 32 EFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGRdvtglpPEK----RNVG-MVFQDYALFPHLTVAE------Nva 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 104 --LKLS--EKQEVkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:COG3842 100 fgLRMRgvPKAEI-RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-214 |
1.10e-21 |
|
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: 92.28 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHlTVLEAmmvsanlklse 108
Cdd:cd03246 29 ESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISqwdPNELGDHVGYLPQDDELFSG-SIAEN----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 kqevkkelvteiltalglmscshtrtaLLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 188
Cdd:cd03246 96 ---------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT 148
|
170 180
....*....|....*....|....*.
gi 2462526932 189 IICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:cd03246 149 RIVIAHRPE--TLASADRILVLEDGR 172
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
32-169 |
1.40e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 96.37 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-------PRElrtfRKMScYIMQDDMLLPHLTVLEammvsaN- 103
Cdd:COG1118 29 ELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGRdlftnlpPRE----RRVG-FVFQHYALFPHMTVAE------Ni 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 104 ------LKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:COG1118 97 afglrvRPPSKAE--IRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-170 |
1.69e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG----------RPRELrtfrkmscyIMQDDMLLPHLTVLE--AMM 99
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGqdhtttppsrRPVSM---------LFQENNLFSHLTVAQniGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 100 VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:PRK10771 96 LNPGLKLNAAQ---REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-197 |
1.82e-21 |
|
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: 98.13 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 31 RELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQddmlLPHLTvleAMMVSANLKLS 107
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGVPLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EKqEVKKELVTEILTALGLMSCS-------HT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:TIGR02857 420 RP-DASDAEIREALERAGLDEFVaalpqglDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180
....*....|....*....|.
gi 2462526932 177 SLMKSLAQgGRTIICTIHQPS 197
Cdd:TIGR02857 499 EALRALAQ-GRTVLLVTHRLA 518
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-195 |
2.01e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGkfcrrELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGR---------PRELRTFRKMSCYIMQDDMLLPH 91
Cdd:PRK11124 23 LDCPQG-----ETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLE-----AMMVsanLKLSEKQEVKKELvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:PRK11124 97 LTVQQnlieaPCRV---LGLSKDQALARAE--KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|....*....
gi 2462526932 167 LDSASCFQVVSLMKSLAQGGRTIICTIHQ 195
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-194 |
2.31e-21 |
|
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: 93.01 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMK----GQILVNGR--------PRELRTFRKMsc 80
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGKdiydldvdVLELRRRVGM-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 81 yIMQDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL--LSGGQRKRLAIALELVNNPPVM 158
Cdd:cd03260 86 -VFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462526932 159 FFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIH 194
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-224 |
2.62e-21 |
|
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: 94.76 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGY-RESGmkGQILVNG-----RPRELR-----TFRKMSCYimqDDmllphLTVLEAM 98
Cdd:TIGR01188 18 EGEVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGydvvrEPRKVRrsigiVPQYASVD---ED-----LTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLK-LSEKqeVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:TIGR01188 88 EMMGRLYgLPKD--EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462526932 178 LMKSLAQGGRTIICTIHQpsakLFE---MFDKLYILSQGQCIFKGVVTNL 224
Cdd:TIGR01188 166 YIRALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-225 |
4.39e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 92.22 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 9 QKRIvasGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTfRKMSCYIM 83
Cdd:cd03218 7 SKRY---GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-VKPDSGKILLDGQditklPMHKRA-RLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 84 QDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEP 163
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLE-ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 164 TSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKGVVTNLI 225
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-225 |
6.17e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.13 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 3 GFSHAFQKRIVASGyktllkcLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR--PRELRTFRKMSC 80
Cdd:PRK13536 46 GVSKSYGDKAVVNG-------LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVpvPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 81 YIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFF 160
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 161 DEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 225
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALI 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-192 |
7.08e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.80 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 20 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---------RELRTfRKMScYIMQDDMLLP 90
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 91 HLTVLE--AM-MVSANLKLSEKQEVKKELvteiLTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*..
gi 2462526932 168 DSASCFQVVSLMKSL--AQGGRTIICT 192
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVT 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-219 |
7.59e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 7.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 20 LLKCLSGKFCRRELIGIMGPSGAGKST-FMNILAGYRESgmKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHL 92
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTlFMNLSGLLRPQ--KGAVLWQGKPldyskRGLLALRQQVATVFQDpEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMMVS-ANLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:PRK13638 94 DIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 172 CFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-194 |
8.72e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 92.17 E-value: 8.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR----------------PRELRTFRKMSCYIMQDDMLLPHL 92
Cdd:COG4598 35 DVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGMVFQSFNLWSHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMM-----VsanLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:COG4598 111 TVLENVIeapvhV---LGRP-KAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180
....*....|....*....|....*..
gi 2462526932 168 DSASCFQVVSLMKSLAQGGRTIICTIH 194
Cdd:COG4598 186 DPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-170 |
1.03e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.62 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG--MKGQILVNGRP-RELRTFRKMSCYIMQDDMLLPHLTV 94
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRlTALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 95 LE--AMMVSANLKLSEKqevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:COG4136 94 GEnlAFALPPTIGRAQR----RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
32-225 |
1.10e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 93.60 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR------PRELRTFRK---MscyIMQDDMLLPHLTVLEamm 99
Cdd:COG1135 32 EIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdltalsERELRAARRkigM---IFQHFNLLSSRTVAE--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 vsaN----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:COG1135 102 ---NvalpLEIAgvPKAEIRKR-VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 174 QVVSLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTNLI 225
Cdd:COG1135 178 SILDLLKDInRELGLTIVLITH-------EMdvvrriCDRVAVLENGRIVEQGPVLDVF 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
36-219 |
1.11e-20 |
|
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: 91.68 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPR------ELRTfrkmscYI------MQDDmLLPHLTVLEaMMVSA- 102
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggedvwELRK------RIglvspaLQLR-FPRDETVLD-VVLSGf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 ------NLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:COG1119 106 fdsiglYREPTDEQR---ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 177 SLMKSLAQ-GGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:COG1119 183 ALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAG 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
32-219 |
1.23e-20 |
|
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: 90.75 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHlTVLEammvsaNLKLSe 108
Cdd:cd03254 30 ETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISRKSLRSMIGVVLQDTFLFSG-TIME------NIRLG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 KQEVKKELVTEILTALGL----MSCSH-------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:cd03254 101 RPNATDEEVIEAAKEAGAhdfiMKLPNgydtvlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462526932 178 LMKSLAQgGRTIICTIHQPSAKLFEmfDKLYILSQGQCIFKG 219
Cdd:cd03254 181 ALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-196 |
1.78e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 111
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFLGGEELD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 112 VkkelvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS-LAQGGRTII 190
Cdd:PRK13539 108 I-----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIA 182
|
....*.
gi 2462526932 191 CTiHQP 196
Cdd:PRK13539 183 AT-HIP 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-195 |
1.79e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.18 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGR----------------PRELRTFRKMS 79
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 80 CYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVM 158
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462526932 159 FFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQ 195
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
32-168 |
5.55e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR------PRElrtfRKMScyiM--QDDMLLPHLTVLEammvsa 102
Cdd:COG3839 30 EFLVLLGPSGCGKSTLLRMIAGlEDPTS--GEILIGGRdvtdlpPKD----RNIA---MvfQSYALYPHMTVYE------ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 103 N----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:COG3839 95 NiafpLKLRkvPKAEIDRR-VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-196 |
8.56e-20 |
|
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: 87.93 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMSC-YIMQDDMLLP 90
Cdd:cd03231 8 CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPlDFQRDSIARGLlYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 91 HLTVLEAMMVSANLKLSEKqevkkelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*.
gi 2462526932 171 SCFQVVSLMKSLAQGGRTIICTIHQP 196
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-196 |
1.34e-19 |
|
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: 87.03 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 12 IVASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPR-ELRTFRKMSC-YIMQDDMLL 89
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPLaEQRDEPHENIlYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 PHLTVLEAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQRTIE-----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*...
gi 2462526932 170 ASCFQVVSLMKS-LAQGGRTIICTiHQP 196
Cdd:TIGR01189 161 AGVALLAGLLRAhLARGGIVLLTT-HQD 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-219 |
2.65e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA- 102
Cdd:PRK13636 31 KGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPidysrKGLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSEKqEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:PRK13636 110 NLKLPED-EVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEM 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462526932 183 AQG-GRTIICTIHQ-PSAKLFemFDKLYILSQGQCIFKG 219
Cdd:PRK13636 188 QKElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQG 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
32-219 |
3.79e-19 |
|
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: 91.47 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNG------RPRELRtfRKMScYIMQDDMLLpHLTVLEammvsaNL 104
Cdd:TIGR03375 492 EKVAIIGRIGSGKSTLLKLLLGlYQPT--EGSVLLDGvdirqiDPADLR--RNIG-YVPQDPRLF-YGTLRD------NI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSeKQEVKKELVTEILTALGLMSC--SHT---------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:TIGR03375 560 ALG-APYADDEEILRAAELAGVTEFvrRHPdgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEE 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 174 QVVSLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 219
Cdd:TIGR03375 639 RFKDRLKRWL-AGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADG 681
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-225 |
4.80e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.94 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR--PRELRTFRKMSCYIMQDDMLLPHLT 93
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP-DAGSISLCGEpvPSRARHARQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEAMMVSAN-LKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 172
Cdd:PRK13537 97 VRENLLVFGRyFGLSAAA--ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 173 FQVVSLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 225
Cdd:PRK13537 175 HLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-219 |
7.96e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 7.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgmKGQILVNGRP------RELRTFRkmsCYIMQDDMLLPHLTV 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG--QGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 LEAMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGG--QRKRLAIALELV---NNPP--VMFFDEPTSGL 167
Cdd:COG4138 87 FQYLALHQPAGASS--EAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 168 DSAScfQVV--SLMKSLAQGGRTIICTIHQPSAKLFEMfDKLYILSQGQCIFKG 219
Cdd:COG4138 165 DVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASG 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-184 |
1.05e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 10 KRIVasGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTfmNILAGYRESGMKGQILVNGRPRELRTFRKMSCY------IM 83
Cdd:PRK15134 293 KRTV--DHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVrhriqvVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 84 QD--DMLLPHLTVLEamMVSANLKLSEKQ---EVKKELVTEILTALGLMSCSHTR-TALLSGGQRKRLAIALELVNNPPV 157
Cdd:PRK15134 369 QDpnSSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSL 446
|
170 180
....*....|....*....|....*..
gi 2462526932 158 MFFDEPTSGLDSASCFQVVSLMKSLAQ 184
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQ 473
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-214 |
1.16e-18 |
|
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: 85.43 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRtfRKMScYIMQDDMLL 89
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPVELR--RKIG-YVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 PHLTVLEAmmVSANLKLSE-KQEVKKELVTEILTALGLMSCSHTR--TALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:cd03295 88 PHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 167 LDSASCFQVVSLMKSLAQG-GRTIICTIHQpsakLFEMF---DKLYILSQGQ 214
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQElGKTIVFVTHD----IDEAFrlaDRIAIMKNGE 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
30-196 |
1.85e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---------RELRTfrKMSCYIMQDDMLLPHLTVLEAMMV 100
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdeearAKLRA--KHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 SANLKlSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 180
Cdd:PRK10584 112 PALLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170
....*....|....*..
gi 2462526932 181 SLAQG-GRTIICTIHQP 196
Cdd:PRK10584 191 SLNREhGTTLILVTHDL 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-190 |
3.10e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 35 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRELRTFRK-------MscyIMQDDMLLPHLTVLEammvsaNLKL 106
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagiaI---IHQELNLVPNLSVAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SekQEVKK----------ELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:COG1129 103 G--REPRRgglidwramrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLF 180
|
170
....*....|....
gi 2462526932 177 SLMKSLAQGGRTII 190
Cdd:COG1129 181 RIIRRLKAQGVAII 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-219 |
3.51e-18 |
|
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: 84.81 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR------PRELRTFRKMSCYIMQddmlLPH-- 91
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkKKKLKDLRKKVGLVFQ----FPEhq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 ---LTVLEAMM-VSANLKLSEKqEVKkELVTEILTALGL------MSCSHtrtalLSGGQRKRLAIALELVNNPPVMFFD 161
Cdd:TIGR04521 95 lfeETVYKDIAfGPKNLGLSEE-EAE-ERVKEALELVGLdeeyleRSPFE-----LSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 162 EPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 219
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDG 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-168 |
3.99e-18 |
|
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: 84.62 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 29 CRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP------RELRTFR--KMScYIMQDDMLLPHLTVLEAmmV 100
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEP-TSGKVLIDGQDiaamsrKELRELRrkKIS-MVFQSFALLPHRTVLEN--V 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 101 SANLKLS-EKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:cd03294 124 AFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
4.25e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 6 HAFQKRIVASGYKTLLKCLSG-KFC--RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMS 79
Cdd:PRK13652 2 HLIETRDLCYSYSGSKEALNNiNFIapRNSRIAVIGPNGAGKSTLFRHFNGILKP-TSGSVLIRGEPitkENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 80 CYIMQ--DDMLLPHLTVLEAMMVSANLKLSEkqEVKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNN 154
Cdd:PRK13652 81 GLVFQnpDDQIFSPTVEQDIAFGPINLGLDE--ETVAHRVSSALHMLGL---EELRDRVphhLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 155 PPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVV 221
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
32-213 |
4.31e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRE--SG--MKGQILVNGRPRELRTFrKMscyIMQDDMLLPHLTVLEAMmvSANLKLS 107
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGV-GM---VFQSYALYPHLSVAENM--SFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 --EKQEVKK--ELVTEILTALGLMScshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ----VVSLM 179
Cdd:PRK11000 104 gaKKEEINQrvNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQmrieISRLH 180
|
170 180 190
....*....|....*....|....*....|....*
gi 2462526932 180 KSLaqgGRTIICTIH-QPSAklFEMFDKLYILSQG 213
Cdd:PRK11000 181 KRL---GRTMIYVTHdQVEA--MTLADKIVVLDAG 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-214 |
4.41e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.53 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP-RE--LRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLSE 108
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDiRDltLESLRRQIGVVPQDTFLF-SGTIRE------NIRYGR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 K----QEV----KKELVTEILTAL--GLmscsHT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 174
Cdd:COG1132 439 PdatdEEVeeaaKAAQAHEFIEALpdGY----DTvvgeRGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 175 VVSLMKSLAQgGRTIIcTI-HQPSAklFEMFDKLYILSQGQ 214
Cdd:COG1132 515 IQEALERLMK-GRTTI-VIaHRLST--IRNADRILVLDDGR 551
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-214 |
5.19e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 85.24 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYrESGMKGQILVNG-----RPRELRTFRKMscyiMQDDMLLPHLTVLEAmmVSANLKL-SEK 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMrKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 110 QEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRT 188
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeQLGIT 153
|
170 180
....*....|....*....|....*.
gi 2462526932 189 IICTIHQPSAKLfEMFDKLYILSQGQ 214
Cdd:TIGR01187 154 FVFVTHDQEEAM-TMSDRIAIMRKGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-184 |
5.52e-18 |
|
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: 85.10 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESGM-KGQILVNGR------PRELRTFR--KMScYIMQDDM--LLPHLTVLEA 97
Cdd:COG0444 30 RGETLGLVGESGSGKSTLARAILGlLPPPGItSGEILFDGEdllklsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MM--VSANLKLSEKQevKKELVTEILTALGLmscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD- 168
Cdd:COG0444 109 IAepLRIHGGLSKAE--ARERAIELLERVGL---PDPERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDv 183
|
170
....*....|....*...
gi 2462526932 169 --SAscfQVVSLMKSLAQ 184
Cdd:COG0444 184 tiQA---QILNLLKDLQR 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
32-219 |
8.27e-18 |
|
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: 82.42 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG-----RPRELRtfRKMScyIMQDDM-LLPHLTVLEAMMVSANLK 105
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGfdvvkEPAEAR--RRLG--FVSDSTgLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:cd03266 107 GLKGDELTAR-LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462526932 186 GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 219
Cdd:cd03266 186 GKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-169 |
8.47e-18 |
|
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: 82.77 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRTFRKMSC-YIMQDDMLLPHLTVLEAmmVSANLKLSEKQ 110
Cdd:cd03296 29 ELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEDATDVPVQERNVgFVFQHYALFRHMTVFDN--VAFGLRVKPRS 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 111 EV-----KKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:cd03296 106 ERppeaeIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
32-196 |
1.11e-17 |
|
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: 86.26 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQDdmllPHL---TVLEammvsaNLK 105
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssLDQDEVRRRVSVCAQD----AHLfdtTVRE------NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSeKQEVKKELVTEILTALGL----------MSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 174
Cdd:TIGR02868 431 LA-RPDATDEELWAALERVGLadwlralpdgLDTVlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|..
gi 2462526932 175 VVSLMKSlAQGGRTIICTIHQP 196
Cdd:TIGR02868 510 LLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
32-219 |
1.30e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGY--RESGmkgQILVNGR-----PRELRTFRKMScYIMQDDMLLPHLTVLEAMMVSANL 104
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDEdisllPLHARARRGIG-YLPQEASIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSEKQEVKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 181
Cdd:PRK10895 106 RDDLSAEQREDRANELMEEFHI---EHLRDSMgqsLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462526932 182 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:PRK10895 183 LRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-219 |
1.83e-17 |
|
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: 81.89 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG---RPRELRTFRKMSCYIMQDDMLLpHLTVLEAMM--------- 99
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDGhdvRDYTLASLRRQIGLVSQDVFLF-NDTVAENIAygrpgatre 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 -VSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:cd03251 107 eVEEAARAANAHEFIMELPEGYDTVIG------ERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 179 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 219
Cdd:cd03251 181 LERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVERG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-168 |
2.05e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILvngRPRELRtfrkMScYIMQDDMLLPHLTVL 95
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVS---IPKGLR----IG-YLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EAMMVS-------------ANLKLSEKQEVKKEL------------------VTEILTALGLMSCSHTR-TALLSGGQRK 143
Cdd:COG0488 80 DTVLDGdaelraleaeleeLEAKLAEPDEDLERLaelqeefealggweaearAEEILSGLGFPEEDLDRpVSELSGGWRR 159
|
170 180
....*....|....*....|....*
gi 2462526932 144 RLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLD 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-219 |
2.08e-17 |
|
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: 86.61 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 28 FCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRE--LRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 105
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGKDIEtnLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180 190
....*....|....*....|....*....|....
gi 2462526932 186 GRTIICTIHQPSAKLfeMFDKLYILSQGQCIFKG 219
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGRLYCSG 1142
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-219 |
2.71e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 9 QKRIVASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTFRKMSCYIMqddmL 88
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-QSGTVFLGDKPISMLSSRQLARRLA----L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 LP-HLTVLEAMMV--------SANL----KLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNP 155
Cdd:PRK11231 81 LPqHHLTPEGITVrelvaygrSPWLslwgRLSAEDN---ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 156 PVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH---QPSaklfEMFDKLYILSQGQCIFKG 219
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-279 |
3.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG----RPRELRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NLK 105
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGidtgDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPeNLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSeKQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:PRK13644 108 LP-PIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 186 GRTIICTIHqpSAKLFEMFDKLYILSQGQCIFKGVVTNLI--PYLKGLGLHCPTyhnpadfIIEVASgeygdlnpmlfRA 263
Cdd:PRK13644 186 GKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPS-------LIELAE-----------NL 245
|
250
....*....|....*.
gi 2462526932 264 VQNGLCAMAEKKSSPE 279
Cdd:PRK13644 246 KMHGVVIPWENTSSPS 261
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
32-168 |
3.39e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELR---TfrkmscyIMQDDMLLPHLTVLEAmmVSAN 103
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDGQdithvPAENRhvnT-------VFQSYALFPHMTVFEN--VAFG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 104 LKLSE--KQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK09452 111 LRMQKtpAAEIT-PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-223 |
3.67e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.50 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG----YRESGMKGQILVNGR---PRELRTFRKMSCYIMQD 85
Cdd:PRK14247 11 VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 86 DMLLPHLTVLEAmmVSANLKLSEKQEVKKEL---VTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVM 158
Cdd:PRK14247 91 PNPIPNLSIFEN--VALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 159 FFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG----VVTN 223
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGptreVFTN 235
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-219 |
5.41e-17 |
|
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: 84.41 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGR------PRELRtfRKMSCyIMQDDMLL------------PHLT 93
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVDGVdlaiadPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAP 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEammVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:TIGR01846 560 FEH---VIHAAKLAGAHDFISELPQGYNTEVG------EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 174 QVVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 219
Cdd:TIGR01846 631 LIMRNMREICR-GRTVIIIAHRLST--VRACDRIIVLEKGQIAESG 673
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
32-223 |
6.11e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.54 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR------PRELRTFRKmscyimQDDMLLPHLTVLEAMMVSA 102
Cdd:PRK11153 32 EIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdltalsEKELRKARR------QIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 N----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:PRK11153 102 NvalpLELAgtPKAEIKAR-VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 177 SLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTN 223
Cdd:PRK11153 181 ELLKDInRELGLTIVLITH-------EMdvvkriCDRVAVIDAGRLVEQGTVSE 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-169 |
6.44e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.68 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-------RELrtfrkmscyIMQDDMLLPHLTVLEAmmVSA 102
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgadRGV---------VFQKDALLPWLNVLDN--VAF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 103 NLKLS--EKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:COG4525 100 GLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-214 |
6.46e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 82.47 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----------PRELRTFRkmscYIMQDDMLLPHLTVLEAMMV 100
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGRtlfdsrkgiflPPEKRRIG----YVFQEARLFPHLSVRGNLRY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 SANLKLSEKQEVKKELVTEILtalGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 180
Cdd:TIGR02142 99 GMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190
....*....|....*....|....*....|....
gi 2462526932 181 SLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQ 214
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-219 |
7.60e-17 |
|
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: 80.22 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLpHLTVLE-------AM--- 98
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF-NRSIRDnialadpGMsme 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:cd03252 107 RVIEAAKLAGAHDFISELPEGYDTIVG------EQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 179 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 219
Cdd:cd03252 181 MHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQG 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-196 |
8.51e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 8.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 19 TLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYResgmkgqilvngRPRELRTFRKMSC---YIMQ---DDMLLPhL 92
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL------------RPTSGTVRRAGGArvaYVPQrseVPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TVLEAMMVSANLKLSEKQEVKKE---LVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 2462526932 170 ASCFQVVSLMKSLAQGGRTIICTIHQP 196
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-196 |
1.03e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE---SGMK--GQILVNGRPR---ELRTFRKMSCYIMQDDMLL 89
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKvdGKVLYFGKDIfqiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 PHLTVLEAmmVSANLK---LSEKQEVKKeLVTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDE 162
Cdd:PRK14246 103 PHLSIYDN--IAYPLKshgIKEKREIKK-IVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 2462526932 163 PTSGLDSASCFQVVSLMKSLaQGGRTIICTIHQP 196
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-213 |
1.41e-16 |
|
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: 79.05 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRTFRKMscYIMQDDMLLPHLTVLE--AMMVSANLKLSEK 109
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniALAVDRVLPDLSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 110 QEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS-LMKSLAQGGRT 188
Cdd:TIGR01184 89 SE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEeLMQIWEEHRVT 167
|
170 180
....*....|....*....|....*
gi 2462526932 189 IICTIHQPSAKLFeMFDKLYILSQG 213
Cdd:TIGR01184 168 VLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-219 |
1.41e-16 |
|
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: 77.74 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPREL--RTFRKMSCYIMQDdmllPHLtvl 95
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKALSSLISVLNQR----PYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 eammvsanlklsekqevkkeLVTEILTALGLMscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:cd03247 87 --------------------FDTTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 176 VSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 219
Cdd:cd03247 138 LSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-219 |
1.59e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCY--IM-QDDMLL 89
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPLAAWSPWELARRraVLpQHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 PHLTVLE--AMMVSANlklSEKQEVKKELVTEILTALGLMSCSHTRTALLSGG--QRKRLAIAL----ELVNNPP-VMFF 160
Cdd:COG4559 88 FPFTVEEvvALGRAPH---GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGeqQRVQLARVLaqlwEPVDGGPrWLFL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 161 DEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSakLFEMF-DKLYILSQGQCIFKG 219
Cdd:COG4559 165 DEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQG 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-216 |
3.21e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR------PRELRTFRKMscyimqddmlLPH-------LTVLE-- 96
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPAELARRRAV----------LPQhsslsfpFTVEEvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSAnlkLSEKQEVKKELVTEILTALGlmsCSHTRTAL---LSGG--QRKRLAIAL----ELVNNPPVMFFDEPTSGL 167
Cdd:PRK13548 98 AMGRAP---HGLSRAEDDALVAAALAQVD---LAHLAGRDypqLSGGeqQRVQLARVLaqlwEPDGPPRWLLLDEPTSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 168 DSASCFQVVSLMKSLA-QGGRTIICTIHqpSAKLFEMF-DKLYILSQGQCI 216
Cdd:PRK13548 172 DLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQGRLV 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-219 |
4.68e-16 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 77.66 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 34 IGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RE--LRTFRKMSCYIMQDdMLLPHLTVLEAMMVsANLKLSEKQ 110
Cdd:cd03253 30 VAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDGQDiREvtLDSLRRAIGVVPQD-TVLFNDTIGYNIRY-GRPDATDEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 111 EV---KKELVTEILTAL-----------GLMscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:cd03253 107 VIeaaKAAQIHDKIMRFpdgydtivgerGLK---------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462526932 177 SLMKSLAQgGRTIICTIHQPS----AklfemfDKLYILSQGQCIFKG 219
Cdd:cd03253 178 AALRDVSK-GRTTIVIAHRLStivnA------DKIIVLKDGRIVERG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-224 |
5.41e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNIL-------AGYRESGmkgQILVNGRP----RELRTFRKMSCYIMQDD 86
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 87 MLLPhLTVLEAMMVSANL-KLSEKQEVKKeLVTEILTALGLMSCSHTRTA----LLSGGQRKRLAIALELVNNPPVMFFD 161
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhKLVPRKEFRG-VAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462526932 162 EPTSGLDSASCFQVVSLMKSLAQggRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-171 |
6.62e-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: 79.37 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 31 RELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTF-----RKMScYIMQDDMLLPHLTVLEammvsa 102
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 103 NLKLSEKQEVK---KELVTEILTALGLmscSH---TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:COG4148 97 NLLYGRKRAPRaerRISFDEVVELLGI---GHlldRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-194 |
6.90e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGRPREL---RTFRKMSCYIMQDdmlLPH--- 91
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLESwssKAFARKVAYLPQQ---LPAaeg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMMVSA---NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK10575 100 MTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*..
gi 2462526932 169 SASCFQVVSLMKSLAQG-GRTIICTIH 194
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-216 |
9.08e-16 |
|
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: 75.16 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRkmscyimqddmllphltvlEAMmvsanlklsek 109
Cdd:cd03216 25 RGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKEVSFASPR-------------------DAR----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 110 qevkkelvteiltALGlMSCSHTrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 189
Cdd:cd03216 74 -------------RAG-IAMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAV 135
|
170 180 190
....*....|....*....|....*....|
gi 2462526932 190 ICTIHqpsaKLFEMF---DKLYILSQGQCI 216
Cdd:cd03216 136 IFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-219 |
1.56e-15 |
|
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: 76.42 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDdmllPHL---TV 94
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGvdiRDLNLRWLRSQIGLVSQE----PVLfdgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 95 LEAMMVSAN-LKLSEKQEV-KKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:cd03249 94 AENIRYGKPdATDEEVEEAaKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 171 SCFQVvslMKSL--AQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 219
Cdd:cd03249 174 SEKLV---QEALdrAMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQG 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-219 |
2.33e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.07 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRPRELRTFRKMScYimqddM-----LLPHLTVLEAMMVSANL 104
Cdd:COG4152 28 EIFGLLGPNGAGKTTTIRIILGilAPDSG---EVLWDGEPLDPEDRRRIG-Y-----LpeergLYPKMKVGEQLVYLARL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqvVSLMKS--- 181
Cdd:COG4152 99 KGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN----VELLKDvir 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462526932 182 -LAQGGRTIICTIHQ-PSAKlfEMFDKLYILSQGQCIFKG 219
Cdd:COG4152 174 eLAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-168 |
2.35e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTFRKMscyiMQDDMLLPHLTVleammvSANLKL 106
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGVdlshvPPYQRPINMM----FQSYALFPHMTV------EQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 107 SEKQE--VKKEL---VTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK11607 115 GLKQDklPKAEIasrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
32-167 |
2.47e-15 |
|
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: 75.79 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMS---CYIMQDDMLLPHLTVLEammvsaNLKL- 106
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPP-RSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVEE------NLLLg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 107 ----SEKQEVKK--ELVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:COG0410 103 ayarRDRAEVRAdlERVYELFPRLKERR--RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-190 |
2.93e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 35 GIMGPSGAGKSTFMNILAG-YR-ESgmkGQILVNGRPRELRTFRK-MSCYI-M--QDDMLLPHLTVLE----AMMVSANL 104
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGlYQpDS---GEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVAEnivlGLEPTKGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASCFQVvslMKS 181
Cdd:COG3845 112 RLDRKAARAR--IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADELFEI---LRR 186
|
....*....
gi 2462526932 182 LAQGGRTII 190
Cdd:COG3845 187 LAAEGKSII 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-219 |
3.11e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG---YResgmkGQILVNG---RPRELRTFRKMSCYIMQDDmLLPH 91
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLKINGielRELDPESWRKHLSWVGQNP-QLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMMVsANLKLSE---KQEVKKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:PRK11174 437 GTLRDNVLL-GNPDASDeqlQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462526932 167 LDSASCFQVVSLMKSLAQGGRTIICTiHQPSAkLFEMfDKLYILSQGQCIFKG 219
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQTTLMVT-HQLED-LAQW-DQIWVMQDGQIVQQG 565
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-219 |
3.95e-15 |
|
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: 75.06 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNG-RP--RELRTFRKMSCYIMQDDMLLPHLT 93
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEVRVAGlVPwkRRKKFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEAMMVSANLKLSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462526932 174 QVVSLMKSL-AQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 219
Cdd:cd03267 191 NIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
32-213 |
5.75e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKmsCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 111
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 112 vKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTII 190
Cdd:PRK11248 105 -RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVL 183
|
170 180
....*....|....*....|...
gi 2462526932 191 CTIHQPSAKLFeMFDKLYILSQG 213
Cdd:PRK11248 184 LITHDIEEAVF-MATELVLLSPG 205
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-196 |
6.14e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRP-RELRT-FRKMSCYIMQDDMLLPHLTVLEammvsaNLKLS 107
Cdd:PRK13538 28 ELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRDeYHQDLLYLGHQPGIKTELTALE------NLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EK--QEVKKELVTEILTALGL-----MSCSHtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 180
Cdd:PRK13538 99 QRlhGPGDDEALWEALAQVGLagfedVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
170
....*....|....*.
gi 2462526932 181 SLAQGGRTIICTIHQP 196
Cdd:PRK13538 174 QHAEQGGMVILTTHQD 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-194 |
8.54e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 105
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:PRK10908 108 GASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
....*....
gi 2462526932 186 GRTIICTIH 194
Cdd:PRK10908 187 GVTVLMATH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-214 |
1.04e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 35 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRELRTFRKM----SCYIMQDDMLLPHLTVLEAMMVS---ANLKL 106
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAENLYLGqlpHKGGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 186
Cdd:PRK11288 112 VNRRLLNYE-AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEG 190
|
170 180
....*....|....*....|....*...
gi 2462526932 187 RTIICTIHQpSAKLFEMFDKLYILSQGQ 214
Cdd:PRK11288 191 RVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-219 |
1.05e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP----RElRTFRKMSCYIMQDdmllPHL---T 93
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-QGEILLNGQPiadySE-AALRQAISVVSQR----VHLfsaT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEammvsaNLKLSEKQEVKKELvTEILTALGLMSCSHTRTAL----------LSGGQRKRLAIALELVNNPPVMFFDEP 163
Cdd:PRK11160 430 LRD------NLLLAAPNASDEAL-IEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462526932 164 TSGLDSASCFQVVSLMKSLAQgGRTIICTIHQpsAKLFEMFDKLYILSQGQCIFKG 219
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQ-NKTVLMITHR--LTGLEQFDRICVMDNGQIIEQG 555
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
35-243 |
1.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 35 GIMGPSGAGKSTFMNILAGYRESGMK----GQILVNG--RPRELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKL 106
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGkvtvGDIVVSStsKQKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SeKQEVKKeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:PRK13643 116 P-KEKAEK-IAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 186 GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCPTYHNPAD 243
Cdd:PRK13643 194 GQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVfqeVDFLKAHELGVPKATHFAD 253
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-194 |
1.20e-14 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 73.35 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRelRTFRKMSCYIMQDDML---LPhLTVLEAMMVSANLKL 106
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQEVKKE---LVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:TIGR03771 81 GWLRRPCVAdfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170
....*....|.
gi 2462526932 184 QGGRTIICTIH 194
Cdd:TIGR03771 161 GAGTAILMTTH 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
32-227 |
1.27e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 77.09 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSE 108
Cdd:TIGR01193 501 SKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiDRHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQ 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 kQEVKKEL-VTEILTALGLMSCS-HTRTAL----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:TIGR01193 579 -DEIWAACeIAEIKDDIENMPLGyQTELSEegssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462526932 183 AQggRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGVVTNLIPY 227
Cdd:TIGR01193 658 QD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-219 |
1.54e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.00 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGR---PRELRTFRKMSCYIMQD-DMLLPHLTVLE 96
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEKWVRSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSA-NLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:PRK13647 100 DVAFGPvNMGLD-KDEVE-RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 176 VSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:PRK13647 178 MEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-219 |
2.01e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---------RPRELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSA 102
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLIDGvdiakisdaELREVR--RKKIAMVFQSFALMPHMTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKS 181
Cdd:PRK10070 132 ELAGINAEE-RREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKL 210
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462526932 182 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:PRK10070 211 QAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVG 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-184 |
2.05e-14 |
|
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: 75.88 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGmkGQILVNGRP------RELRTFRKMSCYIMQDDM--LLPHLTVL----EA 97
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLALLRLIPSE--GEIRFDGQDldglsrRALRPLRRRMQVVFQDPFgsLSPRMTVGqiiaEG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVSAnLKLSEKQevKKELVTEILTALGLmscshTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:COG4172 389 LRVHG-PGLSAAE--RRARVAEALEEVGL-----DPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170
....*....|...
gi 2462526932 172 CFQVVSLMKSLAQ 184
Cdd:COG4172 461 QAQILDLLRDLQR 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-219 |
2.17e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 24 LSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgmKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHLTVLE--AM 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEawsAAELARHRAYLSQQQTPPFAMPVFQylTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSEKQEVkkelVTEILTALGLMSCSHTRTALLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSAs 171
Cdd:PRK03695 93 HQPDKTRTEAVASA----LNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVA- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 172 cfQVV---SLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:PRK03695 168 --QQAaldRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQGKLLASG 215
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
32-224 |
2.67e-14 |
|
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: 72.56 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRE-LRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLKLS 107
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDITkLPPHERARagiAYVPQGREIFPRLTVEENLLTGLAALPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EKQEVKKELVtEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL------DSAscfQVVSLMKs 181
Cdd:TIGR03410 106 RSRKIPDEIY-ELFPVLKEML--GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsiikDIG---RVIRRLR- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462526932 182 lAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:TIGR03410 179 -AEGGMAIL-LVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-219 |
2.69e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyresgM----KGQILVNGR------------------PRELRTFRKMScyiMQDDMLL 89
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVG-----LvkpdSGRIFLDGEdithlpmhkrarlgigylPQEASIFRKLT---VEDNILA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 phltVLEAmmvsanLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:COG1137 102 ----VLEL------RKLSKKE--REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462526932 170 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 219
Cdd:COG1137 170 IAVADIQKIIRHLKERGIGVLITDHNVRETL-GICDRAYIISEGKVLAEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-219 |
3.43e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 28 FCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILV----------------NGRPRELRTF---RKMSCYIMQ-DDM 87
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVgdiyigdkknnhelitNPYSKKIKNFkelRRRVSMVFQfPEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 88 LLPHLTVLEAMMVSAnLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:PRK13631 128 QLFKDTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFgLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462526932 167 LDSASCFQVVSLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 219
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-175 |
4.18e-14 |
|
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: 71.73 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTfrkmSCYIMQDDMLLPHLTVLEAMMVSANLKLSeKQE 111
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQP-QGGQVLLDGKPISQYE----HKYLHSKVSLVGQEPVLFARSLQDNIAYG-LQS 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 112 VKKELVTEI-----------LTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:cd03248 115 CSFECVKEAaqkahahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
32-168 |
6.68e-14 |
|
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: 74.61 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSE 108
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDLAgldVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPLTLDE 557
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 109 KQEVKKEL-VTEILTAL--GLmscsHTRTA----LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:TIGR03797 558 AWEAARMAgLAEDIRAMpmGM----HTVISegggTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-168 |
8.12e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfR--KMscyIMQDDMLLPHLTVLEAMmvSAN 103
Cdd:PRK11650 31 EFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RdiAM---VFQNYALYPHMSVRENM--AYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 104 LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK11650 101 LKIRgmPKAEIEER-VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-214 |
9.72e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 8 FQKRIVASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR---PR-ELRTFRKMSCYIM 83
Cdd:PRK09700 266 FEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRsPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 84 Q---DDMLLPHLTVLEAMMVSANLKLS----------EKQEVKKELVTEILTALGLMSCSHTRTALlSGGQRKRLAIALE 150
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAISRSLKDGgykgamglfhEVDEQRTAENQRELLALKCHSVNQNITEL-SGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 151 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTihqpSAKLFEMF---DKLYILSQGQ 214
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
30-169 |
1.05e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGrprELRTFRKMS----CYIMQDDMLLPHLTVLEAmmVSANLK 105
Cdd:PRK11432 31 QGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDG---EDVTHRSIQqrdiCMVFQSYALFPHMSLGEN--VGYGLK 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462526932 106 LS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PRK11432 105 MLgvPKEERKQR-VKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-190 |
1.22e-13 |
|
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: 70.54 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMN-ILAGYRESGmkGQILVNGR----------PRE---LRtfRKMSCYIMQDDMLLPHLTVLEA 97
Cdd:COG4778 38 ECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVRHDggwvdlaqasPREilaLR--RRTIGYVSQFLRVIPRVSALDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVSAnLKLSEKQEVKKELVTEILTALGLmscshtRTAL-------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:COG4778 114 VAEPL-LERGVDREEARARARELLARLNL------PERLwdlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
170 180
....*....|....*....|
gi 2462526932 171 SCFQVVSLMKSLAQGGRTII 190
Cdd:COG4778 187 NRAVVVELIEEAKARGTAII 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-214 |
1.25e-13 |
|
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: 73.54 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNG---RPRELRTFRKMSCYIMQDDMLLPHlTV----------LEAM 98
Cdd:TIGR01842 345 EALAIIGPSGSGKSTLARLIVGI-WPPTSGSVRLDGadlKQWDRETFGKHIGYLPQDVELFPG-TVaeniarfgenADPE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:TIGR01842 423 KIIEAAKLAGVHELILRLPDGYDTVIG------PGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462526932 179 MKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:TIGR01842 497 IKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-214 |
1.51e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCL-----SGKFcrrelIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPreLRTFRKMSCYIMQDDMLLP 90
Cdd:PRK11247 23 GERTVLNQLdlhipAGQF-----VAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 91 HLTVLEammvsaNLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 170
Cdd:PRK11247 95 WKKVID------NVGLGLKGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462526932 171 SCFQVVSLMKSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQ 214
Cdd:PRK11247 168 TRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-168 |
2.05e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR-----PRELRtfrkmSCYI---MQDDML--LPHLTVLEAMMV 100
Cdd:COG1101 33 DFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGKdvtklPEYKR-----AKYIgrvFQDPMMgtAPSMTIEENLAL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 101 SAN------LKLSEKQEvKKELVTEILTALGL-----MscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:COG1101 106 AYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-190 |
2.20e-13 |
|
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: 68.61 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 29 CRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEammvs 101
Cdd:cd03215 24 RAGEIVGIAGLVGNGQTELAEALFGLR-PPASGEITLDGKPVTRRSPRDAIragiAYVPEDrkrEGLVLDLSVAE----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 102 aNLKLSekqevkkelvteiltalglmscshtrtALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 181
Cdd:cd03215 98 -NIALS---------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
....*....
gi 2462526932 182 LAQGGRTII 190
Cdd:cd03215 150 LADAGKAVL 158
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-168 |
4.42e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQI-----LVNGrprelrtfrkmscYIMQD-DMLLPH 91
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVklgetVKIG-------------YFDQHqEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 92 LTVLEAMmvsanlklseKQEVKKELVTEILTALGLM----SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:COG0488 394 KTVLDEL----------RDGAPGGTEQEVRGYLGRFlfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
.
gi 2462526932 168 D 168
Cdd:COG0488 464 D 464
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-238 |
4.47e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.08 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 31 RELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG-----RPRELRTFRKMSCYIMQddmlLPHLTVLEAMMVS---- 101
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGvditdKKVKLSDIRKKVGLVFQ----YPEYQLFEETIEKdiaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 102 --ANLKLSEkQEVKKElVTEILTALGL-MSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:PRK13637 108 gpINLGLSE-EEIENR-VKRAMNIVGLdYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 178 LMKSLAQG-GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGV---VTNLIPYLKGLGLHCP--TY 238
Cdd:PRK13637 186 KIKELHKEyNMTIILVSHsmEDVAKL---ADRIIVMNKGKCELQGTpreVFKEVETLESIGLAVPqvTY 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-197 |
5.80e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.10 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKST----FMNILAGYRESGMKGQILVNGR--------PRELRTFRKMsc 80
Cdd:PRK14267 12 VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrtFNRLLELNEEARVEGEVRLFGRniyspdvdPIEVRREVGM-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 81 yIMQDDMLLPHLTVLEAmmVSANLKLSEKQEVKKELVTEILTAL---GLMSCSHTR----TALLSGGQRKRLAIALELVN 153
Cdd:PRK14267 90 -VFQYPNPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALkkaALWDEVKDRlndyPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 154 NPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPS 197
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-225 |
6.51e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGR-P-RELRTFRKMSCYIM-QDDMLLPHLTVLEammvSANL-- 104
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGilVPTSG---EVRVLGYvPfKRRKEFARRIGVVFgQRSQLWWDLPAID----SFRLlk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 ---KLSEKqEVKKEL--VTEILTALGLMscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 179
Cdd:COG4586 122 aiyRIPDA-EYKKRLdeLVELLDLGELL---DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462526932 180 KSL-AQGGRTIICTIHqpsaklfEMFD------KLYILSQGQCIFKGVVTNLI 225
Cdd:COG4586 198 KEYnRERGTTILLTSH-------DMDDiealcdRVIVIDHGRIIYDGSLEELK 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-194 |
1.02e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIM---QDDML--------------LPHL 92
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSARAASRRVAsvpQDTSLsfefdvrqvvemgrTPHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TvleammvsanlKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 172
Cdd:PRK09536 107 S-----------RFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180
....*....|....*....|..
gi 2462526932 173 FQVVSLMKSLAQGGRTIICTIH 194
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIH 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-168 |
1.04e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRE------------LRTFrkmscyimQDDMLLPHLTVLE 96
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILLRGQHIEglpghqiarmgvVRTF--------QHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSANLKL----------------SEKQEVkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFF 160
Cdd:PRK11300 100 NLLVAQHQQLktglfsgllktpafrrAESEAL--DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
....*...
gi 2462526932 161 DEPTSGLD 168
Cdd:PRK11300 178 DEPAAGLN 185
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-182 |
1.20e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFRKMSCYIMQDDM--LLPHLTVLEamMVSAN 103
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLVKA-TDGEVAWLGKdllgmkDDEWRAVRSDIQMIFQDPLasLNPRMTIGE--IIAEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 L-----KLSeKQEVKKElVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:PRK15079 125 LrtyhpKLS-RQEVKDR-VKAMMLKVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN 202
|
....*
gi 2462526932 178 LMKSL 182
Cdd:PRK15079 203 LLQQL 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-214 |
1.26e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSA 102
Cdd:TIGR02633 285 RGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNpaqaIRAGIAMVPEDrkrHGIVPILGVGKNITLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSEKQEVKKElvTEILTALGLMSCSHTRTAL-------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:TIGR02633 365 LKSFCFKMRIDAA--AELQIIGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEI 442
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462526932 176 VSLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQ 214
Cdd:TIGR02633 443 YKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-214 |
1.40e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.78 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG---YRESGmkGQILVNG----------RPRE-LrtFrkmscYIMQDDMLLPHLTVLEA 97
Cdd:COG0396 27 EVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGedilelspdeRARAgI--F-----LAFQYPVEIPGVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVSANLKLSEKQEVKK--ELVTEILTALGlMSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASc 172
Cdd:COG0396 98 LRTALNARRGEELSAREflKLLKEKMKELG-LDEDFLDRYVnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462526932 173 FQVVS-LMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQ 214
Cdd:COG0396 176 LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGR 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-184 |
1.70e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 14 ASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTFRKMSCYIMQDDM 87
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRKAFRRDIQMVFQDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 88 --LLPHLTV----LEAMMVSANLKLSEKQEVKKELVTEILTALGLMScshTRTALLSGGQRKRLAIALELVNNPPVMFFD 161
Cdd:PRK10419 100 saVNPRKTVreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD---KRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180
....*....|....*....|...
gi 2462526932 162 EPTSGLDSASCFQVVSLMKSLAQ 184
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQ 199
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
32-219 |
2.72e-12 |
|
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: 66.90 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG---YRESG----MKGQILVNGRPRElRTfRKMSCYIMQDDMLLPHLTVLEAMMVSANL 104
Cdd:TIGR01978 27 EIHAIMGPNGSGKSTLSKTIAGhpsYEVTSgtilFKGQDLLELEPDE-RA-RAGLFLAFQYPEEIPGVSNLEFLRSALNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSEKQEVK------KELVTEILTALGlMSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:TIGR01978 105 RRSARGEEPldlldfEKLLKEKLALLD-MDEEFLNRSVnegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 176 VSLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKG 219
Cdd:TIGR01978 184 AEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-194 |
5.82e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTF---MNIL--------------------AGYRESGMKGQILVNGRPRELRT---FRKMSCYIMQ- 84
Cdd:PRK13651 34 EFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRFKKIKKikeIRRRVGVVFQf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 85 DDMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEP 163
Cdd:PRK13651 114 AEYQLFEQTIEKDIIFGPVSMGVSKEEAKK-RAAKYIELVGLDESYLQRSPFeLSGGQKRRVALAGILAMEPDFLVFDEP 192
|
170 180 190
....*....|....*....|....*....|.
gi 2462526932 164 TSGLDSASCFQVVSLMKSLAQGGRTIICTIH 194
Cdd:PRK13651 193 TAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-190 |
7.70e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 27 KFCRRELIGIMGPSGAGKSTF------MNIL-AGYResgMKGQILVNGR--------PRELRT-----FRK-----MSCY 81
Cdd:COG1117 33 DIPENKVTALIGPSGCGKSTLlrclnrMNDLiPGAR---VEGEILLDGEdiydpdvdVVELRRrvgmvFQKpnpfpKSIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 82 imqDDmllphltvleammVSANLKLSE--KQEVKKELVTEILTALGL---------MScshtrtAL-LSGGQRKRLAIAL 149
Cdd:COG1117 110 ---DN-------------VAYGLRLHGikSKSELDEIVEESLRKAALwdevkdrlkKS------ALgLSGGQQQRLCIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 150 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTII 190
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-224 |
8.30e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPreLRTFRkmSCYIMQDDMLLPHLTVLEAMMVSAN----LKLS 107
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQP-TGGQVLLDGVP--LVQYD--HHYLHRQVALVGQEPVLFSGSVRENiaygLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EKQEVkkelvteilTALGLMSCSHT---------------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 172
Cdd:TIGR00958 583 PDEEI---------MAAAKAANAHDfimefpngydtevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 173 FQVVSLMKslaQGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:TIGR00958 654 QLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-219 |
1.38e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 37 MGPSGAGKSTFMNILAGYReSGMKGQILVNG-------RPRELRTFRKMSCYIMQ-DDMLLPHLTVLEAMMVSA-NLKLS 107
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDtlitstsKNKDIKQIRKKVGLVFQfPESQLFEETVLKDVAFGPqNFGVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EKQEVKkeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 186
Cdd:PRK13649 118 QEEAEA--LAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSG 195
|
170 180 190
....*....|....*....|....*....|...
gi 2462526932 187 RTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 219
Cdd:PRK13649 196 MTIVLVTHLMD-DVANYADFVYVLEKGKLVLSG 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
1.54e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNG---RPRELRTFRKMSCYIMQD-DMLLPHL 92
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGitiSKENLKEIRKKIGIIFQNpDNQFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 TV-------LEAMMVSanlklsekQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:PRK13632 100 TVeddiafgLENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 166 GLDSASCFQVVSLMKSLA-QGGRTIICTIHQPSAKLfeMFDKLYILSQGQCIFKG 219
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-243 |
1.67e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAgyRESGMKGQILVNGRPR-----------ELRTFRKMSCYIMQDD 86
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 87 MLLPhLTVLEAMMVSANL----------KLSEKQEVKKELVTEILTALglmscsHTRTALLSGGQRKRLAIALELVNNPP 156
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIvgwrpkleidDIVESALKDADLWDEIKHKI------HKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 157 VMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQpsaklfemFDKLYILSQGQCIFKGvVTNLIPYLKGLGLHC 235
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKG-NENRIGQLVEFGLTK 241
|
....*...
gi 2462526932 236 PTYHNPAD 243
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-194 |
2.39e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMQD---DMLLPHLTVLEAMMVSAN----LKLSE 108
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVEDVVMMGRYGhmgwLRRAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 KQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 188
Cdd:PRK15056 117 KRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKT 194
|
....*.
gi 2462526932 189 IICTIH 194
Cdd:PRK15056 195 MLVSTH 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
36-224 |
2.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYRESgMKGQILVNG-------RPRELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKL 106
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKP-TTGTVTVDDitithktKDKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQevKKELVTEILTALG----LMSCSHTRtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:PRK13646 117 NLDE--VKNYAHRLLMDLGfsrdVMSQSPFQ---MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462526932 183 A-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:PRK13646 192 QtDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-194 |
3.24e-11 |
|
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: 65.98 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 31 RELIGIMGPSGAGKSTFMNILAGYRESgMKGQILV--------------NGRPRELRtfrkmscYI---MQDDMLLPHLT 93
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEP-TSGEVNVrvgdewvdmtkpgpDGRGRAKR-------YIgilHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEAMMVSANLKLSEKQEVKKELVTeiLTALGLmSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGL 167
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVIT--LKMVGF-DEEKAEEILdkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180
....*....|....*....|....*...
gi 2462526932 168 DSASCFQVV-SLMKSLAQGGRTIICTIH 194
Cdd:TIGR03269 459 DPITKVDVThSILKAREEMEQTFIIVSH 486
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
36-194 |
4.16e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAgyRESGM-KGQILVNGRP------RELRtfRKMScyIM-QDDMLLPHLTVLEamMVS------ 101
Cdd:COG4604 32 LIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGLDvattpsRELA--KRLA--ILrQENHINSRLTVRE--LVAfgrfpy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 102 ANLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 181
Cdd:COG4604 104 SKGRLTAEDR---EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR 180
|
170
....*....|....
gi 2462526932 182 LAQG-GRTIICTIH 194
Cdd:COG4604 181 LADElGKTVVIVLH 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-224 |
4.25e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG-------RPRELRTFRKMScYIMQDDMLLPHLTVLE--AMMV 100
Cdd:PRK11831 32 RGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipamsRSRLYTVRKRMS-MLFQSGALFTDMNVFDnvAYPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 SANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 180
Cdd:PRK11831 110 REHTQLPA--PLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462526932 181 SLAQG-GRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:PRK11831 188 ELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-213 |
4.41e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDDMLL------------PHLT--- 93
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDP-QSGRILIDGtdiRTVTRASLRRNIAVVFQDAGLFnrsiednirvgrPDATdee 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEAMMVSANLKLSEKQEVKKElvteilTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYD------TVVG------ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 174 QVVSLMKSLAQgGRTIICTIHQPS----AKLFEMFDKLYILSQG 213
Cdd:PRK13657 509 KVKAALDELMK-GRTTFIIAHRLStvrnADRILVFDNGRVVESG 551
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-190 |
4.46e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVsA 102
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGadPADSG---EIRLDGKPVRIRSPRDAIragiAYVPEDrkgEGLVLDLSIRENITL-A 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLK-------LSEKQEvkKELVTEILTALGL-MSCSHTRTALLSGG-QRKrLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:COG1129 355 SLDrlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVGAKA 431
|
170
....*....|....*..
gi 2462526932 174 QVVSLMKSLAQGGRTII 190
Cdd:COG1129 432 EIYRLIRELAAEGKAVI 448
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-194 |
7.05e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 22 KCLSGKFcrrelIGIMGPSGAGKSTFM---NIL----------AGYresgmkgQILVNGRPRELRTFRKMSCYIMQ-DDM 87
Cdd:PRK13641 29 ELEEGSF-----VALVGHTGSGKSTLMqhfNALlkpssgtitiAGY-------HITPETGNKNLKKLRKKVSLVFQfPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 88 LLPHLTVLEAMMVSA-NLKLSEKQevKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:PRK13641 97 QLFENTVLKDVEFGPkNFGFSEDE--AKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180
....*....|....*....|....*....
gi 2462526932 166 GLDSASCFQVVSLMKSLAQGGRTIICTIH 194
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-224 |
7.07e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRElRTFRKMSC-----YIMQDDMLLPHLTVLEAMMVSanlKL 106
Cdd:PRK09700 32 EIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVLENLYIG---RH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQ---------EVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:PRK09700 107 LTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462526932 178 LMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 224
Cdd:PRK09700 187 IMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-169 |
7.95e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLEAmmVSANLK 105
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALFRHMTVFDN--IAFGLT 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 106 LSEKQE-----VKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PRK10851 101 VLPRRErpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-218 |
1.07e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP-RELRTFRkmscyIMQDDM-LLPH-LTVLEAMMVSANLKL-- 106
Cdd:PRK11614 32 EIVTLIGANGAGKTTLLGTLCG-DPRATSGRIVFDGKDiTDWQTAK-----IMREAVaIVPEgRRVFSRMTVEENLAMgg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 --SEKQEVKK--ELVTEILTALglMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:PRK11614 106 ffAERDQFQEriKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462526932 183 AQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFK 218
Cdd:PRK11614 184 REQGMTIF-LVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-194 |
1.09e-10 |
|
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: 65.03 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 9 QKRIVASGYKT-------LLKCLSG-------KFC----RRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP- 69
Cdd:TIGR01257 1925 RQRIISGGNKTdilrlneLTKVYSGtsspavdRLCvgvrPGECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSi 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 70 -RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIA 148
Cdd:TIGR01257 2004 lTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 149 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 194
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
36-195 |
1.19e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRT---FRKMSCYIM-QDDMLLPHLTVLEAMMvsanLKLSEKQE 111
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNPCARLTpakAHQLGIYLVpQEPLLFPNLSVKENIL----FGLPKRQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 112 VKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIC 191
Cdd:PRK15439 117 SMQKM-KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVF 195
|
....
gi 2462526932 192 TIHQ 195
Cdd:PRK15439 196 ISHK 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-231 |
1.29e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 24 LSGKFCRRELIGIMGPSGAGKS-TFMNILAGYRESGMK---GQILVNGRPRELRTFRKMSCYIMQD----DM-------- 87
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLvqcDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifqepm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 88 --LLPHLTVLEAMMVSANLKLSEKQEvkkELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMF 159
Cdd:PRK10261 115 tsLNPVFTVGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRIPEAQTILsryphqLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 160 FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 231
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
34-225 |
1.40e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 34 IGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDdmllPHL---TVLEAMMVSANLKLS 107
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDI-DEGEILLDGhdlRDYTLASLRNQVALVSQN----VHLfndTIANNIAYARTEQYS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EKQ---EVKKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:PRK11176 447 REQieeAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462526932 183 aQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKGVVTNLI 225
Cdd:PRK11176 527 -QKNRTSLVIAHRLST--IEKADEILVVEDGEIVERGTHAELL 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-214 |
1.49e-10 |
|
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: 64.00 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRprELRTFRKMSC-----YIMQDDMLLPHlTVLE--AMMvsan 103
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGvWPPTA--GSVRLDGA--DLSQWDREELgrhigYLPQDVELFDG-TIAEniARF---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 lklsekQEVKKELVTE----------IL-------TALGLMSCShtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:COG4618 430 ------GDADPEKVVAaaklagvhemILrlpdgydTRIGEGGAR------LSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 167 LDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMfDKLYILSQGQ 214
Cdd:COG4618 498 LDDEGEAALAAAIRALKARGATVVVITHRPSL-LAAV-DKLLVLRDGR 543
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-194 |
1.69e-10 |
|
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: 59.38 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRelrtfrkmSCYIMQddmllphltvl 95
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------IGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 eammvsanlklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170
....*....|....*....
gi 2462526932 176 VSLMKSLaQGgrTIICTIH 194
Cdd:cd03221 110 EEALKEY-PG--TVILVSH 125
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
32-168 |
2.46e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.63 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 111
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 112 VKkelvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK13543 117 MP----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-216 |
2.56e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELRTFR----KMSCYIMQDDMLLPHLTVLEAMMVSANL-- 104
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEELQASNIRdterAGIAIIHQELALVKELSVLENIFLGNEItp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 -KLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:PRK13549 112 gGIMDYDAMYLR-AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462526932 184 QGGRTIICTIHqpsaKLFEMF---DKLYILSQGQCI 216
Cdd:PRK13549 191 AHGIACIYISH----KLNEVKaisDTICVIRDGRHI 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-193 |
3.94e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKS----TFMNILAGY-RESG---MKGQILVNGRPRELRTFR--KMScYIMQDDM--LLPHLTVLEAMM 99
Cdd:PRK09473 43 ETLGIVGESGSGKSqtafALMGLLAANgRIGGsatFNGREILNLPEKELNKLRaeQIS-MIFQDPMtsLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 VSANL-KLSEKQEVKKELVtEILTALGlMSCSHTRTAL----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 174
Cdd:PRK09473 122 EVLMLhKGMSKAEAFEESV-RMLDAVK-MPEARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQ 199
|
170
....*....|....*....
gi 2462526932 175 VVSLMKSLAQGGRTIICTI 193
Cdd:PRK09473 200 IMTLLNELKREFNTAIIMI 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-169 |
4.61e-10 |
|
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: 60.11 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVngrprELRTFRKMSCYIMQD-DMllphlTVLEAMM 99
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAG-VLKPDEGDIEI-----ELDTVSYKPQYIKADyEG-----TVRDLLS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 VSANLKLSEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:cd03237 84 SITKDFYTHPY-----FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-214 |
4.79e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVSA 102
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIaqgiAMVPEDrkrDGIVPVMGVGKNITLAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSEKQEVKKEL-VTEILTALGLM----SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 177
Cdd:PRK13549 367 LDRFTGGSRIDDAAeLKTILESIQRLkvktASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462526932 178 LMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 214
Cdd:PRK13549 447 LINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGK 482
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-219 |
6.40e-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: 61.74 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE-SGMKGQILVN----------------GRP----------- 69
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyEPTSGRIIYHvalcekcgyverpskvGEPcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 70 ---------RELRTFRKMSCYIMQDDM-LLPHLTVLEAMMVSanlkLSEKQEVKKELVTEILTALGLMSCSHTRTAL--- 136
Cdd:TIGR03269 93 evdfwnlsdKLRRRIRKRIAIMLQRTFaLYGDDTVLDNVLEA----LEEIGYEGKEAVGRAVDLIEMVQLSHRITHIard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQC 215
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSDKAIWLENGEI 247
|
....
gi 2462526932 216 IFKG 219
Cdd:TIGR03269 248 KEEG 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-216 |
6.94e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELR----TFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKL 106
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPLKASnirdTERAGIVIIHQELTLVPELSVAENIFLGNEITL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SEKQEVKKELV---TEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:TIGR02633 108 PGGRMAYNAMYlraKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462526932 183 AQGGRTIICTIHqpsaKLFE---MFDKLYILSQGQCI 216
Cdd:TIGR02633 188 KAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
32-168 |
8.21e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRELRTFRKMS------------CYIMQD--DMLlphltvleA 97
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprDGL--------R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 98 MMVSANLKLSEKqevkkelvteiLTALGLMSCSHTR-TAL-------------------LSGGQRKRLAIALELVNNPPV 157
Cdd:PRK11701 104 MQVSAGGNIGER-----------LMAVGARHYGDIRaTAGdwlerveidaariddlpttFSGGMQQRLQIARNLVTHPRL 172
|
170
....*....|.
gi 2462526932 158 MFFDEPTSGLD 168
Cdd:PRK11701 173 VFMDEPTGGLD 183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-214 |
8.98e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGY--RESGmkgQILVNGRPRELRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSA 102
Cdd:PRK10762 279 EILGVSGLMGAGRTELMKVLYGAlpRTSG---YVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGMSVKENMSLTA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSE-----KQEVKKELVTEILTALGLMSCSHTRT-ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:PRK10762 356 LRYFSRaggslKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 177 SLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 214
Cdd:PRK10762 436 QLINQFKAEGLSIILV----SSEMPEvlgMSDRILVMHEGR 472
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-194 |
9.12e-10 |
|
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: 59.69 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG--------YRESGMKGQILVNGRPRELRTFRKMscyIMQDDM----------LLPHLT 93
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNYFTK---LLEGDVkvivkpqyvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 vleAMMVSANLKLSEKQEVKKELVTeiltALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:cd03236 104 ---KGKVGELLKKKDERGKLDELVD----QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|.
gi 2462526932 174 QVVSLMKSLAQGGRTIICTIH 194
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEH 197
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-192 |
9.89e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTF------MNILAgyRESGMKGQILVNGR----PR----ELRTFRKMscy 81
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGHniysPRtdtvDLRKEIGM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 82 IMQDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTR---TAL-LSGGQRKRLAIALELVNNPPV 157
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhdSALgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 2462526932 158 MFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICT 192
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-214 |
1.19e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 17 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILvngRPRELRTfrkmscyimqddMLLPHltvlE 96
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIA---RPAGARV------------LFLPQ----R 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSANLK--LS---EKQEVKKELVTEILTALGLmscSHTRTAL---------LSGGQRKRLAIALELVNNPPVMFFDE 162
Cdd:COG4178 435 PYLPLGTLReaLLypaTAEAFSDAELREALEAVGL---GHLAERLdeeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 163 PTSGLDSASCFQVVSLMKSLAQGGrTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGT-TVISVGHRST--LAAFHDRVLELTGDG 560
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
99-239 |
1.38e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:NF000106 109 MIGR*LDLSRKD--ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 179 MKSLAQGGRTIICTIhQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYH 239
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-219 |
1.46e-09 |
|
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: 57.92 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG---YRESgmKGQILVNGR-----PRELRTfrKMSCYIM- 83
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGEditdlPPEERA--RLGIFLAf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 84 QDDMLLPHLTVLEaMMVSANLKLSekqevkkelvteiltalglmscshtrtallsGGQRKRLAIALELVNNPPVMFFDEP 163
Cdd:cd03217 84 QYPPEIPGVKNAD-FLRYVNEGFS-------------------------------GGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 164 TSGLDSASCFQVVSLMKSLAQGGRTIICTIHQpsAKLFEMF--DKLYILSQGQCIFKG 219
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
109-236 |
1.96e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 109 KQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGR 187
Cdd:PRK13640 117 RPEMIK-IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNL 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 188 TIICTIHQPSAKlfEMFDKLYILSQGQCIFKGVVTNLIP---YLKGLGLHCP 236
Cdd:PRK13640 196 TVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEIFSkveMLKEIGLDIP 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-236 |
2.15e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 18 KTLLKCLSGKFCRRELIGIMGPSGAGKSTF---MNILAGYREsgmkGQILVNG----RPRELRTFRKMSCYIMQ--DDML 88
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE----GKVYVDGldtsDEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 LPhlTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK13633 99 VA--TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 169 SASCFQVVSLMKSL-AQGGRTIICTIH--QPSAKLfemfDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCP 236
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
36-236 |
2.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTFRKMSCYIMQDDmllphltvlEAMMVSANLKLS----- 107
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFEKLRKHIGIVFQNP---------DNQFVGSIVKYDvafgl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 108 EKQEVK----KELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 183
Cdd:PRK13648 110 ENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 184 QGGR-TIICTIHQPSAKLFEmfDKLYILSQGQCIFKGVVTNLIPYLKGL---GLHCP 236
Cdd:PRK13648 190 SEHNiTIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEIFDHAEELtriGLDLP 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-190 |
2.60e-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: 59.80 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 34 IGIMGPSGAGKSTFMNILAGyresgmkgQILVN-GRPRE-------LRTFRKMscyIMQDdmllpHLTVLeammVSANLK 105
Cdd:COG1245 102 TGILGPNGIGKSTALKILSG--------ELKPNlGDYDEepswdevLKRFRGT---ELQD-----YFKKL----ANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEK-QEVK----------KEL---------VTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:COG1245 162 VAHKpQYVDlipkvfkgtvRELlekvdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180
....*....|....*....|....*
gi 2462526932 166 GLDSASCFQVVSLMKSLAQGGRTII 190
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-214 |
2.99e-09 |
|
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: 57.50 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILagYR-ESGMKGQILVNGRP------RELRtfRKMSCyIMQDDMLL---- 89
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRlVELSSGSILIDGVDiskiglHDLR--SRISI-IPQDPVLFsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 -----PHLTVLEAMMVSAnLKlsekqEVK-KELVTEILTALGLMSCShtRTALLSGGQRKRLAIALELVNNPPVMFFDEP 163
Cdd:cd03244 95 rsnldPFGEYSDEELWQA-LE-----RVGlKEFVESLPGGLDTVVEE--GGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 164 TSGLDSASCFQVVSLMKSlAQGGRTIIC------TIHQpsaklfemFDKLYILSQGQ 214
Cdd:cd03244 167 TASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDKGR 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-184 |
3.18e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYRE--SG---MKGQILVNGRPRELRTFRKMSCYIMQDDM--LLPHLTV---LEAMMVsANLK 105
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETptGGelyYQGQDLLKADPEAQKLLRQKIQIVFQNPYgsLNPRKKVgqiLEEPLL-INTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQevKKELVTEILTALGLMSCSHTRTA-LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 184
Cdd:PRK11308 125 LSAAE--RREKALAMMAKVGLRPEHYDRYPhMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
367-580 |
5.02e-09 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 56.36 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 367 MLFLMFAALMPTVLTFplemaVFMREHLNYWY------SLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFL 440
Cdd:COG0842 11 AMSLLFTALMLTALSI-----AREREQGTLERllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 441 LFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGViltiyg 520
Cdd:COG0842 86 LLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL------ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 521 meRGdltcleercpfrepqSILRALDVEDakLYMDFLVLGIFFLALRLLAYLVLRYRVKS 580
Cdd:COG0842 160 --RA---------------LFLGGAGLAD--VWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
36-215 |
5.51e-09 |
|
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: 55.62 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYRESGmKGQIlvnGRPRELRTFrkmscYIMQddmllphltvlEAMMVSANLKlsekqevkke 115
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEGEDLL-----FLPQ-----------RPYLPLGTLR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 116 lvtEILtalglmscSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLaqgGRTIICTIHQ 195
Cdd:cd03223 82 ---EQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR 147
|
170 180
....*....|....*....|.
gi 2462526932 196 PS-AKLFEMfdKLYILSQGQC 215
Cdd:cd03223 148 PSlWKFHDR--VLDLDGEGGW 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-214 |
5.92e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.83 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLTVleammvsanlk 105
Cdd:PRK10522 348 RGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQPEDYRKLFSAVFTDFHLFDQLLG----------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 lSEKQEVKKELVTEILTALGL---MSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSglDSASCFQVV---S 177
Cdd:PRK10522 415 -PEGKPANPALVEKWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAA--DQDPHFRREfyqV 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462526932 178 LMKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-171 |
5.99e-09 |
|
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: 56.27 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFmnILAGYRES-GMKGQILVNGRP------RELRtfRKMSCyIMQDDMLLphlt 93
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDistiplEDLR--SSLTI-IPQDPTLF---- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 94 vleAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:cd03369 95 ---SGTIRSNLDPFDEYSDE-----EIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-224 |
6.28e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 35 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRelrTFR--KMS-----CYIMQDDMLLPHLTVLEammvsaNLKL 106
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiYTRDA--GSILYLGKEV---TFNgpKSSqeagiGIIHQELNLIPQLTIAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SekQEVK--------KELVTE---ILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASC 172
Cdd:PRK10762 103 G--REFVnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 173 FQVVSLMKslAQGgrtiiCTIHQPSAKLFEMF---DKLYILSQGQCIFKGVVTNL 224
Cdd:PRK10762 181 FRVIRELK--SQG-----RGIVYISHRLKEIFeicDDVTVFRDGQFIAEREVADL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-182 |
6.82e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFRKMSCYIMQDDM--LLPHLTVLEAMMVSAN 103
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 104 LKLSEKQEVKKELVTEILTALGLMSCSHTRTA-LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 182
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-162 |
7.10e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 58.27 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLtvleammvsanlkLS 107
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLDGQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 108 EKQEVKKELVTEILTALGLmscSH---------TRTALlSGGQRKRLAIALELVNNPPVMFFDE 162
Cdd:COG4615 424 LDGEADPARARELLERLEL---DHkvsvedgrfSTTDL-SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-200 |
8.51e-09 |
|
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: 54.69 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGrprelrtfrkmscyimqddmllphltvleammvsanlklsek 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 110 qevkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMKSLA 183
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 2462526932 184 QGGRTIICTIHQPSAKL 200
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-184 |
9.62e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.16 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKS-TFMNI--LAGYRESGMKGQILVNGR------PRELRTFR--KMSCyIMQDDM--LLPHLTVle 96
Cdd:COG4172 35 AGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllglsERELRRIRgnRIAM-IFQEPMtsLNPLHTI-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 ammvsanlklsEKQ--EV--------KKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFF 160
Cdd:COG4172 112 -----------GKQiaEVlrlhrglsGAAARARALELLERVGIPDPERRLdayphqLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180
....*....|....*....|....*..
gi 2462526932 161 DEPTSGLD---SAscfQVVSLMKSLAQ 184
Cdd:COG4172 181 DEPTTALDvtvQA---QILDLLKDLQR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-190 |
1.01e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 25 SGKFCRRELIGIMGPSGAGKSTFMNILAGYRE--SG-MKGQILVNGRPRelrtfrkmscYIMQD-DMllphlTVLEAMMV 100
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGeVDEDLKISYKPQ----------YISPDyDG-----TVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 SANLKLSEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 180
Cdd:COG1245 425 ANTDDFGSSY-----YKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|.
gi 2462526932 181 SLAQG-GRTII 190
Cdd:COG1245 500 RFAENrGKTAM 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-194 |
1.02e-08 |
|
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: 58.02 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 34 IGIMGPSGAGKSTFMNILAGyresgMKGQILVNGRPRELRTFRkmscYIMQDDMLLPHLTVLEAMM-------------- 99
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAG-----VDKDFNGEARPQPGIKVG----YLPQEPQLDPTKTVRENVEegvaeikdaldrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 -VSANL--------KLSEKQEvkkELvTEILTALGLMSCSHT---------------RTALLSGGQRKRLAIALELVNNP 155
Cdd:TIGR03719 105 eISAKYaepdadfdKLAAEQA---EL-QEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462526932 156 PVMFFDEPTSGLDSAScfqVVSLMKSLAQGGRTIICTIH 194
Cdd:TIGR03719 181 DMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTH 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-219 |
1.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 27 KFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG--------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAM 98
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS-ETGQTIVGDyaipanlkKIKEVKRLRKEIGLVFQFPEYQLFQETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSE-KQEVKKElVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:PRK13645 112 IAFGPVNLGEnKQEAYKK-VPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 177 SLMKSLAQG-GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 219
Cdd:PRK13645 191 NLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-185 |
1.12e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 34 IGIMGPSGAGKSTFMNILAG--------YRESGMKGQILVNGRPRELRT-FRKMSC----------YImqdDmLLPHL-- 92
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKRFRGTELQNyFKKLYNgeikvvhkpqYV---D-LIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 93 -TVLEAmmvsanLKLSEKQEVKKELVTEiltaLGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:PRK13409 178 gKVREL------LKKVDERGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170
....*....|....
gi 2462526932 172 CFQVVSLMKSLAQG 185
Cdd:PRK13409 248 RLNVARLIRELAEG 261
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-195 |
1.25e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 20 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR--PRELRTFRKMSCYIMQDDMLLPHLTVLE 96
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQsiKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSANLKLSEKQevkkelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:PRK13540 94 NCLYDIHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 2462526932 177 SLMKSLAQGGRTIICTIHQ 195
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-169 |
1.92e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 31 RELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPREL---RTFRKMSCYIMQDDMLLphltvleAMMVSANLKLS 107
Cdd:PRK10790 367 RGFVALVGHTGSGKSTLASLLMGYY-PLTEGEIRLDGRPLSSlshSVLRQGVAMVQQDPVVL-------ADTFLANVTLG 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462526932 108 ekQEVKKELVTEILTALGLMSCS-------HTRTA----LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PRK10790 439 --RDISEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-219 |
2.13e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 54.85 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 10 KRIVASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR---ELRTFrkmscyimqd 85
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGTVTVRGRVSsllGLGGG---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 86 dmLLPHLTVLE-AMMVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 164
Cdd:cd03220 95 --FNPELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526932 165 SGLDSAscFQ--VVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:cd03220 171 AVGDAA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-168 |
2.50e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyrESGM-KGQI-----LVNGR-----PRE-------------------LRTFRKMSCY 81
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNG--EVLLdDGRIiyeqdLIVARlqqdpPRNvegtvydfvaegieeqaeyLKRYHDISHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 82 IMQD--DMLLPHLTVLEAMMVSANLKLSEKQevkkelVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMF 159
Cdd:PRK11147 108 VETDpsEKNLNELAKLQEQLDHHNLWQLENR------INEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*....
gi 2462526932 160 FDEPTSGLD 168
Cdd:PRK11147 180 LDEPTNHLD 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-196 |
2.53e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQilvngrprelrtfrkmSCYIMQDDMLLPHLTVLEAmmvsanlkLSEKQE 111
Cdd:COG2401 57 EIVLIVGASGSGKSTLLRLLAG-ALKGTPVA----------------GCVDVPDNQFGREASLIDA--------IGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 112 VKkeLVTEILTALGLMSCS--HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRT 188
Cdd:COG2401 112 FK--DAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGIT 189
|
....*...
gi 2462526932 189 IICTIHQP 196
Cdd:COG2401 190 LVVATHHY 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-168 |
2.93e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGR---PRELRTF-----RKMScYIMQDDMLLPHLTVleammvSANLKLS 107
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGL-TRPQKGRIVLNGRvlfDAEKGIClppekRRIG-YVFQDARLFPHYKV------RGNLRYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 108 ekqeVKKELVTEILTALGLMSCSH--TRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK11144 101 ----MAKSMVAQFDKIVALLGIEPllDRYPGsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-184 |
3.96e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 3 GFSHAFQKRIVASGyktllkcLSGKFCRRELIGIMGPSGAGKS-TFMNIL-------AGYRESGMK--GQILVNGRPREL 72
Cdd:PRK15134 14 AFRQQQTVRTVVND-------VSLQIEAGETLALVGESGSGKSvTALSILrllpsppVVYPSGDIRfhGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 73 RTFR--KMScYIMQDDMllphltvleammVSAN-LKLSEKQ--EV--------KKELVTEILTALGLMSCSHTRTAL--- 136
Cdd:PRK15134 87 RGVRgnKIA-MIFQEPM------------VSLNpLHTLEKQlyEVlslhrgmrREAARGEILNCLDRVGIRQAAKRLtdy 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 137 ---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 184
Cdd:PRK15134 154 phqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
32-222 |
4.99e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRE-SGMKGQILVNGR-----PRELRTfrKMSCYI-MQDDMLLPHLTVLEAMMVSANL 104
Cdd:CHL00131 34 EIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGEsildlEPEERA--HLGIFLaFQYPIEIPGVSNADFLRLAYNS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSEKQEVKK------ELVTEILTALGLMSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:CHL00131 112 KRKFQGLPELdpleflEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 177 SLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKGVVT 222
Cdd:CHL00131 192 EGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGDAE 237
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-214 |
5.33e-08 |
|
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: 53.24 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 20 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyrESG-MKGQILVNGRprelrtfrkMScYIMQddmllphltvlEAM 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPGS---------IA-YVSQ-----------EPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLK------LSEKQEVKKELVT--------EILTAlGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 164
Cdd:cd03250 77 IQNGTIRenilfgKPFDEERYEKVIKacalepdlEILPD-GDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 165 SGLDSascfQVVS-LMKSLAQG----GRTIICTIHQPSakLFEMFDKLYILSQGQ 214
Cdd:cd03250 156 SAVDA----HVGRhIFENCILGlllnNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-219 |
6.04e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 31 RELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSC---YIMQD--DMLLPHLTVLEAMMVSANLK 105
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYSYRSQrirMIFQDpsTSLNPRQRISQILDFPLRLN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKELVTEILTALGLMScSHTR--TALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL- 182
Cdd:PRK15112 118 TDLEPEQREKQIIETLRQVGLLP-DHASyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELq 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462526932 183 -AQGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKG 219
Cdd:PRK15112 197 eKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-195 |
6.70e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 36 IMGPSGAGKSTFMNILAGYRESgMKGQI------LVNG-RPRELRTFRKMSCYIMQddmlLPHLTVLEAMMVS------A 102
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQP-TSGTVtigervITAGkKNKKLKPLRKKVGIVFQ----FPEHQLFEETVEKdicfgpM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 103 NLKLSEKQevKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 181
Cdd:PRK13634 113 NFGVSEED--AKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK 190
|
170
....*....|....*
gi 2462526932 182 LAQ-GGRTIICTIHQ 195
Cdd:PRK13634 191 LHKeKGLTTVLVTHS 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-168 |
1.15e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRE--SG-MKGQILVNGRPRelrtfrkmscYIMQDdmllPHLTVlEAMMVSANLKL 106
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKpdEGeVDPELKISYKPQ----------YIKPD----YDGTV-EDLLRSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 107 SEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:PRK13409 429 GSSY-----YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-184 |
1.19e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKS----TFMNIL-AGYRESGmkGQILVNGRPRELRTFR-KMSCYIMQD--DMLLPHLTVleAMMVS 101
Cdd:PRK10418 28 RGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGKPVAPCALRgRKIATIMQNprSAFNPLHTM--HTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 102 ANLKLSEKQEVKKELVtEILTALGLmscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:PRK10418 104 ETCLALGKPADDATLT-AALEAVGL---ENAARVLklypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARI 179
|
....*....
gi 2462526932 176 VSLMKSLAQ 184
Cdd:PRK10418 180 LDLLESIVQ 188
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-210 |
1.69e-07 |
|
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: 51.21 E-value: 1.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462526932 137 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPsaKLFEMFDKLYIL 210
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHI 153
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
137-190 |
1.88e-07 |
|
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: 54.06 E-value: 1.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTII 190
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV 548
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-194 |
3.48e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPRELRTFRKMSCYI--MQDDMLLPHLT 93
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIglLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 94 VLEAMMVSANLK----LSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PRK10253 97 TVQELVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180
....*....|....*....|....*.
gi 2462526932 170 ASCFQVVSLMKSL-AQGGRTIICTIH 194
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-219 |
5.03e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.24 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR---PRELRTfrkmscyIMQddmllPHLTVLE-AMMVSANLKL 106
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGiLEPT--SGRVEVNGRvsaLLELGA-------GFH-----PELTGREnIYLNGRLLGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 107 SeKQEVkKELVTEIL--TALG--LmscsHT--RTalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ--VVSL 178
Cdd:COG1134 119 S-RKEI-DEKFDEIVefAELGdfI----DQpvKT--YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA--FQkkCLAR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462526932 179 MKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 219
Cdd:COG1134 189 IRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDG 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-214 |
5.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR------ELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 105
Cdd:PRK13650 34 EWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLteenvwDIR--HKIGMVFQNPDNQFVGATVEDDVAFGLENK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:PRK13650 111 GIPHEEMK-ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
170 180 190
....*....|....*....|....*....|..
gi 2462526932 186 -GRTIICTIHQpsakLFE--MFDKLYILSQGQ 214
Cdd:PRK13650 190 yQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
137-203 |
5.89e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 5.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIH--QPSAKLFEM 203
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHnmQQAARVSDM 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-168 |
6.07e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.88 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 13 VASGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILvngRPRELRTfrkmsCYIMQD---DMLL 89
Cdd:PRK09544 12 VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-EGVIK---RNGKLRI-----GYVPQKlylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 90 PhLTVLEAMMVSANlklsekqeVKKElvtEILTALGLMSCSHTRTA---LLSGGQRKRLAIALELVNNPPVMFFDEPTSG 166
Cdd:PRK09544 83 P-LTVNRFLRLRPG--------TKKE---DILPALKRVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 2462526932 167 LD 168
Cdd:PRK09544 151 VD 152
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-194 |
1.69e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.01 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAG--YRESGMkgqILVNGRPRELRT---FRKMSCYIMQD-DMLLPHLTV-------LEam 98
Cdd:PRK13635 34 EWVAIVGHNGSGKSTLAKLLNGllLPEAGT---ITVGGMVLSEETvwdVRRQVGMVFQNpDNQFVGATVqddvafgLE-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 mvsaNLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 178
Cdd:PRK13635 109 ----NIGVPREEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170
....*....|....*..
gi 2462526932 179 MKSL-AQGGRTIICTIH 194
Cdd:PRK13635 183 VRQLkEQKGITVLSITH 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-219 |
2.29e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPrelrtfrkmsCYIMQDDMLLPHLTVLEAM------MVSANLK 105
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFHDIP----------LTKLQLDSWRSRLAVVSQTpflfsdTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 LSEKQEVKKEL--------VTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:PRK10789 411 LGRPDATQQEIehvarlasVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462526932 176 vslMKSLAQGG--RTIICTIHQPSAkLFEMfDKLYILSQGQCIFKG 219
Cdd:PRK10789 491 ---LHNLRQWGegRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRG 531
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-187 |
2.61e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 26 GKFCRRELIGIMGPSGAGKSTFMNILAGYREsgmkgqilvngrPRElrtfrkmscyimqDDMLLPHLTVLeammvsanlk 105
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 106 lsekqeVKKELVTeiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 185
Cdd:cd03222 65 ------YKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
..
gi 2462526932 186 GR 187
Cdd:cd03222 121 GK 122
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-182 |
3.10e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTF----RKMSCYIMQDDMLLPHLTVLE 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 176
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
....*.
gi 2462526932 177 SLMKSL 182
Cdd:PRK13642 181 RVIHEI 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-168 |
3.92e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQIlvngrprELRTFRKMSCYIMQDDMLLPHLTVL 95
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTI-------EIGETVKLAYVDQSRDALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EA-------MMV------------SANLKLSEKQEvkkelvteiltalglmscshtRTALLSGGQRKRLAIALELVNNPP 156
Cdd:TIGR03719 405 EEisggldiIKLgkreipsrayvgRFNFKGSDQQK---------------------KVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 2462526932 157 VMFFDEPTSGLD 168
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
131-214 |
4.39e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 131 HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYIL 210
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVM 464
|
....
gi 2462526932 211 SQGQ 214
Cdd:PRK10982 465 SNGL 468
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
32-231 |
5.69e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKS----TFMNiLAGYRESGMKGQILVNGR------PRELRTFRKMS-CYIMQDDM--LLPHLTVLEAM 98
Cdd:PRK11022 34 EVVGIVGESGSGKSvsslAIMG-LIDYPGRVMAEKLEFNGQdlqrisEKERRNLVGAEvAMIFQDPMtsLNPCYTVGFQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 99 MVSANLKLSEKQEVKKELVTEILTALGL---MSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 175
Cdd:PRK11022 113 MEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 176 VSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 231
Cdd:PRK11022 193 IELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFraprhPYTQAL 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-168 |
7.24e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP---RELRTFRK---MScyimQDDMLLPHLTVLEAMMVSAN 103
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPvdaGDIATRRRvgyMS----QAFSLYGELTVRQNLELHAR 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462526932 104 L-KLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 168
Cdd:NF033858 366 LfHLPAAE--IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-214 |
8.25e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRprelrTFRKMSCYIMQDDML--LP-----HLTVLEAMM---VS 101
Cdd:PRK15439 290 EILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGK-----EINALSTAQRLARGLvyLPedrqsSGLYLDAPLawnVC 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 102 A------NLKLSEKQEvkKELVTEILTALGLmSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 173
Cdd:PRK15439 364 AlthnrrGFWIKPARE--NAVLERYRRALNI-KFNHAEQAArtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462526932 174 QVVSLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 214
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-197 |
1.55e-05 |
|
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: 45.78 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKSTFmnILAGYRESGMKgqILVNGRPRelrtfrkmscyimqddmllphltvleammV 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKA--RLISFLPK-----------------------------F 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 101 SANLKLSEKQevkkeLVTEILTALGLMSCSHtRTALLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSL 178
Cdd:cd03238 58 SRNKLIFIDQ-----LQFLIDVGLGYLTLGQ-KLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEV 131
|
170
....*....|....*....
gi 2462526932 179 MKSLAQGGRTIICTIHQPS 197
Cdd:cd03238 132 IKGLIDLGNTVILIEHNLD 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-171 |
1.87e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 34 IGIMGPSGAGKSTFMNILAGY-RESgmkgqilvNGrprELRTFRKMSC-YIMQDDMLLPHLTVLEAMM------------ 99
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVdKEF--------EG---EARPAPGIKVgYLPQEPQLDPEKTVRENVEegvaevkaaldr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 100 ---VSANL--------KLSEKQEvkkELvTEILTALGL-------------MSC--SHTRTALLSGGQRKRLAIALELVN 153
Cdd:PRK11819 105 fneIYAAYaepdadfdALAAEQG---EL-QEIIDAADAwdldsqleiamdaLRCppWDAKVTKLSGGERRRVALCRLLLE 180
|
170
....*....|....*...
gi 2462526932 154 NPPVMFFDEPTSGLDSAS 171
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAES 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-216 |
2.60e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRELRTFR----KMSCYIMQDDMLLPHLTVLEammvsaNL 104
Cdd:NF040905 26 EGEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCRFKDIRdseaLGIVIIHQELALIPYLSIAE------NI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 105 KLSEKQ---------EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAsc 172
Cdd:NF040905 100 FLGNERakrgvidwnETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462526932 173 fQVVSLMKSL-AQGGRTIIctIhqpSAKLFEMF---DKLYILSQGQCI 216
Cdd:NF040905 177 -ALLDLLLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
96-197 |
4.55e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 96 EAMMVSANLKLSEKQEV----KKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 169
Cdd:PTZ00265 533 ELIEMRKNYQTIKDSEVvdvsKKVLIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
90 100
....*....|....*....|....*....
gi 2462526932 170 ASCFQVVSLMKSL-AQGGRTIICTIHQPS 197
Cdd:PTZ00265 613 KSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-214 |
6.57e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 30 RR-ELIGIMGPSGAGKSTF-MNILA---GYRESGmkgQILVNGRPRELRTF--------------RKMSCYIMQDDML-- 88
Cdd:NF040905 284 RRgEIVGIAGLMGAGRTELaMSVFGrsyGRNISG---TVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLIDDIKrn 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 89 --LPHLTvleamMVSANLKLSEKQEVKkeLVTEILTALGLMSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 165
Cdd:NF040905 361 itLANLG-----KVSRRGVIDENEEIK--VAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 166 GLDSASCFQVVSLMKSLAQGGRTIIcTIhqpSAKLFE---MFDKLYILSQGQ 214
Cdd:NF040905 434 GIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPEllgMCDRIYVMNEGR 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-171 |
8.85e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 8.85e-05
10 20 30
....*....|....*....|....*....|....*
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 171
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
137-195 |
1.61e-04 |
|
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: 43.47 E-value: 1.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SASCFQvVSLMKSLAQGGRTIICTIHQ 195
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
137-241 |
1.80e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCI 216
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|
gi 2462526932 217 FKGVVTNLI-----PYLKGLGLHCPTYHNP 241
Cdd:PRK15093 239 ETAPSKELVttphhPYTQALIRAIPDFGSA 268
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
194-251 |
1.93e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 44.13 E-value: 1.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462526932 194 HQPSAKLFEMFDKLYILSQGQCI-FKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASG 251
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-196 |
2.06e-04 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.02 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 21 LKCLSGKFCRRELIGIMGPSGAGKST--FMNILAgyresgmkgqilvNGRPRELRTFrkmSCYIMQ--DDMLLPHLTVLE 96
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlaFDTIYA-------------EGQRRYVESL---SAYARQflGQMDKPDVDSIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 97 AMmvSANLKLSEK---QEVKKEL--VTEI-------------------LTALGLMSCSHTRTA-LLSGG--QRKRLA--I 147
Cdd:cd03270 75 GL--SPAIAIDQKttsRNPRSTVgtVTEIydylrllfarvgirerlgfLVDVGLGYLTLSRSApTLSGGeaQRIRLAtqI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462526932 148 ALELVNnppVMF-FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQP 196
Cdd:cd03270 153 GSGLTG---VLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
133-213 |
3.20e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 133 RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKSLAQGGRTIICT--IHqpsakLFEMFDKLYI 209
Cdd:PLN03232 737 RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIIL 811
|
....
gi 2462526932 210 LSQG 213
Cdd:PLN03232 812 VSEG 815
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-194 |
3.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 137 LSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 194
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-197 |
4.11e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 32 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRprelrtfrkmSCYIMQDDMLLPHLTVLEAMMVSAnLKLSEKQE 111
Cdd:PRK13545 51 EIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKGS----------AALIAISSGLNGQLTGIENIELKG-LMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 112 VKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIC 191
Cdd:PRK13545 119 KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFF 198
|
....*.
gi 2462526932 192 TIHQPS 197
Cdd:PRK13545 199 ISHSLS 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
137-208 |
7.32e-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: 41.05 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 137 LSGGQRK------RLAIALELVNNPPVMFFDEPTSGLDSASC-FQVVSLMKS-LAQGGRTIICTIHQPsaKLFEMFDKLY 208
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
136-197 |
8.64e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 8.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462526932 136 LLSGGQRK---RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPS 197
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
111-190 |
2.22e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 111 EVKKELVTEILTA-LGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 189
Cdd:PRK10938 109 EVKDPARCEQLAQqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL 188
|
.
gi 2462526932 190 I 190
Cdd:PRK10938 189 V 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-194 |
2.33e-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: 41.15 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462526932 137 LSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 194
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
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|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-214 |
3.22e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 137 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMKSLA--QGGrtiICTIHQPSAKLFEMFDKLYILSQGQ 214
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-88 |
3.81e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 16 GYKTLLKCLSGKFCRRELIGIMGPSGAGKS----TFMNIL--AGyresgmkGQILVNGRP------RELRtfRKMScYIM 83
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKStlllTFMRMVevCG-------GEIRVNGREigayglRELR--RQFS-MIP 1390
|
....*
gi 2462526932 84 QDDML 88
Cdd:PTZ00243 1391 QDPVL 1395
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
33-52 |
4.54e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 36.16 E-value: 4.54e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-226 |
5.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 120 ILTALGLMSCSHTRT-ALLSGGQRKRLAIA----LELVNnppVMF-FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTI 193
Cdd:PRK00635 459 ILIDLGLPYLTPERAlATLSGGEQERTALAkhlgAELIG---ITYiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE 535
|
90 100 110
....*....|....*....|....*....|....
gi 2462526932 194 HQpsAKLFEMFDKLYILSQGQCIFKG-VVTNLIP 226
Cdd:PRK00635 536 HD--EQMISLADRIIDIGPGAGIFGGeVLFNGSP 567
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
137-212 |
6.05e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.78 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526932 137 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRtIICTIHQPsaKLFEMFDKLYILSQ 212
Cdd:cd03272 159 LSGGQKSLVALALIFaiqkCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQ-FITTTFRP--ELLEVADKFYGVKF 235
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
34-75 |
8.88e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 38.31 E-value: 8.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2462526932 34 IGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTF 75
Cdd:cd01136 70 IGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGREVREF 111
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