|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-585 |
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: 607.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 18 AGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQ--ILVNGRPRELRTFRKMSCYIMQDDMLLPHL 95
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 96 TVLEAMMVSANLKLSEK--QEVKKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPT 167
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 168 SGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADF 247
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 248 IIEVASGEYGDLNPMlfRAVQNGLCAmAEKKSSPEKNEVPAPCPPCPPEVDPI------ESHTFATSTLTQFCILFKRTF 321
Cdd:TIGR00955 275 YVQVLAVIPGSENES--RERIEKICD-SFAVSDIGRDMLVNTNLWSGKAGGLVkdsenmEGIGYNASWWTQFYALLKRSW 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 322 LSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNYWY 401
Cdd:TIGR00955 352 LSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 402 SLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTA 481
Cdd:TIGR00955 432 RVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFV 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 482 IPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG-MERGDLTC--LEERCPFrEPQSILRALDVEDAKLYMD 558
Cdd:TIGR00955 512 IPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSdVDNIECTSanTTGPCPS-SGEVILETLSFRNADLYLD 590
|
570 580
....*....|....*....|....*..
gi 1131742492 559 FLVLGIFFLALRLLAYLVLRYRVKSER 585
Cdd:TIGR00955 591 LIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-222 |
2.10e-89 |
|
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: 274.43 E-value: 2.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES-GMKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTV 97
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEAMMVSANLKlsekqevkkelvteiltalGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 177
Cdd:cd03213 100 RETLMFAAKLR-------------------GL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 178 VVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-583 |
7.28e-82 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 269.83 E-value: 7.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELRTFRKMScYIMQDDMLLPHLTVLE 99
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKL--SEKQEVKKELVTEILTALGLMSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:PLN03211 160 TLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 173 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVA 252
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 253 SGeYGDLNPMLFRA---VQNGLCAMAEKKSSPEKNEVPAPCPPCPPEVDPIESHTFA----------TSTLTQFCILFKR 319
Cdd:PLN03211 320 NG-VCQTDGVSEREkpnVKQSLVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKehrssdrisiSTWFNQFSILLQR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 320 TfLSILRDTVLTHLRFMSHVVIGVLIGLLYLHigDDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNY 399
Cdd:PLN03211 399 S-LKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 400 WYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPV 479
Cdd:PLN03211 476 MYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTV 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 480 TAIPVLLFSGFFVSfkTIPTYLQWSSYLSYVRYGFEGVILTIYGMERGDLTCLEERCPFREPQSILRALDVE---DAKLY 556
Cdd:PLN03211 556 TMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLLGCSLPHGSDRASCKFVEEDvagQISPA 633
|
570 580
....*....|....*....|....*..
gi 1131742492 557 MDFLVLGIFFLALRLLAYLVLRyRVKS 583
Cdd:PLN03211 634 TSVSVLIFMFVGYRLLAYLALR-RIKH 659
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-523 |
4.30e-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: 4.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 23 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGM--KGQILVNGRPRElRTFRKMSCYIMQDDMLLPHLTVLEA 100
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVSANLKLSEK--QEVKKELVTEILTALGLMSCSHTRTAL----LSGGQRKRLAIALELVNNPP-VMFFDEPTSGLDSA 173
Cdd:TIGR00956 857 LRFSAYLRQPKSvsKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQ 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 174 SCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQG-QCIFKGVV----TNLIPYLKGLGLH-CPTYHNPADF 247
Cdd:TIGR00956 937 TAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLgensHTIINYFEKHGAPkCPEDANPAEW 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 248 IIEVASGEYGD----------LNPMLFRAVQNGLCAM------AEKKSSPEKNevpapcppcppevdpiesHTFATSTLT 311
Cdd:TIGR00956 1017 MLEVIGAAPGAhanqdyhevwRNSSEYQAVKNELDRLeaelskAEDDNDPDAL------------------SKYAASLWY 1078
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 312 QFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFfsMLFLMFAALMPTVL-TF-PLEM 389
Cdd:TIGR00956 1079 QFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVF--MATVLFNPLIQQYLpPFvAQRD 1156
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 390 AVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTG-------QPAETSRFLLFSALATATALVAQSLGLL 462
Cdd:TIGR00956 1157 LYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGfywnaskTGQVHERGVLFWLLSTMFFLYFSTLGQM 1236
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 463 IGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG 523
Cdd:TIGR00956 1237 VISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-222 |
5.47e-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: 199.03 E-value: 5.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 20 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG--MKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTV 97
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEAMMVSANLKLSEKQ---EVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:cd03234 99 RETLTYTAILRLPRKSsdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131742492 175 CFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-523 |
2.37e-54 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 199.69 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 23 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAM 101
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKLSekQEVKKE----LVTEILTALGLMSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:PLN03140 975 IYSAFLRLP--KEVSKEekmmFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 173 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKGVV----TNLIPYLKGL-GL-HCPTYHNPA 245
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYFEAIpGVpKIKEKYNPA 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 246 DFIIEVASgeygdlnpmLFRAVQNGLCAMAEKKSSP----EKNEVPAPCPPCPPEVDPIESHTFATSTLTQFCILFKRTF 321
Cdd:PLN03140 1133 TWMLEVSS---------LAAEVKLGIDFAEHYKSSSlyqrNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQW 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 322 LSILRDTVLTHLRFMSHVVIGVLIGLLYLHIG---DDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLN 398
Cdd:PLN03140 1204 WTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGtkrSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAA 1283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 399 YWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVAT-FVG 477
Cdd:PLN03140 1284 GMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAiFAA 1363
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1131742492 478 PVTAIpVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG 523
Cdd:PLN03140 1364 AFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG 1408
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-222 |
2.41e-53 |
|
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: 180.13 E-value: 2.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRElRTFRKMSCYIMQDDMLLPHLTVLE 99
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKlsekqevkkelvteiltalGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:cd03232 99 ALRFSALLR-------------------GL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 180 SLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKG 222
Cdd:cd03232 149 RFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-518 |
2.02e-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: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 10 KQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES---GMKGQILVNGRPRE--LRTFRKMSCY 84
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhiGVEGVITYDGITPEeiKKHYRGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDDMLLPHLTVLEAMMVSANLK-------LSEKQEVKKELVTEILTALGLmscSHTRTAL--------LSGGQRKRLA 149
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGL---SHTRNTKvgndfvrgVSGGERKRVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 150 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI 228
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 229 PYLKGLGLHCPTYHNPADFIIEVAS-------GEYGDLNPM-------LFRAVQNGLCAMAEKKSSPEKNEVPAPCPPCP 294
Cdd:TIGR00956 300 QYFEKMGFKCPDRQTTADFLTSLTSpaerqikPGYEKKVPRtpqefetYWRNSPEYAQLMKEIDEYLDRCSESDTKEAYR 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 295 PEVDPIES-HTFATSTLT-----QFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFF 368
Cdd:TIGR00956 380 ESHVAKQSkRTRPSSPYTvsfsmQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFF 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 369 SMLFLMFAALMPTVLTFplEMAVFMREHLNY-WYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSA 447
Cdd:TIGR00956 460 AILFNAFSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLL 537
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 448 LATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVI 518
Cdd:TIGR00956 538 ILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
316-518 |
3.60e-47 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 163.98 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 316 LFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASkVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMRE 395
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 396 HLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATF 475
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1131742492 476 VGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVI 518
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
35-228 |
9.05e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.60 E-value: 9.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK-LSE 111
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYgLPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 KQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 191
Cdd:COG1131 106 KE--ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1131742492 192 IICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 228
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 ... |
8-217 |
1.05e-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: 149.54 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCY 84
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQ--DDMLLpHLTVLEAMMVSA-NLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVM 161
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1131742492 162 FFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 217
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
33-217 |
5.76e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.19 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAgyresGM----KGQILVNGRP------RELRTFRKMSC-YIMQDDMLLPHLTVLEAM 101
Cdd:COG1136 33 AGEFVAIVGPSGSGKSTLLNILG-----GLdrptSGEVLIDGQDisslseRELARLRRRHIgFVFQFFNLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKlSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 181
Cdd:COG1136 108 ALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1131742492 182 MKSLA-QGGRTIICTIHqpSAKLFEMFDKLYILSQGQ 217
Cdd:COG1136 187 LRELNrELGTTIVMVTH--DPELAARADRVIRLRDGR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-222 |
1.94e-38 |
|
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: 141.32 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRP---RELRTFRKMSCYIMQ--DDMLLpH 94
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNLRELRRKVGLVFQnpDDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 95 LTVLEAMMVS-ANLKLSEKqEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 173
Cdd:COG1122 91 PTVEEDVAFGpENLGLPRE-EIR-ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1131742492 174 SCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:COG1122 169 GRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADG 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
35-217 |
6.41e-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: 139.55 E-value: 6.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP------RELRTFR--KMScYIMQDDMLLPHLTVLEAMMVSAN 106
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseKELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 LKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 186
Cdd:cd03255 109 LAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 1131742492 187 -QGGRTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:cd03255 188 kEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
35-224 |
7.45e-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: 134.60 E-value: 7.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 112
Cdd:COG4555 28 EITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDvrKEPREARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 QEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 192
Cdd:COG4555 107 EELKKR-IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV 185
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 193 ICTIHQPS--AKLfemFDKLYILSQGQCIFKGVV 224
Cdd:COG4555 186 LFSSHIMQevEAL---CDRVVILHKGKVVAQGSL 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-219 |
2.74e-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: 132.24 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLT 96
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG-ELRPTSGTAYINGYSirTDRKAARQSLGYCPQFDALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEAMMVSANLK-LSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 175
Cdd:cd03263 92 VREHLRFYARLKgLPKSEI--KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1131742492 176 FQVVSLMKSLaQGGRTIICTIHqpSAKLFEMF-DKLYILSQGQ--CI 219
Cdd:cd03263 170 RAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKlrCI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-222 |
4.39e-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: 132.24 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR------ELRTFRKMSCYIMQDDML 91
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglseaELYRLRRRMGMLFQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 92 LPHLTVLE--AMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:cd03261 89 FDSLTVFEnvAFPLREHTRLSE--EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 170 LDSASCFQVVSLMKSL--AQGGRTIICTiHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03261 167 LDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-222 |
5.32e-35 |
|
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: 131.92 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYREsGMKGQILVNG------RPRELRTFRKM 81
Cdd:cd03256 2 EVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGSVLIDGtdinklKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 SCYIMQDDMLLPHLTVLEAMMV---------SANLKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIAL 152
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSgrlgrrstwRSLFGLFPKEE--KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 153 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 222
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-168 |
2.44e-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: 124.30 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLTVLEA 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 101 MMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTS 168
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-517 |
5.32e-33 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 135.36 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 22 TLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMK--GQILVNGRprELRTF--RKMSCYIMQDDMLLPHLTV 97
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGY--RLNEFvpRKTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEAMMVSAN--------------------------------LKLSEKQEVKKELVTE-ILTALGLMSCSHTRTAL----- 139
Cdd:PLN03140 257 KETLDFSARcqgvgtrydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDyTLKILGLDICKDTIVGDemirg 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQC 218
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 219 IFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGE-----YGDLN-PMLFRAV----------------QNGLCAMAE 276
Cdd:PLN03140 417 VYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKdqeqyWADRNkPYRYISVsefaerfksfhvgmqlENELSVPFD 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 277 KKSSPEknevpapcppcppEVDPIESHTFATSTLTQFCilFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHI---- 352
Cdd:PLN03140 497 KSQSHK-------------AALVFSKYSVPKMELLKAC--WDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTemht 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 353 ---GDDASKVfnntGCLFFSMLFLMFAALMPTVLTFPlEMAVFMRE-----HLNYWYSLKAYYLAktmadVPFQVVCPVV 424
Cdd:PLN03140 562 rneEDGALYI----GALLFSMIINMFNGFAELALMIQ-RLPVFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVV 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 425 YCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWS 504
Cdd:PLN03140 632 WVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWA 711
|
570
....*....|...
gi 1131742492 505 SYLSYVRYGFEGV 517
Cdd:PLN03140 712 YWVSPLSYGFNAL 724
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-217 |
7.93e-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: 123.66 E-value: 7.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVL 98
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 EammvsaNLKLSekqevkkelvteiltalglmscshtrtallsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:cd03230 92 E------NLKLS-------------------------------GGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 1131742492 179 VSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQ 217
Cdd:cd03230 135 WELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
2.29e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREVkqlarGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRE---LRTFRK 80
Cdd:COG4619 1 LELEGL-----SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-DPPTSGEIYLDGKPLSampPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MSCYIMQDdmllphlTVLEAMMVSANLKLS---EKQEVKKELVTEILTALGL-MSCSHTRTALLSGGQRKRLAIALELVN 156
Cdd:COG4619 75 QVAYVPQE-------PALWGGTVRDNLPFPfqlRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 157 NPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 217
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-223 |
3.24e-32 |
|
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: 124.33 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG------RPRELRTFRKM 81
Cdd:TIGR02315 3 EVENLSKVYPNG-KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLEGtditklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 SCYIMQDDMLLPHLTVLEAMMVSA-------NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALEL 154
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 155 VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFEmfDKLYILSQGQCIFKGV 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFDGA 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
36-222 |
7.14e-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: 122.30 E-value: 7.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 36 LIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 113
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 114 EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTII 193
Cdd:cd03264 106 EVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVI 183
|
170 180
....*....|....*....|....*....
gi 1131742492 194 CTIHQPSaKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03264 184 LSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-217 |
1.02e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 120.75 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-----RELRTFRKMSCYIMQDDMLLP 93
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEDltdleDELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 94 HLTVLEammvsaNLklsekqevkkelvteiltALGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 173
Cdd:cd03229 90 HLTVLE------NI------------------ALGL-----------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 174 SCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 217
Cdd:cd03229 135 TRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-222 |
3.80e-31 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 120.06 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 15 GHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES--GMKGQILVNGRP--RELRTFRKMSCYIMQDDM 90
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPykEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 91 LLPHLTVLEAMMVSANLKLSEKqeVKKelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:cd03233 94 HFPTLTVRETLDFALRCKGNEF--VRG----------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 171 DSASCFQVVSLMKSLAQG-GRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03233 150 DSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
33-197 |
5.01e-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: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP------RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 106
Cdd:cd03292 26 AGEFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYENVAFALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 LKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 186
Cdd:cd03292 105 VTGVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKIN 183
|
170
....*....|.
gi 1131742492 187 QGGRTIICTIH 197
Cdd:cd03292 184 KAGTTVVVATH 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-227 |
5.42e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 120.93 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREV-KQLARGHTAgyktlLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNG------RPRELR 76
Cdd:COG3638 3 LELRNLsKRYPGGTPA-----LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGqdvtalRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 77 TFRKMSCYIMQDDMLLPHLTVLEAMMV---------SANLKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKR 147
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgrtstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 148 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKGVVT 225
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDGPPA 232
|
..
gi 1131742492 226 NL 227
Cdd:COG3638 233 EL 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-197 |
6.52e-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: 119.67 E-value: 6.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKtLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPRELRTFRKMSCYIM 86
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 87 QD-DMLLPHLTVLEAMMVSANLkLSEKQEVkkelVTEILTALGL--MSCSHTRTalLSGGQRKRLAIALELVNNPPVMFF 163
Cdd:cd03226 78 QDvDYQLFTDSVREELLLGLKE-LDAGNEQ----AETVLKDLDLyaLKERHPLS--LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 164 DEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-199 |
7.72e-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: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHtaGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELR--TFRKMSCYI 85
Cdd:COG4133 4 EAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNGEPIRDAreDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 86 MQDDMLLPHLTVLEAMMVSANLKlseKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 166 PTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQP 199
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
33-222 |
1.96e-30 |
|
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: 119.08 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR------PREL------RTFRKMScyimqddmLLPHLTVLE 99
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLFDGEditglpPHEIarlgigRTFQIPR--------LFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKLSE---------KQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:cd03219 95 NVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 171 DSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03219 175 NPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-217 |
4.13e-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: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 16 HTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP---RELRTFRKMSCYIMQddmll 92
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDGKDiakLPLEELRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 93 phltvleammvsanlklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 173 ASCFQVVSLMKSLAQGGRTIICTIHQPS-AKLFemFDKLYILSQGQ 217
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPElAELA--ADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-225 |
5.63e-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: 5.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 13 ARGHTAGY--KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP------RELRtfRKMScY 84
Cdd:COG1120 4 AENLSVGYggRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrRELA--RRIA-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDDMLLPHLTVLEAMM------VSANLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNP 158
Cdd:COG1120 80 VPQEPPAPFGLTVRELVAlgryphLGLFGRPSAEDR---EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 159 PVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG----VVT 225
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQGppeeVLT 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
35-198 |
1.21e-29 |
|
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: 116.09 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNG-----RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 106
Cdd:cd03262 27 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGlkltdDKKNINELRQKVGMVFQQFNLFPHLTVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 --LKLSEKQEVKKELvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 184
Cdd:cd03262 103 kvKGMSKAEAEERAL--ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD 180
|
170
....*....|....
gi 1131742492 185 LAQGGRTIICTIHQ 198
Cdd:cd03262 181 LAEEGMTMVVVTHE 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-218 |
1.89e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.73 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLarghTAGY--KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRtfRKMSCYI 85
Cdd:COG1121 8 ELENL----TVSYggRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA--RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 86 MQD---DMLLPhLTVLEAMM------VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVN 156
Cdd:COG1121 81 PQRaevDWDFP-ITVRDVVLmgrygrRGLFRRPSRAD---REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 157 NPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQC 218
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-222 |
2.13e-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: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 31 FCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLE--AMM 102
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 182
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 183 KSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 222
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
33-226 |
2.91e-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: 112.57 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPreLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSE 111
Cdd:cd03293 29 EGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEP--VTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 KQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV-VSLMKSLAQGGR 190
Cdd:cd03293 105 KAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGK 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1131742492 191 TIICTIHQPSAKLFeMFDKLYILSQGQCIFKGVVTN 226
Cdd:cd03293 184 TVLLVTHDIDEAVF-LADRVVVLSARPGRIVAEVEV 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
21-222 |
6.39e-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: 112.00 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFR-KMScYIMQDDMLLP 93
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP-DSGEILVDGQditglsEKELYELRrRIG-MLFQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 94 HLTVLE--AMMVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:COG1127 96 SLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 172 SASCFQVVSLMKSL--AQGGRTIICTiHQ-PSAklFEMFDKLYILSQGQCIFKG 222
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 ... |
8-222 |
7.20e-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: 110.22 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHtaGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMq 87
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDLASLSPKELARKIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 88 ddmLLPhlTVLEAMMVSAnlkLSEKQevkkelVTEiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPT 167
Cdd:cd03214 77 ---YVP--QALELLGLAH---LADRP------FNE-----------------LSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 168 SGLDSASCFQVVSLMKSLA-QGGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 222
Cdd:cd03214 126 SHLDIAHQIELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-217 |
2.73e-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: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP-REL--RTFRKMSCY 84
Cdd:cd03228 2 EFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDGVDlRDLdlESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDDMLLpHLTVLEammvsaNLklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:cd03228 81 VPQDPFLF-SGTIRE------NI--------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:cd03228 122 EATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
24-197 |
5.30e-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: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHLTV 97
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRP-QSGAVLIDGEPldysrKGLLERRQRVGLVFQDpDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEAMMVSA-NLKLSEkQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:TIGR01166 87 DQDVAFGPlNLGLSE-AEVE-RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|.
gi 1131742492 177 QVVSLMKSLAQGGRTIICTIH 197
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTH 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-193 |
6.55e-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: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSG---KFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRP------RELRT 77
Cdd:COG1123 262 EVRNLSKRYPVRGKGGVRAVDDvslTLRRGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 78 FRKMSCYIMQD--DMLLPHLTVLEAMMVSA-NLKLSEKQEVKkELVTEILTALGLM-SCSHTRTALLSGGQRKRLAIALE 153
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLrLHGLLSRAERR-ERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 154 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTII 193
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYL 459
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
1.18e-26 |
|
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: 107.61 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREVkqlarGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTF 78
Cdd:cd03259 1 LELKGL-----SKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDGRdvtgvPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 79 rkmsCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNP 158
Cdd:cd03259 75 ----GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 159 PVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPS-AklFEMFDKLYILSQGQ 217
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-198 |
1.26e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.64 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFM---NILagyrESGMKGQILV-----NGRPRELRTFRKMSCYIMQDDM 90
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVdglkvNDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 91 LLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:PRK09493 88 LFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 1131742492 171 DSASCFQVVSLMKSLAQGGRTIICTIHQ 198
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
33-222 |
1.33e-26 |
|
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: 108.97 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR------PREL------RTFrkmscyimQDDMLLPHLTVLE 99
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDGRditglpPHRIarlgiaRTF--------QNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSA-------------NLKLSEKQEVK-KELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:COG0411 99 NVLVAAharlgrgllaallRLPRARREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131742492 166 PTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL-VMGLADRIVVLDFGRVIAEG 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-219 |
1.58e-26 |
|
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: 107.98 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTFRKMSCYIMQDDM--LLPHLTV----LEA 100
Cdd:cd03257 30 KGETLGLVGESGSGKSTLARAILGL-LKPTSGSIIFDGKDllklsrRLRKIRRKEIQMVFQDPMssLNPRMTIgeqiAEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVsanLKLSEKQEVKKELVTEILTALGLmscshTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:cd03257 109 LRI---HGKLSKKEARKEAVLLLLVGVGL-----PEEVLnrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 175 CFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCI 219
Cdd:cd03257 181 QAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
39-197 |
1.66e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.45 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAG-YRESgmKGQILVNG------RPRE---LRtfRKMScYIMQDDMLLPHLTVLEammvsaNLK 108
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrlKRREipyLR--RRIG-VVFQDFRLLPDRTVYE------NVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LS------EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 182
Cdd:COG2884 102 LPlrvtgkSRKEIRRR-VREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL 180
|
170
....*....|....*
gi 1131742492 183 KSLAQGGRTIICTIH 197
Cdd:COG2884 181 EEINRRGTTVLIATH 195
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
35-217 |
3.63e-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: 113.39 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLS 110
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGlYEPT--SGRILIDGIDLrqiDPASLRRQIGVVLQDVFLF-SGTIRE------NITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 eKQEVKKELVTEILTALGLMS--CSH---------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:COG2274 573 -DPDATDEEIIEAARLAGLHDfiEALpmgydtvvgEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
170 180 190
....*....|....*....|....*....|....*...
gi 1131742492 180 SLMKSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:COG2274 652 ENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGR 686
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
35-199 |
3.72e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 106.76 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLE--AMMVSAN 106
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPP-DSGRILWNGQdltalpPAE----RPVS-MLFQENNLFPHLTVAQniGLGLRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 LKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 186
Cdd:COG3840 100 LKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170
....*....|....
gi 1131742492 187 QG-GRTIICTIHQP 199
Cdd:COG3840 177 RErGLTVLMVTHDP 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-228 |
4.18e-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: 106.90 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 15 GHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRELRTFRKMSCYIMQD 88
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 89 DMLLPHLTVLEAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 168
Cdd:cd03258 91 FNLLSSRTVFENVALPLEIAGVPKAEIEER-VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 169 GLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 228
Cdd:cd03258 170 ALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-222 |
8.52e-26 |
|
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: 104.99 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARghTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR--PRELRTFRKMSCy 84
Cdd:cd03268 2 KTNDLTK--TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDS--GEITFDGKsyQKNIEALRRIGA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIRKKRID-----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-216 |
8.74e-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: 105.31 E-value: 8.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLA---RGHTAgyktlLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG----YResgmkGQILVNGRPreLRTFRK 80
Cdd:cd03235 1 EVEDLTvsyGGHPV-----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllkpTS-----GSIRVFGKP--LEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MSCYIMQD---DMLLPhLTVLEAMM------VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIA 151
Cdd:cd03235 69 RIGYVPQRrsiDRDFP-ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 152 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQG 216
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-217 |
1.85e-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: 105.27 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGY--KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTFRKMS 82
Cdd:COG1124 3 EVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 83 CYIMQDDM--LLPHLTVLEAmmVSANLKLSEKQEVKKElVTEILTALGLmscshTRTAL------LSGGQRKRLAIALEL 154
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRI--LAEPLRIHGLPDREER-IAELLEQVGL-----PPSFLdryphqLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 155 VNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPSAKLFeMFDKLYILSQGQ 217
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGR 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-228 |
2.33e-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: 110.23 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-REL--RTFRKMSCYIMQDDMLlPHLTV 97
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSILINGVDlSDLdpASWRRQIAWVPQNPYL-FAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEammvsaNLKLSE----KQEVKKEL----VTEILTAL--GLmscsHTRT----ALLSGGQRKRLAIALELVNNPPVMFF 163
Cdd:COG4988 428 RE------NLRLGRpdasDEELEAALeaagLDEFVAALpdGL----DTPLgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 164 DEPTSGLDSASCFQVVSLMKSLAQGGRTIICTiHQPSakLFEMFDKLYILSQGQCIFKGVVTNLI 228
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-222 |
3.57e-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: 103.53 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------------PRElrtfRKMScYIMQDDMLLPHLTVLEAMM 102
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 VSANLKlseKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 182
Cdd:cd03297 98 FGLKRK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1131742492 183 KSLAQ--GGRTIICTiHQPSaKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03297 175 KQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-222 |
4.15e-25 |
|
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: 109.22 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGY--RESGMKGQILVNGR-----PRELRtfRK 80
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRdllelSEALR--GR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MSCYIMQDDM--LLPhLTVLEAMM-VSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNN 157
Cdd:COG1123 84 RIGMVFQDPMtqLNP-VTVGDQIAeALENLGLSRAE--ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131742492 158 PPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG 222
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDG 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-217 |
1.28e-24 |
|
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: 101.86 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 20 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPR-ELRTFRKMSCYIMQDDMLLPHLTVL 98
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-IEPASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 E--AMMVSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:TIGR01277 89 QniGLGLHPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1131742492 177 QVVSLMKSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 217
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGK 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-171 |
1.63e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.86 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLAR--GHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRElRTFRKMScYI 85
Cdd:COG1116 9 ELRGVSKrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPVT-GPGPDRG-VV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 86 MQDDMLLPHLTVLEAMMVSANLKLSEKQEvKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMF 162
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGL---AGFEDAYphqLSGGMRQRVAIARALANDPEVLL 161
|
....*....
gi 1131742492 163 FDEPTSGLD 171
Cdd:COG1116 162 MDEPFGALD 170
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-222 |
1.65e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLlKCLSGKFCRRELIGIMGPSGAGKST-FMNILAGYRESgmKGQILVNGRP-----RELRTFRKM 81
Cdd:PRK13639 3 ETRDLKYSYPDGTEAL-KGINFKAEKGEMVALLGPNGAGKSTlFLHFNGILKPT--SGEVLIKGEPikydkKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 SCYIMQ--DDMLL-PhlTVLEAMMVSA-NLKLSeKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNN 157
Cdd:PRK13639 80 VGIVFQnpDDQLFaP--TVEEDVAFGPlNLGLS-KEEVEKR-VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131742492 158 PPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQpsAKLFEMF-DKLYILSQGQCIFKG 222
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
33-227 |
1.74e-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: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGY-RESGmkGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKl 109
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLY- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQG 188
Cdd:cd03265 102 GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1131742492 189 GRTIICTIH-QPSAKlfEMFDKLYILSQGQCIFKGVVTNL 227
Cdd:cd03265 182 GMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-199 |
2.04e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.89 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 6 LREVKQLARGHTAGYKTL--LKCLSGKFCRRELIGIMGPSGAGKSTFMNIL-------AG-YRESGMKGQILVNGRPREL 75
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 76 RtfRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELV 155
Cdd:PRK10535 84 R--REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 156 NNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQP 199
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-222 |
2.06e-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: 107.54 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELR--TFRKMSCY 84
Cdd:COG4987 335 ELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLGGVDlRDLDedDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDdmllPHL---TVLEammvsaNLKLSeKQEVKKELVTEILTALGL--MSCS-----HTRT----ALLSGGQRKRLAI 150
Cdd:COG4987 414 VPQR----PHLfdtTLRE------NLRLA-RPDATDEELWAALERVGLgdWLAAlpdglDTWLgeggRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 151 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 222
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILVLEDGRIVEQG 551
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
35-206 |
2.70e-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: 101.61 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGRP-----RELRTFRKMSCYIMQDDMLLPHLTVLE----AMM 102
Cdd:COG1126 28 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDltdskKDINKLRRKVGMVFQQFNLFPHLTVLEnvtlAPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 VSanLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 182
Cdd:COG1126 104 KV--KKMS-KAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVM 179
|
170 180
....*....|....*....|....
gi 1131742492 183 KSLAQGGRTIICTIHqpsaklfEM 206
Cdd:COG1126 180 RDLAKEGMTMVVVTH-------EM 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
35-171 |
5.24e-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: 100.77 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 113
Cdd:cd03300 27 EFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131742492 114 EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:cd03300 106 EIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
35-222 |
9.24e-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: 99.59 E-value: 9.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG------RPRELRtfRKMScYIMQDdmllPHL---TVLEammvsa 105
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGLYKP-TSGSVLLDGtdirqlDPADLR--RNIG-YVPQD----VTLfygTLRD------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSeKQEVKKELVTEILTALGLMSCSHT-----------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:cd03245 97 NITLG-APLADDERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131742492 175 CFQVVSLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03245 176 EERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-200 |
3.23e-23 |
|
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: 98.66 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREV-KQLARGhtAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELR 76
Cdd:COG4181 9 IELRGLtKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGQDlfaldeDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 77 TFRKMSC-YIMQDDMLLPHLTVLEAMMVSANLKlSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELV 155
Cdd:COG4181 86 RLRARHVgFVFQSFQLLPTLTALENVMLPLELA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 156 NNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPS 200
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-222 |
4.22e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.35 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMScYIMQDDMLLPHLTVL 98
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 EAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:cd03269 89 DQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 179 VSLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03269 168 KDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
35-216 |
4.92e-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: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILV-----------NGRPRELRTFRKMSCYIMQDDMLLPHLTVLEA 100
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLlrcINLL----EQPEAGTIRVgditidtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:PRK11264 106 IIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 181 LMKSLAQGGRTIICTIHQPS-----AKLFEMFDKLYILSQG 216
Cdd:PRK11264 186 TIRQLAQEKRTMVIVTHEMSfardvADRAIFMDQGRIVEQG 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
33-222 |
6.23e-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: 97.50 E-value: 6.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLK 108
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSEKQEVKKELVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:cd03224 104 RRAKRKARLERVYELFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 189 GRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03224 182 GVTIL-LVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-198 |
7.66e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGkfcrrELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR---------PRELRTFRKMSCYIMQDDML 91
Cdd:COG4161 23 LECPSG-----ETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 92 LPHLTVLEAMmVSAN---LKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 168
Cdd:COG4161 94 WPHLTVMENL-IEAPckvLGLSKEQAREK--AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 1131742492 169 GLDSASCFQVVSLMKSLAQGGRTIICTIHQ 198
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-183 |
1.46e-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: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR-----PRELRTFrkmsCYIMQDDMLLPHLTVL 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGKditnlPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 EAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
....*
gi 1131742492 179 VSLMK 183
Cdd:cd03299 169 REELK 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
35-222 |
9.63e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 9.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGY----RESGMKGQILVN-----GR-PRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVS 104
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRtvqreGRlARDIRKSRANTGYIFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 105 A-------NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 177
Cdd:PRK09984 111 AlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 178 VVSLMKSLAQG-GRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 222
Cdd:PRK09984 191 VMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-173 |
1.00e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREVkQLARGHtagyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG--MKGQILVNGRP-RELRTFRK 80
Cdd:COG4136 2 LSLENL-TITLGG----RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRlTALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MSCYIMQDDMLLPHLTVLE--AMMVSANLKLSEKqevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNP 158
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGEnlAFALPPTIGRAQR----RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170
....*....|....*
gi 1131742492 159 PVMFFDEPTSGLDSA 173
Cdd:COG4136 153 RALLLDEPFSKLDAA 167
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-217 |
1.15e-21 |
|
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: 93.47 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLL 92
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGRdvtdlpPKD----RDIA-MVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 93 PHLTVLEAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1131742492 173 ASCFQVVSLMKSLAQG-GRTIICTIH-QPSAklFEMFDKLYILSQGQ 217
Cdd:cd03301 164 KLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
35-217 |
1.17e-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: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHlTVLEAmmvsanlklse 111
Cdd:cd03246 29 ESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISqwdPNELGDHVGYLPQDDELFSG-SIAEN----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 kqevkkelvteiltalglmscshtrtaLLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 191
Cdd:cd03246 96 ---------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT 148
|
170 180
....*....|....*....|....*.
gi 1131742492 192 IICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:cd03246 149 RIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-171 |
1.44e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 96.32 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLEammvsaN-- 106
Cdd:COG3842 32 EFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGRdvtglpPEK----RNVG-MVFQDYALFPHLTVAE------Nva 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 107 --LKLS--EKQEVkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:COG3842 100 fgLRMRgvPKAEI-RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-198 |
2.02e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGkfcrrELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGR---------PRELRTFRKMSCYIMQDDMLLPH 94
Cdd:PRK11124 23 LDCPQG-----ETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 95 LTVLE-----AMMVsanLKLSEKQEVKKELvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:PRK11124 97 LTVQQnlieaPCRV---LGLSKDQALARAE--KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|....*....
gi 1131742492 170 LDSASCFQVVSLMKSLAQGGRTIICTIHQ 198
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
35-172 |
2.12e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-------PRElrtfRKMScYIMQDDMLLPHLTVLEammvsaN- 106
Cdd:COG1118 29 ELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGRdlftnlpPRE----RRVG-FVFQHYALFPHMTVAE------Ni 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 107 ------LKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:COG1118 97 afglrvRPPSKAE--IRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
33-227 |
2.65e-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: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGY-RESGmkGQILVNG-----RPRELR-----TFRKMSCYimqDDmllphLTVLEAM 101
Cdd:TIGR01188 18 EGEVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGydvvrEPRKVRrsigiVPQYASVD---ED-----LTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLK-LSEKqeVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:TIGR01188 88 EMMGRLYgLPKD--EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1131742492 181 LMKSLAQGGRTIICTIHQpsakLFE---MFDKLYILSQGQCIFKGVVTNL 227
Cdd:TIGR01188 166 YIRALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-173 |
2.68e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.11 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG----------RPRELrtfrkmscyIMQDDMLLPHLTVLE--AMM 102
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGqdhtttppsrRPVSM---------LFQENNLFSHLTVAQniGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 103 VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 173
Cdd:PRK10771 96 LNPGLKLNAAQ---REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
34-200 |
2.91e-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: 97.36 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 34 RELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQddmlLPHLTvleAMMVSANLKLS 110
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGVPLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EKqEVKKELVTEILTALGLMSCS-------HT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:TIGR02857 420 RP-DASDAEIREALERAGLDEFVaalpqglDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180
....*....|....*....|.
gi 1131742492 180 SLMKSLAQgGRTIICTIHQPS 200
Cdd:TIGR02857 499 EALRALAQ-GRTVLLVTHRLA 518
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
35-228 |
6.95e-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: 91.84 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTfRKMSCYIMQDDMLLPHLTVLEAMMVSANLKL 109
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGL-VKPDSGKILLDGQditklPMHKRA-RLGIGYLPQEASIFRKLTVEENILAVLEIRG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQEVKKELVtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 189
Cdd:cd03218 105 LSKKEREEKLE-ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1131742492 190 RTIICTIHQPSAKLfEMFDKLYILSQGQCIFKGVVTNLI 228
Cdd:cd03218 184 IGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-222 |
7.66e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 23 LLKCLSGKFCRRELIGIMGPSGAGKST-FMNILAGYRESgmKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHL 95
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTlFMNLSGLLRPQ--KGAVLWQGKPldyskRGLLALRQQVATVFQDpEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 96 TVLEAMMVS-ANLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:PRK13638 94 DIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131742492 175 CFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-197 |
8.03e-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: 91.47 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMK----GQILVNGR--------PRELRTFRKMscyIM 86
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGKdiydldvdVLELRRRVGM---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 87 QDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:cd03260 88 QKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190
....*....|....*....|....*....|...
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQgGRTIICTIH 197
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
35-228 |
1.12e-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: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR------PRELRTFRK---MscyIMQDDMLLPHLTVLEamm 102
Cdd:COG1135 32 EIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdltalsERELRAARRkigM---IFQHFNLLSSRTVAE--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 vsaN----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:COG1135 102 ---NvalpLEIAgvPKAEIRKR-VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 177 QVVSLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTNLI 228
Cdd:COG1135 178 SILDLLKDInRELGLTIVLITH-------EMdvvrriCDRVAVLENGRIVEQGPVLDVF 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
35-197 |
1.15e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 91.79 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR----------------PRELRTFRKMSCYIMQDDMLLPHL 95
Cdd:COG4598 35 DVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGMVFQSFNLWSHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 96 TVLEAMM-----VsanLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:COG4598 111 TVLENVIeapvhV---LGRP-KAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180
....*....|....*....|....*..
gi 1131742492 171 DSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:COG4598 186 DPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-228 |
1.19e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR--PRELRTFRKMSCYIMQDDMLLPHLT 96
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVpvPARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEAMMVSANLKLSEKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 177 QVVSLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 228
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
35-222 |
1.24e-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: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHlTVLEammvsaNLKLSe 111
Cdd:cd03254 30 ETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISRKSLRSMIGVVLQDTFLFSG-TIME------NIRLG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 KQEVKKELVTEILTALGL----MSCSH-------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:cd03254 101 RPNATDEEVIEAAKEAGAhdfiMKLPNgydtvlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1131742492 181 LMKSLAQgGRTIICTIHQPSAKLFEmfDKLYILSQGQCIFKG 222
Cdd:cd03254 181 ALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-195 |
1.24e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 23 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---------RELRTfRKMScYIMQDDMLLP 93
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 94 HLTVLE--AM-MVSANLKLSEKQEVKKELvteiLTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*..
gi 1131742492 171 DSASCFQVVSLMKSL--AQGGRTIICT 195
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVT 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-198 |
1.80e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.18 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGR----------------PRELRTFRKMS 82
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 83 CYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVM 161
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1131742492 162 FFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQ 198
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
39-222 |
2.07e-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: 90.91 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPR------ELRTfrkmscYI------MQDDmLLPHLTVLEaMMVSA- 105
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggedvwELRK------RIglvspaLQLR-FPRDETVLD-VVLSGf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 ------NLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:COG1119 106 fdsiglYREPTDEQR---ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 180 SLMKSLAQ-GGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:COG1119 183 ALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAG 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-199 |
2.44e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 114
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFLGGEELD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 115 VkkelvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS-LAQGGRTII 193
Cdd:PRK13539 108 I-----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIA 182
|
....*.
gi 1131742492 194 CTiHQP 199
Cdd:PRK13539 183 AT-HIP 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
35-171 |
8.83e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.90 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR------PRElrtfRKMScyiM--QDDMLLPHLTVLEammvsa 105
Cdd:COG3839 30 EFLVLLGPSGCGKSTLLRMIAGlEDPTS--GEILIGGRdvtdlpPKD----RNIA---MvfQSYALYPHMTVYE------ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 106 N----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
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 ... |
8-199 |
1.35e-19 |
|
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: 87.16 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLarGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMSC-YI 85
Cdd:cd03231 2 EADEL--TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPlDFQRDSIARGLlYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 86 MQDDMLLPHLTVLEAMMVSANLKLSEKqevkkelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 166 PTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQP 199
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
33-222 |
3.78e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA- 105
Cdd:PRK13636 31 KGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPidysrKGLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSEKqEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:PRK13636 110 NLKLPED-EVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEM 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1131742492 186 AQG-GRTIICTIHQ-PSAKLFemFDKLYILSQGQCIFKG 222
Cdd:PRK13636 188 QKElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQG 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-228 |
4.29e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREVKQLArghtaGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR--PRELRTFRKM 81
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP-DAGSISLCGEpvPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 SCYIMQDDMLLPHLTVLEAMMVSAN-LKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPV 160
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRyFGLSAAA--ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 161 MFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 228
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
35-199 |
4.70e-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: 85.49 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPR-ELRTFRKMSC-YIMQDDMLLPHLTVLEAMMVSANLKLSEK 112
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPLaEQRDEPHENIlYLGHLPGLKPELSALENLHFWAAIHGGAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 QEVKkelvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS-LAQGGRT 191
Cdd:TIGR01189 106 RTIE-----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIV 180
|
....*...
gi 1131742492 192 IICTiHQP 199
Cdd:TIGR01189 181 LLTT-HQD 187
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
35-222 |
5.61e-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: 90.70 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNG------RPRELRtfRKMScYIMQDDMLLpHLTVLEammvsaNL 107
Cdd:TIGR03375 492 EKVAIIGRIGSGKSTLLKLLLGlYQPT--EGSVLLDGvdirqiDPADLR--RNIG-YVPQDPRLF-YGTLRD------NI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSeKQEVKKELVTEILTALGLMSC--SHT---------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:TIGR03375 560 ALG-APYADDEEILRAAELAGVTEFvrRHPdgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEE 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 177 QVVSLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 222
Cdd:TIGR03375 639 RFKDRLKRWL-AGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADG 681
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-217 |
1.17e-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: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRtfRKMScYIMQDDMLL 92
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPVELR--RKIG-YVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 93 PHLTVLEAmmVSANLKLSE-KQEVKKELVTEILTALGLMSCSHTR--TALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:cd03295 88 PHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 170 LDSASCFQVVSLMKSLAQG-GRTIICTIHQpsakLFEMF---DKLYILSQGQ 217
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQElGKTIVFVTHD----IDEAFrlaDRIAIMKNGE 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-222 |
1.29e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgmKGQILVNGRP------RELRTFRkmsCYIMQDDMLLPHLTV 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG--QGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEAMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGG--QRKRLAIALELV---NNPP--VMFFDEPTSGL 170
Cdd:COG4138 87 FQYLALHQPAGASS--EAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 171 DSAScfQVV--SLMKSLAQGGRTIICTIHQPSAKLFEMfDKLYILSQGQCIFKG 222
Cdd:COG4138 165 DVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASG 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-199 |
1.91e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---------RELRTfrKMSCYIMQDDMLLPHLTVLEAMMV 103
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdeearAKLRA--KHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 104 SANLKlSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 183
Cdd:PRK10584 112 PALLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170
....*....|....*..
gi 1131742492 184 SLAQG-GRTIICTIHQP 199
Cdd:PRK10584 191 SLNREhGTTLILVTHDL 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-193 |
3.19e-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: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 38 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRELRTFRK-------MscyIMQDDMLLPHLTVLEammvsaNLKL 109
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagiaI---IHQELNLVPNLSVAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SekQEVKK----------ELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:COG1129 103 G--REPRRgglidwramrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLF 180
|
170
....*....|....
gi 1131742492 180 SLMKSLAQGGRTII 193
Cdd:COG1129 181 RIIRRLKAQGVAII 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-187 |
3.67e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 17 TAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTfmNILAGYRESGMKGQILVNGRPRELRTFRKMSCY------IMQD-- 88
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVrhriqvVFQDpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 89 DMLLPHLTVLEamMVSANLKLSEKQ---EVKKELVTEILTALGLMSCSHTR-TALLSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:PRK15134 373 SSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180
....*....|....*....|...
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQ 187
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQ 473
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-216 |
4.35e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRE--SG--MKGQILVNGRPRELRTFrKMscyIMQDDMLLPHLTVLEAMmvSANLKLS 110
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGV-GM---VFQSYALYPHLSVAENM--SFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 --EKQEVKK--ELVTEILTALGLMScshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ----VVSLM 182
Cdd:PRK11000 104 gaKKEEINQrvNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQmrieISRLH 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1131742492 183 KSLaqgGRTIICTIH-QPSAklFEMFDKLYILSQG 216
Cdd:PRK11000 181 KRL---GRTMIYVTHdQVEA--MTLADKIVVLDAG 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-222 |
4.65e-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: 84.43 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR------PRELRTFRKMSCYIMQddmlLPH-- 94
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkKKKLKDLRKKVGLVFQ----FPEhq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 95 ---LTVLEAMM-VSANLKLSEKqEVKkELVTEILTALGL------MSCSHtrtalLSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:TIGR04521 95 lfeETVYKDIAfGPKNLGLSEE-EAE-ERVKEALELVGLdeeyleRSPFE-----LSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 222
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDG 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
35-217 |
5.62e-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: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP-RE--LRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLSE 111
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDiRDltLESLRRQIGVVPQDTFLF-SGTIRE------NIRYGR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 K----QEV----KKELVTEILTAL--GLmscsHT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 177
Cdd:COG1132 439 PdatdEEVeeaaKAAQAHEFIEALpdGY----DTvvgeRGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 178 VVSLMKSLAQgGRTIIcTI-HQPSAklFEMFDKLYILSQGQ 217
Cdd:COG1132 515 IQEALERLMK-GRTTI-VIaHRLST--IRNADRILVLDDGR 551
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-171 |
6.21e-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: 83.85 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 32 CRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP------RELRTFR--KMScYIMQDDMLLPHLTVLEAmmV 103
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEP-TSGKVLIDGQDiaamsrKELRELRrkKIS-MVFQSFALLPHRTVLEN--V 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 104 SANLKLS-EKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:cd03294 124 AFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
33-187 |
7.29e-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: 84.72 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAG-YRESGM-KGQILVNGR------PRELRTFR--KMScYIMQDDM--LLPHLTVLEA 100
Cdd:COG0444 30 RGETLGLVGESGSGKSTLARAILGlLPPPGItSGEILFDGEdllklsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MM--VSANLKLSEKQevKKELVTEILTALGLmscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD- 171
Cdd:COG0444 109 IAepLRIHGGLSKAE--ARERAIELLERVGL---PDPERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDv 183
|
170
....*....|....*...
gi 1131742492 172 --SAscfQVVSLMKSLAQ 187
Cdd:COG0444 184 tiQA---QILNLLKDLQR 198
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-217 |
8.02e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 84.85 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYrESGMKGQILVNG-----RPRELRTFRKMscyiMQDDMLLPHLTVLEAmmVSANLKL-SEK 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMrKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 QEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRT 191
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeQLGIT 153
|
170 180
....*....|....*....|....*.
gi 1131742492 192 IICTIHQPSAKLfEMFDKLYILSQGQ 217
Cdd:TIGR01187 154 FVFVTHDQEEAM-TMSDRIAIMRKGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
35-172 |
8.53e-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: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRTFRKMSC-YIMQDDMLLPHLTVLEAmmVSANLKLSEKQ 113
Cdd:cd03296 29 ELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEDATDVPVQERNVgFVFQHYALFRHMTVFDN--VAFGLRVKPRS 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 114 EV-----KKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:cd03296 106 ERppeaeIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-222 |
1.30e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 17 TAGY--KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTFRKMSCYIMqddmLLP- 93
Cdd:PRK11231 9 TVGYgtKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-QSGTVFLGDKPISMLSSRQLARRLA----LLPq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 94 HLTVLEAMMV--------SANL----KLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVM 161
Cdd:PRK11231 84 HHLTPEGITVrelvaygrSPWLslwgRLSAEDN---ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 162 FFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH---QPSaklfEMFDKLYILSQGQCIFKG 222
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
35-222 |
1.31e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGY--RESGmkgQILVNGR-----PRELRTFRKMScYIMQDDMLLPHLTVLEAMMVSANL 107
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDEdisllPLHARARRGIG-YLPQEASIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSEKQEVKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 184
Cdd:PRK10895 106 RDDLSAEQREDRANELMEEFHI---EHLRDSMgqsLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 1131742492 185 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 222
Cdd:PRK10895 183 LRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
35-222 |
1.39e-17 |
|
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: 81.65 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG-----RPRELRtfRKMScyIMQDDM-LLPHLTVLEAMMVSANLK 108
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGfdvvkEPAEAR--RRLG--FVSDSTgLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:cd03266 107 GLKGDELTAR-LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1131742492 189 GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 222
Cdd:cd03266 186 GKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-199 |
1.45e-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: 85.88 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 3 DLELREVKQLARGHTAGYKTLLKCLSG-----KFCRRelIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RE 74
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAPPVLDGvsldlPPGER--VAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 75 LRTFRKMSCYIMQDdmllPHL---TVLEammvsaNLKLSeKQEVKKELVTEILTALGL----------MSCS-HTRTALL 140
Cdd:TIGR02868 404 QDEVRRRVSVCAQD----AHLfdtTVRE------NLRLA-RPDATDEELWAALERVGLadwlralpdgLDTVlGEGGARL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 141 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSlAQGGRTIICTIHQP 199
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-224 |
1.82e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANL 107
Cdd:PRK13652 29 RNSRIAVIGPNGAGKSTLFRHFNGILKP-TSGSVLIRGEPitkENIREVRKFVGLVFQnpDDQIFSPTVEQDIAFGPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSEkqEVKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 184
Cdd:PRK13652 108 GLDE--ETVAHRVSSALHMLGL---EELRDRVphhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLND 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 185 LAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVV 224
Cdd:PRK13652 183 LPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
35-222 |
1.84e-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: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG---RPRELRTFRKMSCYIMQDDMLLpHLTVLEAMM--------- 102
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDGhdvRDYTLASLRRQIGLVSQDVFLF-NDTVAENIAygrpgatre 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 -VSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 181
Cdd:cd03251 107 eVEEAARAANAHEFIMELPEGYDTVIG------ERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 182 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 222
Cdd:cd03251 181 LERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVERG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-171 |
2.07e-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: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILvngRPRELRtfrkMScYIMQDDMLLPHLTVL 98
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVS---IPKGLR----IG-YLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 EAMMVS-------------ANLKLSEKQEVKKEL------------------VTEILTALGLMSCSHTR-TALLSGGQRK 146
Cdd:COG0488 80 DTVLDGdaelraleaeleeLEAKLAEPDEDLERLaelqeefealggweaearAEEILSGLGFPEEDLDRpVSELSGGWRR 159
|
170 180
....*....|....*....|....*
gi 1131742492 147 RLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLD 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-222 |
2.11e-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: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 31 FCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRE--LRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 108
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGKDIEtnLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 189 GRTIICTIHQPSAKLfeMFDKLYILSQGQCIFKG 222
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-282 |
3.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG----RPRELRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NLK 108
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGidtgDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPeNLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSeKQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:PRK13644 108 LP-PIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 189 GRTIICTIHqpSAKLFEMFDKLYILSQGQCIFKGVVTNLI--PYLKGLGLHCPTyhnpadfIIEVASgeygdlnpmlfRA 266
Cdd:PRK13644 186 GKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPS-------LIELAE-----------NL 245
|
250
....*....|....*.
gi 1131742492 267 VQNGLCAMAEKKSSPE 282
Cdd:PRK13644 246 KMHGVVIPWENTSSPS 261
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
35-171 |
3.43e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELR---TfrkmscyIMQDDMLLPHLTVLEAmmVSAN 106
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDGQdithvPAENRhvnT-------VFQSYALFPHMTVFEN--VAFG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 107 LKLSE--KQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK09452 111 LRMQKtpAAEIT-PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
5.39e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 1 MRDLELREVKqLARGHTagykTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG----YRESGMKGQILVNGR---PR 73
Cdd:PRK14247 1 MNKIEIRDLK-VSFGQV----EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQdifKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 74 ELRTFRKMSCYIMQDDMLLPHLTVLEAmmVSANLKLSEKQEVKKEL---VTEILTALGLMSCSHTR----TALLSGGQRK 146
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPIPNLSIFEN--VALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 147 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG---- 222
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGptre 231
|
....
gi 1131742492 223 VVTN 226
Cdd:PRK14247 232 VFTN 235
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
35-222 |
6.82e-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: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGR------PRELRtfRKMSCyIMQDDMLL------------PHLT 96
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVDGVdlaiadPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAP 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEammVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:TIGR01846 560 FEH---VIHAAKLAGAHDFISELPQGYNTEVG------EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 177 QVVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 222
Cdd:TIGR01846 631 LIMRNMREICR-GRTVIIIAHRLST--VRACDRIIVLEKGQIAESG 673
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-217 |
7.08e-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: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----------PRELRTFRkmscYIMQDDMLLPHLTVLEAMMV 103
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGRtlfdsrkgiflPPEKRRIG----YVFQEARLFPHLSVRGNLRY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 104 SANLKLSEKQEVKKELVTEILtalGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 183
Cdd:TIGR02142 99 GMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 184 SLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQ 217
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
35-222 |
7.66e-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: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLpHLTVLE-------AM--- 101
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF-NRSIRDnialadpGMsme 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 181
Cdd:cd03252 107 RVIEAAKLAGAHDFISELPEGYDTIVG------EQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 182 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 222
Cdd:cd03252 181 MHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
35-226 |
8.35e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.77 E-value: 8.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR------PRELRTFRKmscyimQDDMLLPHLTVLEAMMVSA 105
Cdd:PRK11153 32 EIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdltalsEKELRKARR------QIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 N----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:PRK11153 102 NvalpLELAgtPKAEIKAR-VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 180 SLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTN 226
Cdd:PRK11153 181 ELLKDInRELGLTIVLITH-------EMdvvkriCDRVAVIDAGRLVEQGTVSE 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-199 |
8.74e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 22 TLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYResgmkgqilvngRPRELRTFRKMSC---YIMQ---DDMLLPhL 95
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL------------RPTSGTVRRAGGArvaYVPQrseVPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 96 TVLEAMMVSANLKLSEKQEVKKE---LVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 1131742492 173 ASCFQVVSLMKSLAQGGRTIICTIHQP 199
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
33-172 |
9.64e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 9.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-------RELrtfrkmscyIMQDDMLLPHLTVLEAmmVSA 105
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgadRGV---------VFQKDALLPWLNVLDN--VAF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 106 NLKLS--EKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:COG4525 100 GLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-199 |
1.04e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE---SGMK--GQILVNGRPR---ELRTFRKMSCYIMQDDMLL 92
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKvdGKVLYFGKDIfqiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 93 PHLTVLEAmmVSANLK---LSEKQEVKKeLVTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:PRK14246 103 PHLSIYDN--IAYPLKshgIKEKREIKK-IVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 1131742492 166 PTSGLDSASCFQVVSLMKSLaQGGRTIICTIHQP 199
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-216 |
1.42e-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: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRTFRKMscYIMQDDMLLPHLTVLE--AMMVSANLKLSEK 112
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniALAVDRVLPDLSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 QEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS-LMKSLAQGGRT 191
Cdd:TIGR01184 89 SE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEeLMQIWEEHRVT 167
|
170 180
....*....|....*....|....*
gi 1131742492 192 IICTIHQPSAKLFeMFDKLYILSQG 216
Cdd:TIGR01184 168 VLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-222 |
1.68e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.39 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 17 TAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCY--IM-QDDMLLP 93
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPLAAWSPWELARRraVLpQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 94 HLTVLE--AMMVSANlklSEKQEVKKELVTEILTALGLMSCSHTRTALLSGG--QRKRLAIAL----ELVNNPP-VMFFD 164
Cdd:COG4559 89 PFTVEEvvALGRAPH---GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGeqQRVQLARVLaqlwEPVDGGPrWLFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSakLFEMF-DKLYILSQGQCIFKG 222
Cdd:COG4559 166 EPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQG 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-222 |
2.11e-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: 77.35 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPREL--RTFRKMSCYI 85
Cdd:cd03247 2 SINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 86 MQDdmllPHLtvleammvsanlklsekqevkkeLVTEILTALGLMscshtrtalLSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:cd03247 81 NQR----PYL-----------------------FDTTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 166 PTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 222
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
37-222 |
4.71e-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: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 37 IGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RE--LRTFRKMSCYIMQDdMLLPHLTVLEAMMVsANLKLSEKQ 113
Cdd:cd03253 30 VAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDGQDiREvtLDSLRRAIGVVPQD-TVLFNDTIGYNIRY-GRPDATDEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 114 EV---KKELVTEILTAL-----------GLMscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:cd03253 107 VIeaaKAAQIHDKIMRFpdgydtivgerGLK---------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1131742492 180 SLMKSLAQgGRTIICTIHQPS----AklfemfDKLYILSQGQCIFKG 222
Cdd:cd03253 178 AALRDVSK-GRTTIVIAHRLStivnA------DKIIVLKDGRIVERG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
35-219 |
5.23e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR------PRELRTFRKMscyimqddmlLPH-------LTVLE-- 99
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPAELARRRAV----------LPQhsslsfpFTVEEvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSAnlkLSEKQEVKKELVTEILTALGlmsCSHTRTAL---LSGG--QRKRLAIAL----ELVNNPPVMFFDEPTSGL 170
Cdd:PRK13548 98 AMGRAP---HGLSRAEDDALVAAALAQVD---LAHLAGRDypqLSGGeqQRVQLARVLaqlwEPDGPPRWLLLDEPTSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 171 DSASCFQVVSLMKSLA-QGGRTIICTIHqpSAKLFEMF-DKLYILSQGQCI 219
Cdd:PRK13548 172 DLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQGRLV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-227 |
5.45e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNIL-------AGYRESGmkgQILVNGRP----RELRTFRKMSCYIMQDD 89
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 90 MLLPhLTVLEAMMVSANL-KLSEKQEVKKeLVTEILTALGLMSCSHTRTA----LLSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhKLVPRKEFRG-VAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQggRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 227
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-219 |
9.49e-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: 74.77 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRkmscyimqddmllphltvlEAMmvsanlklsek 112
Cdd:cd03216 25 RGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKEVSFASPR-------------------DAR----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 qevkkelvteiltALGlMSCSHTrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 192
Cdd:cd03216 74 -------------RAG-IAMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAV 135
|
170 180 190
....*....|....*....|....*....|
gi 1131742492 193 ICTIHqpsaKLFEMF---DKLYILSQGQCI 219
Cdd:cd03216 136 IFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-197 |
1.02e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGRPREL---RTFRKMSCYIMQDdmlLPH--- 94
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLESwssKAFARKVAYLPQQ---LPAaeg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 95 LTVLEAMMVSA---NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK10575 100 MTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*..
gi 1131742492 172 SASCFQVVSLMKSLAQG-GRTIICTIH 197
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-174 |
1.22e-15 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 78.60 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 34 RELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTF-----RKMScYIMQDDMLLPHLTVLEammvsa 105
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 106 NLKLSEKQEVK---KELVTEILTALGLmscSH---TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:COG4148 97 NLLYGRKRAPRaerRISFDEVVELLGI---GHlldRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-222 |
1.73e-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: 76.04 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDdmllPHL---TV 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGvdiRDLNLRWLRSQIGLVSQE----PVLfdgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 98 LEAMMVSAN-LKLSEKQEV-KKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 173
Cdd:cd03249 94 AENIRYGKPdATDEEVEEAaKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 174 SCFQVvslMKSL--AQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 222
Cdd:cd03249 174 SEKLV---QEALdrAMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQG 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
35-171 |
2.37e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTFRKMscyiMQDDMLLPHLTVleammvSANLKL 109
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGVdlshvPPYQRPINMM----FQSYALFPHMTV------EQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 110 SEKQE--VKKEL---VTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK11607 115 GLKQDklPKAEIasrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-222 |
2.51e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.69 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRPRELRTFRKMScYimqddM-----LLPHLTVLEAMMVSANL 107
Cdd:COG4152 28 EIFGLLGPNGAGKTTTIRIILGilAPDSG---EVLWDGEPLDPEDRRRIG-Y-----LpeergLYPKMKVGEQLVYLARL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqvVSLMKS--- 184
Cdd:COG4152 99 KGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN----VELLKDvir 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1131742492 185 -LAQGGRTIICTIHQ-PSAKlfEMFDKLYILSQGQCIFKG 222
Cdd:COG4152 174 eLAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSG 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-222 |
3.88e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG---YResgmkGQILVNG---RPRELRTFRKMSCYIMQDDmLLPH 94
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLKINGielRELDPESWRKHLSWVGQNP-QLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 95 LTVLEAMMVsANLKLSE---KQEVKKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:PRK11174 437 GTLRDNVLL-GNPDASDeqlQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 170 LDSASCFQVVSLMKSLAQGGRTIICTiHQPSAkLFEMfDKLYILSQGQCIFKG 222
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQTTLMVT-HQLED-LAQW-DQIWVMQDGQIVQQG 565
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
35-170 |
3.92e-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: 75.02 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMS---CYIMQDDMLLPHLTVLEammvsaNLKL- 109
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPP-RSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVEE------NLLLg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 110 ----SEKQEVKK--ELVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:COG0410 103 ayarRDRAEVRAdlERVYELFPRLKERR--RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
38-193 |
4.07e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 38 GIMGPSGAGKSTFMNILAG-YR-ESgmkGQILVNGRPRELRTFRK-MSCYI-M--QDDMLLPHLTVLE----AMMVSANL 107
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGlYQpDS---GEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVAEnivlGLEPTKGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASCFQVvslMKS 184
Cdd:COG3845 112 RLDRKAARAR--IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADELFEI---LRR 186
|
....*....
gi 1131742492 185 LAQGGRTII 193
Cdd:COG3845 187 LAAEGKSII 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-222 |
5.54e-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: 74.68 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNG-RP--RELRTFRKMSCYIMQDDMLLPHLT 96
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEVRVAGlVPwkRRKKFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEAMMVSANLKLSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1131742492 177 QVVSLMKSL-AQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 222
Cdd:cd03267 191 NIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
35-216 |
8.28e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.35 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKmsCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 114
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 115 vKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTII 193
Cdd:PRK11248 105 -RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVL 183
|
170 180
....*....|....*....|...
gi 1131742492 194 CTIHQPSAKLFeMFDKLYILSQG 216
Cdd:PRK11248 184 LITHDIEEAVF-MATELVLLSPG 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
35-197 |
9.28e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 108
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:PRK10908 108 GASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
....*....
gi 1131742492 189 GRTIICTIH 197
Cdd:PRK10908 187 GVTVLMATH 195
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
35-199 |
9.31e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRP-RELRT-FRKMSCYIMQDDMLLPHLTVLEammvsaNLKLS 110
Cdd:PRK13538 28 ELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRDeYHQDLLYLGHQPGIKTELTALE------NLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EK--QEVKKELVTEILTALGL-----MSCSHtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 183
Cdd:PRK13538 99 QRlhGPGDDEALWEALAQVGLagfedVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
170
....*....|....*.
gi 1131742492 184 SLAQGGRTIICTIHQP 199
Cdd:PRK13538 174 QHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-222 |
9.57e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLlKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGR---PRELRTFRKMSCY 84
Cdd:PRK13647 6 EVEDLHFRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQD-DMLLPHLTVLEAMMVSA-NLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMF 162
Cdd:PRK13647 84 VFQDpDDQVFSSTVWDDVAFGPvNMGLD-KDEVE-RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 163 FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 222
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-217 |
1.05e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 38 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRELRTFRKM----SCYIMQDDMLLPHLTVLEAMMVS---ANLKL 109
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAENLYLGqlpHKGGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 189
Cdd:PRK11288 112 VNRRLLNYE-AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEG 190
|
170 180
....*....|....*....|....*...
gi 1131742492 190 RTIICTIHQpSAKLFEMFDKLYILSQGQ 217
Cdd:PRK11288 191 RVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
38-246 |
1.09e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 38 GIMGPSGAGKSTFMNILAGYRESGMK----GQILVNG--RPRELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKL 109
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGkvtvGDIVVSStsKQKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SeKQEVKKeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:PRK13643 116 P-KEKAEK-IAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 189 GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCPTYHNPAD 246
Cdd:PRK13643 194 GQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVfqeVDFLKAHELGVPKATHFAD 253
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-197 |
1.21e-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: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRelRTFRKMSCYIMQDDML---LPhLTVLEAMMVSANLKL 109
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQEVKKE---LVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 186
Cdd:TIGR03771 81 GWLRRPCVAdfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170
....*....|.
gi 1131742492 187 QGGRTIICTIH 197
Cdd:TIGR03771 161 GAGTAILMTTH 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
35-230 |
1.26e-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: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSE 111
Cdd:TIGR01193 501 SKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiDRHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQ 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 kQEVKKEL-VTEILTALGLMSCS-HTRTAL----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:TIGR01193 579 -DEIWAACeIAEIKDDIENMPLGyQTELSEegssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 186 AQggRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGVVTNLIPY 230
Cdd:TIGR01193 658 QD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-222 |
1.51e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP----RElRTFRKMSCYIMQDdmllPHL---T 96
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-QGEILLNGQPiadySE-AALRQAISVVSQR----VHLfsaT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEammvsaNLKLSEKQEVKKELvTEILTALGLMSCSHTRTAL----------LSGGQRKRLAIALELVNNPPVMFFDEP 166
Cdd:PRK11160 430 LRD------NLLLAAPNASDEAL-IEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1131742492 167 TSGLDSASCFQVVSLMKSLAQgGRTIICTIHQpsAKLFEMFDKLYILSQGQCIFKG 222
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQ-NKTVLMITHR--LTGLEQFDRICVMDNGQIIEQG 555
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-222 |
2.76e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---------RPRELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSA 105
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLIDGvdiakisdaELREVR--RKKIAMVFQSFALMPHMTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKS 184
Cdd:PRK10070 132 ELAGINAEE-RREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKL 210
|
170 180 190
....*....|....*....|....*....|....*...
gi 1131742492 185 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 222
Cdd:PRK10070 211 QAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVG 247
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
35-222 |
2.84e-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: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyresgM----KGQILVNGR------------------PRELRTFRKMScyiMQDDMLL 92
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVG-----LvkpdSGRIFLDGEdithlpmhkrarlgigylPQEASIFRKLT---VEDNILA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 93 phltVLEAmmvsanLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:COG1137 102 ----VLEL------RKLSKKE--REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1131742492 173 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 222
Cdd:COG1137 170 IAVADIQKIIRHLKERGIGVLITDHNVRETL-GICDRAYIISEGKVLAEG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-187 |
3.13e-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: 75.49 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGmkGQILVNGRP------RELRTFRKMSCYIMQDDM--LLPHLTVL----EA 100
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLALLRLIPSE--GEIRFDGQDldglsrRALRPLRRRMQVVFQDPFgsLSPRMTVGqiiaEG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVSAnLKLSEKQevKKELVTEILTALGLmscshTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:COG4172 389 LRVHG-PGLSAAE--RRARVAEALEEVGL-----DPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170
....*....|...
gi 1131742492 175 CFQVVSLMKSLAQ 187
Cdd:COG4172 461 QAQILDLLRDLQR 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-222 |
3.37e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 27 LSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgmKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHLTVLE--AM 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEawsAAELARHRAYLSQQQTPPFAMPVFQylTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKLSEKQEVkkelVTEILTALGLMSCSHTRTALLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSAs 174
Cdd:PRK03695 93 HQPDKTRTEAVASA----LNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVA- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 175 cfQVV---SLMKSLAQGGRTIICTIHQPSAKLFEMfDKLYILSQGQCIFKG 222
Cdd:PRK03695 168 --QQAaldRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASG 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
31-222 |
3.45e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 31 FCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILV----------------NGRPRELRTF---RKMSCYIMQ-DDM 90
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVgdiyigdkknnhelitNPYSKKIKNFkelRRRVSMVFQfPEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 91 LLPHLTVLEAMMVSAnLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:PRK13631 128 QLFKDTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFgLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 170 LDSASCFQVVSLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 222
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
35-227 |
3.85e-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: 72.17 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRE-LRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLKLS 110
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDITkLPPHERARagiAYVPQGREIFPRLTVEENLLTGLAALPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EKQEVKKELVtEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGG 189
Cdd:TIGR03410 106 RSRKIPDEIY-ELFPVLKEML--GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGG 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 1131742492 190 RTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 227
Cdd:TIGR03410 183 MAIL-LVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
35-178 |
4.21e-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: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTfrkmSCYIMQDDMLLPHLTVLEAMMVSANLKLSeKQE 114
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQP-QGGQVLLDGKPISQYE----HKYLHSKVSLVGQEPVLFARSLQDNIAYG-LQS 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 115 VKKELVTEI-----------LTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:cd03248 115 CSFECVKEAaqkahahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-217 |
7.12e-14 |
|
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: 74.31 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNG---RPRELRTFRKMSCY 84
Cdd:TIGR01842 318 SVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGI-WPPTSGSVRLDGadlKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDDMLLPHlTV----------LEAMMVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALEL 154
Cdd:TIGR01842 397 LPQDVELFPG-TVaeniarfgenADPEKIIEAAKLAGVHELILRLPDGYDTVIG------PGGATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 155 VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
35-171 |
9.15e-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: 74.22 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSE 111
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDLAgldVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPLTLDE 557
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 112 KQEVKKEL-VTEILTAL--GLmscsHTRTA----LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:TIGR03797 558 AWEAARMAgLAEDIRAMpmGM----HTVISegggTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-172 |
1.06e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGrprELRTFRKMS----CYIMQDDMLLPHLTVLEAmmVSANLK 108
Cdd:PRK11432 31 QGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDG---EDVTHRSIQqrdiCMVFQSYALFPHMSLGEN--VGYGLK 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131742492 109 LS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:PRK11432 105 MLgvPKEERKQR-VKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
35-171 |
1.12e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfR--KMscyIMQDDMLLPHLTVLEAMmvSAN 106
Cdd:PRK11650 31 EFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RdiAM---VFQNYALYPHMSVRENM--AYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 107 LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK11650 101 LKIRgmPKAEIEER-VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-217 |
1.38e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 27 LSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR---PR-ELRTFRKMSCYIMQ---DDMLLPHLTVLE 99
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRsPLDAVKKGMAYITEsrrDNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKLS----------EKQEVKKELVTEILTALGLMSCSHTRTALlSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:PRK09700 361 NMAISRSLKDGgykgamglfhEVDEQRTAENQRELLALKCHSVNQNITEL-SGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 170 LDSASCFQVVSLMKSLAQGGRTIICTihqpSAKLFEMF---DKLYILSQGQ 217
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-217 |
1.53e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCL-----SGKFcrrelIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPreLRTFRKMSCYIMQDDMLLP 93
Cdd:PRK11247 23 GERTVLNQLdlhipAGQF-----VAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 94 HLTVLEammvsaNLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 173
Cdd:PRK11247 95 WKKVID------NVGLGLKGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 174 SCFQVVSLMKSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQ 217
Cdd:PRK11247 168 TRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
35-193 |
1.81e-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: 70.16 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMN-ILAGYRESGmkGQILVNGR----------PRE---LRtfRKMSCYIMQDDMLLPHLTVLEA 100
Cdd:COG4778 38 ECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVRHDggwvdlaqasPREilaLR--RRTIGYVSQFLRVIPRVSALDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVSAnLKLSEKQEVKKELVTEILTALGL-MSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:COG4778 114 VAEPL-LERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVV 192
|
170
....*....|....
gi 1131742492 180 SLMKSLAQGGRTII 193
Cdd:COG4778 193 ELIEEAKARGTAII 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-193 |
2.22e-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: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 32 CRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEammvs 104
Cdd:cd03215 24 RAGEIVGIAGLVGNGQTELAEALFGLR-PPASGEITLDGKPVTRRSPRDAIragiAYVPEDrkrEGLVLDLSVAE----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 105 aNLKLSekqevkkelvteiltalglmscshtrtALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 184
Cdd:cd03215 98 -NIALS---------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
....*....
gi 1131742492 185 LAQGGRTII 193
Cdd:cd03215 150 LADAGKAVL 158
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-171 |
3.40e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREVkqlarghTAGY--KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQI-----LVNGrprelr 76
Cdd:COG0488 316 LELEGL-------SKSYgdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVklgetVKIG------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 77 tfrkmscYIMQD-DMLLPHLTVLEAMmvsanlklseKQEVKKELVTEILTALGLM----SCSHTRTALLSGGQRKRLAIA 151
Cdd:COG0488 382 -------YFDQHqEELDPDKTVLDEL----------RDGAPGGTEQEVRGYLGRFlfsgDDAFKPVGVLSGGEKARLALA 444
|
170 180
....*....|....*....|
gi 1131742492 152 LELVNNPPVMFFDEPTSGLD 171
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLD 464
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-171 |
3.55e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR-----PRELRtfrkmSCYI---MQDDML--LPHLTVLEAMMV 103
Cdd:COG1101 33 DFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGKdvtklPEYKR-----AKYIgrvFQDPMMgtAPSMTIEENLAL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 104 SAN------LKLSEKQEvKKELVTEILTALGL-----MscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:COG1101 106 AYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-241 |
4.50e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.08 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 34 RELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG-----RPRELRTFRKMSCYIMQddmlLPHLTVLEAMMVS---- 104
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGvditdKKVKLSDIRKKVGLVFQ----YPEYQLFEETIEKdiaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 105 --ANLKLSEkQEVKKElVTEILTALGL-MSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:PRK13637 108 gpINLGLSE-EEIENR-VKRAMNIVGLdYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 181 LMKSLAQG-GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGV---VTNLIPYLKGLGLHCP--TY 241
Cdd:PRK13637 186 KIKELHKEyNMTIILVSHsmEDVAKL---ADRIIVMNKGKCELQGTpreVFKEVETLESIGLAVPqvTY 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-200 |
6.79e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKST----FMNILAGYRESGMKGQILVNGR--------PRELRTFRKMscyIM 86
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrtFNRLLELNEEARVEGEVRLFGRniyspdvdPIEVRREVGM---VF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 87 QDDMLLPHLTVLEAmmVSANLKLSEKQEVKKELVTEILTAL---GLMSCSHTR----TALLSGGQRKRLAIALELVNNPP 159
Cdd:PRK14267 92 QYPNPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALkkaALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 160 VMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPS 200
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-228 |
1.01e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGR-P-RELRTFRKMSCYIM-QDDMLLPHLTVLEammvSANL-- 107
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGilVPTSG---EVRVLGYvPfKRRKEFARRIGVVFgQRSQLWWDLPAID----SFRLlk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 ---KLSEKqEVKKEL--VTEILTALGLMscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 182
Cdd:COG4586 122 aiyRIPDA-EYKKRLdeLVELLDLGELL---DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 183 KSL-AQGGRTIICTIHqpsaklfEMFD------KLYILSQGQCIFKGVVTNLI 228
Cdd:COG4586 198 KEYnRERGTTILLTSH-------DMDDiealcdRVIVIDHGRIIYDGSLEELK 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
33-197 |
1.03e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIM---QDDML--------------LPHL 95
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSARAASRRVAsvpQDTSLsfefdvrqvvemgrTPHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 96 TvleammvsanlKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 175
Cdd:PRK09536 107 S-----------RFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180
....*....|....*....|..
gi 1131742492 176 FQVVSLMKSLAQGGRTIICTIH 197
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIH 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
35-185 |
1.21e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFRKMSCYIMQDDM--LLPHLTVLEamMVSAN 106
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLVKA-TDGEVAWLGKdllgmkDDEWRAVRSDIQMIFQDPLasLNPRMTIGE--IIAEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 L-----KLSeKQEVKKElVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:PRK15079 125 LrtyhpKLS-RQEVKDR-VKAMMLKVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN 202
|
....*
gi 1131742492 181 LMKSL 185
Cdd:PRK15079 203 LLQQL 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-217 |
1.27e-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: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSA 105
Cdd:TIGR02633 285 RGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNpaqaIRAGIAMVPEDrkrHGIVPILGVGKNITLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSEKQEVKKElvTEILTALGLMSCSHTRTAL-------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:TIGR02633 365 LKSFCFKMRIDAA--AELQIIGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEI 442
|
170 180 190
....*....|....*....|....*....|....*....
gi 1131742492 179 VSLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQ 217
Cdd:TIGR02633 443 YKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
33-171 |
1.51e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRE------------LRTFrkmscyimQDDMLLPHLTVLE 99
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILLRGQHIEglpghqiarmgvVRTF--------QHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKL----------------SEKQEVkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFF 163
Cdd:PRK11300 100 NLLVAQHQQLktglfsgllktpafrrAESEAL--DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
....*...
gi 1131742492 164 DEPTSGLD 171
Cdd:PRK11300 178 DEPAAGLN 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
35-217 |
1.72e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG---YRESGmkGQILVNG----------RPRE-LrtFrkmscYIMQDDMLLPHLTVLEA 100
Cdd:COG0396 27 EVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGedilelspdeRARAgI--F-----LAFQYPVEIPGVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVSANLKLSEKQEVKK--ELVTEILTALGlMSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASc 175
Cdd:COG0396 98 LRTALNARRGEELSAREflKLLKEKMKELG-LDEDFLDRYVnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 176 FQVVS-LMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQ 217
Cdd:COG0396 176 LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGR 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-197 |
2.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSG---KFCRRELIGIMGPSGAGKSTF---MNIL--------------------AGYRESG 61
Cdd:PRK13651 4 KVKNIVKIFNKKLPTELKALDNvsvEINQGEFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkkTKEKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 62 MKGQILVNGRPRELRT---FRKMSCYIMQ-DDMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVTEILTALGLMSCSHTRT 137
Cdd:PRK13651 84 LEKLVIQKTRFKKIKKikeIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKK-RAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 138 AL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:PRK13651 163 PFeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
35-222 |
2.84e-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: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG---YRESG----MKGQILVNGRPRElRTfRKMSCYIMQDDMLLPHLTVLEAMMVSANL 107
Cdd:TIGR01978 27 EIHAIMGPNGSGKSTLSKTIAGhpsYEVTSgtilFKGQDLLELEPDE-RA-RAGLFLAFQYPEEIPGVSNLEFLRSALNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSEKQEVK------KELVTEILTALGlMSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:TIGR01978 105 RRSARGEEPldlldfEKLLKEKLALLD-MDEEFLNRSVnegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 179 VSLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKG 222
Cdd:TIGR01978 184 AEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-222 |
3.02e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNG---RPRELRTFRKMSC 83
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGitiSKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 84 YIMQD-DMLLPHLTV-------LEAMMVSanlklsekQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELV 155
Cdd:PRK13632 87 IIFQNpDNQFIGATVeddiafgLENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131742492 156 NNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQPSAKLfeMFDKLYILSQGQCIFKG 222
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQG 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
30-193 |
7.83e-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: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 30 KFCRRELIGIMGPSGAGKSTF------MNIL-AGYResgMKGQILVNGR--------PRELRT-----FRK-----MSCY 84
Cdd:COG1117 33 DIPENKVTALIGPSGCGKSTLlrclnrMNDLiPGAR---VEGEILLDGEdiydpdvdVVELRRrvgmvFQKpnpfpKSIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 imqDDmllphltvleammVSANLKLSE--KQEVKKELVTEILTALGL---------MScshtrtAL-LSGGQRKRLAIAL 152
Cdd:COG1117 110 ---DN-------------VAYGLRLHGikSKSELDEIVEESLRKAALwdevkdrlkKS------ALgLSGGQQQRLCIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 153 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTII 193
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIV 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-197 |
8.41e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 15 GHTAGYKTLLKCLSGkfcrrELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMQD---DML 91
Cdd:PRK15056 19 GHTALRDASFTVPGG-----SIAALVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 92 LPHLTVLEAMMVSAN----LKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 167
Cdd:PRK15056 93 FPVLVEDVVMMGRYGhmgwLRRAKKRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|
gi 1131742492 168 SGLDSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
35-227 |
8.68e-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: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPreLRTFRkmSCYIMQDDMLLPHLTVLEAMMVSAN----LKLS 110
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQP-TGGQVLLDGVP--LVQYD--HHYLHRQVALVGQEPVLFSGSVRENiaygLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EKQEVkkelvteilTALGLMSCSHT---------------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 175
Cdd:TIGR00958 583 PDEEI---------MAAAKAANAHDfimefpngydtevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 176 FQVVSLMKslaQGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGVVTNL 227
Cdd:TIGR00958 654 QLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKGSVVEMGTHKQL 700
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-187 |
1.03e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 17 TAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTFRKMSCYIMQDDM 90
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRKAFRRDIQMVFQDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 91 --LLPHLTV----LEAMMVSANLKLSEKQEVKKELVTEILTALGLMScshTRTALLSGGQRKRLAIALELVNNPPVMFFD 164
Cdd:PRK10419 100 saVNPRKTVreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD---KRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180
....*....|....*....|...
gi 1131742492 165 EPTSGLDSASCFQVVSLMKSLAQ 187
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQ 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
40-222 |
1.55e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.15 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 40 MGPSGAGKSTFMNILAGYReSGMKGQILVNG-------RPRELRTFRKMSCYIMQ-DDMLLPHLTVLEAMMVSA-NLKLS 110
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDtlitstsKNKDIKQIRKKVGLVFQfPESQLFEETVLKDVAFGPqNFGVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EKQEVKkeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 189
Cdd:PRK13649 118 QEEAEA--LAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSG 195
|
170 180 190
....*....|....*....|....*....|...
gi 1131742492 190 RTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 222
Cdd:PRK13649 196 MTIVLVTHLMD-DVANYADFVYVLEKGKLVLSG 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-246 |
1.69e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAgyRESGMKGQILVNGRPR-----------ELRTFRKMSCYIMQDD 89
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 90 MLLPhLTVLEAMMVSANL----------KLSEKQEVKKELVTEILTALglmscsHTRTALLSGGQRKRLAIALELVNNPP 159
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIvgwrpkleidDIVESALKDADLWDEIKHKI------HKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 160 VMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQpsaklfemFDKLYILSQGQCIFKGvVTNLIPYLKGLGLHC 238
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKG-NENRIGQLVEFGLTK 241
|
....*...
gi 1131742492 239 PTYHNPAD 246
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
39-227 |
2.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYRESgMKGQILVNG-------RPRELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKL 109
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKP-TTGTVTVDDitithktKDKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQevKKELVTEILTALG----LMSCSHTRtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:PRK13646 117 NLDE--VKNYAHRLLMDLGfsrdVMSQSPFQ---MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1131742492 186 A-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVTNL 227
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 ... |
34-197 |
3.27e-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: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 34 RELIGIMGPSGAGKSTFMNILAGYRESgMKGQILV--------------NGRPRELRtfrkmscYI---MQDDMLLPHLT 96
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEP-TSGEVNVrvgdewvdmtkpgpDGRGRAKR-------YIgilHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEAMMVSANLKLSEKQEVKKELVTeiLTALGLmSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGL 170
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVIT--LKMVGF-DEEKAEEILdkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180
....*....|....*....|....*...
gi 1131742492 171 DSASCFQVV-SLMKSLAQGGRTIICTIH 197
Cdd:TIGR03269 459 DPITKVDVThSILKAREEMEQTFIIVSH 486
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-197 |
4.35e-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: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLArgHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAgyRESGM-KGQILVNGRP------RELRtfRK 80
Cdd:COG4604 3 EIKNVS--KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGLDvattpsRELA--KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MScyIM-QDDMLLPHLTVLEamMVS------ANLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALE 153
Cdd:COG4604 77 LA--ILrQENHINSRLTVRE--LVAfgrfpySKGRLTAEDR---EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 154 LVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIH 197
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-193 |
4.66e-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: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVsA 105
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGadPADSG---EIRLDGKPVRIRSPRDAIragiAYVPEDrkgEGLVLDLSIRENITL-A 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLK-------LSEKQEvkKELVTEILTALGL-MSCSHTRTALLSGG-QRKrLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:COG1129 355 SLDrlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVGAKA 431
|
170
....*....|....*..
gi 1131742492 177 QVVSLMKSLAQGGRTII 193
Cdd:COG1129 432 EIYRLIRELAAEGKAVI 448
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-227 |
5.70e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.25 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG-------RPRELRTFRKMScYIMQDDMLLPHLTVLE--AMMV 103
Cdd:PRK11831 32 RGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipamsRSRLYTVRKRMS-MLFQSGALFTDMNVFDnvAYPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 104 SANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 183
Cdd:PRK11831 110 REHTQLPA--PLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1131742492 184 SLAQG-GRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 227
Cdd:PRK11831 188 ELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
35-216 |
5.78e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.37 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDDMLL------------PHLT--- 96
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDP-QSGRILIDGtdiRTVTRASLRRNIAVVFQDAGLFnrsiednirvgrPDATdee 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 VLEAMMVSANLKLSEKQEVKKElvteilTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYD------TVVG------ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 177 QVVSLMKSLAQgGRTIICTIHQPS----AKLFEMFDKLYILSQG 216
Cdd:PRK13657 509 KVKAALDELMK-GRTTFIIAHRLStvrnADRILVFDNGRVVESG 551
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-197 |
7.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 25 KCLSGKFcrrelIGIMGPSGAGKSTFM---NIL----------AGYresgmkgQILVNGRPRELRTFRKMSCYIMQ-DDM 90
Cdd:PRK13641 29 ELEEGSF-----VALVGHTGSGKSTLMqhfNALlkpssgtitiAGY-------HITPETGNKNLKKLRKKVSLVFQfPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 91 LLPHLTVLEAMMVSA-NLKLSEKQevKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTS 168
Cdd:PRK13641 97 QLFENTVLKDVEFGPkNFGFSEDE--AKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180
....*....|....*....|....*....
gi 1131742492 169 GLDSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-227 |
7.13e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRElRTFRKMSC-----YIMQDDMLLPHLTVLEAMMVSanlKL 109
Cdd:PRK09700 32 EIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVLENLYIG---RH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQ---------EVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:PRK09700 107 LTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1131742492 181 LMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 227
Cdd:PRK09700 187 IMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
35-172 |
8.01e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLEAmmVSANLK 108
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALFRHMTVFDN--IAFGLT 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 109 LSEKQE-----VKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:PRK10851 101 VLPRRErpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
39-198 |
1.31e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRT---FRKMSCYIM-QDDMLLPHLTVLEAMMvsanLKLSEKQE 114
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNPCARLTpakAHQLGIYLVpQEPLLFPNLSVKENIL----FGLPKRQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 115 VKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIC 194
Cdd:PRK15439 117 SMQKM-KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVF 195
|
....
gi 1131742492 195 TIHQ 198
Cdd:PRK15439 196 ISHK 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
37-228 |
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 1131742492 37 IGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDdmllPHL---TVLEAMMVSANLKLS 110
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDI-DEGEILLDGhdlRDYTLASLRNQVALVSQN----VHLfndTIANNIAYARTEQYS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EKQ---EVKKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:PRK11176 447 REQieeAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1131742492 186 aQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKGVVTNLI 228
Cdd:PRK11176 527 -QKNRTSLVIAHRLST--IEKADEILVVEDGEIVERGTHAELL 566
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
35-221 |
1.54e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP-RELRTFRkmscyIMQDDM-LLPH-LTVLEAMMVSANLKL-- 109
Cdd:PRK11614 32 EIVTLIGANGAGKTTLLGTLCG-DPRATSGRIVFDGKDiTDWQTAK-----IMREAVaIVPEgRRVFSRMTVEENLAMgg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 --SEKQEVKK--ELVTEILTALglMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:PRK11614 106 ffAERDQFQEriKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1131742492 186 AQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFK 221
Cdd:PRK11614 184 REQGMTIF-LVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-197 |
1.82e-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: 64.26 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 112
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 QEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 192
Cdd:TIGR01257 2045 EEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV 2123
|
....*
gi 1131742492 193 ICTIH 197
Cdd:TIGR01257 2124 VLTSH 2128
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-234 |
1.92e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 27 LSGKFCRRELIGIMGPSGAGKS-TFMNILAGYRESGMK---GQILVNGRPRELRTFRKMSCYIMQD----DM-------- 90
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLvqcDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifqepm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 91 --LLPHLTVLEAMMVSANLKLSEKQEvkkELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMF 162
Cdd:PRK10261 115 tsLNPVFTVGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRIPEAQTILsryphqLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 163 FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 234
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
35-217 |
2.09e-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: 63.23 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRprELRTFRKMSC-----YIMQDDMLLPHlTVLE--AMMvsan 106
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGvWPPTA--GSVRLDGA--DLSQWDREELgrhigYLPQDVELFDG-TIAEniARF---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 lklsekQEVKKELVTE----------IL-------TALGLMSCShtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSG 169
Cdd:COG4618 430 ------GDADPEKVVAaaklagvhemILrlpdgydTRIGEGGAR------LSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131742492 170 LDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMfDKLYILSQGQ 217
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 ... |
19-197 |
2.25e-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: 59.00 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRelrtfrkmSCYIMQddmllphltvl 98
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------IGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 eammvsanlklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170
....*....|....*....
gi 1131742492 179 VSLMKSLaQGgrTIICTIH 197
Cdd:cd03221 110 EEALKEY-PG--TVILVSH 125
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-219 |
2.58e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELRTFR----KMSCYIMQDDMLLPHLTVLEAMMVSANL-- 107
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEELQASNIRdterAGIAIIHQELALVKELSVLENIFLGNEItp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 -KLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 186
Cdd:PRK13549 112 gGIMDYDAMYLR-AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 1131742492 187 QGGRTIICTIHqpsaKLFEMF---DKLYILSQGQCI 219
Cdd:PRK13549 191 AHGIACIYISH----KLNEVKaisDTICVIRDGRHI 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-217 |
3.08e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.90 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 2 RDLELRevkqlarghTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILvngRPRELRTfrkm 81
Cdd:COG4178 366 EDLTLR---------TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIA---RPAGARV---- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 scyimqddMLLPHltvlEAMMVSANLK--LS---EKQEVKKELVTEILTALGLmscSHTRTAL---------LSGGQRKR 147
Cdd:COG4178 429 --------LFLPQ----RPYLPLGTLReaLLypaTAEAFSDAELREALEAVGL---GHLAERLdeeadwdqvLSLGEQQR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 148 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGrTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRST--LAAFHDRVLELTGDG 560
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-171 |
3.32e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 114
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 115 VKkelvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK13543 117 MP----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
35-196 |
3.97e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKS----TFMNILAGY-RESG---MKGQILVNGRPRELRTFR--KMScYIMQDDM--LLPHLTVLEAMM 102
Cdd:PRK09473 43 ETLGIVGESGSGKSqtafALMGLLAANgRIGGsatFNGREILNLPEKELNKLRaeQIS-MIFQDPMtsLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 VSANL-KLSEKQEVKKELVtEILTALGlMSCSHTRTAL----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 177
Cdd:PRK09473 122 EVLMLhKGMSKAEAFEESV-RMLDAVK-MPEARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQ 199
|
170
....*....|....*....
gi 1131742492 178 VVSLMKSLAQGGRTIICTI 196
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) ... |
24-172 |
4.65e-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: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVngrprELRTFRKMSCYIMQD-DMllphlTVLEAMM 102
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAG-VLKPDEGDIEI-----ELDTVSYKPQYIKADyEG-----TVRDLLS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 VSANLKLSEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:cd03237 84 SITKDFYTHPY-----FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-217 |
4.83e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVSA 105
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIaqgiAMVPEDrkrDGIVPVMGVGKNITLAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSEKQEVKKEL-VTEILTALGLM----SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 180
Cdd:PRK13549 367 LDRFTGGSRIDDAAeLKTILESIQRLkvktASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1131742492 181 LMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 217
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 ... |
21-222 |
6.46e-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: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE-SGMKGQILVN----------------GRP----------- 72
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyEPTSGRIIYHvalcekcgyverpskvGEPcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 73 ---------RELRTFRKMSCYIMQDDM-LLPHLTVLEAMMVSanlkLSEKQEVKKELVTEILTALGLMSCSHTRTAL--- 139
Cdd:TIGR03269 93 evdfwnlsdKLRRRIRKRIAIMLQRTFaLYGDDTVLDNVLEA----LEEIGYEGKEAVGRAVDLIEMVQLSHRITHIard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQC 218
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSDKAIWLENGEI 247
|
....
gi 1131742492 219 IFKG 222
Cdd:TIGR03269 248 KEEG 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
35-219 |
7.00e-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: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELR----TFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKL 109
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPLKASnirdTERAGIVIIHQELTLVPELSVAENIFLGNEITL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SEKQEVKKELV---TEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:TIGR02633 108 PGGRMAYNAMYlraKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1131742492 186 AQGGRTIICTIHqpsaKLFE---MFDKLYILSQGQCI 219
Cdd:TIGR02633 188 KAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-217 |
9.06e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGY--RESGmkgQILVNGRPRELRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSA 105
Cdd:PRK10762 279 EILGVSGLMGAGRTELMKVLYGAlpRTSG---YVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGMSVKENMSLTA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSE-----KQEVKKELVTEILTALGLMSCSHTRT-ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:PRK10762 356 LRYFSRaggslKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 180 SLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 217
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) ... |
35-197 |
9.19e-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: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG--------YRESGMKGQILVNGRPRELRTFRKMscyIMQDDM----------LLPHLT 96
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNYFTK---LLEGDVkvivkpqyvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 97 vleAMMVSANLKLSEKQEVKKELVTeiltALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:cd03236 104 ---KGKVGELLKKKDERGKLDELVD----QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|.
gi 1131742492 177 QVVSLMKSLAQGGRTIICTIH 197
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEH 197
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-195 |
9.96e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTF------MNILAgyRESGMKGQILVNGR----PR----ELRTFRKMscy 84
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGHniysPRtdtvDLRKEIGM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTR---TAL-LSGGQRKRLAIALELVNNPPV 160
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhdSALgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1131742492 161 MFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICT 195
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-242 |
1.39e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 181
Cdd:NF000106 109 MIGR*LDLSRKD--ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 182 MKSLAQGGRTIICTIhQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYH 242
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
35-171 |
1.40e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRELRTFRKMS------------CYIMQD--DMLlphltvleA 100
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprDGL--------R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 101 MMVSANLKLSEKqevkkelvteiLTALGLMSCSHTR-TAL-------------------LSGGQRKRLAIALELVNNPPV 160
Cdd:PRK11701 104 MQVSAGGNIGER-----------LMAVGARHYGDIRaTAGdwlerveidaariddlpttFSGGMQQRLQIARNLVTHPRL 172
|
170
....*....|.
gi 1131742492 161 MFFDEPTSGLD 171
Cdd:PRK11701 173 VFMDEPTGGLD 183
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
112-239 |
1.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 112 KQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGR 190
Cdd:PRK13640 117 RPEMIK-IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNL 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 191 TIICTIHQPSAKlfEMFDKLYILSQGQCIFKGVVTNLIP---YLKGLGLHCP 239
Cdd:PRK13640 196 TVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEIFSkveMLKEIGLDIP 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-239 |
2.17e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 21 KTLLKCLSGKFCRRELIGIMGPSGAGKSTF---MNILAGYREsgmkGQILVNG----RPRELRTFRKMSCYIMQ--DDML 91
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE----GKVYVDGldtsDEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 92 LPhlTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK13633 99 VA--TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 172 SASCFQVVSLMKSL-AQGGRTIICTIH--QPSAKLfemfDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCP 239
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
39-239 |
2.29e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTFRKMSCYIMQDDmllphltvlEAMMVSANLKLS----- 110
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFEKLRKHIGIVFQNP---------DNQFVGSIVKYDvafgl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 111 EKQEVK----KELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 186
Cdd:PRK13648 110 ENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 187 QGGR-TIICTIHQPSAKLFEmfDKLYILSQGQCIFKGVVTNLIPYLKGL---GLHCP 239
Cdd:PRK13648 190 SEHNiTIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEIFDHAEELtriGLDLP 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-174 |
2.42e-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: 57.42 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFmnILAGYRES-GMKGQILVNGRP------RELRtfRK 80
Cdd:cd03369 8 EVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDistiplEDLR--SS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MSCyIMQDDMLLphltvleAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTrtalLSGGQRKRLAIALELVNNPPV 160
Cdd:cd03369 84 LTI-IPQDPTLF-------SGTIRSNLDPFDEYSDE-----EIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRV 146
|
170
....*....|....
gi 1131742492 161 MFFDEPTSGLDSAS 174
Cdd:cd03369 147 LVLDEATASIDYAT 160
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-193 |
2.63e-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: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 37 IGIMGPSGAGKSTFMNILAGyresgmkgQILVN-GRPRE-------LRTFRKMscyIMQDdmllpHLTVLeammVSANLK 108
Cdd:COG1245 102 TGILGPNGIGKSTALKILSG--------ELKPNlGDYDEepswdevLKRFRGT---ELQD-----YFKKL----ANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSEK-QEVK----------KEL---------VTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 168
Cdd:COG1245 162 VAHKpQYVDlipkvfkgtvRELlekvdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180
....*....|....*....|....*
gi 1131742492 169 GLDSASCFQVVSLMKSLAQGGRTII 193
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-187 |
2.63e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 5 ELREVKQLARGHTAGYKTLlKCLSG-KFC--RRELIGIMGPSGAGKSTFMNILAGYRE--SG---MKGQILVNGRPRELR 76
Cdd:PRK11308 10 DLKKHYPVKRGLFKPERLV-KALDGvSFTleRGKTLAVVGESGCGKSTLARLLTMIETptGGelyYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 77 TFRKMSCYIMQDDM--LLPHLTV---LEAMMVsANLKLSEKQevKKELVTEILTALGLMSCSHTRTA-LLSGGQRKRLAI 150
Cdd:PRK11308 89 LLRQKIQIVFQNPYgsLNPRKKVgqiLEEPLL-INTSLSAAE--RREKALAMMAKVGLRPEHYDRYPhMFSGGQRQRIAI 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1131742492 151 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 187
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
39-222 |
2.80e-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: 57.15 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAG---YRESgmKGQILVNGR-----PRELRTfrKMSCYIM-QDDMLLPHLTVLEaMMVSANLKL 109
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGEditdlPPEERA--RLGIFLAfQYPPEIPGVKNAD-FLRYVNEGF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SekqevkkelvteiltalglmscshtrtallsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 189
Cdd:cd03217 106 S-------------------------------GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1131742492 190 RTIICTIHQpsAKLFEMF--DKLYILSQGQCIFKG 222
Cdd:cd03217 155 KSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
370-583 |
3.18e-09 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 57.13 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 370 MLFLMFAALMPTVLTFplemaVFMREHLNYWY------SLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFL 443
Cdd:COG0842 11 AMSLLFTALMLTALSI-----AREREQGTLERllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 444 LFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGViltiyg 523
Cdd:COG0842 86 LLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL------ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 524 meRGdltcleercpfrepqSILRALDVEDakLYMDFLVLGIFFLALRLLAYLVLRYRVKS 583
Cdd:COG0842 160 --RA---------------LFLGGAGLAD--VWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-217 |
3.76e-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: 57.12 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILagYR-ESGMKGQILVNGRP------RELRtfRKMSCyIMQDDMLL---- 92
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRlVELSSGSILIDGVDiskiglHDLR--SRISI-IPQDPVLFsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 93 -----PHLTVLEAMMVSAnLKlsekqEVK-KELVTEILTALGLMSCShtRTALLSGGQRKRLAIALELVNNPPVMFFDEP 166
Cdd:cd03244 95 rsnldPFGEYSDEELWQA-LE-----RVGlKEFVESLPGGLDTVVEE--GGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131742492 167 TSGLDSASCFQVVSLMKSlAQGGRTIIC------TIHQpsaklfemFDKLYILSQGQ 217
Cdd:cd03244 167 TASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDKGR 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-222 |
5.98e-09 |
|
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: 56.77 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 6 LREVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR---ELRTFrkm 81
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGTVTVRGRVSsllGLGGG--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 scyimqddmLLPHLTVLE-AMMVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPV 160
Cdd:cd03220 95 ---------FNPELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 161 MFFDEPTSGLDSAscFQ--VVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:cd03220 164 LLIDEVLAVGDAA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-227 |
6.33e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 38 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRelrTFR--KMS-----CYIMQDDMLLPHLTVLEammvsaNLKL 109
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiYTRDA--GSILYLGKEV---TFNgpKSSqeagiGIIHQELNLIPQLTIAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 110 SekQEVK--------KELVTE---ILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASC 175
Cdd:PRK10762 103 G--REFVnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 176 FQVVSLMKslAQGgrtiiCTIHQPSAKLFEMF---DKLYILSQGQCIFKGVVTNL 227
Cdd:PRK10762 181 FRVIRELK--SQG-----RGIVYISHRLKEIFeicDDVTVFRDGQFIAEREVADL 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
39-218 |
7.11e-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: 55.24 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYRESGmKGQIlvnGRPRELRTFrkmscYIMQddmllphltvlEAMMVSANLKlsekqevkke 118
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEGEDLL-----FLPQ-----------RPYLPLGTLR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 119 lvtEILtalglmscSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLaqgGRTIICTIHQ 198
Cdd:cd03223 82 ---EQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR 147
|
170 180
....*....|....*....|.
gi 1131742492 199 PS-AKLFEMfdKLYILSQGQC 218
Cdd:cd03223 148 PSlWKFHDR--VLDLDGEGGW 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-217 |
7.96e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLTVleammvsanlk 108
Cdd:PRK10522 348 RGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQPEDYRKLFSAVFTDFHLFDQLLG----------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 lSEKQEVKKELVTEILTALGL---MSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSglDSASCFQVV---S 180
Cdd:PRK10522 415 -PEGKPANPALVEKWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAA--DQDPHFRREfyqV 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 1131742492 181 LMKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-185 |
9.14e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFRKMSCYIMQDDM--LLPHLTVLEAMMVSAN 106
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 107 LKLSEKQEVKKELVTEILTALGLMSCSHTRTA-LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 185
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
35-165 |
9.46e-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: 57.89 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLtvleammvsanlkLS 110
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLDGQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 111 EKQEVKKELVTEILTALGLmscSH---------TRTALlSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:COG4615 424 LDGEADPARARELLERLEL---DHkvsvedgrfSTTDL-SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-193 |
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 1131742492 28 SGKFCRRELIGIMGPSGAGKSTFMNILAGYRE--SG-MKGQILVNGRPRelrtfrkmscYIMQD-DMllphlTVLEAMMV 103
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGeVDEDLKISYKPQ----------YISPDyDG-----TVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 104 SANLKLSEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 183
Cdd:COG1245 425 ANTDDFGSSY-----YKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|.
gi 1131742492 184 SLAQG-GRTII 193
Cdd:COG1245 500 RFAENrGKTAM 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-197 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 37 IGIMGPSGAGKSTFMNILAGyresgMKGQILVNGRPRELRTFRkmscYIMQDDMLLPHLTVLEAMM-------------- 102
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAG-----VDKDFNGEARPQPGIKVG----YLPQEPQLDPTKTVRENVEegvaeikdaldrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 -VSANL--------KLSEKQEvkkELvTEILTALGLMSCSHT---------------RTALLSGGQRKRLAIALELVNNP 158
Cdd:TIGR03719 105 eISAKYaepdadfdKLAAEQA---EL-QEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1131742492 159 PVMFFDEPTSGLDSAScfqVVSLMKSLAQGGRTIICTIH 197
Cdd:TIGR03719 181 DMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTH 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-222 |
1.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 30 KFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG--------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAM 101
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS-ETGQTIVGDyaipanlkKIKEVKRLRKEIGLVFQFPEYQLFQETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKLSE-KQEVKKElVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:PRK13645 112 IAFGPVNLGEnKQEAYKK-VPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 180 SLMKSLAQG-GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 222
Cdd:PRK13645 191 NLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-188 |
1.13e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 37 IGIMGPSGAGKSTFMNILAG--------YRESGMKGQILVNGRPRELRT-FRKMSC----------YImqdDmLLPHL-- 95
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKRFRGTELQNyFKKLYNgeikvvhkpqYV---D-LIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 96 -TVLEAmmvsanLKLSEKQEVKKELVTEiltaLGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:PRK13409 178 gKVREL------LKKVDERGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170
....*....|....
gi 1131742492 175 CFQVVSLMKSLAQG 188
Cdd:PRK13409 248 RLNVARLIRELAEG 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-222 |
1.24e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 6 LREVKQLARghTAGYKTLL---------KCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELR 76
Cdd:PRK15112 4 LLEVRNLSK--TFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 77 TFRKMSC---YIMQD--DMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMScSHTR--TALLSGGQRKRLA 149
Cdd:PRK15112 81 DYSYRSQrirMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP-DHASyyPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 150 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL--AQGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKG 222
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-203 |
1.27e-08 |
|
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: 53.92 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGrprelrtfrkmscyimqddmllphltvleammvsanlklsek 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 113 qevkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMKSLA 186
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 1131742492 187 QGGRTIICTIHQPSAKL 203
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-187 |
1.38e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 57.39 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKS-TFMNI--LAGYRESGMKGQILVNGR------PRELRTFR--KMSCyIMQDDM--LLPHLTVle 99
Cdd:COG4172 35 AGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllglsERELRRIRgnRIAM-IFQEPMtsLNPLHTI-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 ammvsanlklsEKQ--EV--------KKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFF 163
Cdd:COG4172 112 -----------GKQiaEVlrlhrglsGAAARARALELLERVGIPDPERRLdayphqLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180
....*....|....*....|....*..
gi 1131742492 164 DEPTSGLD---SAscfQVVSLMKSLAQ 187
Cdd:COG4172 181 DEPTTALDvtvQA---QILDLLKDLQR 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-198 |
1.67e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 23 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR--PRELRTFRKMSCYIMQDDMLLPHLTVLE 99
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQsiKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKLSEKQevkkelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:PRK13540 94 NCLYDIHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 1131742492 180 SLMKSLAQGGRTIICTIHQ 198
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-171 |
2.52e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyrESGM-KGQI-----LVNGR-----PRE-------------------LRTFRKMSCY 84
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNG--EVLLdDGRIiyeqdLIVARlqqdpPRNvegtvydfvaegieeqaeyLKRYHDISHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 85 IMQD--DMLLPHLTVLEAMMVSANLKLSEKQevkkelVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMF 162
Cdd:PRK11147 108 VETDpsEKNLNELAKLQEQLDHHNLWQLENR------INEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*....
gi 1131742492 163 FDEPTSGLD 171
Cdd:PRK11147 180 LDEPTNHLD 188
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
34-172 |
2.57e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 34 RELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPREL---RTFRKMSCYIMQDDMLLphltvleAMMVSANLKLS 110
Cdd:PRK10790 367 RGFVALVGHTGSGKSTLASLLMGYY-PLTEGEIRLDGRPLSSlshSVLRQGVAMVQQDPVVL-------ADTFLANVTLG 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131742492 111 ekQEVKKELVTEILTALGLMSCS-------HTRTA----LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:PRK10790 439 --RDISEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-225 |
2.81e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 1 MRDLELREVKQLargH-TAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE-SGMKGQILVNGR-----PR 73
Cdd:CHL00131 2 NKNKPILEIKNL---HaSVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGEsildlEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 74 ELRTfrKMSCYI-MQDDMLLPHLTVLEAMMVSANLKLSEKQEVKK------ELVTEILTALGLMSCSHTRTAL--LSGGQ 144
Cdd:CHL00131 79 EERA--HLGIFLaFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELdpleflEIINEKLKLVGMDPSFLSRNVNegFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 145 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKG 222
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTG 234
|
...
gi 1131742492 223 VVT 225
Cdd:CHL00131 235 DAE 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
35-199 |
3.04e-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: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQilvngrprelrtfrkmSCYIMQDDMLLPHLTVLEAmmvsanlkLSEKQE 114
Cdd:COG2401 57 EIVLIVGASGSGKSTLLRLLAG-ALKGTPVA----------------GCVDVPDNQFGREASLIDA--------IGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 115 VKkeLVTEILTALGLMSCS--HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRT 191
Cdd:COG2401 112 FK--DAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGIT 189
|
....*...
gi 1131742492 192 IICTIHQP 199
Cdd:COG2401 190 LVVATHHY 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-171 |
3.76e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGR---PRELRTF-----RKMScYIMQDDMLLPHLTVleammvSANLKLS 110
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGL-TRPQKGRIVLNGRvlfDAEKGIClppekRRIG-YVFQDARLFPHYKV------RGNLRYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 111 EKqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK11144 101 MA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-217 |
5.52e-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: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 23 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyrESG-MKGQILVNGRprelrtfrkMScYIMQddmllphltvlEAM 101
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPGS---------IA-YVSQ-----------EPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLK------LSEKQEVKKELVT--------EILTAlGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 167
Cdd:cd03250 77 IQNGTIRenilfgKPFDEERYEKVIKacalepdlEILPD-GDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 168 SGLDSascfQVVS-LMKSLAQG----GRTIICTIHQPSakLFEMFDKLYILSQGQ 217
Cdd:cd03250 156 SAVDA----HVGRhIFENCILGlllnNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-198 |
6.75e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYRESgMKGQI------LVNG-RPRELRTFRKMSCYIMQddmlLPHLTVLEAMMVS------A 105
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQP-TSGTVtigervITAGkKNKKLKPLRKKVGIVFQ----FPEHQLFEETVEKdicfgpM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 106 NLKLSEKQevKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 184
Cdd:PRK13634 113 NFGVSEED--AKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK 190
|
170
....*....|....*
gi 1131742492 185 LAQ-GGRTIICTIHQ 198
Cdd:PRK13634 191 LHKeKGLTTVLVTHS 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-171 |
1.16e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRE--SG-MKGQILVNGRPRelrtfrkmscYIMQDdmllPHLTVlEAMMVSANLKL 109
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKpdEGeVDPELKISYKPQ----------YIKPD----YDGTV-EDLLRSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 110 SEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK13409 429 GSSY-----YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-213 |
1.64e-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: 1.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131742492 140 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPsaKLFEMFDKLYIL 213
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHI 153
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-187 |
1.81e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKS----TFMNIL-AGYRESGmkGQILVNGRPRELRTFR-KMSCYIMQD--DMLLPHLTVleAMMVS 104
Cdd:PRK10418 28 RGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGKPVAPCALRgRKIATIMQNprSAFNPLHTM--HTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 105 ANLKLSEKQEVKKELVtEILTALGLmscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:PRK10418 104 ETCLALGKPADDATLT-AALEAVGL---ENAARVLklypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARI 179
|
....*....
gi 1131742492 179 VSLMKSLAQ 187
Cdd:PRK10418 180 LDLLESIVQ 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-197 |
1.98e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 10 KQLARGHtaGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPRELRTFRKMSCYI--MQ 87
Cdd:PRK10253 11 EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIglLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 88 DDMLLPHLTVLEAMMVSANLK----LSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFF 163
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1131742492 164 DEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIH 197
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
140-193 |
2.20e-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: 53.67 E-value: 2.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTII 193
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
35-187 |
2.51e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKS-TFMNIL-------AGYRESGMK--GQILVNGRPRELRTFR--KMScYIMQDDMllphltvleamm 102
Cdd:PRK15134 36 ETLALVGESGSGKSvTALSILrllpsppVVYPSGDIRfhGESLLHASEQTLRGVRgnKIA-MIFQEPM------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 VSAN-LKLSEKQ--EV--------KKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDE 165
Cdd:PRK15134 103 VSLNpLHTLEKQlyEVlslhrgmrREAARGEILNCLDRVGIRQAAKRLtdyphqLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180
....*....|....*....|..
gi 1131742492 166 PTSGLDSASCFQVVSLMKSLAQ 187
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQ 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-222 |
3.26e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.62 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 6 LREVKQLARGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR---PRELRTfrkm 81
Cdd:COG1134 24 LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--SGRVEVNGRvsaLLELGA---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 82 scyIMQddmllPHLTVLE-AMMVSANLKLSeKQEVkKELVTEIL--TALG--LmscsHT--RTalLSGGQRKRLAIALEL 154
Cdd:COG1134 98 ---GFH-----PELTGREnIYLNGRLLGLS-RKEI-DEKFDEIVefAELGdfI----DQpvKT--YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 155 VNNPPVMFFDEPTSGLDSAscFQ--VVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 222
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDG 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-171 |
4.24e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLARGHtaGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQIlvngrprELRTFRKMSCYIMQ 87
Cdd:TIGR03719 324 EAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTI-------EIGETVKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 88 DDMLLPHLTVLEA-------MMV------------SANLKLSEKQEvkkelvteiltalglmscshtRTALLSGGQRKRL 148
Cdd:TIGR03719 394 RDALDPNKTVWEEisggldiIKLgkreipsrayvgRFNFKGSDQQK---------------------KVGQLSGGERNRV 452
|
170 180
....*....|....*....|...
gi 1131742492 149 AIALELVNNPPVMFFDEPTSGLD 171
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-217 |
5.04e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 8 EVKQLA-RGHTAGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR------ELRtfRK 80
Cdd:PRK13650 6 EVKNLTfKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLteenvwDIR--HK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 81 MSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPV 160
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMK-ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 161 MFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQpsakLFE--MFDKLYILSQGQ 217
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
140-206 |
5.93e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 5.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIH--QPSAKLFEM 206
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHnmQQAARVSDM 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-197 |
1.70e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.01 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAG--YRESGMkgqILVNGRPRELRT---FRKMSCYIMQD-DMLLPHLTV-------LEam 101
Cdd:PRK13635 34 EWVAIVGHNGSGKSTLAKLLNGllLPEAGT---ITVGGMVLSEETvwdVRRQVGMVFQNpDNQFVGATVqddvafgLE-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 mvsaNLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 181
Cdd:PRK13635 109 ----NIGVPREEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170
....*....|....*..
gi 1131742492 182 MKSL-AQGGRTIICTIH 197
Cdd:PRK13635 183 VRQLkEQKGITVLSITH 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
39-171 |
2.04e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 39 IMGPSGAGKSTFMNILAGYRESGmKGQILvngRPRELRTfrkmsCYIMQD---DMLLPhLTVLEAMMVSANlklsekqeV 115
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPD-EGVIK---RNGKLRI-----GYVPQKlylDTTLP-LTVNRFLRLRPG--------T 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 116 KKElvtEILTALGLMSCSHTRTA---LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:PRK09544 97 KKE---DILPALKRVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-190 |
2.68e-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: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 29 GKFCRRELIGIMGPSGAGKSTFMNILAGYREsgmkgqilvngrPRElrtfrkmscyimqDDMLLPHLTVLeammvsanlk 108
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 lsekqeVKKELVTeiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 188
Cdd:cd03222 65 ------YKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
..
gi 1131742492 189 GR 190
Cdd:cd03222 121 GK 122
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-222 |
2.97e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPrelrtfrkmsCYIMQDDMLLPHLTVLEAM------MVSANLK 108
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFHDIP----------LTKLQLDSWRSRLAVVSQTpflfsdTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 109 LSEKQEVKKEL--------VTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:PRK10789 411 LGRPDATQQEIehvarlasVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131742492 179 vslMKSLAQGG--RTIICTIHQPSAkLFEMfDKLYILSQGQCIFKG 222
Cdd:PRK10789 491 ---LHNLRQWGegRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRG 531
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-185 |
3.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTF----RKMSCYIMQDDMLLPHLTVLE 99
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 179
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
....*.
gi 1131742492 180 SLMKSL 185
Cdd:PRK13642 181 RVIHEI 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-217 |
4.50e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 134 HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYIL 213
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVM 464
|
....
gi 1131742492 214 SQGQ 217
Cdd:PRK10982 465 SNGL 468
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-234 |
6.21e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKS----TFMNiLAGYRESGMKGQILVNGR------PRELRTFRKMS-CYIMQDDM--LLPHLTVLEAM 101
Cdd:PRK11022 34 EVVGIVGESGSGKSvsslAIMG-LIDYPGRVMAEKLEFNGQdlqrisEKERRNLVGAEvAMIFQDPMtsLNPCYTVGFQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 102 MVSANLKLSEKQEVKKELVTEILTALGL---MSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 178
Cdd:PRK11022 113 MEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 179 VSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 234
Cdd:PRK11022 193 IELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFraprhPYTQAL 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-171 |
8.89e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP---RELRTFRK---MScyimQDDMLLPHLTVLEAMMVSAN 106
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPvdaGDIATRRRvgyMS----QAFSLYGELTVRQNLELHAR 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131742492 107 L-KLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 171
Cdd:NF033858 366 LfHLPAAE--IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-217 |
9.22e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 35 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRprelrTFRKMSCYIMQDDML--LP-----HLTVLEAMM---VS 104
Cdd:PRK15439 290 EILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGK-----EINALSTAQRLARGLvyLPedrqsSGLYLDAPLawnVC 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 105 A------NLKLSEKQEvkKELVTEILTALGLmSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 176
Cdd:PRK15439 364 AlthnrrGFWIKPARE--NAVLERYRRALNI-KFNHAEQAArtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1131742492 177 QVVSLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 217
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-200 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKSTFmnILAGYRESGMKgqILVNGRPRelrtfrkmscyimqddmllphltvleammV 103
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKA--RLISFLPK-----------------------------F 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 104 SANLKLSEKQevkkeLVTEILTALGLMSCSHtRTALLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSL 181
Cdd:cd03238 58 SRNKLIFIDQ-----LQFLIDVGLGYLTLGQ-KLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEV 131
|
170
....*....|....*....
gi 1131742492 182 MKSLAQGGRTIICTIHQPS 200
Cdd:cd03238 132 IKGLIDLGNTVILIEHNLD 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-174 |
1.88e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 37 IGIMGPSGAGKSTFMNILAGY-RESgmkgqilvNGrprELRTFRKMSC-YIMQDDMLLPHLTVLEAMM------------ 102
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVdKEF--------EG---EARPAPGIKVgYLPQEPQLDPEKTVRENVEegvaevkaaldr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 ---VSANL--------KLSEKQEvkkELvTEILTALGL-------------MSC--SHTRTALLSGGQRKRLAIALELVN 156
Cdd:PRK11819 105 fneIYAAYaepdadfdALAAEQG---EL-QEIIDAADAwdldsqleiamdaLRCppWDAKVTKLSGGERRRVALCRLLLE 180
|
170
....*....|....*...
gi 1131742492 157 NPPVMFFDEPTSGLDSAS 174
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAES 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
33-219 |
2.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRELRTFR----KMSCYIMQDDMLLPHLTVLEammvsaNL 107
Cdd:NF040905 26 EGEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCRFKDIRdseaLGIVIIHQELALIPYLSIAE------NI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 108 KLSEKQ---------EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAsc 175
Cdd:NF040905 100 FLGNERakrgvidwnETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131742492 176 fQVVSLMKSL-AQGGRTIIctIhqpSAKLFEMF---DKLYILSQGQCI 219
Cdd:NF040905 177 -ALLDLLLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
99-200 |
4.58e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 99 EAMMVSANLKLSEKQEV----KKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 172
Cdd:PTZ00265 533 ELIEMRKNYQTIKDSEVvdvsKKVLIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
90 100
....*....|....*....|....*....
gi 1131742492 173 ASCFQVVSLMKSL-AQGGRTIICTIHQPS 200
Cdd:PTZ00265 613 KSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
33-217 |
6.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 33 RR-ELIGIMGPSGAGKSTF-MNILA---GYRESGmkgQILVNGRPRELRTF--------------RKMSCYIMQDDML-- 91
Cdd:NF040905 284 RRgEIVGIAGLMGAGRTELaMSVFGrsyGRNISG---TVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLIDDIKrn 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 92 --LPHLTvleamMVSANLKLSEKQEVKkeLVTEILTALGLMSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 168
Cdd:NF040905 361 itLANLG-----KVSRRGVIDENEEIK--VAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 169 GLDSASCFQVVSLMKSLAQGGRTIIcTIhqpSAKLFE---MFDKLYILSQGQ 217
Cdd:NF040905 434 GIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPEllgMCDRIYVMNEGR 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-174 |
7.27e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 4 LELREV--KQLARGHTAGYKTL-LKCLSGKfcrreLIGIMGPSGAGKSTFMNILAGY----------------------- 57
Cdd:PTZ00265 1166 IEIMDVnfRYISRPNVPIYKDLtFSCDSKK-----TTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 58 -------RESGMK-----------------------GQILVNGR---PRELRTFRKMSCYIMQDDMLLpHLTVLEAMM-- 102
Cdd:PTZ00265 1241 dyqgdeeQNVGMKnvnefsltkeggsgedstvfknsGKILLDGVdicDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKfg 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 103 --------VSANLKLSEKQEVKKELVTEILTALGLMSCShtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 174
Cdd:PTZ00265 1320 kedatredVKRACKFAAIDEFIESLPNKYDTNVGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
140-198 |
1.62e-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: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SASCFQvVSLMKSLAQGGRTIICTIHQ 198
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
140-244 |
1.81e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCI 219
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|
gi 1131742492 220 FKGVVTNLI-----PYLKGLGLHCPTYHNP 244
Cdd:PRK15093 239 ETAPSKELVttphhPYTQALIRAIPDFGSA 268
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
197-254 |
1.86e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 44.13 E-value: 1.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742492 197 HQPSAKLFEMFDKLYILSQGQCI-FKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASG 254
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-200 |
1.95e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 1 MRDLELREVKQLARGHTAG-YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRprelrtfr 79
Cdd:PRK13545 16 MYNKPFDKLKDLFFRSKDGeYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKGS-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 80 kmSCYIMQDDMLLPHLTVLEAMMVSAnLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPP 159
Cdd:PRK13545 87 --AALIAISSGLNGQLTGIENIELKG-LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131742492 160 VMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPS 200
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLS 204
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-199 |
2.08e-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: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 24 LKCLSGKFCRRELIGIMGPSGAGKST--FMNILAgyresgmkgqilvNGRPRELRTFrkmSCYIMQ--DDMLLPHLTVLE 99
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlaFDTIYA-------------EGQRRYVESL---SAYARQflGQMDKPDVDSIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 100 AMmvSANLKLSEK---QEVKKEL--VTEI-------------------LTALGLMSCSHTRTA-LLSGG--QRKRLA--I 150
Cdd:cd03270 75 GL--SPAIAIDQKttsRNPRSTVgtVTEIydylrllfarvgirerlgfLVDVGLGYLTLSRSApTLSGGeaQRIRLAtqI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1131742492 151 ALELVNnppVMF-FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQP 199
Cdd:cd03270 153 GSGLTG---VLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
136-216 |
3.28e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 136 RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKSLAQGGRTIICT--IHqpsakLFEMFDKLYI 212
Cdd:PLN03232 737 RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIIL 811
|
....
gi 1131742492 213 LSQG 216
Cdd:PLN03232 812 VSEG 815
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-197 |
3.87e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 140 LSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
140-211 |
8.23e-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: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 140 LSGGQRK------RLAIALELVNNPPVMFFDEPTSGLDSASC-FQVVSLMKS-LAQGGRTIICTIHQPsaKLFEMFDKLY 211
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
139-200 |
9.67e-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: 9.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131742492 139 LLSGGQRK---RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPS 200
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
114-193 |
2.23e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 114 EVKKELVTEILTA-LGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 192
Cdd:PRK10938 109 EVKDPARCEQLAQqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL 188
|
.
gi 1131742492 193 I 193
Cdd:PRK10938 189 V 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-197 |
2.35e-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: 2.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131742492 140 LSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 197
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
140-217 |
3.24e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 140 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMKSLA--QGGrtiICTIHQPSAKLFEMFDKLYILSQGQ 217
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-91 |
4.14e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 19 GYKTLLKCLSGKFCRRELIGIMGPSGAGKS----TFMNILagyreSGMKGQILVNGRP------RELRtfRKMScYIMQD 88
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKStlllTFMRMV-----EVCGGEIRVNGREigayglRELR--RQFS-MIPQD 1392
|
...
gi 1131742492 89 DML 91
Cdd:PTZ00243 1393 PVL 1395
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
36-55 |
4.39e-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: 4.39e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-229 |
5.66e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 123 ILTALGLMSCSHTRT-ALLSGGQRKRLAIA----LELVNnppVMF-FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTI 196
Cdd:PRK00635 459 ILIDLGLPYLTPERAlATLSGGEQERTALAkhlgAELIG---ITYiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE 535
|
90 100 110
....*....|....*....|....*....|....
gi 1131742492 197 HQpsAKLFEMFDKLYILSQGQCIFKG-VVTNLIP 229
Cdd:PRK00635 536 HD--EQMISLADRIIDIGPGAGIFGGeVLFNGSP 567
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
140-215 |
6.04e-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: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742492 140 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRtIICTIHQPsaKLFEMFDKLYILSQ 215
Cdd:cd03272 159 LSGGQKSLVALALIFaiqkCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQ-FITTTFRP--ELLEVADKFYGVKF 235
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
37-78 |
9.26e-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: 9.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1131742492 37 IGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTF 78
Cdd:cd01136 70 IGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGREVREF 111
|
|
| |
