|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-475 |
1.44e-63 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 214.11 E-value: 1.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 24 SFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPspstsfsypfLKGKSDSPWQAIQLLDFKSSgQQRAAYYSERYHS--F 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL----------LSGERQSQFSHITRLSFEQL-QKLVSDEWQRNNTdmL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 102 RDKEHDT--TLEKWLLGAYRGNEKfasqhVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGL 179
Cdd:PRK10938 92 SPGEDDTgrTTAEIIQDEVKDPAR-----CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 180 DVTSRSVLSSLLGEMsNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQ-----YIPMTSHSTNI-------P 247
Cdd:PRK10938 167 DVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEilqqaLVAQLAHSEQLegvqlpeP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 248 VKPQMKKSKPItiGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASNIKFFGK 327
Cdd:PRK10938 246 DEPSARHALPA--NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 328 SigPGTGISIFDIQENIGHCSPEIHNHFPKQHTCFEALLSAWSTTFTIPKLTETRLAAISSilEEFEL----KDIKDKPL 403
Cdd:PRK10938 324 R--RGSGETIWDIKKHIGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQ--QWLDIlgidKRTADAPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 404 SSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTkyvhmahnyLNEKL-----------SPSQaMVIISHYEDELPACV 472
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP---------LNRQLvrrfvdvliseGETQ-LLFVSHHAEDAPACI 469
|
...
gi 19115286 473 NRR 475
Cdd:PRK10938 470 THR 472
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
263-484 |
1.14e-62 |
|
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: 204.16 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASNIKFFGKSIGpgtGISIFDIQE 342
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRG---GEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGHCSPEIHNHFPKQHTCFEALLSA-WSTTFTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIV 421
Cdd:COG1119 79 RIGLVSPALQLRFPRDETVLDVVLSGfFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 422 KQPRLVVLDEPFQGVDtkyVHMAHNYLN--EKL--SPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:COG1119 159 KDPELLILDEPTAGLD---LGARELLLAllDKLaaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-437 |
1.35e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.50 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 1 MASFVKFAN--TTFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGsFTPSPSTSFSYPFLKGKSdspwqaI 78
Cdd:COG1123 1 MTPLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLDGRD------L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 79 QLLDFKSSGQQRAAYYSERYHSFrdkeHDTTLEKWL---LGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSR 155
Cdd:COG1123 74 LELSEALRGRRIGMVFQDPMTQL----NPVTVGDQIaeaLENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 156 RAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQ 235
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 236 YI--PMTSHSTNIPVKPQMKKSKPITIGKPLISMEHLNCVYWGR-----KVLSDINWTIREGERWALTGSNGSGKTTLLA 308
Cdd:COG1123 230 ILaaPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 309 YVVG-DHPKlfASNIKFFGKSIGPGTGISIFDIQENIG-------HCspeihnhFPKQHTCFEALLSAWSTTFTIPKltE 380
Cdd:COG1123 310 LLLGlLRPT--SGSILFDGKDLTKLSRRSLRELRRRVQmvfqdpySS-------LNPRMTVGDIIAEPLRLHGLLSR--A 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 381 TRLAAISSILEEFEL-KDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:COG1123 379 ERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
263-471 |
2.80e-27 |
|
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: 108.72 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIGpgtgISIFDIQE 342
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP-PSAGEVLWNGEPIR----DAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NI---GHcSPEIHNHFpkqhTCFEaLLSAWSTTFTIPKLTETRLAAissiLEEFELKDIKDKPLSSISVGMQRFILFCRA 419
Cdd:COG4133 76 RLaylGH-ADGLKPEL----TVRE-NLRFWAALYGLRADREAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115286 420 IVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSpSQAMVII-SHYEDELPAC 471
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLtTHQPLELAAA 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
263-439 |
1.91e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.48 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIGPGtgisifdiQE 342
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PTSGTVRLFGKPPRRA--------RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGHC--SPEIHNHFPKqhTCFEALLS-AWSTTFTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVG-MQRfILFCR 418
Cdd:COG1121 76 RIGYVpqRAEVDWDFPI--TVRDVVLMgRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGqQQR-VLLAR 152
|
170 180
....*....|....*....|.
gi 19115286 419 AIVKQPRLVVLDEPFQGVDTK 439
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAA 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
266-477 |
3.79e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 105.69 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 266 SMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASnIKFFGKSIGpgtgisifDIQENIG 345
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS-IRVFGKPLE--------KERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 346 HCsPEIHN---HFPKqhTCFE-ALLSAWSTTFTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIV 421
Cdd:cd03235 72 YV-PQRRSidrDFPI--SVRDvVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115286 422 KQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH-------YEDELpACVNRRAH 477
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHdlglvleYFDRV-LLLNRTVV 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-432 |
5.24e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCI-------QGSFTPSPSTSFSY-----PFLKGKS--------DSPWQA 77
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILagelepdSGEVSIPKGLRIGYlpqepPLDDDLTvldtvldgDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 78 IQlldfkssgQQRAAYYSERYHSFRDKEHDTTLEKWL--LGAYRgnekfASQHVQEAASMTQLSHLLPSSLI-NLSNGQS 154
Cdd:COG0488 92 LE--------AELEELEAKLAEPDEDLERLAELQEEFeaLGGWE-----AEARAEEILSGLGFPEEDLDRPVsELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 155 RRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEmsnhcSPKIVLslrpqdkipdFITH-----------VLELK 223
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN-----YPGTVL----------VVSHdryfldrvatrILELD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 224 NKKIT-YQGP---------------------------KEQ-----YIPMTSHST---------------NIPV---KPQM 252
Cdd:COG0488 224 RGKLTlYPGNysayleqraerleqeaaayakqqkkiaKEEefirrFRAKARKAKqaqsrikaleklereEPPRrdkTVEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 253 KKSKPITIGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASNIKFFGKSIGPG 332
Cdd:COG0488 304 RFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL--------KLLAGELEPDSGTVKLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 333 TGISI--FDiQEnighcspeiHNHFPKQHTCFEALLSAWsttftiPKLTETRlaaISSILEEFELK-DIKDKPLSSISVG 409
Cdd:COG0488 376 ETVKIgyFD-QH---------QEELDPDKTVLDELRDGA------PGGTEQE---VRGYLGRFLFSgDDAFKPVGVLSGG 436
|
490 500
....*....|....*....|...
gi 19115286 410 MQRFILFCRAIVKQPRLVVLDEP 432
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEP 459
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-235 |
6.02e-25 |
|
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: 103.24 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPStsfsypflkgksdspwQAIQLLDFKSSG------QQRA 91
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----------------NDVRLFGERRGGedvwelRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 92 AYYS-ERYHSFRDkehDTTLEKWLLGAYrgnekFAS------------QHVQEAASMTQLSHLLPSSLINLSNGQSRRAM 158
Cdd:COG1119 81 GLVSpALQLRFPR---DETVLDVVLSGF-----FDSiglyreptdeqrERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 159 LASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVL-SLRPQDkIPDFITHVLELKNKKITYQGPKEQ 235
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLvTHHVEE-IPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
266-482 |
3.49e-24 |
|
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: 99.85 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 266 SMEHLNCVYWG--RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIgpgTGISIFDIQEN 343
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT-SGEVLVDGKDL---TKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGhcspeihnhF----PKQ----HTCFEALlsAWS-TTFTIPKltETRLAAISSILEEFELKDIKDKPLSSISVGMQRFI 414
Cdd:cd03225 77 VG---------LvfqnPDDqffgPTVEEEV--AFGlENLGLPE--EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 415 LFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGK 482
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
264-486 |
4.49e-24 |
|
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: 100.70 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASNIKffgksigPGTG-ISIFDI-- 340
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLL--------RMLAGLLK-------PDSGsILIDGEdv 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 341 -------QENIGHcSPEIhNHFPKQHTCFEALLSAwSTTFTIPKltETRLAAISSILEEFELKDIKDKPLSSISVGMQRF 413
Cdd:COG4555 66 rkepreaRRQIGV-LPDE-RGLYDRLTVRENIRYF-AELYGLFD--EELKKRIEELIELLGLEEFLDRRVGELSTGMKKK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 414 ILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEkLSPSQAMVIIS-HYEDELPACVNRRAHIDNGKLVIH 486
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSsHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
265-484 |
5.86e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.14 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASNIKffgksigPGTG-ISIFDiqEN 343
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTI--------RMLLGLLR-------PTSGeVRVLG--ED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCSPEIHNHF---PkQHTCFEALLSAW------STTFTIPKltETRLAAISSILEEFELKDIKDKPLSSISVGMQRFI 414
Cdd:COG1131 64 VARDPAEVRRRIgyvP-QEPALYPDLTVRenlrffARLYGLPR--KEARERIDELLELFGLTDAADRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 415 LFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEkLSPSQAMVIIS-HYEDELPACVNRRAHIDNGKLV 484
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRE-LAAEGKTVLLStHYLEEAERLCDRVAIIDKGRIV 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
266-482 |
1.91e-23 |
|
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: 96.16 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 266 SMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKlFASNIKFFGKSIGPgtgISIFDIQENIG 345
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP-TSGEILIDGKDIAK---LPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 346 HCspeihnhfpkqhtcfeallsawsttftipkltetrlaaissileeFELkdikdkplssiSVGMQRFILFCRAIVKQPR 425
Cdd:cd00267 77 YV---------------------------------------------PQL-----------SGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 426 LVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGK 482
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
265-483 |
4.53e-23 |
|
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: 95.93 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHpKLFASNIKFFGKSIGPGTGisifDIQENI 344
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL-KPDSGEIKVLGKDIKKEPE----EVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GHCsPEiHNHFPKQHTCFEALlsawsttftipKLtetrlaaissileefelkdikdkplssiSVGMQRFILFCRAIVKQP 424
Cdd:cd03230 76 GYL-PE-EPSLYENLTVRENL-----------KL----------------------------SGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 425 RLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKL 483
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-484 |
1.52e-22 |
|
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: 100.65 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQG--SFTPS-----------PSTSFSYPFLKGKSDSPW----QAIQ 79
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTsgriiyhvalcEKCGYVERPSKVGEPCPVcggtLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 80 LLDF-------KSSGQQRAAYYSERyhSFRDKEHDTTLEKWLLG----AYRGNEkfASQHVQEAASMTQLSHLLPSSLIN 148
Cdd:TIGR03269 93 EVDFwnlsdklRRRIRKRIAIMLQR--TFALYGDDTVLDNVLEAleeiGYEGKE--AVGRAVDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD-VTSRSVLSSLLGEMSNHCSPKIVLSLRPQdKIPDFITHVLELKNKKI 227
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVLTSHWPE-VIEDLSDKAIWLENGEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 228 TYQGPKEQYIPMTSHSTnipvkPQMKKSKPITIGKPLISMEHLNCVYWG-----RKVLSDINWTIREGERWALTGSNGSG 302
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGV-----SEVEKECEVEVGEPIIKVRNVSKRYISvdrgvVKAVDNVSLEVKEGEIFGIVGTSGAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 303 KTTLLAYVVGDHPklfasnikffgksigPGTGISIFDIQE-----------NIGHCSPEI------HNHFPkQHTCFEAL 365
Cdd:TIGR03269 323 KTTLSKIIAGVLE---------------PTSGEVNVRVGDewvdmtkpgpdGRGRAKRYIgilhqeYDLYP-HRTVLDNL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 366 LSAWSTTFtiPKLTETRLAAI---SSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD--TKy 440
Cdd:TIGR03269 387 TEAIGLEL--PDELARMKAVItlkMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpiTK- 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19115286 441 VHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:TIGR03269 464 VDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
280-433 |
1.90e-22 |
|
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: 93.48 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 280 LSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASN-------IKFFGKSIgpgTGISIFDIQENIGHCsPEIH 352
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLL--------KLIAGLlsptegtILLDGQDL---TDDERKSLRKEIGYV-FQDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 353 NHFPkQHTCFEALLSAWSTTFTIPKLTETRLAAissILEEFELKDIKDKPL----SSISVGMQRFILFCRAIVKQPRLVV 428
Cdd:pfam00005 69 QLFP-RLTVRENLRLGLLLKGLSKREKDARAEE---ALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*
gi 19115286 429 LDEPF 433
Cdd:pfam00005 145 LDEPT 149
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
265-484 |
1.12e-20 |
|
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: 90.26 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVY--WGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIGPgtgiSIFDIQE 342
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINGYSIRT----DRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGHCsPEiHNHFPKQHTCFEALLsawstTFT----IPKLTETrlAAISSILEEFELKDIKDKPLSSISVGMQRFILFCR 418
Cdd:cd03263 76 SLGYC-PQ-FDALFDELTVREHLR-----FYArlkgLPKSEIK--EEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 419 AIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNeKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLIL-EVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
265-485 |
4.39e-20 |
|
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: 89.10 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGPGTGIS------- 336
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDISGLSEAElyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 337 ---------IFD---IQENIGhcspeihnhFP-KQHTcfeallsawsttftipKLTETRLAAI-SSILEEFELKDIKDKP 402
Cdd:cd03261 79 mgmlfqsgaLFDsltVFENVA---------FPlREHT----------------RLSEEEIREIvLEKLEAVGLRGAEDLY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 403 LSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD----TKYVHMAHNyLNEKLSPSqaMVIISHYEDELPACVNRRAHI 478
Cdd:cd03261 134 PAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasGVIDDLIRS-LKKELGLT--SIMVTHDLDTAFAIADRIAVL 210
|
....*..
gi 19115286 479 DNGKLVI 485
Cdd:cd03261 211 YDGKIVA 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-235 |
5.58e-20 |
|
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: 88.76 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYPFLKGKSDSPW--QAIQLLdfkssGQQRAAYYS 95
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDVRKEPREarRQIGVL-----PDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 eryhsfrdkehdTTLEKWLL---GAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLL 172
Cdd:COG4555 89 ------------LTVRENIRyfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 173 DEPYAGLDVTSRSVLSSLLGEMSNhcSPKIVLslrpqdkipdFITHVLE-----------LKNKKITYQGPKEQ 235
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKK--EGKTVL----------FSSHIMQevealcdrvviLHKGKVVAQGSLDE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-231 |
9.66e-20 |
|
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: 87.59 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQLLDFKSSGQQRAAYYSER 97
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT----------SGS-------IRVFGKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 YHSFrDKEHDTTLE----------KWLLGAYRGNEKfasQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRP 167
Cdd:cd03235 76 RRSI-DRDFPISVRdvvlmglyghKGLFRRLSKADK---AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 168 QLLLLDEPYAGLDVTSRSVLSSLLGEM--SNHCspkIVLSLRPQDKIPDFITHVLELkNKKITYQG 231
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELrrEGMT---ILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
265-484 |
1.14e-19 |
|
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: 87.77 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYW-GRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFAS-------NIKFFGKSIGPGTGIS 336
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLL--------RLLNGllkptsgEVLVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 337 I-------F---DIQ--------------ENIGHCSPEIHnhfpkqhtcfeallsawsttftipkltetrlAAISSILEE 392
Cdd:COG1122 73 LrrkvglvFqnpDDQlfaptveedvafgpENLGLPREEIR-------------------------------ERVEEALEL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 393 FELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACV 472
Cdd:COG1122 122 VGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELA 201
|
250
....*....|..
gi 19115286 473 NRRAHIDNGKLV 484
Cdd:COG1122 202 DRVIVLDDGRIV 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-231 |
1.59e-19 |
|
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: 85.95 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSfsypFLKGKSDSPWQAIQLLdfkssgqQRAAYyser 97
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI----LLDGKDLASLSPKELA-------RKIAY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 yhsfrdkehdttlekwllgayrgnekfasqhVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYA 177
Cdd:cd03214 78 -------------------------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19115286 178 GLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG 231
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
264-432 |
3.36e-19 |
|
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: 87.02 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHpKLFASNIKFFGKSIgpgTGISIFDIQEN 343
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL-KPSSGEVLLDGRDL---ASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCSPEIHNHFPkqHTCFEALL-------SAWSTtftipkLTETRLAAISSILEEFELKDIKDKPLSSISVG-MQRfIL 415
Cdd:COG1120 77 IAYVPQEPPAPFG--LTVRELVAlgryphlGLFGR------PSAEDREAVEEALERTGLEHLADRPVDELSGGeRQR-VL 147
|
170
....*....|....*..
gi 19115286 416 FCRAIVKQPRLVVLDEP 432
Cdd:COG1120 148 IARALAQEPPLLLLDEP 164
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-226 |
4.87e-19 |
|
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: 85.60 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQAIQLLdfkssgqQRAAYyser 97
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL----VDGKDLTKLSLKELR-------RKVGL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 yhSFRDKEH----DTTLE--KWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:cd03225 80 --VFQNPDDqffgPTVEEevAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPqDKIPDFITHVLELKNKK 226
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
265-485 |
7.08e-19 |
|
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: 84.96 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGpgtgiSIFDIQEN 343
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPD--SGEITFDGKSYQ-----KNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHC--SPEIHNHFpkqhTCFEALLsawsttfTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVGM-QRFILfCRAI 420
Cdd:cd03268 74 IGALieAPGFYPNL----TARENLR-------LLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMkQRLGI-ALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 421 VKQPRLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVII-SHYEDELPACVNRRAHIDNGKLVI 485
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELI-LSLRDQGITVLIsSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
268-435 |
2.32e-18 |
|
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: 83.64 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 268 EHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIgpgTGISIFDI-QENIGH 346
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSIRFDGRDI---TGLPPHERaRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 347 CsPEIHNHFPkQHTCFEALLSAWSTtftipKLTETRLAAISSILEEF-ELKDIKDKPLSSISVGMQRFILFCRAIVKQPR 425
Cdd:cd03224 80 V-PEGRRIFP-ELTVEENLLLGAYA-----RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170
....*....|
gi 19115286 426 LVVLDEPFQG 435
Cdd:cd03224 153 LLLLDEPSEG 162
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
274-486 |
2.65e-18 |
|
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: 83.48 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 274 YWGRK-VLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpkLFASN---IKFFGKSIGpgtgisiFDIQENIGHCsP 349
Cdd:cd03269 9 RFGRVtALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG----IILPDsgeVLFDGKPLD-------IAARNRIGYL-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 350 EIHNHFPKQhTCFEALLsaWSTTFTIPKLTETRlAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVL 429
Cdd:cd03269 77 EERGLYPKM-KVIDQLV--YLAQLKGLKKEEAR-RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 430 DEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLVIH 486
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-221 |
3.11e-18 |
|
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: 83.11 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 16 RFPLFK-NVSFELaRKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGK---SDSPWQAIQLLDFKSSGQQRA 91
Cdd:cd03297 9 RLPDFTlKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPD----------GGTivlNGTVLFDSRKKINLPPQQRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 92 AYYSERYHSFrdkEHDTTLEKWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:cd03297 78 GLVFQQYALF---PHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMSNHCspkivlslrpqdKIPD-FITHVLE 221
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNL------------NIPViFVTHDLS 193
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-198 |
2.69e-17 |
|
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: 80.22 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDspWQAIQLLDFKSSGQQRAAYyseR 97
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS----------AGEVL--WNGEPIRDAREDYRRRLAY---L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 YHSFRDKEHDTTLE--KWLLGAYrgNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:COG4133 81 GHADGLKPELTVREnlRFWAALY--GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180
....*....|....*....|...
gi 19115286 176 YAGLDVTSRSVLSSLLGEmsnHC 198
Cdd:COG4133 159 FTALDAAGVALLAELIAA---HL 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
265-484 |
3.25e-17 |
|
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: 80.31 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGeRWALTGSNGSGKTTLLAYVVGdhpkLF---ASNIKFFGKSIgpgtGISIFDIQ 341
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAT----LTppsSGTIRIDGQDV----LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIGHCsPEiHNHFPKQHTCFEAL-LSAWsttftIPKLTETRL-AAISSILEEFELKDIKDKPLSSISVGMQRFILFCRA 419
Cdd:cd03264 72 RRIGYL-PQ-EFGVYPNFTVREFLdYIAW-----LKGIPSKEVkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 420 IVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEkLSpSQAMVIIS-HYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSE-LG-EDRIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
265-484 |
1.00e-16 |
|
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: 78.95 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLlayvvgdhpklfasnIKFFGKSIGPGTG---ISIFDI- 340
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTT---------------IKMLTTLLKPTSGratVAGHDVv 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 341 ------QENIGHCSpeihnhfpkQHTCFEALLSAWSTTFTIPKL----TETRLAAISSILEEFELKDIKDKPLSSISVGM 410
Cdd:cd03265 66 reprevRRRIGIVF---------QDLSVDDELTGWENLYIHARLygvpGAERRERIDELLDFVGLLEAADRLVKTYSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 411 QRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVII--SHYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03265 137 RRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI-EKLKEEFGMTILltTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
261-484 |
1.15e-16 |
|
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: 79.25 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 261 GKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGPGTG----- 334
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGQDITGLSEkelye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 335 ----ISI-------FD---IQENIGhcspeihnhFP-KQHTcfeallsawsttftipKLTETRLAAI-SSILEEFELKDI 398
Cdd:COG1127 80 lrrrIGMlfqggalFDsltVFENVA---------FPlREHT----------------DLSEAEIRELvLEKLELVGLPGA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 399 KDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD----TKYVHMAHNyLNEKLspSQAMVIISHYEDELPACVNR 474
Cdd:COG1127 135 ADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIRE-LRDEL--GLTSVVVTHDLDSAFAIADR 211
|
250
....*....|
gi 19115286 475 RAHIDNGKLV 484
Cdd:COG1127 212 VAVLADGKII 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
265-442 |
1.41e-16 |
|
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: 78.74 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklfasnikffgkSIGPGTGISIFDiQENI 344
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG---------------LVKPDSGKILLD-GQDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GHCspEIHN-------HFPKQHTCFEAL-----LSAWSTTFTIPKltETRLAAISSILEEFELKDIKDKPLSSISVGMQR 412
Cdd:cd03218 65 TKL--PMHKrarlgigYLPQEASIFRKLtveenILAVLEIRGLSK--KEREEKLEELLEEFHITHLRKSKASSLSGGERR 140
|
170 180 190
....*....|....*....|....*....|
gi 19115286 413 FILFCRAIVKQPRLVVLDEPFQGVDTKYVH 442
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
265-462 |
1.13e-15 |
|
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: 76.45 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVY-WGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIGPGTGISIFDIQEN 343
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHcspeIHNHFP--KQHTCFEALL-------SAWSTTFTIPKLTETRLAAisSILEEFELKDIKDKPLSSISVGMQRFI 414
Cdd:cd03256 80 IGM----IFQQFNliERLSVLENVLsgrlgrrSTWRSLFGLFPKEEKQRAL--AALERVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19115286 415 LFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIIS 462
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVS 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-226 |
1.56e-15 |
|
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: 73.82 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQLldfkssgqqraayyser 97
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT----------SGE-------ILI----------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 yhsfrdkeHDTTLEKWLLGAYRgnekfasqhvQEAASMTQLSHllpsslinlsnGQSRRAMLASKLVQRPQLLLLDEPYA 177
Cdd:cd00267 59 --------DGKDIAKLPLEELR----------RRIGYVPQLSG-----------GQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115286 178 GLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDkIPDFITHVLELKNKK 226
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-235 |
2.00e-15 |
|
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: 75.45 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGK---------SDSPWQA---IQLLdfks 85
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT----------SGEvlvdgkditKKNLRELrrkVGLV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 86 sgqqraayyseryhsFRDKEH---DTTLEKWLlgAY----RG-NEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRA 157
Cdd:COG1122 81 ---------------FQNPDDqlfAPTVEEDV--AFgpenLGlPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMsNHCSPKIVLS---LrpqDKIPDFITHVLELKNKKITYQGPKE 234
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVthdL---DLVAELADRVIVLDDGRIVADGTPR 219
|
.
gi 19115286 235 Q 235
Cdd:COG1122 220 E 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
268-486 |
2.00e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 268 EHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKlfasnikFFGKSIGPGTGISIFDIQE----N 343
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR-------DAGNIIIDDEDISLLPLHArarrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHcspeihnhFPKQHTCFEALlSAWSTTFTIPKL-----TETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCR 418
Cdd:PRK10895 80 IGY--------LPQEASIFRRL-SVYDNLMAVLQIrddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 419 AIVKQPRLVVLDEPFQGVDTKYVhMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHI-DNGKLVIH 486
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISV-IDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIvSQGHLIAH 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-175 |
2.62e-15 |
|
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: 73.07 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSfsypFLKGKSDSPWQAIQLldfkssgQQRAAYYSERYH 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI----LLDGQDLTDDERKSL-------RKEIGYVFQDPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 100 SFRDKEHDTTLEKWLLGAYRGNEKFASQhVQEAASMTQLSHLLPSSL----INLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:pfam00005 70 LFPRLTVRENLRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
266-440 |
2.65e-15 |
|
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: 74.01 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 266 SMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASnIKFFGKSIgpgtgisifdiqenig 345
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE-ILLDGKDL---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 346 hcspeihnhfpkqhtcfeallSAWSttftiPKLTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPR 425
Cdd:cd03214 64 ---------------------ASLS-----PKELARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170
....*....|....*
gi 19115286 426 LVVLDEPFQGVDTKY 440
Cdd:cd03214 118 ILLLDEPTSHLDIAH 132
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
267-483 |
1.15e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 267 MEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPklFASNIkffgkSIGPGTGISIFDiQEnig 345
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEP--DSGEV-----SIPKGLRIGYLP-QE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 346 hcspeihNHFPKQHTCFEALLSAWSTTFTI----------PKLTETRLAAISSILEEFELKD-------IK--------- 399
Cdd:COG0488 70 -------PPLDDDLTVLDTVLDGDAELRALeaeleeleakLAEPDEDLERLAELQEEFEALGgweaearAEeilsglgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 400 ----DKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPfqgvdTKY--VHMAH---NYLNEklSPSqAMVIISHYEDELPA 470
Cdd:COG0488 143 eedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEP-----TNHldLESIEwleEFLKN--YPG-TVLVVSHDRYFLDR 214
|
250
....*....|...
gi 19115286 471 CVNRRAHIDNGKL 483
Cdd:COG0488 215 VATRILELDRGKL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-191 |
1.41e-14 |
|
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: 73.14 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQAIQlldfkssgqQRAAYYSERYHS 100
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL----LNGKDITNLPPEK---------RDISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 FrdkEHDTTLEKWLLG--AYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAG 178
Cdd:cd03299 83 F---PHMTVYKNIAYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170
....*....|...
gi 19115286 179 LDVTSRSVLSSLL 191
Cdd:cd03299 160 LDVRTKEKLREEL 172
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
263-482 |
2.37e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIgPGTGISIfdiQ 341
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPD--AGSISLCGEPV-PSRARHA---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIGhCSPEIHNHFPkQHTCFEALLsAWSTTFTIPklTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIV 421
Cdd:PRK13537 80 QRVG-VVPQFDNLDP-DFTVRENLL-VFGRYFGLS--AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 422 KQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGK 482
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
262-484 |
4.73e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 71.23 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYW----GRKVLSDINWTIREGERWALTGSNGSGKTTLLaYVVG--DHPklFASNIKFFGKSIgpgTGI 335
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGglDRP--TSGEVLIDGQDI---SSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 336 SifDIQ------ENIG------HCSPEIhnhfpkqhTCFE-----ALLSAWSttftipklTETRLAAISSILEEFELKDI 398
Cdd:COG1136 76 S--ERElarlrrRHIGfvfqffNLLPEL--------TALEnvalpLLLAGVS--------RKERRERARELLERVGLGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 399 KDKPLSSISVG-MQRfILFCRAIVKQPRLVVLDEPFQGVDTK---YVHMAHNYLNEKLspSQAMVIISHyEDELPACVNR 474
Cdd:COG1136 138 LDHRPSQLSGGqQQR-VAIARALVNRPKLILADEPTGNLDSKtgeEVLELLRELNREL--GTTIVMVTH-DPELAARADR 213
|
250
....*....|
gi 19115286 475 RAHIDNGKLV 484
Cdd:COG1136 214 VIRLRDGRIV 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
263-437 |
5.43e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklfasnikffgkSIGPGTGISIFDIQE 342
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG---------------LVAPDEGVIKRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGHCSPEIHnhfpkqhtcFEALLSAWSTTFTIPKlTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVK 422
Cdd:PRK09544 68 RIGYVPQKLY---------LDTTLPLTVNRFLRLR-PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170
....*....|....*
gi 19115286 423 QPRLVVLDEPFQGVD 437
Cdd:PRK09544 138 RPQLLVLDEPTQGVD 152
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
265-484 |
6.34e-14 |
|
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: 74.10 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVY--WGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFAS-------NIKFFGKSIgpgTGI 335
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL--------KLLLGlyeptsgRILIDGIDL---RQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 336 SIFDIQENIGHCSPEIHnhfpkqhtcfeaLLSAwsttfTI--------PKLTETRL---AAISSILEefelkDIKDKPL- 403
Cdd:COG2274 543 DPASLRRQIGVVLQDVF------------LFSG-----TIrenitlgdPDATDEEIieaARLAGLHD-----FIEALPMg 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 404 ---------SSISVGM-QRfILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEkLSPSQAMVIISHYEDELPACvN 473
Cdd:COG2274 601 ydtvvgeggSNLSGGQrQR-LAIARALLRNPRILILDEATSALDAETEAIILENLRR-LLKGRTVIIIAHRLSTIRLA-D 677
|
250
....*....|.
gi 19115286 474 RRAHIDNGKLV 484
Cdd:COG2274 678 RIIVLDKGRIV 688
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
264-437 |
6.93e-14 |
|
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: 71.00 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVY----WGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdHPKLFASNIKFFGKSIGPGTGISIFD 339
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQENIGHCSPEIHNHFPKQHTCFEALLSAwSTTFTIPKLTETRLAAISSILEEFEL-KDIKDKPLSSISVGMQRFILFCR 418
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEP-LRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170
....*....|....*....
gi 19115286 419 AIVKQPRLVVLDEPFQGVD 437
Cdd:cd03257 159 ALALNPKLLIADEPTSALD 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-232 |
2.30e-13 |
|
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: 69.52 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQLLDFKSSGQQRAAYYSERYH- 99
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGS-----------------VLIDGTDINKLKGKALRQLRRQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 100 -----SFRDKEHDTTLEKWLLG--AYRGNEK-----FASQHVQEAASMTQLSHLLPSSLI---NLSNGQSRRAMLASKLV 164
Cdd:cd03256 81 gmifqQFNLIERLSVLENVLSGrlGRRSTWRslfglFPKEEKQRALAALERVGLLDKAYQradQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 165 QRPQLLLLDEPYAGLD-VTSRSVLsSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGP 232
Cdd:cd03256 161 QQPKLILADEPVASLDpASSRQVM-DLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-221 |
3.30e-13 |
|
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: 67.42 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 16 RFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQLLDFKssgqqraayys 95
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD----------SGE-------IKVLGKD----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 eryhsfrdkehdttlekwllgaYRGNEKFASQHV----QEAASMTQLShllPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:cd03230 64 ----------------------IKKEPEEVKRRIgylpEEPSLYENLT---VRENLKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMSNHcsPKIVLslrpqdkipdFITHVLE 221
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE--GKTIL----------LSSHILE 156
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-231 |
5.03e-13 |
|
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: 68.45 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 19 LFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSfTPSPSTSFSYPFLKGKSDSPWQAiqlldfkssgQQRAAYY--SE 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTSGQILFNGQPRKPDQF----------QKCVAYVrqDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 RYHSfrdkeHDTTLEKWLLGA-YRGNEKFASQHVQEAASMTQLSHLLPSSLIN-----LSNGQSRRAMLASKLVQRPQLL 170
Cdd:cd03234 91 ILLP-----GLTVRETLTYTAiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 171 LLDEPYAGLDvtsrSVLSSLLGEM-SNHC-SPKIVL-SL-RPQDKIPDFITHVLELKNKKITYQG 231
Cdd:cd03234 166 ILDEPTSGLD----SFTALNLVSTlSQLArRNRIVIlTIhQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
265-437 |
5.73e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpkLFASN---IKFFGKSIGPgtgisifDIQ 341
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG----ILAPDsgeVLWDGEPLDP-------EDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIGHCsPEIHNHFPKQhTCFEAL--------LSAwsttftipklTETRlAAISSILEEFELKDIKDKPLSSISVGMQRF 413
Cdd:COG4152 71 RRIGYL-PEERGLYPKM-KVGEQLvylarlkgLSK----------AEAK-RRADEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180
....*....|....*....|....
gi 19115286 414 ILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLD 161
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-208 |
6.35e-13 |
|
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: 66.86 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 14 DARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSdspwqaiqLLDfkssGQqraay 93
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT----------SGRV--------RLD----GA----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 yseryhsfrdkehdtTLEKWLLGAYRGNEKFASQHVQeaasmtqlshLLPSSLIN--LSNGQSRRAMLASKLVQRPQLLL 171
Cdd:cd03246 65 ---------------DISQWDPNELGDHVGYLPQDDE----------LFSGSIAEniLSGGQRQRLGLARALYGNPRILV 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRP 208
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-194 |
8.09e-13 |
|
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: 67.54 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDS---PWQ-AIQLLdFkssgQQRAAY 93
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL----IDGRDVTgvpPERrNIGMV-F----QDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 yseryhsfrdkEHDTTLEKWLLGAYRGNEKFASQH--VQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:cd03259 85 -----------PHLTVAENIAFGLKLRGVPKAEIRarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180
....*....|....*....|...
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEM 194
Cdd:cd03259 154 LDEPLSALDAKLREELREELKEL 176
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
274-467 |
9.25e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 274 YWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklfasnikffgkSIGPGTG-ISIFDIQE---------N 343
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG---------------MTSPDAGkITVLGVPVpararlaraR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGhCSPEIHNhFPKQHTCFEALLsAWSTTFTIPklTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQ 423
Cdd:PRK13536 116 IG-VVPQFDN-LDLEFTVRENLL-VFGRYFGMS--TREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19115286 424 PRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDE 467
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEE 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
259-433 |
1.10e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.81 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 259 TIGKPLISMEHLNCVYWGRK----VLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPklFASNIKFFGKSI-GPG 332
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGlEKP--TSGEVLVDGKPVtGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 333 TGIS-IFdiQEnighcspeiHNHFPkqhtcfeallsaWSTTF----------TIPKltETRLAAISSILEEFELKDIKDK 401
Cdd:COG1116 80 PDRGvVF--QE---------PALLP------------WLTVLdnvalglelrGVPK--AERRERARELLELVGLAGFEDA 134
|
170 180 190
....*....|....*....|....*....|...
gi 19115286 402 -PlSSISVGMQRFILFCRAIVKQPRLVVLDEPF 433
Cdd:COG1116 135 yP-HQLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-484 |
1.11e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.17 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKLfasnikffGKSIGPGTGISIFDIQ----------ENIg 345
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPDS--------GTVTVRGRVSSLLGLGggfnpeltgrENI- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 346 hcspeihnhfpkqhtCFEALLSAWSttftiPKLTETRLAAIssilEEF-ELKDIKDKPLSSISVGMQRFILFCRAIVKQP 424
Cdd:cd03220 106 ---------------YLNGRLLGLS-----RKEIDEKIDEI----IEFsELGDFIDLPVKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 425 RLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-235 |
1.48e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 67.01 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQLLDFKSSGQQRAA-----YYS 95
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT----------SGE-------VRVLGEDVARDPAEVrrrigYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 ER---YHSFRDKEHdttLEkwLLGAYRG-NEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:COG1131 80 QEpalYPDLTVREN---LR--FFARLYGlPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMSNhcSPKIVLslrpqdkipdFITHVLE-----------LKNKKITYQGPKEQ 235
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAA--EGKTVL----------LSTHYLEeaerlcdrvaiIDKGRIVADGTPDE 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-235 |
1.62e-12 |
|
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: 69.41 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 14 DARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPspsTSFSYpFLKGKSDSPWQAIQLldfkssgQQRAAY 93
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP---QSGSI-TLGGVDLRDLDEDDL-------RRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 YSERYHSFrdkehDTTLekwllgayRGNEKFAS-----QHVQEAASMTQLSHL---LPSSL--------INLSNGQSRRA 157
Cdd:COG4987 414 VPQRPHLF-----DTTL--------RENLRLARpdatdEELWAALERVGLGDWlaaLPDGLdtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLD-VTSRSVLSSLLgemsNHCSPKIVLslrpqdkipdFITH----------VLELKNKK 226
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDaATEQALLADLL----EALAGRTVL----------LITHrlaglermdrILVLEDGR 546
|
....*....
gi 19115286 227 ITYQGPKEQ 235
Cdd:COG4987 547 IVEQGTHEE 555
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-191 |
1.78e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSftpsPSTSFSYPFLKGKSDSPWQAiqlldfkssGQQRAAYYSERYHSF 101
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGL----EHQTSGHIRFHGTDVSRLHA---------RDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 102 RdkeHDTTLEKWLLGAY------RGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:PRK10851 87 R---HMTVFDNIAFGLTvlprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170
....*....|....*.
gi 19115286 176 YAGLDVTSRSVLSSLL 191
Cdd:PRK10851 164 FGALDAQVRKELRRWL 179
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-231 |
1.86e-12 |
|
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: 66.54 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTP-SPSTSFSYpflKGKSDSPWQAIQLLDfkssgQQRAAY------ 93
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDG---KPLDIAARNRIGYLP-----EERGLYpkmkvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 ----YSERYHSFRDKEHDTTLEKWLlgayrgnEKFasqhvqeaasmtQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQL 169
Cdd:cd03269 89 dqlvYLAQLKGLKKEEARRRIDEWL-------ERL------------ELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 170 LLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPkIVLSLRPQDKIPDFITHVLELKNKKITYQG 231
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
265-443 |
2.30e-12 |
|
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: 65.84 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIGPGTGISifdiQENI 344
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD-SGEVRWNGTPLAEQRDEP----HENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 ---GHcSPEIhnhfpkqhtcfEALLSAWST-TFTIPKLTETRLaAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAI 420
Cdd:TIGR01189 76 lylGH-LPGL-----------KPELSALENlHFWAAIHGGAQR-TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLW 142
|
170 180
....*....|....*....|...
gi 19115286 421 VKQPRLVVLDEPFQGVDTKYVHM 443
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVAL 165
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-436 |
2.53e-12 |
|
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: 66.31 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPklfASN--IKFFGKSIgpgTGISIFDI---------Qeni 344
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR---PTSgsVLFDGEDI---TGLPPHEIarlgigrtfQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 ghcspeIHNHFPKQhTCFEALL--------SAWSTTFTIPKLTETRlAAISSILEEFELKDIKDKPLSSISVGMQRFILF 416
Cdd:cd03219 83 ------IPRLFPEL-TVLENVMvaaqartgSGLLLARARREEREAR-ERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180
....*....|....*....|
gi 19115286 417 CRAIVKQPRLVVLDEPFQGV 436
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGL 174
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-484 |
2.56e-12 |
|
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: 65.63 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdHP--KLFASNIKFFGKSIgpgTGISIFDIqenighcspeihn 353
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyEVTEGEILFKGEDI---TDLPPEER------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 354 hfpkqhtcfeALLS---AWSTTFTIPKLTetrlaaissiLEEFelkdikdkpLSSISVG-----MQRFILfCRAIVKQPR 425
Cdd:cd03217 75 ----------ARLGiflAFQYPPEIPGVK----------NADF---------LRYVNEGfsggeKKRNEI-LQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 426 LVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHI-DNGKLV 484
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVlYDGRIV 184
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-237 |
2.65e-12 |
|
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: 69.09 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGK---SDSPWQAIQLLDFkssgQQRAAYY 94
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT----------SGRiliDGIDLRQIDPASL----RRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHSFrdkeHDTTLEKWLLGayrgNEKFASQHVQEAASMTQLSHL---LPSSL--------INLSNGQSRRAMLASKL 163
Cdd:COG2274 555 LQDVFLF----SGTIRENITLG----DPDATDEEIIEAARLAGLHDFieaLPMGYdtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 164 VQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSpkIVlslrpqdkipdFITH----------VLELKNKKITYQGPK 233
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRT--VI-----------IIAHrlstirladrIIVLDKGRIVEDGTH 693
|
....
gi 19115286 234 EQYI 237
Cdd:COG2274 694 EELL 697
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-197 |
2.66e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 23 VSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSypflkGKSDSPWQAIQLLDFKS--SGQQRAAYYSERYHS 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFA-----GQPLEAWSAAELARHRAylSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 frdkehdttlekWLLGAYRGNEKFASQH-VQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQ-----RP--QLLLL 172
Cdd:PRK03695 90 ------------LTLHQPDKTRTEAVASaLNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLL 157
|
170 180 190
....*....|....*....|....*....|....
gi 19115286 173 DEPYAGLDVTSRSVLSSLLGE---------MSNH 197
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSElcqqgiavvMSSH 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-231 |
2.72e-12 |
|
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: 65.03 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 11 TFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQLldfkssgqqr 90
Cdd:cd03247 9 SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-----------------ITL---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 91 aayyseryhsfrDKEHDTTLEKWLlgayrgnekfaSQHVqeaASMTQLSHLLPSSLIN-----LSNGQSRRAMLASKLVQ 165
Cdd:cd03247 62 ------------DGVPVSDLEKAL-----------SSLI---SVLNQRPYLFDTTLRNnlgrrFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 166 RPQLLLLDEPYAGLD-VTSRSVLSSLLGEMSNhcspKIVLslrpqdkipdFITH----------VLELKNKKITYQG 231
Cdd:cd03247 116 DAPIVLLDEPTVGLDpITERQLLSLIFEVLKD----KTLI----------WITHhltgiehmdkILFLENGKIIMQG 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-197 |
4.32e-12 |
|
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: 65.92 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQAiqlldfkssgQQRAAYYSERyhS 100
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL----FDGEDITGLPP----------HEIARLGIGR--T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 F---RDKEHDTTLE------------KWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQ 165
Cdd:cd03219 81 FqipRLFPELTVLEnvmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190
....*....|....*....|....*....|..
gi 19115286 166 RPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNH 197
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER 192
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
276-482 |
4.47e-12 |
|
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: 64.33 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIgpgTGISIFDIQENIGHCSPEIHnhf 355
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-PTSGEILIDGVDL---RDLDLESLRKNIAYVPQDPF--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 356 pkqhtcfeaLLSAwsttftipkltetrlaaisSILEEFelkdikdkplssISVG-MQRfILFCRAIVKQPRLVVLDEPFQ 434
Cdd:cd03228 87 ---------LFSG-------------------TIRENI------------LSGGqRQR-IAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19115286 435 GVDTKYVHMAHNYLnEKLSPSQAMVIISHYEDELPACvNRRAHIDNGK 482
Cdd:cd03228 126 ALDPETEALILEAL-RALAKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
262-484 |
4.56e-12 |
|
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: 68.01 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWG--RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPK--LFASNIKFFGKSIgpgTGISI 337
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggRISGEVLLDGRDL---LELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 338 FDIQENIGHCSPEIHNHF-PkqHTCFEALlsawstTFTIPKLTETRLAA---ISSILEEFELKDIKDKPLSSISVGMQRF 413
Cdd:COG1123 79 ALRGRRIGMVFQDPMTQLnP--VTVGDQI------AEALENLGLSRAEArarVLELLEAVGLERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 414 ILFCRAIVKQPRLVVLDEPFQGVD---TKYVHMAHNYLNEKLspSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDvttQAEILDLLRELQRER--GTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
148-483 |
4.71e-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: 67.93 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 148 NLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLS--LRPQDKIPDFIT------HV 219
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIShkLNEVKAVCDTICvirdgqHV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 220 LELKNKKITyqgpKEQYIPMTSHSTNIPVKPQmkksKPITIGKPLISMEHLNC---VYWGRKVLSDINWTIREGERWALT 296
Cdd:TIGR02633 221 ATKDMSTMS----EDDIITMMVGREITSLYPH----EPHEIGDVILEARNLTCwdvINPHRKRVDDVSFSLRRGEILGVA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 297 GSNGSGKTTLLAYVVGDHPKLFASNIKFFGKSigpgtgISIFDIQENIGH---CSPE---IHNHFPKQHTCFEALLSAWS 370
Cdd:TIGR02633 293 GLVGAGRTELVQALFGAYPGKFEGNVFINGKP------VDIRNPAQAIRAgiaMVPEdrkRHGIVPILGVGKNITLSVLK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 371 TTFTIPKLTETrlAAISSILEEFELKDIK----DKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHN 446
Cdd:TIGR02633 367 SFCFKMRIDAA--AELQIIGSAIQRLKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK 444
|
330 340 350
....*....|....*....|....*....|....*..
gi 19115286 447 YLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKL 483
Cdd:TIGR02633 445 LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-231 |
5.59e-12 |
|
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: 64.91 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQnWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDspWQAIQLLDFKSSGQQRAAYYSER-- 97
Cdd:cd03264 16 LDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPS----------SGTIR--IDGQDVLKQPQKLRRRIGYLPQEfg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 -YHSFRDKEHDTTLeKWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRPQLLLLDEPY 176
Cdd:cd03264 83 vYPNFTVREFLDYI-AWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSL---SGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 177 AGLDVTSRSVLSSLLGEMS-NHCspkIVLSLRPQDKIPDFITHVLELKNKKITYQG 231
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGeDRI---VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-235 |
5.71e-12 |
|
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: 65.22 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQLLDFKSSGQQRAAYYSERYH 99
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD----------SGE-------VLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 100 --------------------SFRDKEHdTTLEKWLLGAyRGNEKFasqhvqEAASMTQLSHLLPSsliNLSNGQSRRAML 159
Cdd:cd03261 79 mgmlfqsgalfdsltvfenvAFPLREH-TRLSEEEIRE-IVLEKL------EAVGLRGAEDLYPA---ELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 160 ASKLVQRPQLLLLDEPYAGLDVTSRSVLSSL---LGEMSNHCSpkIVLS--LRPQDKIPDfitHVLELKNKKITYQGPKE 234
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLTS--IMVThdLDTAFAIAD---RIAVLYDGKIVAEGTPE 222
|
.
gi 19115286 235 Q 235
Cdd:cd03261 223 E 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
262-432 |
8.33e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKlFASNIKFFGKSIGPGT-------G 334
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQP-DSGEILLDGEPVRFRSprdaqaaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 335 ISI----------FDIQENIghcspeihnhfpkqhtcfeaLLSAWSTTFTIPKLTETRLAAiSSILEEFELkDIK-DKPL 403
Cdd:COG1129 81 IAIihqelnlvpnLSVAENI--------------------FLGREPRRGGLIDWRAMRRRA-RELLARLGL-DIDpDTPV 138
|
170 180
....*....|....*....|....*....
gi 19115286 404 SSISVGMQRFILFCRAIVKQPRLVVLDEP 432
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEP 167
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-194 |
8.85e-12 |
|
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: 65.05 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSpwqaiqlldfK 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL----FGGEDAT----------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 SSGQQR-AAYYSERYHSFRdkeHDTTLEKWLLG------AYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRA 157
Cdd:cd03296 69 VPVQERnVGFVFQHYALFR---HMTVFDNVAFGlrvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRV 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEM 194
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
149-432 |
8.93e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.02 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRS-VLsSLLGE------MSnhcspkiVLslrpqdkipdFITH--- 218
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAqIL-DLLKDlqrelgMA-------LL----------LITHdlg 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 219 --------VLELKNKKITYQGPKEQYI-----PMTSHStnIPVKPQMKKSKPITIGKPLISMEHLNCVYWGR-------- 277
Cdd:COG4172 219 vvrrfadrVAVMRQGEIVEQGPTAELFaapqhPYTRKL--LAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKrglfrrtv 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 278 ---KVLSDINWTIREGERWALTGSNGSGKTTL-LAYVvgdhpKLFAS--NIKFFGKSIgpgTGIS-------------IF 338
Cdd:COG4172 297 ghvKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-----RLIPSegEIRFDGQDL---DGLSrralrplrrrmqvVF 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 339 diQENIGHCSP-----EI-----HNHFPKqhtcfealLSAwsttftipkltETRLAAISSILEEFELK-DIKDK-P--LS 404
Cdd:COG4172 369 --QDPFGSLSPrmtvgQIiaeglRVHGPG--------LSA-----------AERRARVAEALEEVGLDpAARHRyPheFS 427
|
330 340
....*....|....*....|....*....
gi 19115286 405 sisvGMQR-FILFCRAIVKQPRLVVLDEP 432
Cdd:COG4172 428 ----GGQRqRIAIARALILEPKLLVLDEP 452
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-221 |
8.99e-12 |
|
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: 64.42 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 14 DARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS-------------PSTSFSYPFlkgKSDS--PWQAI 78
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsgevlvdgepvtgPGPDRGYVF---QQDAllPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 79 Q---LLDFKSSGQQRAAyyseryhsfrdkehdttlekwllgayrgnekfASQHVQEAASMTQLS---HLLPSSLinlSNG 152
Cdd:cd03293 91 LdnvALGLELQGVPKAE--------------------------------ARERAEELLELVGLSgfeNAYPHQL---SGG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 153 QSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVlslrpqdkipdFITHVLE 221
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVL-----------LVTHDID 193
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
277-484 |
9.82e-12 |
|
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: 64.53 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpkLF---ASNIKFFGKSIgpgTGISIFDIQENIGHCSPEIHN 353
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG----LYkptSGSVLLDGTDI---RQLDPADLRRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 354 HFpkqHTCFEALlsawstTFTIPKLTETRLAAISSI--LEEFELKDIK--DKPLS----SISVGMQRFILFCRAIVKQPR 425
Cdd:cd03245 90 FY---GTLRDNI------TLGAPLADDERILRAAELagVTDFVNKHPNglDLQIGergrGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 426 LVVLDEPFQGVDTkyvhMAHNYLNEKLS---PSQAMVIISHYEDELpACVNRRAHIDNGKLV 484
Cdd:cd03245 161 ILLLDEPTSAMDM----NSEERLKERLRqllGDKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-191 |
1.40e-11 |
|
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: 62.97 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflkgksdspwqaiqlldfksSGQQraayyseryhS 100
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD----------------------------SGSI----------L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 FRDKEHDTTLEkwLLGAYRGNEKFASQHVQEAASMTQLSHL-LPsslinLSNGQSRRAMLASKLVQRPQLLLLDEPYAGL 179
Cdd:cd03229 59 IDGEDLTDLED--ELPPLRRRIGMVFQDFALFPHLTVLENIaLG-----LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170
....*....|..
gi 19115286 180 DVTSRSVLSSLL 191
Cdd:cd03229 132 DPITRREVRALL 143
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
2.08e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYPflKGKSDSPWQAIQLldfkssgqqraayyseR 97
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-AGTIKLD--GGDIDDPDVAEAC----------------H 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 YHSFRD--KEHDTTLEK---W--LLGAYRGnekfasqHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLL 170
Cdd:PRK13539 77 YLGHRNamKPALTVAENlefWaaFLGGEEL-------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180
....*....|....*....|....*..
gi 19115286 171 LLDEPYAGLDVTSRSVLSSLlgeMSNH 197
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAEL---IRAH 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
263-437 |
2.39e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG----DHPKlfasnIKFFGKSIgpgT----- 333
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkpDSGR-----IFLDGEDI---Thlpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 334 -----GI-------SIF---DIQENIghcspeihnhfpkqhtcfEALLSawstTFTIPKltETRLAAISSILEEFELKDI 398
Cdd:COG1137 74 krarlGIgylpqeaSIFrklTVEDNI------------------LAVLE----LRKLSK--KEREERLEELLEEFGITHL 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115286 399 KDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:COG1137 130 RKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-184 |
2.50e-11 |
|
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: 65.69 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 16 RFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFsypFLKGKSDSPWQAIQLLDFKSSGQ---QRAa 92
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT-SGSI---LFDGKDLTKLSRRSLRELRRRVQmvfQDP- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 93 yyserYHSF--RDKEHDTtLEKWL--LGAYRGNEkfASQHVQEAASMTQLS----HLLPSSLinlSNGQSRRAMLASKLV 164
Cdd:COG1123 352 -----YSSLnpRMTVGDI-IAEPLrlHGLLSRAE--RRERVAELLERVGLPpdlaDRYPHEL---SGGQRQRVAIARALA 420
|
170 180
....*....|....*....|
gi 19115286 165 QRPQLLLLDEPYAGLDVTSR 184
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQ 440
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
286-484 |
3.22e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 286 TIREGERWALTGSNGSGKTTLLAYVVGDHPKLfasnikffgksigpgtgisifdiqenighcSPEIHNHFpkQHT---CF 362
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLL------------------------------SGERQSQF--SHItrlSF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 363 EAL---LSA-W---STTFTIPKLTETRLAAISSILEE-------------FELKDIKDKPLSSISVGMQRFILFCRAIVK 422
Cdd:PRK10938 73 EQLqklVSDeWqrnNTDMLSPGEDDTGRTTAEIIQDEvkdparceqlaqqFGITALLDRRFKYLSTGETRKTLLCQALMS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 423 QPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PRK10938 153 EPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-234 |
3.67e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPStsfsYPFLKGK------SDSPWQAIQLLDFKSSG------Q 88
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHG----HVWLDGEhiqhyaSKEVARRIGLLAQNATTpgditvQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 89 QRAAyySERYhsfrdkEHDTTLEKWllgayrgnEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQ 168
Cdd:PRK10253 100 ELVA--RGRY------PHQPLFTRW--------RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 169 LLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKE 234
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGaPKE 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
268-437 |
3.84e-11 |
|
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: 62.51 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 268 EHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIGPGTGIsifdIQEN---I 344
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRVLLNGGPLDFQRDS----IARGllyL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GHcSPEIhnhfpkqhtcfEALLSAWSTTFTIPKLTETrlAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQP 424
Cdd:cd03231 79 GH-APGI-----------KTTLSVLENLRFWHADHSD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170
....*....|...
gi 19115286 425 RLVVLDEPFQGVD 437
Cdd:cd03231 145 PLWILDEPTTALD 157
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
265-482 |
4.11e-11 |
|
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: 60.93 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDhpklfasnikffgksIGPGTGISIFDIQENI 344
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE---------------LEPDEGIVTWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GHcspeihnhfpkqhtcFEALlsawsttftipkltetrlaaissileefelkdikdkplssiSVGMQRFILFCRAIVKQP 424
Cdd:cd03221 66 GY---------------FEQL-----------------------------------------SGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 425 RLVVLDEPFQGVDTKYVHMAHNYLNEKlspSQAMVIISHYEDELPACVNRRAHIDNGK 482
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEY---PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-255 |
6.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.90 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSF--SYPFLKGKSDSPWQAIQLLdFKSSGQQraaYYSERY 98
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirGEPITKENIREVRKFVGLV-FQNPDDQ---IFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 99 hsfrdkEHDTTLEKWLLGAyrgNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAG 178
Cdd:PRK13652 97 ------EQDIAFGPINLGL---DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 179 LDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQYIP----MTSHSTNIPVKPQMKK 254
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLqpdlLARVHLDLPSLPKLIR 247
|
.
gi 19115286 255 S 255
Cdd:PRK13652 248 S 248
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-195 |
8.51e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.76 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 19 LFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPspsTSFSYPFlKGKSDSPWQAIQLLDFKSsgqQRAAYYSERY 98
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIF-NGQPMSKLSSAAKAELRN---QKLGFIYQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 99 HSFRDKehdTTLEK----WLLGAYRGNEkfASQHVQE---AASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRPQLLL 171
Cdd:PRK11629 97 HLLPDF---TALENvampLLIGKKKPAE--INSRALEmlaAVGLEHRANHRPSEL---SGGERQRVAIARALVNNPRLVL 168
|
170 180
....*....|....*....|....
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMS 195
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELN 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-191 |
8.84e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCI-------QGSFTPSPSTSFSY-----PFLKGkSDSPWQAIQllDFKS 85
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLagelepdSGTVKLGETVKIGYfdqhqEELDP-DKTVLDELR--DGAP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 86 SGQQRAAyyseryHSFrdkehdttLEKWLlgayrgnekFASQHVQEAASmtqlshllpssliNLSNGQSRRAMLASKLVQ 165
Cdd:COG0488 406 GGTEQEV------RGY--------LGRFL---------FSGDDAFKPVG-------------VLSGGEKARLALAKLLLS 449
|
170 180
....*....|....*....|....*.
gi 19115286 166 RPQLLLLDEPYAGLDVTSRSVLSSLL 191
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEAL 475
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-236 |
9.46e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfSYPFLKGKSDSPWQAIQLLDFKSSGQQraayyseryh 99
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS-----SGRILFDGKPIDYSRKGLMKLRESVGM---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 100 SFRDKEHD----TTLEKWLLGAYRGN--EKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLD 173
Cdd:PRK13636 87 VFQDPDNQlfsaSVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 174 EPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKEQY 236
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnPKEVF 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
265-437 |
1.04e-10 |
|
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: 61.33 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVY----WGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSI-GPGTGIS-I 337
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPT--SGEVLVDGEPVtGPGPDRGyV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 338 F---------DIQENI--GhcsPEIHNHFPKQhtcfeallsawsttftipkltetRLAAISSILEEFELKDIKDKPLSSI 406
Cdd:cd03293 79 FqqdallpwlTVLDNValG---LELQGVPKAE-----------------------ARERAEELLELVGLSGFENAYPHQL 132
|
170 180 190
....*....|....*....|....*....|.
gi 19115286 407 SVGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:cd03293 133 SGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
261-483 |
1.10e-10 |
|
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: 60.52 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 261 GKPLISMEHLncvyWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIGPGTGISIfdI 340
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-PASGEITLDGKPVTRRSPRDA--I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 341 QENIGHCSPEIHNHfpkqhtcfeALLSAWSTTFTIpkltetrlaAISSILeefelkdikdkplssiSVG-MQRFILfCRA 419
Cdd:cd03215 74 RAGIAYVPEDRKRE---------GLVLDLSVAENI---------ALSSLL----------------SGGnQQKVVL-ARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 420 IVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKL 483
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
265-439 |
1.37e-10 |
|
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: 61.10 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIgpgTGISIFDIQEN 343
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPT--SGEILLDGKDI---TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCSPEIHNHFpkqhTCFEALlsawstTF--TIPKLTETRLAA-ISSILEEFELKDIKDKPLSSISVGMQRFILFCRAI 420
Cdd:cd03300 76 TVFQNYALFPHL----TVFENI------AFglRLKKLPKAEIKErVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170
....*....|....*....
gi 19115286 421 VKQPRLVVLDEPFQGVDTK 439
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLK 164
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
262-436 |
1.62e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDhPKLFASNIKFFGKSIGPGTGISIfdIQ 341
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDITDWQTAKI--MR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIGhCSPEIHNHFPKQhTCFEALlsAWSTTFTIPKLTETRLAAISSILEefELKDIKDKPLSSISVGMQRFILFCRAIV 421
Cdd:PRK11614 80 EAVA-IVPEGRRVFSRM-TVEENL--AMGGFFAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170
....*....|....*
gi 19115286 422 KQPRLVVLDEPFQGV 436
Cdd:PRK11614 154 SQPRLLLLDEPSLGL 168
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-196 |
2.01e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQAIQLldfkssgqqraayysERYHSF 101
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF----LGDKPISMLSSRQL---------------ARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 102 RDKEHDT----TLEKwlLGAYrGNEKFAS----------QHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRP 167
Cdd:PRK11231 81 LPQHHLTpegiTVRE--LVAY-GRSPWLSlwgrlsaednARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180
....*....|....*....|....*....
gi 19115286 168 QLLLLDEPYAGLDVTSRSVLSSLLGEMSN 196
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNT 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
149-437 |
2.15e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNhcspKIVLSLRpqdkipdFITHVLE------- 221
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ----ELNMGLL-------FITHNLSivrklad 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 222 ----LKNKKITYQGPKEQYIPMTSHstniPVKPQMKKSKPI-------TIGKPLISMEHLNCVYWGRK-----------V 279
Cdd:PRK15134 226 rvavMQNGRCVEQNRAATLFSAPTH----PYTQKLLNSEPSgdpvplpEPASPLLDVEQLQVAFPIRKgilkrtvdhnvV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 280 LSDINWTIREGERWALTGSNGSGK-TTLLAYVvgdhpKLFASNikffgksigpgtGISIFDIQenighcspEIHNHFPKQ 358
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKsTTGLALL-----RLINSQ------------GEIWFDGQ--------PLHNLNRRQ 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 359 --------HTCFEALLSAWSTTFTI------------PKLT-ETRLAAISSILEEFELK-DIKDKPLSSISVGMQRFILF 416
Cdd:PRK15134 357 llpvrhriQVVFQDPNSSLNPRLNVlqiieeglrvhqPTLSaAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAI 436
|
330 340
....*....|....*....|.
gi 19115286 417 CRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD 457
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-197 |
2.44e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGksdspwQAIQLLdfksSGQQRAAYYSER-YHS 100
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL----LRG------QHIEGL----PGHQIARMGVVRtFQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 FRDKEHDTTLEKWLLG-----------------AYRGNEKFAsqhVQEAASMTQLSHLLP---SSLINLSNGQSRRAMLA 160
Cdd:PRK11300 89 VRLFREMTVIENLLVAqhqqlktglfsgllktpAFRRAESEA---LDRAATWLERVGLLEhanRQAGNLAYGQQRRLEIA 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115286 161 SKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNH 197
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNE 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-234 |
2.44e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDSPWQAIQLldfKSSGQQRAAYYSERYHSF 101
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS----------SGTITIAGYHITP---ETGNKNLKKLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 102 RDKE----HDTTLEKWLLGAYrgNEKFASQHVQEAASMTQLSHLLPSSLIN-----LSNGQSRRAMLASKLVQRPQLLLL 172
Cdd:PRK13641 92 QFPEaqlfENTVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISkspfeLSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 173 DEPYAGLDVTSRSVLSSLLGEM--SNHcspKIVLSLRPQDKIPDFITHVLELKNKK-ITYQGPKE 234
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYqkAGH---TVILVTHNMDDVAEYADDVLVLEHGKlIKHASPKE 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
246-484 |
2.44e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 246 IPvKPQMKKSKPITigkPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklFASnikff 325
Cdd:PRK11607 5 IP-RPQAKTRKALT---PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-----FEQ----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 326 gksigPGTGISIFDIQEnIGHCSPEIH--NHFPKQHTCFEALLSAWSTTFTIP--KLTETRLAA-ISSILEEFELKDIKD 400
Cdd:PRK11607 71 -----PTAGQIMLDGVD-LSHVPPYQRpiNMMFQSYALFPHMTVEQNIAFGLKqdKLPKAEIASrVNEMLGLVHMQEFAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 401 KPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYV-HMAHNYLN--EKLSPSQAMViiSHYEDELPACVNRRAH 477
Cdd:PRK11607 145 RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVVDilERVGVTCVMV--THDQEEAMTMAGRIAI 222
|
....*..
gi 19115286 478 IDNGKLV 484
Cdd:PRK11607 223 MNRGKFV 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-222 |
2.56e-10 |
|
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: 59.96 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 19 LFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQaiqlldfkssgQQRAAYYSE-- 96
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL----LNGKPIKAKE-----------RRKSIGYVMqd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 -RYHSFRDkehdTTLEKWLLG---AYRGNEKfaSQHVQEAASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRPQLLLL 172
Cdd:cd03226 80 vDYQLFTD----SVREELLLGlkeLDAGNEQ--AETVLKDLDLYALKERHPLSL---SGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19115286 173 DEPYAGLDvtsrsvlsslLGEMSNHCspKIVLSLRPQDKIPDFITHVLEL 222
Cdd:cd03226 151 DEPTSGLD----------YKNMERVG--ELIRELAAQGKAVIVITHDYEF 188
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-235 |
2.64e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.62 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 23 VSFELARKQNWAIIGNTGSGRTTFLRCIQGsFTPSPSTSFsypfLKGKSDSPWQAIQLLDFKS--SGQQRAA-------Y 93
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIL----LNGRPLSDWSAAELARHRAylSQQQSPPfampvfqY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 YSERYHSFRDKEHDTTLekwllgayrgnekfasqhVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQ-------R 166
Cdd:COG4138 90 LALHQPAGASSEAVEQL------------------LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 167 PQLLLLDEPYAGLDVTSRSVLSSLLGE---------MSNHcspKIVLSLRPQDkipdfitHVLELKNKKITYQGPKEQ 235
Cdd:COG4138 152 GQLLLLDEPMNSLDVAQQAALDRLLRElcqqgitvvMSSH---DLNHTLRHAD-------RVWLLKQGKLVASGETAE 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-231 |
3.29e-10 |
|
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: 59.49 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 15 ARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSfTPSPSTSFSYpFLKGKSDSPwqaiqlldfkssgqqraayy 94
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR-RTGLGVSGEV-LINGRPLDK-------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 seryHSFRDK-----EHDTTlekwllgayrgnekFASQHVQEAASMTqlshllpSSLINLSNGQSRRAMLASKLVQRPQL 169
Cdd:cd03213 78 ----RSFRKIigyvpQDDIL--------------HPTLTVRETLMFA-------AKLRGLSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 170 LLLDEPYAGLD-VTSRSVLSSLLGEMSNHCSpkIVLSL-RPQDKIPDFITHVLELKNKKITYQG 231
Cdd:cd03213 133 LFLDEPTSGLDsSSALQVMSLLRRLADTGRT--IICSIhQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-221 |
3.44e-10 |
|
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: 59.69 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGK--------SDSPWQAIQLLDFKSSGqqRAA 92
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD----------AGFatvdgfdvVKEPAEARRRLGFVSDS--TGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 93 YysERYhsfrdkehdTTLE--KWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLL 170
Cdd:cd03266 90 Y--DRL---------TAREnlEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115286 171 LLDEPYAGLDVTSRSVLSSLLGEmsnhcspkivlsLRPQDKIPDFITHVLE 221
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQ------------LRALGKCILFSTHIMQ 197
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
277-446 |
3.86e-10 |
|
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: 59.98 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG--DHPKLFASNIKFFGKSIGPGTgisifdIQENIGHCSpeihnh 354
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTTSGQILFNGQPRKPDQ------FQKCVAYVR------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 355 fpkQHTCFEALLSAWST-TFTIP-KLTETRLAAISSILEEFE------LKDIKDKPLSSISVGMQRFILFCRAIVKQPRL 426
Cdd:cd03234 88 ---QDDILLPGLTVRETlTYTAIlRLPRKSSDAIRKKRVEDVllrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180
....*....|....*....|
gi 19115286 427 VVLDEPFQGVDTkyvHMAHN 446
Cdd:cd03234 165 LILDEPTSGLDS---FTALN 181
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-191 |
4.34e-10 |
|
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: 58.97 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypFLKGKSDSPWQAIQLLDFKssgqQRAAYYseryhs 100
Cdd:TIGR01166 9 KGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGA-----VLIDGEPLDYSRKGLLERR----QRVGLV------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 FRDKE---------HDTTLEKWLLGayrGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:TIGR01166 74 FQDPDdqlfaadvdQDVAFGPLNLG---LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180
....*....|....*....|
gi 19115286 172 LDEPYAGLDVTSRSVLSSLL 191
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAIL 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-483 |
4.96e-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: 62.34 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIGpgtgISIFDIQENIGHCsPE----I 351
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGKDIE----TNLDAVRQSLGMC-PQhnilF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 352 HNHFPKQHTCFEALLSAWSTTftipkltETRLAaISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDE 431
Cdd:TIGR01257 1016 HHLTVAEHILFYAQLKGRSWE-------EAQLE-MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115286 432 PFQGVDtKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKL 483
Cdd:TIGR01257 1088 PTSGVD-PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-193 |
5.44e-10 |
|
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: 59.37 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 15 ARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYPFLKGKSD----SPWQAIQLLdfkssgQQR 90
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD-SGSILVRHDGGWVDlaqaSPREILALR------RRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 91 AAYYSEryhsF-----RDKEHDTTLEKWLLgayRGNEKFASQhvQEAASMtqLSHL-LPSSLINL-----SNGQSRRAML 159
Cdd:COG4778 95 IGYVSQ----FlrvipRVSALDVVAEPLLE---RGVDREEAR--ARAREL--LARLnLPERLWDLppatfSGGEQQRVNI 163
|
170 180 190
....*....|....*....|....*....|....
gi 19115286 160 ASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGE 193
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-198 |
5.95e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGsftpspstsfsypFLkgksdsPWQA------IQL--LDfKSSGQQ 89
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-------------FL------PYQGslkingIELreLD-PESWRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 90 RAAYYSERYHSFrdkeHDTTLEKWLLGAYRGNEKfASQHVQEAASMTQLSHLLPSSL--------INLSNGQSRRAMLAS 161
Cdd:PRK11174 424 HLSWVGQNPQLP----HGTLRDNVLLGNPDASDE-QLQQALENAWVSEFLPLLPQGLdtpigdqaAGLSVGQAQRLALAR 498
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115286 162 KLVQRPQLLLLDEPYAGLDVTS-RSVLSSLLGEMSNHC 198
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSeQLVMQALNAASRRQT 536
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-181 |
6.28e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.01 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFLDarfplfkNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGksdspwQAIQLLDFK 84
Cdd:PRK09536 11 VEFGDTTVLD-------GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL----VAG------DDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 SSGQQRAAYYSERYHSFrDKEHDTTLEkwlLGAYRGNEKFASQH------VQEAASMTQLSHLLPSSLINLSNGQSRRAM 158
Cdd:PRK09536 74 AASRRVASVPQDTSLSF-EFDVRQVVE---MGRTPHRSRFDTWTetdraaVERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180
....*....|....*....|...
gi 19115286 159 LASKLVQRPQLLLLDEPYAGLDV 181
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDI 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
264-485 |
6.32e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.25 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYW-GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHpKLFASNIKFFGKSIGPGTGiSIFDIQE 342
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL-KPSSGRILFDGKPIDYSRK-GLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGHC--SPEihnhfpkqHTCFEAL----LSAWSTTFTIPKlTETRlAAISSILEEFELKDIKDKPLSSISVGMQRFILF 416
Cdd:PRK13636 83 SVGMVfqDPD--------NQLFSASvyqdVSFGAVNLKLPE-DEVR-KRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 417 CRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSP-SQAMVIISHYEDELPACVNRRAHIDNGKLVI 485
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
262-437 |
7.00e-10 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 59.46 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAyVVGDHPKLFASNIKFFGKSIGPgtgISIFDIQ 341
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLG-CLAGRLAPDHGTATYIMRSGAE---LELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIGHCSPEIHNHFPKQHTC--FEALLSAWSTTFTIPKLTETR-----LAAISSILEEFELKD--IKDKPlSSISVGMQR 412
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARhygniRATAQDWLEEVEIDPtrIDDLP-RAFSGGMQQ 155
|
170 180
....*....|....*....|....*
gi 19115286 413 FILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLD 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-190 |
7.56e-10 |
|
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: 58.81 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQA----IQLLdFkssgQQRAAYysE 96
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY----IGGRDVTDLPPkdrdIAMV-F----QNYALY--P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 RYHSFRDKEHDTTLEKwllgayrGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPY 176
Cdd:cd03301 86 HMTVYDNIAFGLKLRK-------VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170
....*....|....*...
gi 19115286 177 AGLD----VTSRSVLSSL 190
Cdd:cd03301 159 SNLDaklrVQMRAELKRL 176
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
263-438 |
7.92e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPkLFASNIKFFGKSIGpgtgisifdiqe 342
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-PAAGTIKLDGGDID------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 nIGHCSPEIH--NHfpkQHTCFEAL-----LSAWSTTFTipklteTRLAAISSILEEFELKDIKDKPLSSISVGMQRFIL 415
Cdd:PRK13539 68 -DPDVAEACHylGH---RNAMKPALtvaenLEFWAAFLG------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVA 137
|
170 180
....*....|....*....|...
gi 19115286 416 FCRAIVKQPRLVVLDEPFQGVDT 438
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDA 160
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
262-484 |
9.33e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTlLAYVVGDHP--KLFASNIKFFGKsigpgtgiSIFD 339
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKST-LSKVIAGHPayKILEGDILFKGE--------SILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQenighcsPEIHNHFpkqhtcfeALLSAWSTTFTIPKLTET---RLA----AISSILEEFE----LKDIKDK-PLssis 407
Cdd:CHL00131 76 LE-------PEERAHL--------GIFLAFQYPIEIPGVSNAdflRLAynskRKFQGLPELDplefLEIINEKlKL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 408 VGM-QRF------------------ILfcRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDEL 468
Cdd:CHL00131 137 VGMdPSFlsrnvnegfsggekkrneIL--QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLL 214
|
250
....*....|....*..
gi 19115286 469 PACVNRRAHI-DNGKLV 484
Cdd:CHL00131 215 DYIKPDYVHVmQNGKII 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-184 |
9.39e-10 |
|
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: 58.67 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFsypFLKGKSDSPWQAIQLLDFKSSGQ---QRAayyser 97
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-SGSI---IFDGKDLLKLSRRLRKIRRKEIQmvfQDP------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 YHSFrdkehDT--TLEKWLLGAYRGNEKFASQHVQEAASMTQLSHL-LPSSLIN-----LSNGQSRRAMLASKLVQRPQL 169
Cdd:cd03257 92 MSSL-----NPrmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVgLPEEVLNrypheLSGGQRQRVAIARALALNPKL 166
|
170
....*....|....*
gi 19115286 170 LLLDEPYAGLDVTSR 184
Cdd:cd03257 167 LIADEPTSALDVSVQ 181
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-196 |
1.09e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 1 MASFVKFANTTFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaiql 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 81 ldFKSSGQQRAAYYSERYHsfRDKEHDTTLEKWLLgaYRGNEKfaSQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLA 160
Cdd:PRK09544 61 --IKRNGKLRIGYVPQKLY--LDTTLPLTVNRFLR--LRPGTK--KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLA 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 19115286 161 SKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSN 196
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-198 |
1.20e-09 |
|
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: 57.89 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 19 LFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSYPFLKGKSDSPWQAIQLLDFKSSGQQRAAYYSERY 98
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 99 HSFRDKEHDTTLEKWLlgayrgnekfasqhvqEAASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRPQLLLLDEPYAG 178
Cdd:cd03231 95 RFWHADHSDEQVEEAL----------------ARVGLNGFEDRPVAQL---SAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|
gi 19115286 179 LDVTSRSVLSSLlgeMSNHC 198
Cdd:cd03231 156 LDKAGVARFAEA---MAGHC 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
287-476 |
1.23e-09 |
|
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: 61.18 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 287 IREGERWALTGSNGSGKTTLLAYVVGDhPKLFASNIKFFGKSIGpgtgISIFDIQENIGHCSpeihnhfpkQHTCFEALL 366
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGKSIL----TNISDVHQNMGYCP---------QFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 367 SAWSTTFTIPKLTETRLAAISSI----LEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVH 442
Cdd:TIGR01257 2028 TGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190
....*....|....*....|....*....|....
gi 19115286 443 MAHNYLNEKLSPSQAMVIISHYEDELPACVNRRA 476
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHSMEECEALCTRLA 2141
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-231 |
1.34e-09 |
|
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: 58.50 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypfLKGKSDSPW-QAIQLLdfkssgQQRAAYYSE 96
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE------VRVAGLVPWkRRKKFL------RRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 RYHSFRDKEHDTTLEkwLLGA-YRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:cd03267 103 KTQLWWDLPVIDSFY--LLAAiYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 176 YAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG 231
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
289-468 |
1.41e-09 |
|
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: 58.08 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 289 EGERWALTGSNGSGKTTLLAYVVGdHPKLFASNIKFfgksigpgTGISIFDIQENIgHCSPE---IHNHFpKQHTCFEAL 365
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG-LEKPDGGTIVL--------NGTVLFDSRKKI-NLPPQqrkIGLVF-QQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 366 LSAWSTTFTIPKLTET-RLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMA 444
Cdd:cd03297 91 NVRENLAFGLKRKRNReDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|....*
gi 19115286 445 HNYLNEKLSPSQAMVI-ISHYEDEL 468
Cdd:cd03297 171 LPELKQIKKNLNIPVIfVTHDLSEA 195
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-271 |
2.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSfsypflkgksdspwQAIQLLDFKSSGQQRAAYYSERYHS- 100
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--------------TVGDIVVSSTSKQKEIKPVRKKVGVv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 101 FRDKEHDTTLEKWLLGAYRGNEKF------ASQHVQEAASMTQLS-HLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLD 173
Cdd:PRK13643 90 FQFPESQLFEETVLKDVAFGPQNFgipkekAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 174 EPYAGLDVTSRSVLSSLLgEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKEQYIP---MTSHSTNIP-- 247
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtPSDVFQEvdfLKAHELGVPka 248
|
250 260
....*....|....*....|....*..
gi 19115286 248 --VKPQMKKSKPITIGK-PLISMEHLN 271
Cdd:PRK13643 249 thFADQLQKTGAVTFEKlPITRAELVT 275
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
265-483 |
2.58e-09 |
|
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: 57.11 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLnCVYWGR-----KVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPklFASNIKFFGKSIgpgTGIS-- 336
Cdd:cd03255 1 IELKNL-SKTYGGggekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRP--TSGEVRVDGTDI---SKLSek 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 337 --IFDIQENIGhcspeihnhFPKQHTcfeALLSawstTFTI-----------PKLTETRLAAISSILEEFELKDIKDKPL 403
Cdd:cd03255 75 elAAFRRRHIG---------FVFQSF---NLLP----DLTAlenvelplllaGVPKKERRERAEELLERVGLGDRLNHYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 404 SSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPS-QAMVIISHyEDELPACVNRRAHIDNGK 482
Cdd:cd03255 139 SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTH-DPELAEYADRIIELRDGK 217
|
.
gi 19115286 483 L 483
Cdd:cd03255 218 I 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-236 |
2.62e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflkgKSDSPWQAiQLLDFKSSG-----QQRAA 92
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ------------KGAVLWQG-KPLDYSKRGllalrQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 93 YYS--ERYHSFRDKEHDTTLEKWLLGAyrgNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLL 170
Cdd:PRK13638 82 VFQdpEQQIFYTDIDSDIAFSLRNLGV---PEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 171 LLDEPYAGLDVTSRSVLSSLLGEM---SNHcspkIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKEQY 236
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIvaqGNH----VIISSHDIDLIYEISDAVYVLRQGQILTHGaPGEVF 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-197 |
2.99e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 1 MASFVKFANTTFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS-----------PSTSFSYPFLKG 69
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDhgeilfdgeniPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 70 KSDSP-WQAIQLLDFKSSGQQRAayYSERYHSFRDKE--HDTTLEKWllgayrgnekfasqhvqEAASMTQLSHLLPSSL 146
Cdd:PRK11831 84 KRMSMlFQSGALFTDMNVFDNVA--YPLREHTQLPAPllHSTVMMKL-----------------EAVGLRGAAKLMPSEL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115286 147 inlSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMsNH 197
Cdd:PRK11831 145 ---SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISEL-NS 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-235 |
3.75e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 57.75 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSYPFlkgksDSPWQAIQLLDF-KSSG---QqraayYSE 96
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV-----DITDKKVKLSDIrKKVGlvfQ-----YPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 rYHSFRDkehdtTLEKWL------LGAyrgNEKFASQHVQEAASMTQLSH--LLPSSLINLSNGQSRRAMLASKLVQRPQ 168
Cdd:PRK13637 94 -YQLFEE-----TIEKDIafgpinLGL---SEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 169 LLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQ 235
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
265-439 |
4.06e-09 |
|
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: 56.76 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIgpgTGISIfdIQEN 343
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPD--SGEILIDGRDV---TGVPP--ERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCsPEIHNHFPkqH-TCFEALLSAwsttftiPKL----TETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCR 418
Cdd:cd03259 74 IGMV-FQDYALFP--HlTVAENIAFG-------LKLrgvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALAR 143
|
170 180
....*....|....*....|.
gi 19115286 419 AIVKQPRLVVLDEPFQGVDTK 439
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAK 164
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
265-439 |
4.62e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.17 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIgpgTGISIFDiqEN 343
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlEHQT--SGHIRFHGTDV---SRLHARD--RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGhcspeihnhFPKQH-------TCFEALlsAWSTTfTIPKLTETRLAAISS----ILEEFELKDIKDKPLSSISVGMQR 412
Cdd:PRK10851 76 VG---------FVFQHyalfrhmTVFDNI--AFGLT-VLPRRERPNAAAIKAkvtqLLEMVQLAHLADRYPAQLSGGQKQ 143
|
170 180
....*....|....*....|....*..
gi 19115286 413 FILFCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQ 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
156-432 |
4.65e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 156 RAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSnhcSPKIVLSlrpQDKipDFI----THVLELKNKKIT-YQ 230
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERN---STMIIIS---HDR--HFLnsvcTHMADLDYGELRvYP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 231 GPKEQYipMTS--------HSTNIPVKPQMK--------------KSKPIT-----IGK-------------PLISME-- 268
Cdd:PRK15064 235 GNYDEY--MTAatqarerlLADNAKKKAQIAelqsfvsrfsanasKAKQATsrakqIDKikleevkpssrqnPFIRFEqd 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 269 ---HLNCV--------YWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDhpklfasnikffgksIGPGTGISI 337
Cdd:PRK15064 313 kklHRNALevenltkgFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE---------------LEPDSGTVK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 338 FDIQENIGHCsPEIHNH-FPKQHTCFEallsaWSTTFTIPKLTETrlaAISSILEE--FELKDIKdKPLSSISVGMQRFI 414
Cdd:PRK15064 378 WSENANIGYY-AQDHAYdFENDLTLFD-----WMSQWRQEGDDEQ---AVRGTLGRllFSQDDIK-KSVKVLSGGEKGRM 447
|
330
....*....|....*...
gi 19115286 415 LFCRAIVKQPRLVVLDEP 432
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEP 465
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
264-437 |
5.02e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.02 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSI-GPGT--GIsIF-- 338
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVeGPGAerGV-VFqn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 339 -------DIQENIGhcspeihnhfpkqhtcFEALLSAwsttftIPKltETRLAAISSILEEFELKDIKDKPLSSISVGMQ 411
Cdd:PRK11248 79 egllpwrNVQDNVA----------------FGLQLAG------VEK--MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQR 134
|
170 180
....*....|....*....|....*.
gi 19115286 412 RFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK11248 135 QRVGIARALAANPQLLLLDEPFGALD 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
256-437 |
5.98e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 256 KPITIGKPLISMEHLNcvywGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIGPGT-- 333
Cdd:COG1129 248 RAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD-SGEIRLDGKPVRIRSpr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 334 -----GIS-------------IFDIQENIghcspeihnhfpkqhTCfeALLSAWSTTFTIPKLTETRLAAisSILEEFel 395
Cdd:COG1129 323 dairaGIAyvpedrkgeglvlDLSIRENI---------------TL--ASLDRLSRGGLLDRRRERALAE--EYIKRL-- 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19115286 396 kDIK----DKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:COG1129 382 -RIKtpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-221 |
6.97e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPS---TSFSYPflKGKSDSPWqaiqllDFKssgqQRAAYY 94
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSndlTLFGRR--RGSGETIW------DIK----KHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHsfRDKEHDTTLEKWLLGAYrgnekFASQHVQEAASMTQ-------LSHL-LPSSLIN-----LSNGQSRRAMLAS 161
Cdd:PRK10938 342 SSSLH--LDYRVSTSVRNVILSGF-----FDSIGIYQAVSDRQqklaqqwLDILgIDKRTADapfhsLSWGQQRLALIVR 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 162 KLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEM-SNHCSPKIVLSLRPQDKiPDFITHVLE 221
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLFVSHHAEDA-PACITHRLE 474
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
265-463 |
8.87e-09 |
|
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: 55.61 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIgPGTGISIFDIQEN 343
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEPD--SGTIIIDGLKL-TDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IG----HcspeiHNHFPkqH-TCFEALLSAWSTTFTIPKLTETRLAaiSSILEEFELKDIKDKPLSSISVGMQRFILFCR 418
Cdd:cd03262 78 VGmvfqQ-----FNLFP--HlTVLENITLAPIKVKGMSKAEAEERA--LELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19115286 419 AIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH 463
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
264-484 |
1.42e-08 |
|
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: 57.14 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPK-LFASNIKFFGKSIGPGT-------GI 335
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgTWDGEIYWSGSPLKASNirdteraGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 336 SIfdiqenighcspeIHnhfpkQHTCFEALLSAWSTTFTIPKLTE----TRLAAI----SSILEEFELKDIKD-KPLSSI 406
Cdd:TIGR02633 81 VI-------------IH-----QELTLVPELSVAENIFLGNEITLpggrMAYNAMylraKNLLRELQLDADNVtRPVGDY 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 407 SVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-231 |
1.52e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.25 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPST-SFSYPFLKGKSDSPWQAIQLLD----------FKSSGQQ 89
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiEWIFKDEKNKKKTKEKEKVLEKlviqktrfkkIKKIKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 90 R----AAYYSERYHSFrdkehDTTLEK-WLLGAYR-GNEKfaSQHVQEAASMTQLSHL----LPSSLINLSNGQSRRAML 159
Cdd:PRK13651 104 RrrvgVVFQFAEYQLF-----EQTIEKdIIFGPVSmGVSK--EEAKKRAAKYIELVGLdesyLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115286 160 ASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMsnHCSPK-IVLSLRPQDKIPDFITHVLELKNKKITYQG 231
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL--NKQGKtIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-180 |
1.90e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.16 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPWQAIQLldfkssGQQRAAYyseR 97
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR----LNGRPLADWSPAEL------ARRRAVL---P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 YHS-----FrdkehdTTLEKWLLGAY--RGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQ----- 165
Cdd:PRK13548 83 QHSslsfpF------TVEEVVAMGRAphGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170
....*....|....*.
gi 19115286 166 -RPQLLLLDEPYAGLD 180
Cdd:PRK13548 157 gPPRWLLLDEPTSALD 172
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-205 |
2.28e-08 |
|
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: 54.43 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 11 TFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSpwqaiqlldfkssgqqr 90
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY----INGYSIR----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 91 aayySERYHSFRD----KEHDTTLEK-------WLLGAYRG-NEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAM 158
Cdd:cd03263 68 ----TDRKAARQSlgycPQFDALFDEltvrehlRFYARLKGlPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19115286 159 LASKLVQRPQLLLLDEPYAGLDVTSRS-VLSSLLGEMSNHCspkIVLS 205
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRaIWDLILEVRKGRS---IILT 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-191 |
2.61e-08 |
|
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: 52.84 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaiqlldFKSSGQQRAAYYSEr 97
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI----------------------VTWGSTVKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 yhsfrdkehdttlekwllgayrgnekfasqhvqeaasmtqlshllpsslinLSNGQSRRAMLASKLVQRPQLLLLDEPYA 177
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170
....*....|....
gi 19115286 178 GLDVTSRSVLSSLL 191
Cdd:cd03221 100 HLDLESIEALEEAL 113
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
265-439 |
2.63e-08 |
|
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: 54.65 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSigpgtgISIFDIQE- 342
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPD--SGTILFGGED------ATDVPVQEr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGhcspeihnhFPKQH-------TCFEAL---LSAWSTTFTIPKLTETRlaAISSILEEFELKDIKDKPLSSISVGMQR 412
Cdd:cd03296 75 NVG---------FVFQHyalfrhmTVFDNVafgLRVKPRSERPPEAEIRA--KVHELLKLVQLDWLADRYPAQLSGGQRQ 143
|
170 180
....*....|....*....|....*..
gi 19115286 413 FILFCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAK 170
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
263-437 |
2.66e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYV------------VGDHP--KLFASNIKFFGKS 328
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIngtltptagtvlVAGDDveALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 329 IGPGTGISI-FDIQENIghcspEIHNHfpkQHTcfeALLSAWsttftipklTETRLAAISSILEEFELKDIKDKPLSSIS 407
Cdd:PRK09536 82 VPQDTSLSFeFDVRQVV-----EMGRT---PHR---SRFDTW---------TETDRAAVERAMERTGVAQFADRPVTSLS 141
|
170 180 190
....*....|....*....|....*....|
gi 19115286 408 VGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
20-235 |
2.68e-08 |
|
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: 54.60 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGK-----------SDSPWQAIQL----LdFk 84
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD----------SGEilvdgqditglSEKELYELRRrigmL-F- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 ssgqQRAAYYSeryhS--------FRDKEHdTTLekwllgayrgNEKFASQHVQEAASMTQLS---HLLPSSLinlSNGQ 153
Cdd:COG1127 89 ----QGGALFD----SltvfenvaFPLREH-TDL----------SEAEIRELVLEKLELVGLPgaaDKMPSEL---SGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 154 SRRAMLASKLVQRPQLLLLDEPYAGLD-VTSRsVLSSLLGEM--SNHCSpkIVLslrpqdkipdfITHVLE--------- 221
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELrdELGLT--SVV-----------VTHDLDsafaiadrv 212
|
250
....*....|....*.
gi 19115286 222 --LKNKKITYQGPKEQ 235
Cdd:COG1127 213 avLADGKIIAEGTPEE 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
263-463 |
3.33e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVvgDHPKLFASNIKFFGKSigPGTGISIFDIQE 342
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL--NRMNELESEVRVEGRV--EFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 NIGHCSPEIHNHFPK---------QHTCFEALLSAWSTTFTIPKLTEtrlaaisSILEEFELKD-IKDKPLSS---ISVG 409
Cdd:PRK14258 82 NLNRLRRQVSMVHPKpnlfpmsvyDNVAYGVKIVGWRPKLEIDDIVE-------SALKDADLWDeIKHKIHKSaldLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 410 MQRFILFCRAIVKQPRLVVLDEPFQGVD----TKYVHMAHNYlneKLSPSQAMVIISH 463
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL---RLRSELTMVIVSH 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
255-437 |
3.59e-08 |
|
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: 55.76 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 255 SKPITIGKPL-ISMEHLNCVYWGR-KVLSDINWTIREGERWALTGSNGSGKTTLL------------AYVVGDHPkLFAS 320
Cdd:TIGR02857 311 KAPVTAAPASsLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLnlllgfvdptegSIAVNGVP-LADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 321 NIKFFGKSIG---------PGTgisifdIQENIGHCSPEIhnhfpkqhtcfeallsawsttftipKLTETRLAAISSILE 391
Cdd:TIGR02857 390 DADSWRDQIAwvpqhpflfAGT------IAENIRLARPDA-------------------------SDAEIREALERAGLD 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115286 392 EF--ELKDIKDKPL----SSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:TIGR02857 439 EFvaALPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
3.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSYPFLKG-KSDSPWQAIQLLDFKSSGQQR------AAYY 94
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdKKNNHELITNPYSKKIKNFKElrrrvsMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHSFRDK-EHDTTLEKWLLGAYRGN-EKFASQHVQEaasMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLL 172
Cdd:PRK13631 124 FPEYQLFKDTiEKDIMFGPVALGVKKSEaKKLAKFYLNK---MGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115286 173 DEPYAGLDVTSRSvlssllgEMSnhcspKIVLSLRPQDKIPDFITHVLE 221
Cdd:PRK13631 201 DEPTAGLDPKGEH-------EMM-----QLILDAKANNKTVFVITHTME 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-231 |
3.84e-08 |
|
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: 53.65 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFLDARFPLFKNVSFelARKQNWAIIGNTGSGRTTFLRCIQGSFTPspstsfsypflkgksDSPWQAIQLLDFK 84
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETP---------------QSGRVLINGVDVT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 ssgqqrAAYYSERYHS--FRDKE---HDTTLEKWLLG---AYRGNEKfASQHVQEAASMTQLSHLLPSSLINLSNGQSRR 156
Cdd:cd03298 64 ------AAPPADRPVSmlFQENNlfaHLTVEQNVGLGlspGLKLTAE-DRQAIEVALARVGLAGLEKRLPGELSGGERQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 157 AMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMsnHCSPK---IVLSLRPQDkIPDFITHVLELKNKKITYQG 231
Cdd:cd03298 137 VALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL--HAETKmtvLMVTHQPED-AKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-220 |
4.20e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.60 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 11 TFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLR-------CIQGSFTpspstsfsypfLKGKSDSPWqaiqlldf 83
Cdd:PRK11160 347 TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQlltrawdPQQGEIL-----------LNGQPIADY-------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 84 kSSGQQRAA--YYSERYHSFRDkehdtTLekwllgayRGNEKFAsqhvQEAASMTQLSHLLP----SSLIN--------- 148
Cdd:PRK11160 408 -SEAALRQAisVVSQRVHLFSA-----TL--------RDNLLLA----APNASDEALIEVLQqvglEKLLEddkglnawl 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 149 ------LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD-VTSRSVLSSLLgemsNHCSPKIVLslrpqdkipdFITHVL 220
Cdd:PRK11160 470 geggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaETERQILELLA----EHAQNKTVL----------MITHRL 534
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
265-437 |
4.22e-08 |
|
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: 53.84 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWG-RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVvgdhPKLFASN---IKFFGKSIgpgTGISIFDI 340
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI----NRLIEPTsgeIFIDGEDI---REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 341 QENIGHCSPEIhNHFPkqHtcfealLSAWSTTFTIPKLT----ETRLAAISSILEEFEL--KDIKDKPLSSISVGMQRFI 414
Cdd:cd03295 74 RRKIGYVIQQI-GLFP--H------MTVEENIALVPKLLkwpkEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRV 144
|
170 180
....*....|....*....|...
gi 19115286 415 LFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALD 167
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
265-482 |
4.82e-08 |
|
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: 52.57 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGPGTGIsIFDIQEN 343
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPD--SGSILIDGEDLTDLEDE-LPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGhcspeihnhFPKQHTCFeallsawsttftIPKLTetrlaaissILEEFELkdikdkPLSSisvGMQRFILFCRAIVKQ 423
Cdd:cd03229 78 IG---------MVFQDFAL------------FPHLT---------VLENIAL------GLSG---GQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 424 PRLVVLDEPFQGVD---TKYVHMAHNYLNEKLspSQAMVIISHYEDELPACVNRRAHIDNGK 482
Cdd:cd03229 119 PDVLLLDEPTSALDpitRREVRALLKSLQAQL--GITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
265-483 |
5.50e-08 |
|
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: 53.18 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVY-WGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHpKLFASNIKFFGKSIGPGTGISIFDIQEN 343
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE-LPTSGTIRVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCSPEihNHFPKQHTCFEALLSAWSTTFTIPKLTETRLAAIssiLEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQ 423
Cdd:cd03292 80 IGVVFQD--FRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA---LELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 424 PRLVVLDEPFQGVDTKYVHMAHNYLNeKLSPSQAMVIISHYEDELPACVNRRA-HIDNGKL 483
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELVDTTRHRViALERGKL 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-184 |
5.70e-08 |
|
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: 54.72 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLfkNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGK---SDSPWQAIQLLDFKSSGQQRAAY 93
Cdd:COG4148 14 FTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD----------SGRirlGGEVLQDSARGIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 YSERYHSFrdkEHDTTLEKWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLD 173
Cdd:COG4148 82 VFQEARLF---PHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170
....*....|.
gi 19115286 174 EPYAGLDVTSR 184
Cdd:COG4148 159 EPLAALDLARK 169
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
265-484 |
6.09e-08 |
|
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: 52.05 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPklfasnikffgksigPGTGISIFDIQEni 344
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK---------------PDSGEILVDGKE-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 ghcspeihnhfpkqhtcfeallsawsTTFTIPKltETRLAAISSIleeFELkdikdkplssiSVGMQRFILFCRAIVKQP 424
Cdd:cd03216 64 --------------------------VSFASPR--DARRAGIAMV---YQL-----------SVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 425 RLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-236 |
6.17e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaiqlldFKSSGQQRAAYYSE- 96
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT----------------------VKWSENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 RYHSFrdkEHDTTLEKWlLGAYRgNEKFASQHVQEAasmtqLSHLLPS------SLINLSNGQSRRaMLASKLV-QRPQL 169
Cdd:PRK15064 391 HAYDF---ENDLTLFDW-MSQWR-QEGDDEQAVRGT-----LGRLLFSqddikkSVKVLSGGEKGR-MLFGKLMmQKPNV 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 170 LLLDEPYAGLDVTSrsvLSSLLGEMSNHCSPKIVLSlrpQDKipDFI----THVLELKNKKIT-YQGPKEQY 236
Cdd:PRK15064 460 LVMDEPTNHMDMES---IESLNMALEKYEGTLIFVS---HDR--EFVsslaTRIIEITPDGVVdFSGTYEEY 523
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
262-486 |
6.59e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASnikffgkSIGPGTGISIFDIQ 341
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLL--------KIVAS-------LISPTSGTLLFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 EnIGHCSPEIHNhfpKQ------------HTCFEALLSAWSTTFTIPKltETRLAAissILEEFELKD-IKDKPLSSISV 408
Cdd:PRK10247 70 D-ISTLKPEIYR---QQvsycaqtptlfgDTVYDNLIFPWQIRNQQPD--PAIFLD---DLERFALPDtILTKNIAELSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 409 GMQRFILFCRAIVKQPRLVVLDEPFQGVD----TKYVHMAHNYLNEKlspSQAMVIISHYEDELpacvnrrAHIDNgklV 484
Cdd:PRK10247 141 GEKQRISLIRNLQFMPKVLLLDEITSALDesnkHNVNEIIHRYVREQ---NIAVLWVTHDKDEI-------NHADK---V 207
|
..
gi 19115286 485 IH 486
Cdd:PRK10247 208 IT 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
278-484 |
7.23e-08 |
|
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: 53.14 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 278 KVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGD-HPKLFASNIKFFGKSIGPgtgisiFDIQENIGhcspeihnhFP 356
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGFDVVKEP------AEARRRLG---------FV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 357 KQHTCFEALLSAWSTTFTIPKLTETRLAAISSILEE----FELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEP 432
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEEladrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115286 433 FQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-234 |
8.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 19 LFkNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYPFLKGKSDSPWQaiqllDFKSSGQQRAAYYSery 98
Cdd:PRK13649 23 LF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT-QGSVRVDDTLITSTSKNK-----DIKQIRKKVGLVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 99 hsFRDKE--HDTTLEKWLLGA--YRGNEKFASQHVQEAASMTQLSH-LLPSSLINLSNGQSRRAMLASKLVQRPQLLLLD 173
Cdd:PRK13649 93 --FPESQlfEETVLKDVAFGPqnFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 174 EPYAGLDVTSRSVLSSLLGEMsNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKE 234
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGkPKD 231
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
276-485 |
1.02e-07 |
|
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: 53.03 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdHPKLFASN--IKFFGksigpgtgisifdiqENIGHCSPEIHN 353
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-HPSYEVTSgtILFKG---------------QDLLELEPDERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 354 HfpkqhtcfEALLSAWSTTFTIPKLTETRL--AAISSILEEFELKDIKD----KPLSSI--SVGMQRFIL---------- 415
Cdd:TIGR01978 76 R--------AGLFLAFQYPEEIPGVSNLEFlrSALNARRSARGEEPLDLldfeKLLKEKlaLLDMDEEFLnrsvnegfsg 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 416 -------FCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHI-DNGKLVI 485
Cdd:TIGR01978 148 gekkrneILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHVlLDGRIVK 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-221 |
1.05e-07 |
|
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: 52.58 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 16 RFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSfsypFLKGKSDSPWQAIQLLDFkssgQQRAAYYS 95
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV----LVDGTDLTLLSGKELRKA----RRRIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 ERYHSF--RDKEHDTTLEKWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSsliNLSNGQSRRAMLASKLVQRPQLLLLD 173
Cdd:cd03258 89 QHFNLLssRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPA---QLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115286 174 EPYAGLD-VTSRSVLsSLLGEMSNHCSPKIVLslrpqdkipdfITHVLE 221
Cdd:cd03258 166 EATSALDpETTQSIL-ALLRDINRELGLTIVL-----------ITHEME 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
34-180 |
1.13e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.83 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 34 AIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQLLDF-----KSSGQQRAAYYSERYH------SFR 102
Cdd:PRK11264 33 AIIGPSGSGKTTLLRCINLLEQPEAGT-----------------IRVGDItidtaRSLSQQKGLIRQLRQHvgfvfqNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 103 DKEHDTTLEKWLLGAY--RGNEK-FASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGL 179
Cdd:PRK11264 96 LFPHRTVLENIIEGPVivKGEPKeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
.
gi 19115286 180 D 180
Cdd:PRK11264 176 D 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
261-439 |
1.16e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 261 GKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklFASnikffgksigPGTGISIFDI 340
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-----FET----------PDSGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 341 QeNIGHCSPEiHNH----------FPkqH-TCFEallsawSTTFTIpKLTETRLAAISSILEE----FELKDIKDKPLSS 405
Cdd:PRK09452 76 Q-DITHVPAE-NRHvntvfqsyalFP--HmTVFE------NVAFGL-RMQKTPAAEITPRVMEalrmVQLEEFAQRKPHQ 144
|
170 180 190
....*....|....*....|....*....|....
gi 19115286 406 ISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-184 |
1.32e-07 |
|
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: 52.24 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSdspwqaIQLLD---------FKSsg 87
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL----LDGKD------ITNLPphkrpvntvFQN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 88 qqraayyserYHSFrdkEHDTTLEKWLLG--AYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQ 165
Cdd:cd03300 81 ----------YALF---PHLTVFENIAFGlrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170
....*....|....*....
gi 19115286 166 RPQLLLLDEPYAGLDVTSR 184
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLR 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-191 |
1.43e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.78 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQL--LDFKSSGQQRAAYY- 94
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-----------------ITLdgKPVEGPGAERGVVFq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHSFRDKEHDTTLEKWLLGAYRgnekfaSQHVQEAASMTQLSHLLPSS---LINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEK------MQRLEIAHQMLKKVGLEGAEkryIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180
....*....|....*....|
gi 19115286 172 LDEPYAGLDVTSRSVLSSLL 191
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLL 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
264-441 |
1.47e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklFASnikffgksigPGTGiSIFDIQEN 343
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-----LAR----------PDAG-EVLWQGEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCSPEIHN------HfpkqHTCFEALLSAWST-TFTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILF 416
Cdd:PRK13538 65 IRRQRDEYHQdllylgH----QPGIKTELTALENlRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVAL 140
|
170 180
....*....|....*....|....*
gi 19115286 417 CRAIVKQPRLVVLDEPFQGVDTKYV 441
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGV 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
1.50e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 14 DARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQG--SFTPSpSTSFSYPFLK-----------GKSDSPWQAIQL 80
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPV-AGCVDVPDNQfgreaslidaiGRKGDFKDAVEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 81 LDfkSSGQQRAAYYSERYHsfrdkehdttlekwllgayrgnekfasqhvqeaasmtqlshllpssliNLSNGQSRRAMLA 160
Cdd:COG2401 119 LN--AVGLSDAVLWLRRFK------------------------------------------------ELSTGQKFRFRLA 148
|
170 180 190
....*....|....*....|....*....|....*
gi 19115286 161 SKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMS 195
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLA 183
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-194 |
1.77e-07 |
|
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: 52.78 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTS--FSYPFLKgKSDSPWQAIQLLdfkssGQQRAAYy 94
Cdd:TIGR01188 6 FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTArvAGYDVVR-EPRKVRRSIGIV-----PQYASVD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 seryhsfrdkEHDTTLEKWLL--GAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLL 172
Cdd:TIGR01188 79 ----------EDLTGRENLEMmgRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180
....*....|....*....|..
gi 19115286 173 DEPYAGLDVTSRSVLSSLLGEM 194
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRAL 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
265-484 |
1.86e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.98 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYW-GRKVLSDINWTIREGErWA-LTGSNGSGKTTLL------------AYVVGDHP--KLFASNIKFFGKS 328
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGE-FVfLTGPSGAGKSTLLkllygeerptsgQVLVNGQDlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 329 IGPgtgisIF-DIQ--------ENI-------GHCSPEIHnhfpkqhtcfeallsawsttftipkltetrlAAISSILEE 392
Cdd:COG2884 81 IGV-----VFqDFRllpdrtvyENValplrvtGKSRKEIR-------------------------------RRVREVLDL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 393 FELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVII-SHYE---DEL 468
Cdd:COG2884 125 VGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIaTHDLelvDRM 203
|
250
....*....|....*.
gi 19115286 469 PAcvnRRAHIDNGKLV 484
Cdd:COG2884 204 PK---RVLELEDGRLV 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-270 |
1.94e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.71 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 34 AIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQLLDFKSSGQQRAayysERYHSFRDK--------E 105
Cdd:PRK13634 37 AIIGHTGSGKSTLLQHLNGLLQPT----------SGT-------VTIGERVITAGKKN----KKLKPLRKKvgivfqfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 106 H---DTTLEKWL------LGAyrgNEKFASQHVQEAASMTQLSH-LLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:PRK13634 96 HqlfEETVEKDIcfgpmnFGV---SEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 176 YAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKEQYIP---MTSHSTNIP---- 247
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGtPREIFADpdeLEAIGLDLPetvk 252
|
250 260
....*....|....*....|...
gi 19115286 248 VKPQMKKSKPITIGKPLISMEHL 270
Cdd:PRK13634 253 FKRALEEKFGISFPKPCLTLEEL 275
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-196 |
2.11e-07 |
|
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: 51.80 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQG-----SFTPSPSTSFsypfLKGKSDSPWQAIQLLDFKSSG---QQRA 91
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVL----LDGKDIYDLDVDVLELRRRVGmvfQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 92 AY---------YSERYHSFRDKEHdttlekwllgayrgnekfASQHVQEAASMTQL-----SHLLPSSLinlSNGQSRRA 157
Cdd:cd03260 92 PFpgsiydnvaYGLRLHGIKLKEE------------------LDERVEEALRKAALwdevkDRLHALGL---SGGQQQRL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSN 196
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
262-484 |
2.15e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKS-------IGPGTG 334
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-KGTITINNINynkldhkLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 335 ISI----------FDIQENIghcspEIHNHfPKQHTCFEALLSaWSttftipkltETRLAAiSSILEEFELKDIKDKPLS 404
Cdd:PRK09700 82 IGIiyqelsvideLTVLENL-----YIGRH-LTKKVCGVNIID-WR---------EMRVRA-AMMLLRVGLKVDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 405 SISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
276-463 |
2.27e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdHPKLFASNIKFFGKSIGPGtgisifdIQENIGHCSP---EIH 352
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMG-FVRLASGKISILGQPTRQA-------LQKNLVAYVPqseEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 353 NHFPkqhTCFE--ALLSAWSTTFTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLD 430
Cdd:PRK15056 91 WSFP---VLVEdvVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190
....*....|....*....|....*....|...
gi 19115286 431 EPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH 463
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-235 |
2.40e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 9 NTTFLDARF---PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPST-SFSYPFLKGKSDSPWQaIQLLDfK 84
Cdd:PRK10619 7 NVIDLHKRYgehEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSiVVNGQTINLVRDKDGQ-LKVAD-K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 SSGQQRAAYYSERYHSFRDKEHDTTLEKWL------LGAYRGNEK------FASQHVQEAASMTQLSHLlpsslinlSNG 152
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEAReravkyLAKVGIDERAQGKYPVHL--------SGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 153 QSRRAMLASKLVQRPQLLLLDEPYAGLDvtsrsvlSSLLGEMSnhcspKIVLSLRPQDKIPDFITHVLE----------- 221
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALD-------PELVGEVL-----RIMQQLAEEGKTMVVVTHEMGfarhvsshvif 224
|
250
....*....|....
gi 19115286 222 LKNKKITYQGPKEQ 235
Cdd:PRK10619 225 LHQGKIEEEGAPEQ 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-484 |
2.60e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAyVVGDHPKLFASNIKFFGKSIGPGTGISIFD---IQENIGHCSPEiHN 353
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaikLRKEVGMVFQQ-PN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 354 HFPkqHTCFEALLSAWSTTFTIPKLTEtrlaaISSILEEF--------ELKDIKDKPLSSISVGMQRFILFCRAIVKQPR 425
Cdd:PRK14246 101 PFP--HLSIYDNIAYPLKSHGIKEKRE-----IKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 426 LVVLDEPFQGVDTKYVHMAHNYLNEkLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITE-LKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-243 |
2.63e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 7 FANTTFLDarfplfkNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSYPFLKGkSDSPWQAIQLLDFKss 86
Cdd:PRK14271 31 FAGKTVLD-------QVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG-GRSIFNYRDVLEFR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 87 gqQRAAYYSERYHSFRDKEHDTTLEKWLLGAYRGNEKF---ASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKL 163
Cdd:PRK14271 101 --RRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 164 VQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVL-SLRPQDKIPDFITHVLElknKKITYQGPKEQYIPMTSH 242
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVThNLAQAARISDRAALFFD---GRLVEEGPTEQLFSSPKH 255
|
.
gi 19115286 243 S 243
Cdd:PRK14271 256 A 256
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
261-439 |
2.63e-07 |
|
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: 53.13 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 261 GKPLISMEHLNCVYWG-RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfASNIKFFGKSIgpgTGISIFD 339
Cdd:TIGR02868 331 GKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-QGEVTLDGVPV---SSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQENIGHCSPEIHnhfpkqhtcfeallsAWSTT------FTIPKLTETRL-AAISSI-LEEF--ELKDIKDKPL----SS 405
Cdd:TIGR02868 407 VRRRVSVCAQDAH---------------LFDTTvrenlrLARPDATDEELwAALERVgLADWlrALPDGLDTVLgeggAR 471
|
170 180 190
....*....|....*....|....*....|....
gi 19115286 406 ISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
279-484 |
2.68e-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: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 279 VLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFAS-------NIKFFGKS---IGPGTGisiFDIQ----ENI 344
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLL--------KLIAGileptsgRVEVNGRVsalLELGAG---FHPEltgrENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GH-CSpeIHNHFPKQhtcfeallsawsttftipklTETRLAAIssilEEF-ELKDIKDKPLSSISVGMQ-RFiLFCRAIV 421
Cdd:COG1134 110 YLnGR--LLGLSRKE--------------------IDEKFDEI----VEFaELGDFIDQPVKTYSSGMRaRL-AFAVATA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115286 422 KQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-235 |
3.20e-07 |
|
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: 51.07 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 3 SFVKFANTTF-LDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDSPWQAIQLL 81
Cdd:cd03254 1 GEIEFENVNFsYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ----------KGQILIDGIDIRDI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 82 DFKSSgQQRAAYYSERYHSFRdkehDTTLEKWLLGAYRGNEKfasqHVQEAASMTQLSHL---LPSSLI--------NLS 150
Cdd:cd03254 71 SRKSL-RSMIGVVLQDTFLFS----GTIMENIRLGRPNATDE----EVIEAAKEAGAHDFimkLPNGYDtvlgenggNLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 151 NGQSRRAMLASKLVQRPQLLLLDEPYAGLDV-TSRSVLSSLLGEMSNHCSpkIVLSLRPQ-----DKIpdfithvLELKN 224
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTeTEKLIQEALEKLMKGRTS--IIIAHRLStiknaDKI-------LVLDD 212
|
250
....*....|.
gi 19115286 225 KKITYQGPKEQ 235
Cdd:cd03254 213 GKIIEEGTHDE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
265-439 |
3.77e-07 |
|
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: 50.72 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHpKLFASNIKFFGKSI---GPGT-GIS-IFD 339
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE-EPTSGRIYIGGRDVtdlPPKDrDIAmVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 ---------IQENIGHcsPEIHNHFPKQhtcfeallsawsttfTIPKltetRLAAISSILEEFELKDIKDKPLSSisvGM 410
Cdd:cd03301 80 nyalyphmtVYDNIAF--GLKLRKVPKD---------------EIDE----RVREVAELLQIEHLLDRKPKQLSG---GQ 135
|
170 180
....*....|....*....|....*....
gi 19115286 411 QRFILFCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:cd03301 136 RQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-194 |
3.89e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.33 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS---------PSTSFSYPFLKGK----------SDSPWQAI-QL 80
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTsgelliddhPLHFGDYSYRSQRirmifqdpstSLNPRQRIsQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 81 LDFKssgqqrAAYYSERYHSFRDKEHDTTLEKWLLgayrgnekfASQHVQEAASMtqlshllpsslinLSNGQSRRAMLA 160
Cdd:PRK15112 110 LDFP------LRLNTDLEPEQREKQIIETLRQVGL---------LPDHASYYPHM-------------LAPGQKQRLGLA 161
|
170 180 190
....*....|....*....|....*....|....
gi 19115286 161 SKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEM 194
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-250 |
4.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSfsypfLKGKSDSPWQAIQLLDFKSSGQQRAAYYS- 95
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-----IVGDYAIPANLKKIKEVKRLRKEIGLVFQf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 ERYHSFRDK-EHDTTLEKWLLGAyrgNEKFASQHVQEAASMTQLSH-LLPSSLINLSNGQSRRAMLASKLVQRPQLLLLD 173
Cdd:PRK13645 99 PEYQLFQETiEKDIAFGPVNLGE---NKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 174 EPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQYIPMTSHSTNIPVKP 250
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEIDP 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
129-180 |
4.09e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 4.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 19115286 129 VQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD 180
Cdd:PRK09452 125 VMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
261-432 |
4.21e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 261 GKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpklfasNIkFFGkSIGPGTG-ISIFD 339
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLM-------------KI-LYG-LYQPDSGeILIDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQENIGhcSPE---------IHNHFpkqhTCFEAL-------LSAWSTTFTIPKLTETRlAAISSILEEFELkDIK-DKP 402
Cdd:COG3845 67 KPVRIR--SPRdaialgigmVHQHF----MLVPNLtvaenivLGLEPTKGGRLDRKAAR-ARIRELSERYGL-DVDpDAK 138
|
170 180 190
....*....|....*....|....*....|..
gi 19115286 403 LSSISVGM-QRF-ILfcRAIVKQPRLVVLDEP 432
Cdd:COG3845 139 VEDLSVGEqQRVeIL--KALYRGARILILDEP 168
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
262-439 |
4.41e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 51.64 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIG------PGTG 334
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD--SGRILLDGRDVTglppekRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 335 IsIF---------DIQENIGhcspeihnhFPkqhtcfealLSAWSttftIPKltETRLAAISSILEEFELKDIKDKPLSS 405
Cdd:COG3842 81 M-VFqdyalfphlTVAENVA---------FG---------LRMRG----VPK--AEIRARVAELLELVGLEGLADRYPHQ 135
|
170 180 190
....*....|....*....|....*....|....*
gi 19115286 406 ISVG-MQRFILfCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:COG3842 136 LSGGqQQRVAL-ARALAPEPRVLLLDEPLSALDAK 169
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-191 |
4.56e-07 |
|
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: 50.55 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFLDARFP---LFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS---------PSTSFSYPFLKGKSD 72
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQggqvlldgkPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 73 SPWQAIQLldFKSSGQQRAAY-----YSERYHSFRDKEH-DTTLEKWLLGAYRGnekfasqhVQEAASMtqlshllpssl 146
Cdd:cd03248 92 LVGQEPVL--FARSLQDNIAYglqscSFECVKEAAQKAHaHSFISELASGYDTE--------VGEKGSQ----------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19115286 147 inLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLL 191
Cdd:cd03248 151 --LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
137-180 |
4.61e-07 |
|
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: 50.62 E-value: 4.61e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 19115286 137 QLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD 180
Cdd:cd03218 122 HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
129-184 |
4.65e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 51.64 E-value: 4.65e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 129 VQEAASMTQLSHL---LPSsliNLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSR 184
Cdd:COG3842 116 VAELLELVGLEGLadrYPH---QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLR 171
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
34-184 |
4.94e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.83 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 34 AIIGNTGSGRTTFLRCIQGSFTPSPST--SFSYPFLKGKSDSP--WQAIQLLDFKSsgqqraayyseryhsfrdkehdtT 109
Cdd:PRK11247 42 AVVGRSGCGKSTLLRLLAGLETPSAGEllAGTAPLAEAREDTRlmFQDARLLPWKK-----------------------V 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 110 LEKWLLGaYRGNEKFASQHVQEAASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSR 184
Cdd:PRK11247 99 IDNVGLG-LKGQWRDAALQALAAVGLADRANEWPAAL---SGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
127-184 |
5.08e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 5.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 127 QHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSR 184
Cdd:PRK11000 112 QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-180 |
5.58e-07 |
|
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: 50.22 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSfsypFLKGKS-DSPWQAIQLLDfkssgqQRAAYYS 95
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI----IIDGLKlTDDKKNINELR------QKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 ERYHSFrdkEHDTTLE------KWLLGAyrgNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQL 169
Cdd:cd03262 83 QQFNLF---PHLTVLEnitlapIKVKGM---SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170
....*....|.
gi 19115286 170 LLLDEPYAGLD 180
Cdd:cd03262 157 MLFDEPTSALD 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
265-437 |
6.19e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYV----VGDHPKLFASNIKF-FGKSIGPGTgisIFD 339
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnlleMPRSGTLNIAGNHFdFSKTPSDKA---IRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQENIGHCSPEIH--NHFpkqhTCFEALLSAWSTTFTIPKlTETRLAAIsSILEEFELKDIKDK-PLsSISVGMQRFILF 416
Cdd:PRK11124 80 LRRNVGMVFQQYNlwPHL----TVQQNLIEAPCRVLGLSK-DQALARAE-KLLERLRLKPYADRfPL-HLSGGQQQRVAI 152
|
170 180
....*....|....*....|.
gi 19115286 417 CRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALD 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
277-437 |
6.52e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.84 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGP--GTGISIF--DI----QENIGHC 347
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPS--QGNVSWRGEPLAKlnRAQRKAFrrDIqmvfQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 348 SP-----EIHNHfPKQHtcfeaLLSawsttftipkLTET-RLAAISSILEEFELKD-IKDKPLSSISVG-MQRFILfCRA 419
Cdd:PRK10419 103 NPrktvrEIIRE-PLRH-----LLS----------LDKAeRLARASEMLRAVDLDDsVLDKRPPQLSGGqLQRVCL-ARA 165
|
170
....*....|....*...
gi 19115286 420 IVKQPRLVVLDEPFQGVD 437
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD 183
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
35-219 |
6.55e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 35 IIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKS-DSPWQAIQLLdfkssgQQRAAYYSERYHSFrdkEHDTTLEKW 113
Cdd:PRK09493 32 IIGPSGSGKSTLLRCINKLEEITSGDLI----VDGLKvNDPKVDERLI------RQEAGMVFQQFYLF---PHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 114 LLGA--YRGNEKFASQHVQEA----ASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD------- 180
Cdd:PRK09493 99 MFGPlrVRGASKEEAEKQAREllakVGLAERAHHYPSEL---SGGQQQRVAIARALAVKPKLMLFDEPTSALDpelrhev 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 181 ----------------VT-----SRSVLSSLL----GEMSNHCSPKIVLSLRPQDKIPDFITHV 219
Cdd:PRK09493 176 lkvmqdlaeegmtmviVTheigfAEKVASRLIfidkGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-194 |
6.89e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 51.30 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 15 ARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaIQL----LDFKSSGQQR 90
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD----------SGR-------IVLngrdLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 91 A-AYYSERYHSFRdkeHDTTLEkwllgayrgNEKF-----------ASQHVQEAASMTQLSHL---LPSsliNLSNGQSR 155
Cdd:COG1118 76 RvGFVFQHYALFP---HMTVAE---------NIAFglrvrppskaeIRARVEELLELVQLEGLadrYPS---QLSGGQRQ 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115286 156 RAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEM 194
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRL 179
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-205 |
7.06e-07 |
|
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: 51.75 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFtpsPSTSFSYPFLKGKS---DSPWQAIQlldfkssgqQRAAYYSERy 98
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAY---PGKFEGNVFINGKPvdiRNPAQAIR---------AGIAMVPED- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 99 hsfRDKE---------HDTTLEKWLLGAYRGNEKFASQHVQEAASMTQL-----SHLLPssLINLSNGQSRRAMLASKLV 164
Cdd:TIGR02633 345 ---RKRHgivpilgvgKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLkvktaSPFLP--IGRLSGGNQQKAVLAKMLL 419
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19115286 165 QRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLS 205
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS 460
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
127-180 |
8.03e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.14 E-value: 8.03e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 127 QHVQEAASMTQLSHL---LPSSLinlSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD 180
Cdd:COG3840 108 AQVEQALERVGLAGLldrLPGQL---SGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
276-463 |
8.61e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG---------DHPK----LFASNikffgKS-IGPGTgisifdIQ 341
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgriARPAgarvLFLPQ-----RPyLPLGT------LR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIghCSPEIHNHFPKqhtcfEALLSAwsttftipkLTETRLAAISSILEEfelkdikDKPLSSI-SVGMQRFILFCRAI 420
Cdd:COG4178 444 EAL--LYPATAEAFSD-----AELREA---------LEAVGLGHLAERLDE-------EADWDQVlSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115286 421 VKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLsPSQAMVIISH 463
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREEL-PGTTVISVGH 542
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
263-313 |
8.62e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.16 E-value: 8.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGD 313
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGE 51
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-212 |
8.79e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaiqlldFKSSGqqRAAYYSEr 97
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS----------EGK------------IKHSG--RISFSPQ- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 yhsfrdkehdttlEKWLL-GAYRGN-------EKFASQHVQEAASMTQLSHLLPSSL--------INLSNGQSRRAMLAS 161
Cdd:TIGR01271 495 -------------TSWIMpGTIKDNiifglsyDEYRYTSVIKACQLEEDIALFPEKDktvlgeggITLSGGQRARISLAR 561
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 162 KLVQRPQLLLLDEPYAGLDV-TSRSVLSSLLGEMSNHCSPKIVLS----LRPQDKI 212
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVvTEKEIFESCLCKLMSNKTRILVTSklehLKKADKI 617
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
264-463 |
1.11e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSI------------- 329
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQSIkkdlctyqkqlcf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 330 -GPGTGISIF-DIQENighCSPEIHnhfpkqhtcfeallsawsttftipklTETRLAAISSILEEFELKDIKDKPLSSIS 407
Cdd:PRK13540 79 vGHRSGINPYlTLREN---CLYDIH--------------------------FSPGAVGITELCRLFSLEHLIDYPCGLLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 408 VGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH 463
Cdd:PRK13540 130 SGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
115-194 |
1.15e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.88 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 115 LGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEM 194
Cdd:PRK15056 109 MGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
1.22e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQgsftpSPSTSFSYPFLKGKSDSPWQAI--QLLD 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-----RMNELESEVRVEGRVEFFNQNIyeRRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 83 FKSSGQQRAAYYSeRYHSFRDKEHDTTLEKWLLGAYRGN---EKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAML 159
Cdd:PRK14258 83 LNRLRRQVSMVHP-KPNLFPMSVYDNVAYGVKIVGWRPKleiDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 160 ASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVL---SLRPQDKIPDF----------ITHVLELKNKK 226
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIvshNLHQVSRLSDFtaffkgnenrIGQLVEFGLTK 241
|
....*.
gi 19115286 227 ITYQGP 232
Cdd:PRK14258 242 KIFNSP 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-196 |
1.32e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSfTPSPSTSFSYPFLKGKSDSPWQAIQlldfkssgqQRAAYYSER--- 97
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKDISPRSPLDAVK---------KGMAYITESrrd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 ---YHSFRDKEHDTTLEKWLLGAYRG-----NEKFASQHVQEAASMTQLS-HLLPSSLINLSNGQSRRAMLASKLVQRPQ 168
Cdd:PRK09700 350 ngfFPNFSIAQNMAISRSLKDGGYKGamglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180
....*....|....*....|....*...
gi 19115286 169 LLLLDEPYAGLDVTSRSVLSSLLGEMSN 196
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLAD 457
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
286-484 |
1.36e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 286 TIREGERWALTGSNGSGKTTLLAYVVGDHP----KL-FASNIKFFGKSIGPGTGI--SIFD-IQENIGHCSP--EIHNHF 355
Cdd:PRK11147 25 HIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgRIiYEQDLIVARLQQDPPRNVegTVYDfVAEGIEEQAEylKRYHDI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 356 PKQ--HTCFEALLS-------------AWSTtftipkltETRlaaISSILEEFELKdiKDKPLSSISVGMQRFILFCRAI 420
Cdd:PRK11147 105 SHLveTDPSEKNLNelaklqeqldhhnLWQL--------ENR---INEVLAQLGLD--PDAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 421 VKQPRLVVLDEPFQGVDTKYVHMAHNYLnekLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFL---KTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
264-437 |
1.57e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.63 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAY----VVGDhpKLFASNIKFFGKSIgPGTGISIFD 339
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHlsglITGD--KSAGSHIELLGRTV-QREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQENIGHcSPEIHNHFP--KQHTCFEALLSA-------WSTTFT--IPKLTETRLAAISSIleefELKDIKDKPLSSISV 408
Cdd:PRK09984 81 IRKSRAN-TGYIFQQFNlvNRLSVLENVLIGalgstpfWRTCFSwfTREQKQRALQALTRV----GMVHFAHQRVSTLSG 155
|
170 180
....*....|....*....|....*....
gi 19115286 409 GMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
149-234 |
1.57e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMsNHCSPKIVLSLRPQDKIPDFITHVLELKNKKIT 228
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
....*..
gi 19115286 229 YQG-PKE 234
Cdd:PRK13639 217 KEGtPKE 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-223 |
1.62e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.58 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSftpspstsfsYPFLKGKsdspwqaIQLLDfkssgQQRAAYYSER 97
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL----------WPYGSGR-------IARPA-----GARVLFLPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 -Y---HSFRDkehdttlekwLLgAY-RGNEKFASQHVQEAASMTQLSHLLPS-------SLInLSNGQSRRAMLASKLVQ 165
Cdd:COG4178 435 pYlplGTLRE----------AL-LYpATAEAFSDAELREALEAVGLGHLAERldeeadwDQV-LSLGEQQRLAFARLLLH 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 166 RPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCspkIVLSLRPQDKIPDFITHVLELK 223
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELPGT---TVISVGHRSTLAAFHDRVLELT 557
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-180 |
1.62e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.22 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDS---PWQAIQLLDFKS-------SGQQRA 91
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM----LDGVDLShvpPYQRPINMMFQSyalfphmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 92 AYYSERyhsfrDKehdttLEKWLLGAyRGNEKFASQHVQEAASmtQLSHllpssliNLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:PRK11607 113 AFGLKQ-----DK-----LPKAEIAS-RVNEMLGLVHMQEFAK--RKPH-------QLSGGQRQRVALARSLAKRPKLLL 172
|
....*....
gi 19115286 172 LDEPYAGLD 180
Cdd:PRK11607 173 LDEPMGALD 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
82-313 |
1.70e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 82 DFKSSGQQRAAYYSERYHSF-RDKEHDTTlEKWLlgayrgNEKFASQHVQEAASMTQLS----------HLLP-SSLINL 149
Cdd:PRK11147 85 DFVAEGIEEQAEYLKRYHDIsHLVETDPS-EKNL------NELAKLQEQLDHHNLWQLEnrinevlaqlGLDPdAALSSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 150 SNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNhcspKIVlslrpqdkipdFITH----------- 218
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SII-----------FISHdrsfirnmatr 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 219 ----------------------------VLELKN----KKITY------QGPK------------------EQyipmtSH 242
Cdd:PRK11147 223 ivdldrgklvsypgnydqyllekeealrVEELQNaefdRKLAQeevwirQGIKarrtrnegrvralkalrrER-----SE 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 243 STNIPVKPQMKKSKPITIGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGD 313
Cdd:PRK11147 298 RREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQ 368
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
265-484 |
1.72e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 49.36 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYV-VGDHPKlfASNIKF------FGKSIGPGTGIsI 337
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPE--AGTIRVgditidTARSLSQQKGL-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 338 FDIQENIGHCSPEIhNHFPKQhTCFEALLSAWSTTFTIPKLTETRLAaiSSILEEFELKDIKDKPLSSISVGMQRFILFC 417
Cdd:PRK11264 81 RQLRQHVGFVFQNF-NLFPHR-TVLENIIEGPVIVKGEPKEEATARA--RELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 418 RAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
143-238 |
1.98e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 143 PSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLEL 222
Cdd:TIGR00955 161 PGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILM 240
|
90
....*....|....*.
gi 19115286 223 KNKKITYQGPKEQYIP 238
Cdd:TIGR00955 241 AEGRVAYLGSPDQAVP 256
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-191 |
2.01e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.83 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQLLDFKSSGQQRAAyyseR 97
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK-----------------ITVLGVPVPARARLA----R 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 YH-----SFRDKEHDTTLEKWLL--GAYRGnekFASQHVQEA-ASMTQLSHL---LPSSLINLSNGQSRRAMLASKLVQR 166
Cdd:PRK13536 114 ARigvvpQFDNLDLEFTVRENLLvfGRYFG---MSTREIEAViPSLLEFARLeskADARVSDLSGGMKRRLTLARALIND 190
|
170 180
....*....|....*....|....*....
gi 19115286 167 PQLLLLDEPYAGLDVTSRSV----LSSLL 191
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLiwerLRSLL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
265-484 |
2.57e-06 |
|
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: 49.80 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASNIKFFGKSIGPGTGIsiFDIQENI 344
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCGY--VERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GHCSPEIHNHFPKQHTCFeallsaWSTTFTIPKLTETRLA--------------AISSILE-----EFELKDIKDKPLSS 405
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEVDF------WNLSDKLRRRIRKRIAimlqrtfalygddtVLDNVLEaleeiGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 406 I----------------SVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQ-AMVIISHYEDEL 468
Cdd:TIGR03269 153 IemvqlshrithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVI 232
|
250
....*....|....*.
gi 19115286 469 PACVNRRAHIDNGKLV 484
Cdd:TIGR03269 233 EDLSDKAIWLENGEIK 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-199 |
2.99e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGsftpspstsFSYP-----FLKGksdspwQAIQlldfkssgQQRAA 92
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG---------LARPdagevLWQG------EPIR--------RQRDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 93 YYSER-Y--HSFRDKEHDTTLE--KWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLinlSNGQSRRAMLASKLVQRP 167
Cdd:PRK13538 72 YHQDLlYlgHQPGIKTELTALEnlRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQL---SAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|..
gi 19115286 168 QLLLLDEPYAGLDVTSRSVLSSLLGEmsnHCS 199
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQ---HAE 177
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
265-445 |
3.18e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.47 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpklfasniKFFGKSIGPGTGiSIFDIQENI 344
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLL---------------KCFARLLTPQSG-TVFLGDKPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 345 GHCSP-EIHNH---FPKQHTCFEAL-------------LSAWSttftipKLTETRLAAISSILEEFELKDIKDKPLSSIS 407
Cdd:PRK11231 67 SMLSSrQLARRlalLPQHHLTPEGItvrelvaygrspwLSLWG------RLSAEDNARVNQAMEQTRINHLADRRLTDLS 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115286 408 VGMQRFILFCRAIVKQPRLVVLDEPfqgvdTKYVHMAH 445
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEP-----TTYLDINH 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
264-484 |
3.41e-06 |
|
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: 48.35 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGR----KVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGPGTGISIF 338
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT--SGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 339 DIQENIGHcspeIHNHFP--KQHTCFE--AL---LSAWSTTFTIPKLTETrlaaissiLEEFELKDIKDKPLSSISVGMQ 411
Cdd:cd03258 79 KARRRIGM----IFQHFNllSSRTVFEnvALpleIAGVPKAEIEERVLEL--------LELVGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 412 RFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYL---NEKLSPSqaMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLrdiNRELGLT--IVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-221 |
3.72e-06 |
|
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: 48.10 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 17 FPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPspstsfsypfLKGK---SDSPWQAIQLLDFKSSGQQRAAY 93
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT----------LEGKvhwSNKNESEPSFEATRSRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 94 YSERyhsfrdkehdttleKWLLGA-YRGNEKFAS-------QHVQEAASMTQLSHLLP--------SSLINLSNGQSRRA 157
Cdd:cd03290 84 AAQK--------------PWLLNAtVEENITFGSpfnkqryKAVTDACSLQPDIDLLPfgdqteigERGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLDVtsrsvlssllgEMSNHCSPKIVLSLRPQDK-IPDFITHVLE 221
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDI-----------HLSDHLMQEGILKFLQDDKrTLVLVTHKLQ 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
265-484 |
3.73e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAY---------------------VVGD---------- 313
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYmamhaidgipkncqilhveqeVVGDdttalqcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 314 ----HPKLFASNIKF--------FGKSIGPGTGISIFDIQEN-IGHCSPEIHNHFpkqhtcfeALLSAWSttftipklTE 380
Cdd:PLN03073 258 tdieRTQLLEEEAQLvaqqreleFETETGKGKGANKDGVDKDaVSQRLEEIYKRL--------ELIDAYT--------AE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 381 TRLAAISSILeEFElKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLnekLSPSQAMVI 460
Cdd:PLN03073 322 ARAASILAGL-SFT-PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL---LKWPKTFIV 396
|
250 260
....*....|....*....|....
gi 19115286 461 ISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHGQKLV 420
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-183 |
3.95e-06 |
|
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: 47.97 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFL--DARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPspsTSFSYpFLKGKSdspwqaIQLLD 82
Cdd:cd03245 3 IEFRNVSFSypNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKP---TSGSV-LLDGTD------IRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 83 fKSSGQQRAAYYSEryhsfrdkehDTTLekwLLGAYRGNEKFASQHVQ--------EAASMTQLSHLLPSSL-------- 146
Cdd:cd03245 73 -PADLRRNIGYVPQ----------DVTL---FYGTLRDNITLGAPLADderilraaELAGVTDFVNKHPNGLdlqigerg 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115286 147 INLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTS 183
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-234 |
4.06e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYPFL------KGKSDSPWQAIQLLDFKSSGQQRAAYY 94
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-TGTVTVDDItithktKDKYIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHSFRDKEHDTTLEKWLLGAYRgnekfasqhvqeaaSMTQLS---HLLPSSLINLSNGQSRRAMLASKLVQRPQLLL 171
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHR--------------LLMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 172 LDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQG-PKE 234
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTsPKE 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
263-474 |
4.30e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHP-------------KLFASNIKFFGKSi 329
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiifegeELQASNIRDTERA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 330 gpgtGISI----------FDIQENI--GHcspEIHNH----FPKQHTCFEALLSawsttftipkltetrlaaissileef 393
Cdd:PRK13549 83 ----GIAIihqelalvkeLSVLENIflGN---EITPGgimdYDAMYLRAQKLLA-------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 394 ELK-DIK-DKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPA- 470
Cdd:PRK13549 130 QLKlDINpATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAi 209
|
....*...
gi 19115286 471 ----CVNR 474
Cdd:PRK13549 210 sdtiCVIR 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
265-307 |
4.73e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 48.53 E-value: 4.73e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLL 46
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-191 |
4.77e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.26 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQLLDfkSSGQQRAAYYSERYH-- 99
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS-----------------ISLCG--EPVPSRARHARQRVGvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 100 -SFRDKEHDTTLEKWLL--GAYRG-NEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:PRK13537 86 pQFDNLDPDFTVRENLLvfGRYFGlSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180
....*....|....*....|
gi 19115286 176 YAGLDVTSRSV----LSSLL 191
Cdd:PRK13537 166 TTGLDPQARHLmwerLRSLL 185
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
276-307 |
5.15e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.01 E-value: 5.15e-06
10 20 30
....*....|....*....|....*....|..
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
264-465 |
5.85e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKLFASNIKFFGK---SIGP----GTGI 335
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGrEDYEVTGGTVEFKGKdllELSPedraGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 336 SI-FDIQENIghcsPEIHNHFPKQHTcfealLSAWSTTFTIPKLteTRLAAISSILEEFELKDIKDKPLS-SISVGM--- 410
Cdd:PRK09580 81 FMaFQYPVEI----PGVSNQFFLQTA-----LNAVRSYRGQEPL--DRFDFQDLMEEKIALLKMPEDLLTrSVNVGFsgg 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 411 ---QRFILFCRAIvkQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYE 465
Cdd:PRK09580 150 ekkRNDILQMAVL--EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQ 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
276-463 |
6.11e-06 |
|
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: 47.61 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVvgdhPKLF---ASNIKFFGKSIgpgTGISIFDIQENIGHCSPEIh 352
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYdvdSGRILIDGHDV---RDYTLASLRRQIGLVSQDV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 353 nhFPKQHTCFEallsawSTTFTIPKLT--ETRLAAISSILEEF--ELKDIKDKPL----SSISVGMQRFILFCRAIVKQP 424
Cdd:cd03251 86 --FLFNDTVAE------NIAYGRPGATreEVEEAARAANAHEFimELPEGYDTVIgergVKLSGGQRQRIAIARALLKDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115286 425 RLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVIISH 463
Cdd:cd03251 158 PILILDEATSALDTESERLVQAAL-ERLMKNRTTFVIAH 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-179 |
6.56e-06 |
|
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: 47.04 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTP-SPSTSFsypflKGKSDSPWQAiqlldfkssgQQRA----AYYS 95
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRF-----DGRDITGLPP----------HERAragiGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 96 ERYHSFRDKehdTTLEKWLLGAYRGNEKFASQHVQEAASM--------TQLSHllpssliNLSNGQsrRAMLA--SKLVQ 165
Cdd:cd03224 82 EGRRIFPEL---TVEENLLLGAYARRRAKRKARLERVYELfprlkerrKQLAG-------TLSGGE--QQMLAiaRALMS 149
|
170
....*....|....
gi 19115286 166 RPQLLLLDEPYAGL 179
Cdd:cd03224 150 RPKLLLLDEPSEGL 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-222 |
6.65e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.80 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 6 KFANTTFLDarfplfkNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypfLKGKSDSPW--QAI----- 78
Cdd:COG4152 10 RFGDKTAVD-------DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL----WDGEPLDPEdrRRIgylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 79 ------------QLLDF-------KSSGQQRAAYYSERyhsfrdkehdttLEkwlLGAYRgNEKfasqhVQEaasmtqls 139
Cdd:COG4152 79 erglypkmkvgeQLVYLarlkglsKAEAKRRADEWLER------------LG---LGDRA-NKK-----VEE-------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 140 hllpsslinLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPkIVLSlrpqdkipdfiTHV 219
Cdd:COG4152 130 ---------LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIFS-----------SHQ 188
|
...
gi 19115286 220 LEL 222
Cdd:COG4152 189 MEL 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-204 |
6.79e-06 |
|
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: 47.48 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFL---DARFPLfKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSYPFLKGKSDSPWQAIQLl 81
Cdd:cd03252 1 ITFEHVRFRykpDGPVIL-DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 82 dfkSSGQQRAAYYSEryhSFRDkehDTTLekwllgayrGNEKFASQHVQEAASMTQlSHLLPSSL------------INL 149
Cdd:cd03252 79 ---GVVLQENVLFNR---SIRD---NIAL---------ADPGMSMERVIEAAKLAG-AHDFISELpegydtivgeqgAGL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 150 SNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSllgEMSNHCSPKIVL 204
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMR---NMHDICAGRTVI 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
276-463 |
7.38e-06 |
|
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: 47.22 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG--DHPKlfaSNIKFFGKSIGPGTGIS-------------IF-- 338
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQK---GQILIDGIDIRDISRKSlrsmigvvlqdtfLFsg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 339 DIQENIGHCSPEIhnhfpKQHTCFEALLSAWSTTF--TIPKLTETRLAAISSILeefelkdikdkplssiSVGMQRFILF 416
Cdd:cd03254 92 TIMENIRLGRPNA-----TDEEVIEAAKEAGAHDFimKLPNGYDTVLGENGGNL----------------SQGERQLLAI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19115286 417 CRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVIISH 463
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEAL-EKLMKGRTSIIIAH 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-193 |
7.39e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.27 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTFLDARFPLfkNVSFELARKQNWAIIGNTGSGRTTFLRCIQGsFTPSPSTSFsypFLKGKSdspwqaiqlldfk 84
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAG-FLTPASGSL---TLNGQD------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 ssgqQRAAYYSERYHSFRDKE-----HDTTLEKWLLGAYRGNEKFASQH--VQEAASMTQLSHLLPSSLINLSNGQSRRA 157
Cdd:PRK10771 63 ----HTTTPPSRRPVSMLFQEnnlfsHLTVAQNIGLGLNPGLKLNAAQRekLHAIARQMGIEDLLARLPGQLSGGQRQRV 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGE 193
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-189 |
8.20e-06 |
|
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: 47.02 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 35 IIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDSPWQAI----QLLDFKSSGQQRAAYYSeryhsfRDKEHDTTl 110
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPD----------EGDIEIELDTVsykpQYIKADYEGTVRDLLSS------ITKDFYTH- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 111 ekwllgayrgnekfaSQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSS 189
Cdd:cd03237 93 ---------------PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
265-439 |
8.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVY-----WGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdHPKLFASNIKFFGKSIgPGTGISIFD 339
Cdd:PRK13637 3 IKIENLTHIYmegtpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNG-LLKPTSGKIIIDGVDI-TDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 IQENIGhcspeIHNHFPkQHTCFEAllsawsttfTIPK----------LTETRL-----AAISSILEEFElkDIKDKPLS 404
Cdd:PRK13637 81 IRKKVG-----LVFQYP-EYQLFEE---------TIEKdiafgpinlgLSEEEIenrvkRAMNIVGLDYE--DYKDKSPF 143
|
170 180 190
....*....|....*....|....*....|....*
gi 19115286 405 SISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTK 439
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
264-321 |
8.40e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 8.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 264 LISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASN 321
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPR 58
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
264-437 |
9.23e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYWG-RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGPGTGISIFDIQ 341
Cdd:PRK10908 1 MIRFEHVSKAYLGgRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPS--AGKIWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 ENIGHCSPEihNHFPKQHTCFE----ALLSAWSTTFTIPKltetrlaAISSILEEFELKD-IKDKPLsSISVGMQRFILF 416
Cdd:PRK10908 79 RQIGMIFQD--HHLLMDRTVYDnvaiPLIIAGASGDDIRR-------RVSAALDKVGLLDkAKNFPI-QLSGGEQQRVGI 148
|
170 180
....*....|....*....|.
gi 19115286 417 CRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
282-437 |
9.27e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.20 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 282 DINWTIREGERWALTGSNGSGKTT-------LLAyvvgdhpklfAS--NIKFFGKSIGPGtgisifDIQ--ENIGHCSP- 349
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLP----------ASegEAWLFGQPVDAG------DIAtrRRVGYMSQa 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 350 -------------EIHnhfpkqhtcfeALLsawsttFTIPKltETRLAAISSILEEFELKDIKDKPLSSISVGM-QRFIL 415
Cdd:NF033858 348 fslygeltvrqnlELH-----------ARL------FHLPA--AEIAARVAEMLERFDLADVADALPDSLPLGIrQRLSL 408
|
170 180
....*....|....*....|..
gi 19115286 416 fCRAIVKQPRLVVLDEPFQGVD 437
Cdd:NF033858 409 -AVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-181 |
9.64e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 11 TFLDARF-----P-LFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFsypflkgksdspwqaiqlldfk 84
Cdd:PLN03073 510 SFSDASFgypggPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------------------- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 85 SSGQQRAAYYSERYHSFRDKEHDTTLekWLLGAYRG-NEKFASQHVqeaASMTQLSHLLPSSLINLSNGQSRRAMLASKL 163
Cdd:PLN03073 568 RSAKVRMAVFSQHHVDGLDLSSNPLL--YMMRCFPGvPEQKLRAHL---GSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 642
|
170
....*....|....*...
gi 19115286 164 VQRPQLLLLDEPYAGLDV 181
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDL 660
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
263-308 |
1.06e-05 |
|
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: 46.66 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRK----VLSDINWTIREGERWALTGSNGSGKTTLLA 308
Cdd:COG4181 7 PIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLG 56
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-218 |
1.16e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 16 RFPLFKNVSFELARKQNWAIIGNTGSGRT----TFLRCIQGSFTPSPSTSFsypFLKGKSDspwQAIQLLDFKSSGQQR- 90
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKM---LLRRRSR---QVIELSEQSAAQMRHv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 91 -----AAYYSERYHS----FRDKEHDTTLEKWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLAS 161
Cdd:PRK10261 102 rgadmAMIFQEPMTSlnpvFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 162 KLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVlslrpqdkipdFITH 218
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVI-----------FITH 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
258-345 |
1.31e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 46.91 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 258 ITIGKPLISMEHLNCVYWGRK--VLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHpKLFASNIKFFGKSIgpgTGI 335
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL-KPQSGEIKIDGITI---SKE 76
|
90
....*....|
gi 19115286 336 SIFDIQENIG 345
Cdd:PRK13632 77 NLKEIRKKIG 86
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-191 |
1.50e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYpflkGKSDSPWQAIQLLdfkSSGQQRA-------- 91
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVHY----RMRDGQLRDLYAL---SEAERRRllrtewgf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 92 ----------------AYYSER--------YHSFRDKEHDttlekWLlgayrgnekfasQHVQEAASMTQlshLLPSSli 147
Cdd:PRK11701 94 vhqhprdglrmqvsagGNIGERlmavgarhYGDIRATAGD-----WL------------ERVEIDAARID---DLPTT-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19115286 148 nLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVtsrSVLSSLL 191
Cdd:PRK11701 152 -FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV---SVQARLL 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-194 |
1.56e-05 |
|
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: 45.92 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTF-----LDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCI-------QGSFTPSPSTSFSypflkgkSD 72
Cdd:cd03250 1 ISVEDASFtwdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgeleklSGSVSVPGSIAYV-------SQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 73 SPWqaIQlldfksSGQQR------AAYYSERYhsfrdkehdttlekwllgayrgnekfasQHVQEAASMTQLSHLLPSSL 146
Cdd:cd03250 74 EPW--IQ------NGTIRenilfgKPFDEERY----------------------------EKVIKACALEPDLEILPDGD 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 147 --------INLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDV-TSRSVLSSLLGEM 194
Cdd:cd03250 118 lteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGL 174
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
262-345 |
1.59e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 46.55 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWG--RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpkLF---ASNIKFFGKSIGPGTgis 336
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNG----LLlpeAGTITVGGMVLSEET--- 75
|
....*....
gi 19115286 337 IFDIQENIG 345
Cdd:PRK13635 76 VWDVRRQVG 84
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
7-212 |
1.74e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.39 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 7 FANTTFLDArfPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKsdspwqaiqlldFKSS 86
Cdd:cd03291 42 FSNLCLVGA--PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS----------EGK------------IKHS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 87 GqqRAAYYSEryhsFRDKEHDTTLEKWLLGA----YRGNEKFASQHVQE--AASMTQLSHLLPSSLINLSNGQSRRAMLA 160
Cdd:cd03291 98 G--RISFSSQ----FSWIMPGTIKENIIFGVsydeYRYKSVVKACQLEEdiTKFPEKDNTVLGEGGITLSGGQRARISLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 161 SKLVQRPQLLLLDEPYAGLDV-TSRSVLSSLLGEMSNHCSPKIVLS----LRPQDKI 212
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVfTEKEIFESCVCKLMANKTRILVTSkmehLKKADKI 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-181 |
1.78e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFtpsPSTSFSYPFLKGKS---DSPWQAIQlldfkssgqQRAAYYSEry 98
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY---PGRWEGEIFIDGKPvkiRNPQQAIA---------QGIAMVPE-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 99 hsfrDKEHDTTL------EKWLLGAYRgneKFASQHVQEAA--------SMTQLSHLLPSSLI---NLSNGQSRRAMLAS 161
Cdd:PRK13549 346 ----DRKRDGIVpvmgvgKNITLAALD---RFTGGSRIDDAaelktileSIQRLKVKTASPELaiaRLSGGNQQKAVLAK 418
|
170 180
....*....|....*....|
gi 19115286 162 KLVQRPQLLLLDEPYAGLDV 181
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDV 438
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-180 |
1.93e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 29 RKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDSPWQAIQLLDFKSSGQQRAAYYSERYHSFRDKEHDT 108
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGS----------SGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115286 109 TLEKWLLGAYRGNEKFASQHVQEAASMTQLS-----HLLPSsliNLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD 180
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGlgkrlDHLPA---QLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
280-437 |
2.18e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 45.99 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 280 LSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklfasnikffgksIGPGTGiSIFDIQENIGHCSP-EIHNH---F 355
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG----------------LLPGQG-EILLNGRPLSDWSAaELARHrayL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 356 PKQHT------CFEAL-LSAWSTTftipkLTETRLAAISSILEEFELKDIKDKPLSSISVG-MQR------FILFCRAIV 421
Cdd:COG4138 75 SQQQSppfampVFQYLaLHQPAGA-----SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGeWQRvrlaavLLQVWPTIN 149
|
170
....*....|....*.
gi 19115286 422 KQPRLVVLDEPFQGVD 437
Cdd:COG4138 150 PEGQLLLLDEPMNSLD 165
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
132-234 |
2.33e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 45.88 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 132 AASMTQLSHLLPSsliNLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHcSPKIVLSLRPQDK 211
Cdd:PRK13647 125 AVRMWDFRDKPPY---HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDL 200
|
90 100
....*....|....*....|...
gi 19115286 212 IPDFITHVLELKNKKITYQGPKE 234
Cdd:PRK13647 201 AAEWADQVIVLKEGRVLAEGDKS 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
262-437 |
2.35e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.07 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 262 KPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdHPKLFASNIKFFGKSigpGTGISIFDIQ 341
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRD---GQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 342 EnighcsPE-----------IHNHfPKQhtcfeALLSAWSTTFTIPKltetRLAAI------------SSILEEFEL--K 396
Cdd:PRK11701 80 E------AErrrllrtewgfVHQH-PRD-----GLRMQVSAGGNIGE----RLMAVgarhygdirataGDWLERVEIdaA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19115286 397 DIKDKPlSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVD 437
Cdd:PRK11701 144 RIDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
150-220 |
2.40e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 2.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 150 SNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLslrpqdkipdfITHVL 220
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIM-----------ITHDL 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
279-483 |
2.58e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.58 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 279 VLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFFGKSIGPGTGISIFDIQENIGHCSPEIHNHFPk 357
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPT--SGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 358 QHTCFE----ALLSAWSTTFTIPKLTETRLAAISsiLEefelKDIKDKPlSSISVGMQRFILFCRAIVKQPRLVVLDEPF 433
Cdd:PRK11629 101 DFTALEnvamPLLIGKKKPAEINSRALEMLAAVG--LE----HRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115286 434 QGVDTKYVHMAHNYLNEkLSPSQ--AMVIISHyEDELPACVNRRAHIDNGKL 483
Cdd:PRK11629 174 GNLDARNADSIFQLLGE-LNRLQgtAFLVVTH-DLQLAKRMSRQLEMRDGRL 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
149-250 |
2.72e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHcSPKIVLSL-RPQDKIPDFITHVLELKNKKI 227
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMhQPSSRVYQMFDSVLVLSEGRC 285
|
90 100
....*....|....*....|....*.
gi 19115286 228 TYQGPKEQ---YIPMTSHSTNIPVKP 250
Cdd:PLN03211 286 LFFGKGSDamaYFESVGFSPSFPMNP 311
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-216 |
2.80e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.81 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 19 LFKNVSFELARKQNWAIIGNTGSGRTTFLRC-------------IQGSFTPSPSTSFSYPFLKGKSDSPWQAIQLLDFKS 85
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieiydskikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 86 SGQQRAAYYSERYHSFRDKehdttlekwllgayRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQ 165
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEK--------------REIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115286 166 RPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSpKIVLSLRPQD--KIPDFI 216
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIA-IVIVSHNPQQvaRVADYV 222
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-224 |
3.46e-05 |
|
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: 44.27 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 144 SSLINLSNGQSRRAMLASKL----VQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIvlslrpqdkipdFITHV 219
Cdd:cd03227 73 FTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVI------------VITHL 140
|
....*
gi 19115286 220 LELKN 224
Cdd:cd03227 141 PELAE 145
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
255-307 |
3.69e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 3.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 19115286 255 SKPITIGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLL 54
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
148-234 |
4.17e-05 |
|
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: 44.44 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 148 NLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQ--DKI-PDFItHVleLKN 224
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRllDYIkPDRV-HV--LYD 180
|
90
....*....|
gi 19115286 225 KKITYQGPKE 234
Cdd:cd03217 181 GRIVKSGDKE 190
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
271-344 |
5.84e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.85 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 271 NCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDhpkLFASN--IKFFGKS--------IGPGTgisifdI 340
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGE---LEPSEgkIKHSGRIsfssqfswIMPGT------I 114
|
....
gi 19115286 341 QENI 344
Cdd:cd03291 115 KENI 118
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
276-432 |
6.07e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPK-------LFASNIKFFgKSI--GPGTGISI--------- 337
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsyegeiLFDGEVCRF-KDIrdSEALGIVIihqelalip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 338 -FDIQENI--GHcspEIHNHfpkqhtcfeALLSaWSTTFtipklTETRlaaisSILEEFELKDIKDKPLSSISVGMQRFI 414
Cdd:NF040905 92 yLSIAENIflGN---ERAKR---------GVID-WNETN-----RRAR-----ELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170
....*....|....*...
gi 19115286 415 LFCRAIVKQPRLVVLDEP 432
Cdd:NF040905 149 EIAKALSKDVKLLILDEP 166
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
114-183 |
6.15e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 6.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115286 114 LLGA-YRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTS 183
Cdd:COG4586 119 LLKAiYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
148-196 |
6.38e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 6.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 19115286 148 NLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSN 196
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-260 |
6.57e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.08 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 23 VSFELARKQNWAIIGNTGSGRTTFLRCIQGSFtpsPSTSFSYPF----LKGKSDSPWQA----IQLLdFkssgQQRAAYY 94
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLV---KATDGEVAWlgkdLLGMKDDEWRAvrsdIQMI-F----QDPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHSfrdkeHDTTLEKwlLGAYRgnEKFASQHVQE--AASMTQLShLLPSsLIN-----LSNGQSRRAMLASKLVQRP 167
Cdd:PRK15079 112 NPRMTI-----GEIIAEP--LRTYH--PKLSRQEVKDrvKAMMLKVG-LLPN-LINrypheFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 168 QLLLLDEPYAGLDVTSRS----VLSSLLGEMS-------------NHCSPKIVLSlrpqdkipdFITHVLELKNKKITYQ 230
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAqvvnLLQQLQREMGlslifiahdlavvKHISDRVLVM---------YLGHAVELGTYDEVYH 251
|
250 260 270
....*....|....*....|....*....|
gi 19115286 231 GPKEQYIPMTSHSTNIPvKPQMKKSKPITI 260
Cdd:PRK15079 252 NPLHPYTKALMSAVPIP-DPDLERNKTIQL 280
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
245-484 |
6.85e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.22 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 245 NIPVKPQMKKSKPITIGKPlISMEHLNCV---YWGRKVLSDINWTIREGERWALTGSNGSGKTTL-------LAYV---- 310
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDP-VTIEAEDLEilsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLlnallgfLPYQgslk 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 311 --------------------VGDHPKLFAsnikffgksigpGTgisifdIQENIGHCSPEIHNHFPKQhtcfeALLSAWS 370
Cdd:PRK11174 408 ingielreldpeswrkhlswVGQNPQLPH------------GT------LRDNVLLGNPDASDEQLQQ-----ALENAWV 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 371 TTFtIPKLT---ETrlaaissileefelkDIKDKPlSSISVGM-QRFILfCRAIVKQPRLVVLDEPFQGVDTKYVHMAHN 446
Cdd:PRK11174 465 SEF-LPLLPqglDT---------------PIGDQA-AGLSVGQaQRLAL-ARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
250 260 270
....*....|....*....|....*....|....*...
gi 19115286 447 YLNEkLSPSQAMVIISHYEDELpACVNRRAHIDNGKLV 484
Cdd:PRK11174 527 ALNA-ASRRQTTLMVTHQLEDL-AQWDQIWVMQDGQIV 562
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
245-445 |
7.34e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 245 NIPVKPQMKKSKPItigKPLIS-MEHLNCVYWGRK-VLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPK--LFAS 320
Cdd:TIGR00955 7 NSDVFGRVAQDGSW---KQLVSrLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 321 NIKFFGKSIGPG--TGISIFDIQENIghcspeihnhFPKQHTCFEALLsaWSTTFTIPKLT--ETRLAAISSILEEFELK 396
Cdd:TIGR00955 84 SVLLNGMPIDAKemRAISAYVQQDDL----------FIPTLTVREHLM--FQAHLRMPRRVtkKEKRERVDEVLQALGLR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 397 DIKD------KPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTkyvHMAH 445
Cdd:TIGR00955 152 KCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS---FMAY 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
149-222 |
7.53e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 7.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLslrpqdkipdfITHVLEL 222
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVL-----------ITHDLAL 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
115-235 |
7.64e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.39 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 115 LGAYRGNEKfasQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEM 194
Cdd:PRK10575 117 LGRFGAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 19115286 195 SNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQ 235
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
276-307 |
8.96e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 44.75 E-value: 8.96e-05
10 20 30
....*....|....*....|....*....|..
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLL 45
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
265-344 |
9.69e-05 |
|
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: 43.61 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLnCVYWGRK------VLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASniKFFGKSIG-------- 330
Cdd:cd03250 1 ISVEDA-SFTWDSGeqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGS--VSVPGSIAyvsqepwi 77
|
90
....*....|....*
gi 19115286 331 -PGTgisifdIQENI 344
Cdd:cd03250 78 qNGT------IRENI 86
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
256-335 |
1.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 256 KPITIGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASNIKFFGKSIGPGTGI 335
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLI--------KLLAGELAPVSGEIGLAKGI 375
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
265-484 |
1.03e-04 |
|
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: 43.63 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYW--GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPklfASNikffGKSIGPGTGISIFD--- 339
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV---PEN----GRVLVDGHDLALADpaw 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 340 ------------------IQENIGHCSPEihnhfPKQHTCFEALLSAWSTTFtIPKLTEtrlaAISSILEEFElkdikdk 401
Cdd:cd03252 74 lrrqvgvvlqenvlfnrsIRDNIALADPG-----MSMERVIEAAKLAGAHDF-ISELPE----GYDTIVGEQG------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 402 plSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVIISHYEDELpACVNRRAHIDNG 481
Cdd:cd03252 137 --AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNM-HDICAGRTVIIIAHRLSTV-KNADRIIVMEKG 212
|
...
gi 19115286 482 KLV 484
Cdd:cd03252 213 RIV 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
252-463 |
1.12e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 252 MKKSKpiTIGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKlFASNIKFFGKSIGP 331
Cdd:PRK15439 1 MQTSD--TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP-DSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 332 GT-------GISIFDiQEnighcsPEIhnhFPKQhTCFEALLsawsttFTIPK--LTETRLAAISSILE-EFELkdikDK 401
Cdd:PRK15439 78 LTpakahqlGIYLVP-QE------PLL---FPNL-SVKENIL------FGLPKrqASMQKMKQLLAALGcQLDL----DS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115286 402 PLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH 463
Cdd:PRK15439 137 SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-57 |
1.17e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.53 E-value: 1.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 19115286 16 RFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS 57
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
278-313 |
1.21e-04 |
|
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: 42.69 E-value: 1.21e-04
10 20 30
....*....|....*....|....*....|....*.
gi 19115286 278 KVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGD 313
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGD 51
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
137-183 |
1.26e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.73 E-value: 1.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 19115286 137 QLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTS 183
Cdd:PRK10895 126 HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-215 |
1.30e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCI----------------------------QG--------------SFT 55
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyQGdeeqnvgmknvnefSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 56 PSPSTSFSYPFLKGKSDSPWQAIQLLD---------FKSSGQQRAAYYSERYHSFRDKEHDTTLEKwllgayrgnekfaS 126
Cdd:PTZ00265 1262 KEGGSGEDSTVFKNSGKILLDGVDICDynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKEDATRED-------------V 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 127 QHVQEAASMTQLSHLLPSSL--------INLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHC 198
Cdd:PTZ00265 1329 KRACKFAAIDEFIESLPNKYdtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1408
|
250 260
....*....|....*....|...
gi 19115286 199 SPKIVL------SLRPQDKIPDF 215
Cdd:PTZ00265 1409 DKTIITiahriaSIKRSDKIVVF 1431
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
276-448 |
1.39e-04 |
|
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: 42.92 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFAS-NIKFFGKSIGPGT--GISIFDIQENIghcspeih 352
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSgEVLINGRPLDKRSfrKIIGYVPQDDI-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 353 nHFPKQhTCFEALlsawsttftipkltetrlaaissileEFELKdikdkpLSSISVGMQRFILFCRAIVKQPRLVVLDEP 432
Cdd:cd03213 93 -LHPTL-TVRETL--------------------------MFAAK------LRGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170
....*....|....*.
gi 19115286 433 FQGVDTkyvHMAHNYL 448
Cdd:cd03213 139 TSGLDS---SSALQVM 151
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
121-242 |
1.45e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 43.36 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 121 NEKFASQHVQEAASMTQL----SHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSN 196
Cdd:PRK14247 115 SKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19115286 197 HCSPKIVLSLRPQ-DKIPDFITHvleLKNKKITYQGPKEQYIPMTSH 242
Cdd:PRK14247 195 DMTIVLVTHFPQQaARISDYVAF---LYKGQIVEWGPTREVFTNPRH 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
150-185 |
1.46e-04 |
|
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: 43.13 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*.
gi 19115286 150 SNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRS 185
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-315 |
1.64e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.15 E-value: 1.64e-04
10 20 30
....*....|....*....|....*....|....*....
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHP 315
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP 57
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-190 |
1.72e-04 |
|
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: 42.99 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTF-LDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDSPWQAIQLLDF 83
Cdd:cd03253 1 IEFENVTFaYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS----------SGSILIDGQDIREVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 84 kssgqqraayyseryHSFRDK----EHDTTLEKWLLG---AYrGNEKFASQHVQEAASMTQLsHLLPSSL---------- 146
Cdd:cd03253 71 ---------------DSLRRAigvvPQDTVLFNDTIGyniRY-GRPDATDEEVIEAAKAAQI-HDKIMRFpdgydtivge 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19115286 147 --INLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDV-TSRSVLSSL 190
Cdd:cd03253 134 rgLKLSGGEKQRVAIARAILKNPPILLLDEATSALDThTEREIQAAL 180
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-195 |
1.97e-04 |
|
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: 42.03 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 20 FKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSypfLKGKS---DSPWQAIQLldfkssgqqRAAYYSE 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-SGEIT---LDGKPvtrRSPRDAIRA---------GIAYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 97 -RyhsfrdKEHdttlekwllGAyrgnekFASQHVQEAASMTQLshllpsslinLSNGQSRRAMLASKLVQRPQLLLLDEP 175
Cdd:cd03215 83 dR------KRE---------GL------VLDLSVAENIALSSL----------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180
....*....|....*....|
gi 19115286 176 YAGLDVTSRSVLSSLLGEMS 195
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELA 151
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
265-432 |
2.05e-04 |
|
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: 42.20 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRK--VLSDINWTIREGERWALTGSNGSGKTTLLayvvgdhpKLFASNIKffgksigPGTGISIFDIQE 342
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLA--------RLILGLLR-------PTSGRVRLDGAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 343 nighcspeihnhfpkqhtcfealLSAWsttftipKLTETRlAAISSILEEFELKD--IKDKPLSSisvG-MQRfILFCRA 419
Cdd:cd03246 66 -----------------------ISQW-------DPNELG-DHVGYLPQDDELFSgsIAENILSG---GqRQR-LGLARA 110
|
170
....*....|...
gi 19115286 420 IVKQPRLVVLDEP 432
Cdd:cd03246 111 LYGNPRILVLDEP 123
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
276-480 |
2.09e-04 |
|
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: 41.76 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGdhpklfasnikffgksIGP-GTGisifdiqeNIGHcsPEIHNH 354
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG----------------LWPwGSG--------RIGM--PEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 355 F--PkQHTCF------EALLSAWSTTFtipkltetrlaaissileefelkdikdkplssiSVGMQRFILFCRAIVKQPRL 426
Cdd:cd03223 67 LflP-QRPYLplgtlrEQLIYPWDDVL---------------------------------SGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19115286 427 VVLDEPFQGVDTKYVHMAHNYLNEKLSpsqAMVIISHYEdELPACVNRRAHIDN 480
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI---TVISVGHRP-SLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-180 |
2.43e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 43.08 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 14 DARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSpSTSFSYPFLKGKSDSPWQ-------AIQLLDFKSS 86
Cdd:PRK13635 17 DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMVLSEETVWDvrrqvgmVFQNPDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 87 G---QQRAAYYSERyhsfRDKEHDTTLEKwllgayrgnekfasqhVQEA---ASMTQLSHLLPSSLinlSNGQSRRAMLA 160
Cdd:PRK13635 96 GatvQDDVAFGLEN----IGVPREEMVER----------------VDQAlrqVGMEDFLNREPHRL---SGGQKQRVAIA 152
|
170 180
....*....|....*....|
gi 19115286 161 SKLVQRPQLLLLDEPYAGLD 180
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLD 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-191 |
2.50e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTT----FLRCI--QGSFTpspstsfsypfLKGKSDSPWQAIQLLDFKSSGQqraAYY 94
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsQGEIW-----------FDGQPLHNLNRRQLLPVRHRIQ---VVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 95 SERYHSFRDKehdTTLEKWLLGAYRGNEKFASQHVQEA---ASMTQLS------HLLPSSLinlSNGQSRRAMLASKLVQ 165
Cdd:PRK15134 369 QDPNSSLNPR---LNVLQIIEEGLRVHQPTLSAAQREQqviAVMEEVGldpetrHRYPAEF---SGGQRQRIAIARALIL 442
|
170 180
....*....|....*....|....*.
gi 19115286 166 RPQLLLLDEPYAGLDVTSRSVLSSLL 191
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALL 468
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
265-307 |
2.53e-04 |
|
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: 42.55 E-value: 2.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 19115286 265 ISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLL 43
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
265-432 |
2.55e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.80 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYW-GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASnIKFFGKSIGPGTgisIFDIQEN 343
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-VKVMGREVNAEN---EKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 344 IGHCSPEihnhfPKQHTcFEAllSAWSTTFTIPKLTETRLAAISSILEE----FELKDIKDKPLSSISVGMQRFILFCRA 419
Cdd:PRK13647 81 VGLVFQD-----PDDQV-FSS--TVWDDVAFGPVNMGLDKDEVERRVEEalkaVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170
....*....|...
gi 19115286 420 IVKQPRLVVLDEP 432
Cdd:PRK13647 153 LAMDPDVIVLDEP 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
127-184 |
2.76e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.17 E-value: 2.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115286 127 QHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSR 184
Cdd:PRK11432 115 QRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
149-182 |
3.00e-04 |
|
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: 42.73 E-value: 3.00e-04
10 20 30
....*....|....*....|....*....|....
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVT 182
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVT 184
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-181 |
3.70e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFtpsPSTSFSYPfLKGKS---DSPWQAIqlldfkSSGqqrAAYYSEr 97
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAL---PRTSGYVT-LDGHEvvtRSPQDGL------ANG---IVYISE- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 yhsfrDKEHD------TTLEKWLLGAYRGNEKFASQ--HVQEAASMTQLSHLL----PS---SLINLSNGQSRRAMLASK 162
Cdd:PRK10762 335 -----DRKRDglvlgmSVKENMSLTALRYFSRAGGSlkHADEQQAVSDFIRLFniktPSmeqAIGLLSGGNQQKVAIARG 409
|
170
....*....|....*....
gi 19115286 163 LVQRPQLLLLDEPYAGLDV 181
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDV 428
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
149-180 |
4.67e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 41.92 E-value: 4.67e-04
10 20 30
....*....|....*....|....*....|..
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD 180
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
263-484 |
4.81e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 263 PLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLfaSNIKFFGKSIGPGTGI----SIF 338
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKV--SGYRYSGDVLLGGRSIfnyrDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 339 DIQENIGHCSpEIHNHFPKqhTCFEALLSAWSTTFTIPKlTETRLAAISSILEEFELKDIKDKPLSS---ISVGMQRFIL 415
Cdd:PRK14271 98 EFRRRVGMLF-QRPNPFPM--SIMDNVLAGVRAHKLVPR-KEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLC 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115286 416 FCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLnEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLV 484
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI-RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
277-431 |
4.86e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKlfasnikffgksiGPGTGisIFDIQEnighcspeihNHFP 356
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG-------------TPVAG--CVDVPD----------NQFG 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 357 KQHTCFEALLSAWSTtftipkLTETRLAAISSILEEFELKdikdKPLSSISVGMQ-RFILfCRAIVKQPRLVVLDE 431
Cdd:COG2401 98 REASLIDAIGRKGDF------KDAVELLNAVGLSDAVLWL----RRFKELSTGQKfRFRL-ALLLAERPKLLVIDE 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
273-432 |
5.30e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 273 VYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDH------------PKLFASNikffGKSIGPGTGIsIFdi 340
Cdd:PRK11288 13 TFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYqpdagsilidgqEMRFAST----TAALAAGVAI-IY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 341 QENigHCSPEIhnhfpkqhTCFEAL-LSAWSTTFTIPKLTETRLAAiSSILEEFELKDIKDKPLSSISVGMQRFILFCRA 419
Cdd:PRK11288 86 QEL--HLVPEM--------TVAENLyLGQLPHKGGIVNRRLLNYEA-REQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170
....*....|...
gi 19115286 420 IVKQPRLVVLDEP 432
Cdd:PRK11288 155 LARNARVIAFDEP 167
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-57 |
5.71e-04 |
|
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: 41.36 E-value: 5.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 19115286 16 RFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS 57
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD 75
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
208-449 |
5.91e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 208 PQDKIPDFITHVLelkNKKITYQGPKEQYIPMTS-HSTNIPVKPqmkkskpitiGKPLISMEHLNcVYWGRKV----LSD 282
Cdd:PLN03232 570 PLNMLPNLLSQVV---NANVSLQRIEELLLSEERiLAQNPPLQP----------GAPAISIKNGY-FSWDSKTskptLSD 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 283 INWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASNIKFFGkSIGPGTGIS-IFD--IQENIGHCSpeihNHFPKQH 359
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG-SVAYVPQVSwIFNatVRENILFGS----DFESERY 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 360 tcfeallsaWSTtftipkLTETRLAAISSILEEFELKDIKDKPLsSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTk 439
Cdd:PLN03232 711 ---------WRA------IDVTALQHDLDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA- 773
|
250
....*....|
gi 19115286 440 yvHMAHNYLN 449
Cdd:PLN03232 774 --HVAHQVFD 781
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
265-345 |
7.76e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.32 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 265 ISMEHLNCVYWGRK--VLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-----DHPKlfaSNIKFFGKSIGPGTgisI 337
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPN---SKITVDGITLTAKT---V 79
|
....*...
gi 19115286 338 FDIQENIG 345
Cdd:PRK13640 80 WDIREKVG 87
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
257-307 |
8.05e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 42.12 E-value: 8.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 19115286 257 PITIGKPLISMEHLNCVYWGR--KVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-227 |
1.08e-03 |
|
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: 40.47 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 22 NVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTsfsypflkgksdspwqaIQLLDFKSSG-QQRAAYYSER--- 97
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGT-----------------IRVNGQDVSDlRGRAIPYLRRkig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 98 --YHSFRDKEHDTTLEKWLLgAYRGNE---KFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLL 172
Cdd:cd03292 82 vvFQDFRLLPDRNVYENVAF-ALEVTGvppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 173 DEPYAGLDV-TSRSVLSSLlgEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKI 227
Cdd:cd03292 161 DEPTGNLDPdTTWEIMNLL--KKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-50 |
1.13e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.79 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|
gi 19115286 21 KNVSFELARKQNWAIIGNTGSGRTTFLRCI 50
Cdd:COG1117 28 KDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-180 |
1.23e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.24 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 18 PLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS---------PSTSFSYPFLKgksdspwQAIQLLdfkssgQ 88
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTegeirldgrPLSSLSHSVLR-------QGVAMV------Q 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 89 QRAAYYSEryhSFRDkehDTTLekwllgayrGNEkFASQHVQEAASMTQLSHL---LPSSLI--------NLSNGQSRRA 157
Cdd:PRK10790 422 QDPVVLAD---TFLA---NVTL---------GRD-ISEEQVWQALETVQLAELarsLPDGLYtplgeqgnNLSVGQKQLL 485
|
170 180
....*....|....*....|...
gi 19115286 158 MLASKLVQRPQLLLLDEPYAGLD 180
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANID 508
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-57 |
1.25e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.49 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19115286 5 VKFANTTF-LDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPS 57
Cdd:PRK13657 335 VEFDDVSFsYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ 388
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
277-307 |
1.69e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.39 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|.
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLL 50
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
277-437 |
1.82e-03 |
|
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: 39.53 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLL---------AYVVGDhpklfasnIKFFGKSIGPgtgisifDIQENIGHC 347
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagrktaGVITGE--------ILINGRPLDK-------NFQRSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 348 sPEIHNHFPKQhTCFEALL-SAWsttftipkltetrLAAISsileefelkdIKDKPLSSISVGMqrfilfcraiVKQPRL 426
Cdd:cd03232 85 -EQQDVHSPNL-TVREALRfSAL-------------LRGLS----------VEQRKRLTIGVEL----------AAKPSI 129
|
170
....*....|.
gi 19115286 427 VVLDEPFQGVD 437
Cdd:cd03232 130 LFLDEPTSGLD 140
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
148-183 |
1.82e-03 |
|
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: 40.69 E-value: 1.82e-03
10 20 30
....*....|....*....|....*....|....*.
gi 19115286 148 NLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTS 183
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
264-312 |
1.98e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 39.97 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19115286 264 LISMEHLNCVYW-GRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG 312
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNG 50
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
384-484 |
2.11e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 384 AAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH 463
Cdd:NF000106 123 ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
90 100
....*....|....*....|.
gi 19115286 464 YEDELPACVNRRAHIDNGKLV 484
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVI 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
149-180 |
2.22e-03 |
|
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: 39.15 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|..
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLD 180
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
2.29e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 39.97 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 5 VKFANTTF--LDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPspstsfsypfLKGKsdspwqaIQLLD 82
Cdd:PRK13632 8 IKVENVSFsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP----------QSGE-------IKIDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 83 FKSSgqqraayySERYHSFRDK-----------------EHDTT--LEkwllgayrgNEKFASQHVQ----EAASMTQLS 139
Cdd:PRK13632 71 ITIS--------KENLKEIRKKigiifqnpdnqfigatvEDDIAfgLE---------NKKVPPKKMKdiidDLAKKVGME 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 140 HLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSsllgemsnhcspKIVLSLRPQ-DKIPDFITH 218
Cdd:PRK13632 134 DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIK------------KIMVDLRKTrKKTLISITH 201
|
250 260
....*....|....*....|....*..
gi 19115286 219 ----------VLELKNKKITYQG-PKE 234
Cdd:PRK13632 202 dmdeailadkVIVFSEGKLIAQGkPKE 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-188 |
2.36e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 35 IIGNTGSGRTTFLRCIQGSFTPSpstsfsypflKGKSDSpwqaiqllDFKSSgqqraayYSERYHSfrdKEHDTTLEKWL 114
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPD----------EGEVDP--------ELKIS-------YKPQYIK---PDYDGTVEDLL 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 115 LGAyrgNEKFASQHVQ-EAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLS 188
Cdd:PRK13409 422 RSI---TDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
277-470 |
2.72e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 277 RKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVG-DHPKlfASNIKFfgksigpgTGISIFDIQENigHCSPEIHNHF 355
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGiMQPS--SGNIYY--------KNCNINNIAKP--YCTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 356 PKQHTCFEALLSAWSTTFTIpklTETRLAAISSileeFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQG 435
Cdd:PRK13541 81 LKLEMTVFENLKFWSEIYNS---AETLYAAIHY----FKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190
....*....|....*....|....*....|....*
gi 19115286 436 VDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPA 470
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKS 188
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
140-235 |
3.33e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.47 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115286 140 HLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVL---SLrpqDKIPDFI 216
Cdd:PRK11144 120 PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYvshSL---DEILRLA 196
|
90
....*....|....*....
gi 19115286 217 THVLELKNKKITYQGPKEQ 235
Cdd:PRK11144 197 DRVVVLEQGKVKAFGPLEE 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
149-222 |
4.18e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 38.90 E-value: 4.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEmsnhcspkivlsLRPQDKIPD-FITHVLEL 222
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKK------------LQQQFGTAClFITHDLRL 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
271-313 |
4.28e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.89 E-value: 4.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 19115286 271 NCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGD 313
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGE 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
267-329 |
4.32e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 4.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115286 267 MEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKlFASNIKFFGKSI 329
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQK-DSGSILFQGKEI 62
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
265-307 |
4.39e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 39.29 E-value: 4.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 19115286 265 ISMEHLNCVYWGRK----VLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLI 48
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
137-191 |
4.48e-03 |
|
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: 39.38 E-value: 4.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 19115286 137 QLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLL 191
Cdd:COG1245 444 GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
149-191 |
5.50e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.26 E-value: 5.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 19115286 149 LSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLL 191
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI 446
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
150-191 |
6.30e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 6.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 19115286 150 SNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLL 191
Cdd:PRK10636 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
278-307 |
6.66e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.53 E-value: 6.66e-03
10 20 30
....*....|....*....|....*....|
gi 19115286 278 KVLSDINWTIREGERWALTGSNGSGKTTLL 307
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTI 65
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
276-308 |
6.92e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.12 E-value: 6.92e-03
10 20 30
....*....|....*....|....*....|...
gi 19115286 276 GRKVLSDINWTIREGERWALTGSNGSGKTTLLA 308
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
401-463 |
7.20e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 7.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115286 401 KPLSSISVG-MQRFILFCR--AIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISH 463
Cdd:PRK00635 805 RPLSSLSGGeIQRLKLAYEllAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
148-183 |
7.83e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 7.83e-03
10 20 30
....*....|....*....|....*....|....*.
gi 19115286 148 NLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTS 183
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
150-185 |
9.38e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.18 E-value: 9.38e-03
10 20 30
....*....|....*....|....*....|....*.
gi 19115286 150 SNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRS 185
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
|
| |
