|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
34-512 |
9.59e-117 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 354.37 E-value: 9.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRP--ERVGYLPQHLVLQSDRTVADVL--GIEAVLAALATIDAGQGQPADFE 109
Cdd:COG0488 28 GLVGRNGAGKSTLLKILAGELEPDSGEVSIPkgLRIGYLPQEPPLDDDLTVLDTVldGDAELRALEAELEELEAKLAEPD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 110 VVGDQ-------------WDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGA 176
Cdd:COG0488 108 EDLERlaelqeefealggWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 177 RARLYAALTSWRGQAIVVSHDRDLLD-LVQHMAEMRAGGITFFGGNFTAFtdalaVEQEAAARgvRAAESDLKRQQRELA 255
Cdd:COG0488 188 IEWLEEFLKNYPGTVLVVSHDRYFLDrVATRILELDRGKLTLYPGNYSAY-----LEQRAERL--EQEAAAYAKQQKKIA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 256 EArikldrrQRFARSQAGNVPKivagAKKGTAEVSA-GKLRgghqadvadarrrleeAEERVRDDDSIEVDLsRTSVPPG 334
Cdd:COG0488 261 KE-------EEFIRRFRAKARK----AKQAQSRIKAlEKLE----------------REEPPRRDKTVEIRF-PPPERLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 335 RDIVVTENL--------VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV----SLRVPYRLLPQRL 402
Cdd:COG0488 313 KKVLELEGLsksygdktLLDD---LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgeTVKIGYFDQHQEE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 403 QllDDRDSVLAAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSepPPQLLILDEPTNNLDL 482
Cdd:COG0488 390 L--DPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLS--PPNVLLLDEPTNHLDI 465
|
490 500 510
....*....|....*....|....*....|
gi 1863768389 483 DSIRQLTQALTQYRGALLVASHDDAFLSEL 512
Cdd:COG0488 466 ETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-512 |
7.66e-52 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 184.71 E-value: 7.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRP--ERVGYLPQHLVLQSDRTVADV--LGIEAVLAALATIDAGQGQP---- 105
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnERLGKLRQDQFAFEEFTVLDTviMGHTELWEVKQERDRIYALPemse 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 106 ------ADFEVVGDQWDlpdrSIAMLARFGFADLDLRRPI----GTLSggEV-------ILLALAaqFLSEPDLLLLDEP 168
Cdd:PRK15064 111 edgmkvADLEVKFAEMD----GYTAEARAGELLLGVGIPEeqhyGLMS--EVapgwklrVLLAQA--LFSNPDILLLDEP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 169 TNNLDSGARARLYAALTSWRGQAIVVSHDRDLLDLV-QHMAEMRAGGITFFGGNFTAFTDALAVEQEaaargvraaesdl 247
Cdd:PRK15064 183 TNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVcTHMADLDYGELRVYPGNYDEYMTAATQARE------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 248 kRQQRELAEARIKLDRRQRFARSQAGNVPKivagAKKGTAEvsAGKLrgghqadvadarrrleeaeervrddDSIEVDLS 327
Cdd:PRK15064 250 -RLLADNAKKKAQIAELQSFVSRFSANASK----AKQATSR--AKQI-------------------------DKIKLEEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 328 RTS--VPP----------GRDIVVTENL-------VLRNGavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGT 388
Cdd:PRK15064 298 KPSsrQNPfirfeqdkklHRNALEVENLtkgfdngPLFKN--LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 389 V----SLRVPYRLLPQRLQLLDDRdSVLAAVSRLAPTADDNQ-LRAELARFLLDADTIARPVGTLSGGERFRATLAALLL 463
Cdd:PRK15064 376 VkwseNANIGYYAQDHAYDFENDL-TLFDWMSQWRQEGDDEQaVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1863768389 464 SEPppQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFLSEL 512
Cdd:PRK15064 455 QKP--NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSL 501
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-509 |
3.13e-51 |
|
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: 183.60 E-value: 3.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAG-------ELMPTRGSvsrpeRVGYLPQHLVLQSDRTV-----ADVLGIEAVLAAL 95
Cdd:TIGR03719 29 FPGAKIGVLGLNGAGKSTLLRIMAGvdkdfngEARPQPGI-----KVGYLPQEPQLDPTKTVrenveEGVAEIKDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 ATIDAGQGQP-ADFEVV-------------GDQWDLPDR-SIAMLArfgfadldLRRP-----IGTLSGGEVILLALAAQ 155
Cdd:TIGR03719 104 NEISAKYAEPdADFDKLaaeqaelqeiidaADAWDLDSQlEIAMDA--------LRCPpwdadVTKLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 156 FLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQAIVVSHDRDLLDLV-QHMAEM-RAGGITfFGGNFTAFTDALA--V 231
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVaGWILELdRGRGIP-WEGNYSSWLEQKQkrL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 232 EQEAaargvRAAESDLKRQQRELAEARIKLDRRQ--------RFARSQAGNVPKivagaKKGTAE--VSAGKLRGGHQAD 301
Cdd:TIGR03719 255 EQEE-----KEESARQKTLKRELEWVRQSPKGRQakskarlaRYEELLSQEFQK-----RNETAEiyIPPGPRLGDKVIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 302 VADARRRLeeaeervrDDDSIEVDLSrTSVPPgrdivvtenlvlrnGAVvslhirgperVGLVGPNGSGKTTLIDTIRGE 381
Cdd:TIGR03719 325 AENLTKAF--------GDKLLIDDLS-FKLPP--------------GGI----------VGVIGPNGAGKSTLFRMITGQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 382 IEPRSGTVSL----RVPYrlLPQRLQLLDDRDSVLAAVS----------RLAPTaddnqlRAELARFLLDADTIARPVGT 447
Cdd:TIGR03719 372 EQPDSGTIEIgetvKLAY--VDQSRDALDPNKTVWEEISggldiiklgkREIPS------RAYVGRFNFKGSDQQKKVGQ 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 448 LSGGERFRATLAALLLSepPPQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFL 509
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKS--GGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFL 503
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-505 |
8.20e-49 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 178.44 E-value: 8.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRP---------ERVGYLPQ---HLVLQSDRtvaDVLGIEAVLAALA 96
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvnQETPALPQpalEYVIDGDR---EYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 97 TIDAGQgqpADFEVVG-----DQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNN 171
Cdd:PRK10636 103 ERNDGH---AIATIHGkldaiDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 172 LDSGARARLYAALTSWRGQAIVVSHDRDLLD-LVQHMAEMRAGGITFFGGNFTAFtdalavEQEAAARgVRAAESDLKRQ 250
Cdd:PRK10636 180 LDLDAVIWLEKWLKSYQGTLILISHDRDFLDpIVDKIIHIEQQSLFEYTGNYSSF------EVQRATR-LAQQQAMYESQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 251 QRELAEARIKLDRRQrfarsqagnvpkivagAKKGTAEVSAGKLRGGHQADVADARRRLEEAEERVRDDDSIEVDLSRTS 330
Cdd:PRK10636 253 QERVAHLQSYIDRFR----------------AKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 331 -VPPGRDivvtENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL----RVPYRLLPQRLQLL 405
Cdd:PRK10636 317 kVSAGYG----DRIILDS---IKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgiKLGYFAQHQLEFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 406 DDrDSVLAAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSI 485
Cdd:PRK10636 390 AD-ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRP--NLLLLDEPTNHLDLDMR 466
|
490 500
....*....|....*....|
gi 1863768389 486 RQLTQALTQYRGALLVASHD 505
Cdd:PRK10636 467 QALTEALIDFEGALVVVSHD 486
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-509 |
1.04e-44 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 165.68 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAG-------ELMPTRGSvsrpeRVGYLPQHLVLQSDRTVADVL--GIEAVLAALA-- 96
Cdd:PRK11819 31 FPGAKIGVLGLNGAGKSTLLRIMAGvdkefegEARPAPGI-----KVGYLPQEPQLDPEKTVRENVeeGVAEVKAALDrf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 97 -TIDAGQGQP-ADFEVV-------------GDQWDLpDR--SIAMLArfgfadldLRRP-----IGTLSGGEVILLALAA 154
Cdd:PRK11819 106 nEIYAAYAEPdADFDALaaeqgelqeiidaADAWDL-DSqlEIAMDA--------LRCPpwdakVTKLSGGERRRVALCR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 155 QFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQAIVVSHDRDLLDLV-QHMAEM-RAGGITfFGGNFTAFTDA---- 228
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVaGWILELdRGRGIP-WEGNYSSWLEQkakr 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 229 LAVEQ-EAAARgvraaesdLKRQQRELAEARIKLDRRQ-----RFAR-----SQAGNvpkivagAKKGTAE--VSAGKlR 295
Cdd:PRK11819 256 LAQEEkQEAAR--------QKALKRELEWVRQSPKARQakskaRLARyeellSEEYQ-------KRNETNEifIPPGP-R 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 296 GGHQAdvadarrrleeaeervrdddsIEVD-LSRTSvppgRDIVVTENL---VLRNGavvslhIrgperVGLVGPNGSGK 371
Cdd:PRK11819 320 LGDKV---------------------IEAEnLSKSF----GDRLLIDDLsfsLPPGG------I-----VGIIGPNGAGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 372 TTLIDTIRGEIEPRSGTVSL----RVPYrlLPQRLQLLDDRDSVLAAVS----------RLAPTaddnqlRAELARFLLD 437
Cdd:PRK11819 364 STLFKMITGQEQPDSGTIKIgetvKLAY--VDQSRDALDPNKTVWEEISggldiikvgnREIPS------RAYVGRFNFK 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 438 ADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFL 509
Cdd:PRK11819 436 GGDQQKKVGVLSGGERNRLHLAKTLKQG--GNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFL 505
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
34-225 |
2.00e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 161.39 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRPE--RVGYLPQHL-VLQSDRTVADVLGieavlaalatidagQGQPADFEV 110
Cdd:COG0488 345 GLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQHQeELDPDKTVLDELR--------------DGAPGGTEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 111 vgdqwdlpdRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ 190
Cdd:COG0488 411 ---------EVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGT 481
|
170 180 190
....*....|....*....|....*....|....*.
gi 1863768389 191 AIVVSHDRDLLD-LVQHMAEMRAGGITFFGGNFTAF 225
Cdd:COG0488 482 VLLVSHDRYFLDrVATRILEFEDGGVREYPGGYDDY 517
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-508 |
1.58e-41 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 157.80 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGS--------VSR----PER-----------------VGYLPQ-----HLVLQ--S 78
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdliVARlqqdPPRnvegtvydfvaegieeqAEYLKRyhdisHLVETdpS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 79 DRTVADVLGIEAVLAALatidagqgqpadfevvgDQWDLPDRSIAMLARFGfadLDLRRPIGTLSGGEVILLALAAQFLS 158
Cdd:PRK11147 114 EKNLNELAKLQEQLDHH-----------------NLWQLENRINEVLAQLG---LDPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 159 EPDLLLLDEPTNNLDSGARARLYAALTSWRGQAIVVSHDRDLldlVQHMA----EMRAGGITFFGGNFTAFTD----ALA 230
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSF---IRNMAtrivDLDRGKLVSYPGNYDQYLLekeeALR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 231 VEQEAAARGVR--AAESDLKRQ----QRELAEARIKLDRRQRFARSQAGNVpkiVAGAKKGTAEVS-AGKLrgghqadva 303
Cdd:PRK11147 251 VEELQNAEFDRklAQEEVWIRQgikaRRTRNEGRVRALKALRRERSERREV---MGTAKMQVEEASrSGKI--------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 304 darrrleeaeerVRDDDSIEVDLsrtsvpPGRdivvteNLVLRNGAVVslhIRGpERVGLVGPNGSGKTTLIDTIRGEIE 383
Cdd:PRK11147 319 ------------VFEMENVNYQI------DGK------QLVKDFSAQV---QRG-DKIALIGPNGCGKTTLLKLMLGQLQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 384 PRSGTV----SLRVPYRllpqrlqllddrDSVLAAvsrLAP--TADDN------------QLR---AELARFLLDADTIA 442
Cdd:PRK11147 371 ADSGRIhcgtKLEVAYF------------DQHRAE---LDPekTVMDNlaegkqevmvngRPRhvlGYLQDFLFHPKRAM 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 443 RPVGTLSGGERFRATLAALLLSepPPQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAF 508
Cdd:PRK11147 436 TPVKALSGGERNRLLLARLFLK--PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-510 |
1.01e-37 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 147.70 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAG---ELMPTRGSVSRPER--VGYLPQHL--VLQSDRTVADVLGIEAVLAA------------ 94
Cdd:PLN03073 207 GLVGRNGTGKTTFLRYMAMhaiDGIPKNCQILHVEQevVGDDTTALqcVLNTDIERTQLLEEEAQLVAqqrelefetetg 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 ---LATIDAGQGQPAD--FEVVGDQWDLPD------RSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLL 163
Cdd:PLN03073 287 kgkGANKDGVDKDAVSqrLEEIYKRLELIDaytaeaRAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 164 LLDEPTNNLDSGARARLYAALTSWRGQAIVVSHDRDLLD-LVQHMAEMRAGGITFFGGNFTAFTdalaveqeaaargvRA 242
Cdd:PLN03073 367 LLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNtVVTDILHLHGQKLVTYKGDYDTFE--------------RT 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 243 AESDLKRQQRELAEARIKLDRRQRFarsqagnVPKIVAGAKKGTAEVSAGKL--RGGHQADVadarrrleeaeerVRDDD 320
Cdd:PLN03073 433 REEQLKNQQKAFESNERSRSHMQAF-------IDKFRYNAKRASLVQSRIKAldRLGHVDAV-------------VNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 321 sIEVDLSRTSVPPGRDIVVTEN---------LVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL 391
Cdd:PLN03073 493 -YKFEFPTPDDRPGPPIISFSDasfgypggpLLFKN---LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 392 RVPYRLLPQRLQLLDDRD---SVLAAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPpp 468
Cdd:PLN03073 569 SAKVRMAVFSQHHVDGLDlssNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKP-- 646
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1863768389 469 QLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFLS 510
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
351-509 |
1.33e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.65 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVS----LRVPYRLLPQRLQLLDD-RDSVLAAVSRLA------ 419
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSipkgLRIGYLPQEPPLDDDLTvLDTVLDGDAELRaleael 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 ---------PTADDNQL-----------------RAE--LARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLL 471
Cdd:COG0488 97 eeleaklaePDEDLERLaelqeefealggweaeaRAEeiLSGLGFPEEDLDRPVSELSGGWRRRVALARALLSE--PDLL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 472 ILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFL 509
Cdd:COG0488 175 LLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFL 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-208 |
1.77e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 1 MPSSVVCSDLWFAWpSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------RPERVGYLP 71
Cdd:COG1121 3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkpprrARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 72 QHlvLQSDR----TVADV--LGIEAVLAALATIDAgqgqpADFEVVgdqwdlpdrsIAMLARFGFADLdLRRPIGTLSGG 145
Cdd:COG1121 82 QR--AEVDWdfpiTVRDVvlMGRYGRRGLFRRPSR-----ADREAV----------DEALERVGLEDL-ADRPIGELSGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 146 EV--ILLALAaqFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDrdlLDLVQHMA 208
Cdd:COG1121 144 QQqrVLLARA--LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGktiLVVTHD---LGAVREYF 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-512 |
3.57e-33 |
|
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: 123.33 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVS----LRVPYrllpqrlqllddrdsvlaavs 416
Cdd:cd03221 12 GKLLLKD---ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTwgstVKIGY--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 rlaptaddnqlraelarflldadtiarpVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYR 496
Cdd:cd03221 68 ----------------------------FEQLSGGEKMRLALAKLLLENP--NLLLLDEPTNHLDLESIEALEEALKEYP 117
|
170
....*....|....*.
gi 1863768389 497 GALLVASHDDAFLSEL 512
Cdd:cd03221 118 GTVILVSHDRYFLDQV 133
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-505 |
1.05e-31 |
|
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: 128.10 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 1 MPSSVVCSDLWFAWPSGEL-AIAGLTCA-FPDQVTGLVGRNGVGKSTLLKIIAGeLMPTRGSVS---------------- 62
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVpAVDGVSLTiAPGETVALVGESGSGKSTLALALMG-LLPHGGRISgevlldgrdllelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 63 -RPERVGYLPQHLVLQSDR-TVADVLgIEAVLAALATIDAGQgqpadfevvgdqwdlpDRSIAMLARFGFADLdLRRPIG 140
Cdd:COG1123 80 lRGRRIGMVFQDPMTQLNPvTVGDQI-AEALENLGLSRAEAR----------------ARVLELLEAVGLERR-LDRYPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 141 TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAA---LTSWRGQAIV-VSHD-RDLLDLVQHMAEMRAGGI 215
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLlreLQRERGTTVLlITHDlGVVAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 216 tffggnftaftdalaVEQEAAArgvraaesDLKRQQRELAeARIKLDRRQRFARSQAGNVPKIVAgakkgtaevsagklr 295
Cdd:COG1123 222 ---------------VEDGPPE--------EILAAPQALA-AVPRLGAARGRAAPAAAAAEPLLE--------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 296 gghqadvadarrrleeaeerVRDddsievdLSRTSVPPGRDIVVtenlVLRNgavVSLHIRGPERVGLVGPNGSGKTTLI 375
Cdd:COG1123 263 --------------------VRN-------LSKRYPVRGKGGVR----AVDD---VSLTLRRGETLGLVGESGSGKSTLA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 376 DTIRGEIEPRSGTVSLR-VPYRLLPQRLQLL----------------DDRDSVLAAVS---RLAPTADDNQLRAELARFL 435
Cdd:COG1123 309 RLLLGLLRPTSGSILFDgKDLTKLSRRSLRElrrrvqmvfqdpysslNPRMTVGDIIAeplRLHGLLSRAERRERVAELL 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 436 ----LDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD-------LDSIRQLTQaltQYRGALLVASH 504
Cdd:COG1123 389 ervgLPPDLADRYPHELSGGQRQRVAIARALALE--PKLLILDEPTSALDvsvqaqiLNLLRDLQR---ELGLTYLFISH 463
|
.
gi 1863768389 505 D 505
Cdd:COG1123 464 D 464
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
34-204 |
1.09e-31 |
|
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: 119.09 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRPE--RVGYLPQhlvlqsdrtvadvlgieavlaalatidagqgqpadfevv 111
Cdd:cd03221 30 GLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ--------------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 112 gdqwdlpdrsiamlarfgfadldlrrpigtLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA 191
Cdd:cd03221 71 ------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTV 120
|
170
....*....|...
gi 1863768389 192 IVVSHDRDLLDLV 204
Cdd:cd03221 121 ILVSHDRYFLDQV 133
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-201 |
4.18e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.95 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 7 CSDLWFAWpSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSR--------PERVGYLPQHLVLQ 77
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPgEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekeRKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 78 SDR--TVADVLGieavLAALATIDAGQGQPAdfevvgDQWDLPDRSIAMLARFGFADldlrRPIGTLSGGEV--ILLALA 153
Cdd:cd03235 81 RDFpiSVRDVVL----MGLYGHKGLFRRLSK------ADKAKVDEALERVGLSELAD----RQIGELSGGQQqrVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 154 aqFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ---AIVVSHDRDLL 201
Cdd:cd03235 147 --LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgmtILVVTHDLGLV 195
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
31-219 |
5.11e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.47 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPE---RVGYLPQHLVLQSDRTVADVLgieAVLAALATI 98
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardPAEvrrRIGYVPQEPALYPDLTVRENL---RFFARLYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 DAGQgqpadfevvgdqwdLPDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:COG1131 104 PRKE--------------ARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 179 RLYAALTSWRGQA---IVVSHdrdLLDLVQHMAE----MRAGGITFFG 219
Cdd:COG1131 169 ELWELLRELAAEGktvLLSTH---YLEEAERLCDrvaiIDKGRIVADG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-219 |
2.70e-28 |
|
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: 113.21 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 21 IAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE---RVGYLPQHLVLQSDRTVADV- 85
Cdd:COG1120 17 LDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaslSRRElarRIAYVPQEPPAPFGLTVRELv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 -LGIEAVLAALatidaGQGQPADFEVVgdqwdlpDRSIAMLARFGFADldlrRPIGTLSGGE---ViLLALA-AQflsEP 160
Cdd:COG1120 97 aLGRYPHLGLF-----GRPSAEDREAV-------EEALERTGLEHLAD----RPVDELSGGErqrV-LIARAlAQ---EP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 161 DLLLLDEPTNNLDSGARARLY---AALTSWRGQAIV-VSHDrdlLDLV----QHMAEMRAGGITFFG 219
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLellRRLARERGRTVVmVLHD---LNLAaryaDRLVLLKDGRIVAQG 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-170 |
9.77e-28 |
|
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: 108.50 E-value: 9.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQHLVLQSDRTVADVLGIEAVLAAL 95
Cdd:pfam00005 10 PGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderkSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLKGL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 96 ATIDAGqgqpadfevvgdqwdlpDRSIAMLARFGFADLD---LRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTN 170
Cdd:pfam00005 90 SKREKD-----------------ARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-233 |
1.51e-27 |
|
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: 110.50 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE---RVGYL 70
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkkNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 71 PQH----LVlqsDRTVA-DV-LGIEAvlaalatidagQGQPADfEVVgdqwdlpDRSIAMLARFGFADLdLRRPIGTLSG 144
Cdd:COG1122 81 FQNpddqLF---APTVEeDVaFGPEN-----------LGLPRE-EIR-------ERVEEALELVGLEHL-ADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 145 GEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLL-DLVQHMAEMRAGGITFFGG 220
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGktvIIVTHDLDLVaELADRVIVLDDGRIVADGT 217
|
250
....*....|...
gi 1863768389 221 NFTAFTDALAVEQ 233
Cdd:COG1122 218 PREVFSDYELLEE 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
34-215 |
4.62e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE---RVGYLPQHLVLQSDrTVADVLgieavlaalatida 100
Cdd:COG4619 30 AITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsamPPPEwrrQVAYVPQEPALWGG-TVRDNL-------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 101 gqgqPADFEVVGDQWDlPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARL 180
Cdd:COG4619 95 ----PFPFQLRERKFD-RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1863768389 181 YAALTSWRGQA----IVVSHDRDLLDLV-QHMAEMRAGGI 215
Cdd:COG4619 170 EELLREYLAEEgravLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-206 |
5.71e-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: 107.95 E-value: 5.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 17 GELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSR------------PERVGYLPQHLVLQSDRTVA 83
Cdd:COG4133 14 ERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdaredyRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 84 DVLgieAVLAALATIDAGQGQPADfevvgdqwdlpdrsiaMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLL 163
Cdd:COG4133 94 ENL---RFWAALYGLRADREAIDE----------------ALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1863768389 164 LLDEPTNNLDSGARARLYAALTSWRGQ---AIVVSHDRDLLDLVQH 206
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARggaVLLTTHQPLELAAARV 199
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
341-505 |
5.59e-26 |
|
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: 104.44 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaVSRLAP 420
Cdd:cd03214 11 GRTVLDD---LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL--------------DGKD-----LASLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 taddnqlrAELARFL---------LDADTIA-RPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLD-------LD 483
Cdd:cd03214 69 --------KELARKIayvpqalelLGLAHLAdRPFNELSGGERQRVLLARALAQEPP--ILLLDEPTSHLDiahqielLE 138
|
170 180
....*....|....*....|..
gi 1863768389 484 SIRQLTQaltQYRGALLVASHD 505
Cdd:cd03214 139 LLRRLAR---ERGKTVVMVLHD 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
341-524 |
1.52e-25 |
|
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: 104.10 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLD-----DRDSV---- 411
Cdd:COG4133 14 ERLLFSG---LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlaylgHADGLkpel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 -----LAAVSRLAPT-ADDNQLRAELARFLLdADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSI 485
Cdd:COG4133 91 tvrenLRFWAALYGLrADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAP--LWLLDEPFTALDAAGV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1863768389 486 RQLTQALTQYR---GALLVASHDDaflSELGLTYRIDLGAVA 524
Cdd:COG4133 168 ALLAELIAAHLargGAVLLTTHQP---LELAAARVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-512 |
9.51e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.86 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 335 RDIVVT--ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRL------QLLD 406
Cdd:COG1121 10 ENLTVSygGRPVLED---VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvpqRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 407 DRD---SVLAAVS----------RLAPTADDNQLRAELARflLDADTIA-RPVGTLSGGERFRATLAALLLSEppPQLLI 472
Cdd:COG1121 87 DWDfpiTVRDVVLmgrygrrglfRRPSRADREAVDEALER--VGLEDLAdRPIGELSGGQQQRVLLARALAQD--PDLLL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 473 LDEPTNNLDLDSIRQLTQALTQYRG---ALLVASHDDAFLSEL 512
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREY 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
26-209 |
1.67e-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: 102.24 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 26 CAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------RP----ERVGYLPQHLVLQSDRTVADVLgieavla 93
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkEPrearRQIGVLPDERGLYDRLTVRENI------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 94 alatidagqgqpadfEVVGDQWDLPDRSIA-----MLARFGFaDLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEP 168
Cdd:COG4555 96 ---------------RYFAELYGLFDEELKkrieeLIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1863768389 169 TNNLDSGARARLYAALTSWRGQ--AIVVS-HDrdlLDLVQHMAE 209
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEgkTVLFSsHI---MQEVEALCD 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-201 |
1.90e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 20 AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRP--ERVGYLPQHLVLqSDR---TVADV--LGIEAV 91
Cdd:NF040873 7 VLHGVDLTIPAgSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggARVAYVPQRSEV-PDSlplTVRDLvaMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 92 LAALATIDAgqgqpADFEVVGDqwdlpdrsiaMLARFGFADLDlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNN 171
Cdd:NF040873 86 RGLWRRLTR-----DDRAAVDD----------ALERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 172 LDSGARARLYAALTSWRGQA---IVVSHDRDLL 201
Cdd:NF040873 150 LDAESRERIIALLAEEHARGatvVVVTHDLELV 182
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-213 |
4.45e-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: 100.23 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 6 VCSDLWFAWPSGE-LAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYL 70
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 71 PQHlvlqSDR-----TVAD--VLGIEAvlaalatidagQGQPADfevvgdqwDLPDRSIAMLARFGFADLdLRRPIGTLS 143
Cdd:cd03225 81 FQN----PDDqffgpTVEEevAFGLEN-----------LGLPEE--------EIEERVEEALELVGLEGL-RDRSPFTLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 144 GGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ---AIVVSHDRDLL-DLVQHMAEMRAG 213
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-219 |
2.07e-23 |
|
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: 98.35 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 19 LAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV------------SRPERVGYLPQHLVLQSDRTVADV 85
Cdd:cd03263 16 PAVDDLSLNVyKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrkAARQSLGYCPQFDALFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIEAVLAALATIDAGQGQPADFEVVG--DQWDlpdrsiamlarfgfadldlrRPIGTLSGGEVILLALAAQFLSEPDLL 163
Cdd:cd03263 96 LRFYARLKGLPKSEIKEEVELLLRVLGltDKAN--------------------KRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 164 LLDEPTNNLDSGARARLYAALTSWRGQAIVV--SHDRDLLD-LVQHMAEMRAGGITFFG 219
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIIltTHSMDEAEaLCDRIAIMSDGKLRCIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
340-512 |
3.38e-23 |
|
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: 97.54 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVLAAVSR-- 417
Cdd:cd03225 12 GARPALDD---ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-----------DGKDLTKLSLKELRRkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 418 -----------LAPTADD----------------NQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqL 470
Cdd:cd03225 78 glvfqnpddqfFGPTVEEevafglenlglpeeeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD--I 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1863768389 471 LILDEPTNNLDLDSIRQLTQALTQYRGA---LLVASHDDAFLSEL 512
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLEL 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-214 |
3.88e-23 |
|
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: 97.33 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGELAIAGLT-CAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS----------RPERVGYLPQHLVLQ 77
Cdd:cd03226 4 NISFSYKKGTEILDDLSlDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpikakeRRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 78 --SDrTVADVLGIEAVLAALATIDAGQgqpadfevvgdqwdlpdrsiaMLARFGFADLDLRRPIgTLSGGEVILLALAAQ 155
Cdd:cd03226 84 lfTD-SVREELLLGLKELDAGNEQAET---------------------VLKDLDLYALKERHPL-SLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 156 FLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLLDLVQHMAEMRAGG 214
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGkavIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-219 |
5.04e-23 |
|
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: 96.88 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 20 AIAGLTCAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------SRPE----RVGYLPQHLVLQSDRTVADVLg 87
Cdd:cd03264 15 ALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlKQPQklrrRIGYLPQEFGVYPNFTVREFL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 88 ieAVLAALATIDAGQgqpadfevvgdqwdLPDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDE 167
Cdd:cd03264 94 --DYIAWLKGIPSKE--------------VKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 168 PTNNLDSGARARLYAALTSWRGQAIVV--SHD-RDLLDLVQHMAEMRAGGITFFG 219
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVIlsTHIvEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
31-215 |
5.74e-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: 95.54 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSR------------PERVGYLPQHLVLQSDRTVADVLgieavlaalati 98
Cdd:cd03230 27 EIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepeevKRRIGYLPEEPSLYENLTVRENL------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 dagqgqpadfevvgdqwdlpdrsiamlarfgfadldlrrpigTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:cd03230 95 ------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1863768389 179 RLYAALTSWRGQA---IVVSHD-RDLLDLVQHMAEMRAGGI 215
Cdd:cd03230 133 EFWELLRELKKEGktiLLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-225 |
7.37e-23 |
|
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: 101.94 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 19 LAIAGLTCAFP-DQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERV--GYLPQ-HLVLQSDRTVadvlgIEAVLAA 94
Cdd:TIGR03719 336 LLIDDLSFKLPpGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQsRDALDPNKTV-----WEEISGG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LATIDAGqgqpaDFEVvgdqwdlPDRsiAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDS 174
Cdd:TIGR03719 411 LDIIKLG-----KREI-------PSR--AYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 175 GARARLYAALTSWRGQAIVVSHDRDLLDLV-QH-MAEMRAGGITFFGGNFTAF 225
Cdd:TIGR03719 477 ETLRALEEALLNFAGCAVVISHDRWFLDRIaTHiLAFEGDSHVEWFEGNFSEY 529
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-512 |
1.21e-22 |
|
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: 94.77 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVLAAVSRLAPT 421
Cdd:cd03230 13 KTALDD---ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------LGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 422 ADDNQLRAEL-ARFLLDadtiarpvgtLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQYR---G 497
Cdd:cd03230 79 PEEPSLYENLtVRENLK----------LSGGMKQRLALAQALLHDPE--LLILDEPTSGLDPESRREFWELLRELKkegK 146
|
170
....*....|....*
gi 1863768389 498 ALLVASHDDAFLSEL 512
Cdd:cd03230 147 TILLSSHILEEAERL 161
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
341-505 |
1.62e-22 |
|
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: 96.47 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL------RVPYRLLPQRLQLLD-----DRD 409
Cdd:COG4555 13 KVPALKD---VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrKEPREARRQIGVLPDerglyDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 SV---LAAVSRLAPTADD-NQLRAE-LARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDS 484
Cdd:COG4555 90 TVrenIRYFAELYGLFDEeLKKRIEeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK--VLLLDEPTNGLDVMA 167
|
170 180
....*....|....*....|....
gi 1863768389 485 IRQLTQALTQYRG---ALLVASHD 505
Cdd:COG4555 168 RRLLREILRALKKegkTVLFSSHI 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
344-505 |
1.72e-22 |
|
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: 95.68 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-------------VPYRLLPQRLQLLDDRDS 410
Cdd:cd03235 14 VLED---VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekerkrigyVPQRRSIDRDFPISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VL-AAVSRLAPTADDNQLRAELARFLLD----ADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSI 485
Cdd:cd03235 91 VLmGLYGHKGLFRRLSKADKAKVDEALErvglSELADRQIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQ 168
|
170 180
....*....|....*....|...
gi 1863768389 486 RQLTQALTQYRG---ALLVASHD 505
Cdd:cd03235 169 EDIYELLRELRRegmTILVVTHD 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
341-513 |
2.10e-22 |
|
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: 93.46 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSvlaavsrlaP 420
Cdd:cd00267 11 GRTALDN---VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI--------------DGKDI---------A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 TADDNQLRAELARflldadtiarpVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQYRG--- 497
Cdd:cd00267 65 KLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEegr 131
|
170
....*....|....*.
gi 1863768389 498 ALLVASHDDAFLSELG 513
Cdd:cd00267 132 TVIIVTHDPELAELAA 147
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-219 |
3.16e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 100.22 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 2 PSSVVCSDLWFAWPSGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERV 67
Cdd:COG4988 334 PPSIELEDVSFSYPGGRPALDGLSLTIpPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 68 GYLPQHLVLQSDrTVADVLGI-------EAVLAALATIDAgqgqpADFevvgdqwdlpdrsIAMLARfgfadlDLRRPIG 140
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLgrpdasdEELEAALEAAGL-----DEF-------------VAALPD------GLDTPLG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 141 ----TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA--IVVSHDRDLLDLVQHMAEMRAGG 214
Cdd:COG4988 469 eggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRILVLDDGR 548
|
....*
gi 1863768389 215 ITFFG 219
Cdd:COG4988 549 IVEQG 553
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
344-505 |
3.26e-22 |
|
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: 95.88 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD-------------- 409
Cdd:COG1120 16 VLDD---VSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL--------------DGRDlaslsrrelarria 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ------------SVLAAVS--RLA-------PTADDNQLRAE-LARflLDADTIA-RPVGTLSGGERFRATLAALLLSEP 466
Cdd:COG1120 79 yvpqeppapfglTVRELVAlgRYPhlglfgrPSAEDREAVEEaLER--TGLEHLAdRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 467 PpqLLILDEPTNNLDLD---SIRQLTQALTQYRG-ALLVASHD 505
Cdd:COG1120 157 P--LLLLDEPTSHLDLAhqlEVLELLRRLARERGrTVVMVLHD 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-519 |
7.09e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 99.11 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPT-----------------RGS----------------VSRPERVGYLPQHLv 75
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTelqnyfkklyngeikvVHKPQYVDLIPKVF- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 76 lqsDRTVADVLgieavlaalATIDagqgqpadfevvgdqwdlpDRSIA--MLARFGFADLdLRRPIGTLSGGEVILLALA 153
Cdd:PRK13409 177 ---KGKVRELL---------KKVD-------------------ERGKLdeVVERLGLENI-LDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 154 AQFLSEPDLLLLDEPTNNLDSGAR---ARLYAALTSWRgQAIVVSHDRDLLDLVQ---HMAemraggitfFGgnftaftd 227
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQRlnvARLIRELAEGK-YVLVVEHDLAVLDYLAdnvHIA---------YG-------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 228 alaveqEAAARGVRaaesdlkrqqrelaearikldrrqrfarSQagnvPKivaGAKKGTAEVSAGKLRgghqadvadarr 307
Cdd:PRK13409 287 ------EPGAYGVV----------------------------SK----PK---GVRVGINEYLKGYLP------------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 308 rleeaEERVR-DDDSIEVDLSRTSVPPGRDIVVT-ENLVLRNGA----VVSLHIRGPERVGLVGPNGSGKTTLIDTIRGE 381
Cdd:PRK13409 314 -----EENMRiRPEPIEFEERPPRDESERETLVEyPDLTKKLGDfsleVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 382 IEPRSGTVS--LRVPYrllPQRLQLLDDRDSVLAAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLA 459
Cdd:PRK13409 389 LKPDEGEVDpeLKISY---KPQYIKPDYDGTVEDLLRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 460 ALLLSEppPQLLILDEPTNNLDLD-------SIRQLTQaltQYRGALLVASHD--------------------------- 505
Cdd:PRK13409 466 ACLSRD--ADLYLLDEPSAHLDVEqrlavakAIRRIAE---EREATALVVDHDiymidyisdrlmvfegepgkhghasgp 540
|
570 580
....*....|....*....|.
gi 1863768389 506 -------DAFLSELGLTYRID 519
Cdd:PRK13409 541 mdmregmNRFLKELGITFRRD 561
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
338-512 |
7.99e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 94.36 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 338 VVTENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPQR---------- 401
Cdd:COG1131 1 IEVRGLTKRYGDKtaldgVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgEDVARDPAEvrrrigyvpq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 402 LQLLDDRDSV---LAAVSRLAP-TADDNQLRAE--LARFLLDaDTIARPVGTLSGGERFRATLAALLLSEppPQLLILDE 475
Cdd:COG1131 81 EPALYPDLTVrenLRFFARLYGlPRKEARERIDelLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHD--PELLILDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1863768389 476 PTNNLDLDSIRQLTQALTQYRG---ALLVASHDdafLSEL 512
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAegkTVLLSTHY---LEEA 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-213 |
9.84e-22 |
|
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: 91.92 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 8 SDLWFAWPSGELAIAGLTCAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpervgylpqhlvlqsdrtvadvlg 87
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 88 ieavlaalatidagqgqpadfevvgdQWDLPDRSIAMLARfgfadldLRRPIGT---LSGGEVILLALAAQFLSEPDLLL 164
Cdd:cd00267 57 --------------------------LIDGKDIAKLPLEE-------LRRRIGYvpqLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 165 LDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLLDLV-QHMAEMRAG 213
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGrtvIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-291 |
1.02e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 99.09 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--SRPERVGYLPQHlvlQSDRTVADvlgiEAVLAALATIdagqgQPA 106
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglAKGIKLGYFAQH---QLEFLRAD----ESPLQHLARL-----APQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 107 DFEvvgdqWDLPDrsiaMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTS 186
Cdd:PRK10636 405 ELE-----QKLRD----YLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 187 WRGQAIVVSHDRDLL-DLVQHMAEMRAGGITFFGGNFTAFTDALAVEQeaaaRGVRAAESDLKRQQRELAEARIKLDRRQ 265
Cdd:PRK10636 476 FEGALVVVSHDRHLLrSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQ----KQENQTDEAPKENNANSAQARKDQKRRE 551
|
250 260
....*....|....*....|....*.
gi 1863768389 266 RFARSQAGNVPKIVAGAKKGTAEVSA 291
Cdd:PRK10636 552 AELRTQTQPLRKEIARLEKEMEKLNA 577
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-519 |
2.05e-21 |
|
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: 97.93 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPE--------------------------RVGYLPQHLVLQSDR---T 81
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkrfrgtelqdyfkklangeiKVAHKPQYVDLIPKVfkgT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 82 VADVLgiEAVlaalatidagqgqpadfevvgDQWDLPDRSIAMLarfgfaDLD--LRRPIGTLSGGEVILLALAAQFLSE 159
Cdd:COG1245 180 VRELL--EKV---------------------DERGKLDELAEKL------GLEniLDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 160 PDLLLLDEPTNNLDSGAR---ARLYAALTSWRGQAIVVSHDRDLLDLVqhmaemraggitffggnftafTDALAVEQ-EA 235
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRlnvARLIRELAEEGKYVLVVEHDLAILDYL---------------------ADYVHILYgEP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 236 AARGVRaaeSDLKrqqrelaearikldrrqrfarsqagnvpkivaGAKKGTAEVSAGKLRgghqadvadarrrleeaEER 315
Cdd:COG1245 290 GVYGVV---SKPK--------------------------------SVRVGINQYLDGYLP-----------------EEN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 316 VR-DDDSIEVDlsrtsVPPGRDIVVTENLVLRNGAVVSL----------HIRGPERVGLVGPNGSGKTTLIDTIRGEIEP 384
Cdd:COG1245 318 VRiRDEPIEFE-----VHAPRREKEEETLVEYPDLTKSYggfsleveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 385 RSGTVS--LRVPYRLLPQRLQLLDDRDSVLAAVSrlAPTADDNQLRAELAR-----FLLDadtiaRPVGTLSGGERFRAT 457
Cdd:COG1245 393 DEGEVDedLKISYKPQYISPDYDGTVEEFLRSAN--TDDFGSSYYKTEIIKplgleKLLD-----KNVKDLSGGELQRVA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 458 LAALLLSEppPQLLILDEPTNNLDLDS-------IRQLTQaltQYRGALLVASHD------------------------- 505
Cdd:COG1245 466 IAACLSRD--ADLYLLDEPSAHLDVEQrlavakaIRRFAE---NRGKTAMVVDHDiylidyisdrlmvfegepgvhghas 540
|
570 580
....*....|....*....|...
gi 1863768389 506 ---------DAFLSELGLTYRID 519
Cdd:COG1245 541 gpmdmregmNRFLKELGITFRRD 563
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
2.29e-21 |
|
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: 91.34 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGElaiagltcafpdqVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPER---VGYLP 71
Cdd:cd03214 13 TVLDDLSLSIEAGE-------------IVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaslSPKELarkIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 72 QhlvlqsdrtvadvlgieavlaalatidagqgqpadfevvgdqwdlpdrsiaMLARFGFADLdLRRPIGTLSGGEVILLA 151
Cdd:cd03214 80 Q---------------------------------------------------ALELLGLAHL-ADRPFNELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 152 LAAQFLSEPDLLLLDEPTNNLDSGARARLY---AALTSWRGQAIV-VSHDrdlLDLVQHMAE----MRAGGITFFG 219
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLellRRLARERGKTVVmVLHD---LNLAARYADrvilLKDGRIVAQG 180
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-225 |
3.08e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 97.11 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERV--GYLPQ-HLVLQSDRTVADVlgieavlaalatIDAGQgqpaDFEV 110
Cdd:PRK11819 354 GIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVklAYVDQsRDALDPNKTVWEE------------ISGGL----DIIK 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 111 VGDQwDLPDRsiAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ 190
Cdd:PRK11819 418 VGNR-EIPSR--AYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGC 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 1863768389 191 AIVVSHDRDLLD-LVQHMAEMRAGG-ITFFGGNFTAF 225
Cdd:PRK11819 495 AVVISHDRWFLDrIATHILAFEGDSqVEWFEGNFQEY 531
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-213 |
4.61e-21 |
|
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: 90.13 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGE-LAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGY 69
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIkPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 70 LPQHLVLQSDrTVADVLgieavlaalatidagqgqpadfevvgdqwdlpdrsiamlarfgfadldlrrpigtLSGGEVIL 149
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------------------------LSGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 150 LALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ--AIVVSHDRDLLDLVQHMAEMRAG 213
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
35-206 |
4.85e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.65 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPERVGYLPQHL--VLQ-----SDRTVADVLgieavlaALATi 98
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIPYLRRRIgvVFQdfrllPDRTVYENV-------ALPL- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 dagqgqpadfEVVG-DQWDLPDRSIAMLARFGFADLDLRRPIgTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR 177
Cdd:COG2884 105 ----------RVTGkSRKEIRRRVREVLDLVGLSDKAKALPH-ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS 173
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 178 ARLYAALTSW--RGQAIVV-SHDRDLLDLVQH 206
Cdd:COG2884 174 WEIMELLEEInrRGTTVLIaTHDLELVDRMPK 205
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-232 |
4.86e-21 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 96.50 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 36 VGRNGVGKSTLLKIIAGELMPTRGSVSRPE--RVGYLPQ-HLV-LQSDRTVADVLGieavlaalatidagqgqpadfevv 111
Cdd:PRK15064 351 IGENGVGKTTLLRTLVGELEPDSGTVKWSEnaNIGYYAQdHAYdFENDLTLFDWMS------------------------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 112 gdQWDLP---DRSI-AMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW 187
Cdd:PRK15064 407 --QWRQEgddEQAVrGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1863768389 188 RGQAIVVSHDRDLLD-LVQHMAEMRAGGITFFGGNFTAFTDALAVE 232
Cdd:PRK15064 485 EGTLIFVSHDREFVSsLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
341-505 |
6.08e-21 |
|
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: 91.63 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSVLAAVSRLA- 419
Cdd:COG1122 13 GTPALDD---VSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV--------------DGKDITKKNLRELRr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 --------PtadDNQL-----RAELA----RFLLDADTIA-----------------RPVGTLSGGERFRATLAALLLSE 465
Cdd:COG1122 76 kvglvfqnP---DDQLfaptvEEDVAfgpeNLGLPREEIRerveealelvglehladRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 466 PppQLLILDEPTNNLDLDSIRQLTQALTQYRGA---LLVASHD 505
Cdd:COG1122 153 P--EVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHD 193
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-213 |
1.41e-20 |
|
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: 90.24 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGEL---AIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------------R 63
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIeKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklsekelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 64 PERVGYLPQHLVLQSDRTVadvlgIEAVLAALatidagqgqpadfEVVGDQW-DLPDRSIAMLARFGFADLdLRRPIGTL 142
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTA-----LENVELPL-------------LLAGVPKkERRERAEELLERVGLGDR-LNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 143 SGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA---RLYAALTSWRGQAIV-VSHDRDLLDLVQHMAEMRAG 213
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKevmELLRELNKEAGTTIVvVTHDPELAEYADRIIELRDG 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-215 |
5.92e-20 |
|
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: 88.42 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 12 FAWPSGE-LAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-------------RPERVGYLPQHLVL 76
Cdd:cd03245 10 FSYPNQEiPALDNVSLTIrAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqldpadLRRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 77 -----QSDRTVADVLGI-EAVLAA--LATIDA-GQGQPADFEVvgdqwdlpdrsiaMLARFGFAdldlrrpigtLSGGEV 147
Cdd:cd03245 90 fygtlRDNITLGAPLADdERILRAaeLAGVTDfVNKHPNGLDL-------------QIGERGRG----------LSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 148 ILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ--AIVVSHDRDLLDLVQHMAEMRAGGI 215
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
6.06e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.56 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 1 MPSSVVCSDLWFAWPSGEL---AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-------------- 62
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGevtALRGVSLSIEAgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 63 ---RPERVGYLPQ--HLVlqSDRTVAD-VlgieavlaALATIDAGQGQPADFEvvgdqwdlpdRSIAMLARFGFADLDLR 136
Cdd:COG1136 81 arlRRRHIGFVFQffNLL--PELTALEnV--------ALPLLLAGVSRKERRE----------RARELLERVGLGDRLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 137 RPiGTLSGGE---VillALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW---RGQAIV-VSHDRDLLDLVQHMAE 209
Cdd:COG1136 141 RP-SQLSGGQqqrV---AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnreLGTTIVmVTHDPELAARADRVIR 216
|
....*..
gi 1863768389 210 MRAGGIT 216
Cdd:COG1136 217 LRDGRIV 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
351-478 |
1.70e-19 |
|
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: 85.01 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLL------------DDRDSV------- 411
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigyvfqdpqlFPRLTVrenlrlg 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 412 --LAAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTN 478
Cdd:pfam00005 84 llLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPK--LLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
340-507 |
1.77e-19 |
|
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: 85.90 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaavsrlA 419
Cdd:cd03228 13 RPKPVLKD---VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI--------------DGVD---------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 PTADDNQLRAELA----RFLLDADTIARPVgtLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQY 495
Cdd:cd03228 67 RDLDLESLRKNIAyvpqDPFLFSGTIRENI--LSGGQRQRIAIARALLRDPP--ILILDEATSALDPETEALILEALRAL 142
|
170
....*....|....
gi 1863768389 496 RG--ALLVASHDDA 507
Cdd:cd03228 143 AKgkTVIVIAHRLS 156
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
35-219 |
2.33e-19 |
|
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: 87.45 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPT-----------RGSVSRPE---RVGYLPQHLvlqSDRTVADVLGIEAVLAALatida 100
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTygndvrlfgerRGGEDVWElrkRIGLVSPAL---QLRFPRDETVLDVVLSGF----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 101 gqgqpadFEVVG--DQWDLPDRSIA--MLARFGFADLdLRRPIGTLSGGE--VILLALAaqFLSEPDLLLLDEPTNNLDS 174
Cdd:COG1119 106 -------FDSIGlyREPTDEQRERAreLLELLGLAHL-ADRPFGTLSQGEqrRVLIARA--LVKDPELLILDEPTAGLDL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1863768389 175 GARARLYAALTSWRGQ---AIV-VSHDR-DLLDLVQHMAEMRAGGITFFG 219
Cdd:COG1119 176 GARELLLALLDKLAAEgapTLVlVTHHVeEIPPGITHVLLLKDGRVVAAG 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
330-509 |
2.63e-19 |
|
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: 91.15 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 330 SVPPGRDIVVTENLVLRNGAvvslhirgpeRVGLVGPNGSGKTTL------IDT-IRGEIEPRSGtvsLRVPYRLLPQRL 402
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGA----------KIGVLGLNGAGKSTLlrimagVDKdFNGEARPQPG---IKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 403 QLLDD-RDSVLAAVSRL---------------APTADDNQLRAELARF-----LLDADTIAR----------------PV 445
Cdd:TIGR03719 80 DPTKTvRENVEEGVAEIkdaldrfneisakyaEPDADFDKLAAEQAELqeiidAADAWDLDSqleiamdalrcppwdaDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 446 GTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFL 509
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKP--DMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFL 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
351-515 |
3.19e-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: 86.12 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRllpqrlqllDDRDSVLAAVSRL--AP------TA 422
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY---------QKNIEALRRIGALieAPgfypnlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 423 DDN--------QLRAELARFLLD----ADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSI---RQ 487
Cdd:cd03268 90 RENlrllarllGIRKKRIDEVLDvvglKDSAKKKVKGFSLGMKQRLGIALALLGNP--DLLILDEPTNGLDPDGIkelRE 167
|
170 180
....*....|....*....|....*...
gi 1863768389 488 LTQALTQYRGALLVASHddaFLSELGLT 515
Cdd:cd03268 168 LILSLRDQGITVLISSH---LLSEIQKV 192
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
34-264 |
5.47e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 86.40 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQH--LVLQSDRTVADVLGiEAVLAalati 98
Cdd:COG1124 35 GLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrrkAFRRRVQMVFQDpyASLHPRHTVDRILA-EPLRI----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 dagQGQPadfevvgdqwDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:COG1124 109 ---HGLP----------DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 179 RLYAALTSWRGQA----IVVSHDrdlLDLVQHMAE----MRAGGItffggnftaftdalaVEQEAAARGVRAAESDLkrq 250
Cdd:COG1124 176 EILNLLKDLREERgltyLFVSHD---LAVVAHLCDrvavMQNGRI---------------VEELTVADLLAGPKHPY--- 234
|
250
....*....|....
gi 1863768389 251 QRELAEARIKLDRR 264
Cdd:COG1124 235 TRELLAASLAFERA 248
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-219 |
6.86e-19 |
|
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: 90.28 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 4 SVVCSDLWFAWP-SGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------------RpERV 67
Cdd:COG2274 473 DIELENVSFRYPgDSPPVLDNISLTIkPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpaslR-RQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 68 GYLPQHLVLQSDrTVAD--VLG-----IEAVLAALAtiDAG-----QGQPADFE-VVGDQwdlpdrsiamlarfGfadld 134
Cdd:COG2274 552 GVVLQDVFLFSG-TIREniTLGdpdatDEEIIEAAR--LAGlhdfiEALPMGYDtVVGEG--------------G----- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 135 lrrpiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA--IVVSHDRDLLDLVQHMAEMRA 212
Cdd:COG2274 610 -----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRtvIIIAHRLSTIRLADRIIVLDK 684
|
....*..
gi 1863768389 213 GGITFFG 219
Cdd:COG2274 685 GRIVEDG 691
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
344-524 |
9.19e-19 |
|
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: 89.44 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyRLLPQRLQLLDDRDSVLAAVS------- 416
Cdd:COG4987 350 VLDG---LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL----GGVDLRDLDEDDLRRRIAVVPqrphlfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 -------RLA-PTADDNQLRAELARFLLDADTIARPVG----------TLSGGERFRATLAALLLSEPPpqLLILDEPTN 478
Cdd:COG4987 423 ttlrenlRLArPDATDEELWAALERVGLGDWLAALPDGldtwlgeggrRLSGGERRRLALARALLRDAP--ILLLDEPTE 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 479 NLDLDSIRQLTQALTQYRG--ALLVASHDDAFLSELGLTYRIDLGAVA 524
Cdd:COG4987 501 GLDAATEQALLADLLEALAgrTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-206 |
2.97e-18 |
|
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: 83.61 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 14 WPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPERVGYLPQHL--VLQSDRT 81
Cdd:cd03292 10 YPNGTAALDGINISISAgEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlRGRAIPYLRRKIgvVFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 82 VADVLGIEAVLAALATIDAGQGqpadfevvgdqwDLPDRSIAMLARFGFADLDLRRPIGtLSGGEVILLALAAQFLSEPD 161
Cdd:cd03292 90 LPDRNVYENVAFALEVTGVPPR------------EIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 162 LLLLDEPTNNLDSGARARLYAALTSW--RGQAIVVS-HDRDLLDLVQH 206
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRH 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-202 |
3.88e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 87.70 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVSRPER--VGYLPQH-LVLQSDRTVADVLGieavlaalatiDAGQgqpaDFEVV 111
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQHrAELDPEKTVMDNLA-----------EGKQ----EVMVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 112 GDqwdlpDRSI-AMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ 190
Cdd:PRK11147 415 GR-----PRHVlGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGT 489
|
170
....*....|..
gi 1863768389 191 AIVVSHDRDLLD 202
Cdd:PRK11147 490 VLLVSHDRQFVD 501
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
342-511 |
5.24e-18 |
|
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: 82.69 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLL-------DD---RDSV 411
Cdd:cd03226 13 TEILDD---LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIgyvmqdvDYqlfTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 LAAVSRLAPTADDNQLRAE--LARFLLDADTIARPVgTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLT 489
Cdd:cd03226 90 REELLLGLKELDAGNEQAEtvLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVG 166
|
170 180
....*....|....*....|....*
gi 1863768389 490 QA---LTQYRGALLVASHDDAFLSE 511
Cdd:cd03226 167 ELireLAAQGKAVIVITHDYEFLAK 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-215 |
5.37e-18 |
|
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: 82.57 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSR---------PER--VGYLPQHLVLQSDRTVAD--VLGIEAVLAALAT 97
Cdd:cd03259 27 EFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvpPERrnIGMVFQDYALFPHLTVAEniAFGLKLRGVPKAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 98 IDAgqgqpadfevvgdqwdlpdRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR 177
Cdd:cd03259 107 IRA-------------------RVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 178 ARLYAALTSWRGQ----AIVVSHDR-DLLDLVQHMAEMRAGGI 215
Cdd:cd03259 167 EELREELKELQRElgitTIYVTHDQeEALALADRIAVMNEGRI 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-231 |
9.07e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 86.84 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 2 PSSVVCSDLWFAWPSGELAIAGLTCAFP-DQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPE--RVGYLPQHLVLQS 78
Cdd:PLN03073 506 PPIISFSDASFGYPGGPLLFKNLNFGIDlDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkvRMAVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 79 DRTVADVLGIEAVLAAlatidagqgqpadfevvgdqwdLPDRSI-AMLARFGFADLDLRRPIGTLSGGEVILLALAAQFL 157
Cdd:PLN03073 586 DLSSNPLLYMMRCFPG----------------------VPEQKLrAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 158 SEPDLLLLDEPTNNLDSGARARLYAALTSWRGQAIVVSHDRDLLD-LVQHMAEMRAGGITFFGGNFTAFTDALAV 231
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISgSVDELWVVSEGKVTPFHGTFHDYKKTLQS 718
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
351-505 |
1.61e-17 |
|
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: 82.00 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--RVPYRLLPQRLQLLD----------------DRDSVL 412
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVagLVPWKRRKKFLRRIGvvfgqktqlwwdlpviDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 413 AAVSRLAPTADDNQLRaELARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDS---IRQLT 489
Cdd:cd03267 120 AAIYDLPPARFKKRLD-ELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE--PEILFLDEPTIGLDVVAqenIRNFL 196
|
170
....*....|....*..
gi 1863768389 490 QALTQYRGA-LLVASHD 505
Cdd:cd03267 197 KEYNRERGTtVLLTSHY 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-505 |
2.23e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.21 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 349 AV--VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--RVPYrllpqrlqllDDR---------------- 408
Cdd:COG4586 37 AVddISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgYVPF----------KRRkefarrigvvfgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 409 --------DS--VLAAVSRLaptaDDNQLRAELARF--LLD-ADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDE 475
Cdd:COG4586 107 lwwdlpaiDSfrLLKAIYRI----PDAEYKKRLDELveLLDlGELLDTPVRQLSLGQRMRCELAAALLHR--PKILFLDE 180
|
170 180 190
....*....|....*....|....*....|....
gi 1863768389 476 PTNNLDLDS---IRQLTQALTQYRGA-LLVASHD 505
Cdd:COG4586 181 PTIGLDVVSkeaIREFLKEYNRERGTtILLTSHD 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-219 |
2.69e-17 |
|
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: 80.80 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 24 LTCAF--PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-----------------SRPERVGYLPQHLVLQSDRTVAd 84
Cdd:cd03297 15 LKIDFdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinlpPQQRKIGLVFQQYALFPHLNVR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 85 vlgiEAVLAALATIDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLL 164
Cdd:cd03297 94 ----ENLAFGLKRKRNREDR--------------ISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 165 LDEPTNNLDSGARARLYAAL----TSWRGQAIVVSHDrdlLDLVQHMAE----MRAGGITFFG 219
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD---LSEAEYLADrivvMEDGRLQYIG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
35-197 |
3.16e-17 |
|
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: 80.59 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS--------RPERVGYLPQHLVLQSDRTVAD--VLGIEAvlaalatidagQGQ 104
Cdd:cd03293 35 LVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgPGPDRGYVFQQDALLPWLTVLDnvALGLEL-----------QGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 105 PADfevvgdqwDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAAL 184
Cdd:cd03293 104 PKA--------EARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEEL 174
|
170
....*....|....*..
gi 1863768389 185 TS-WR--GQAIV-VSHD 197
Cdd:cd03293 175 LDiWRetGKTVLlVTHD 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
341-513 |
4.02e-17 |
|
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: 79.15 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqRLQLLDDRDSVLAAVSRLAP 420
Cdd:cd03229 12 QKTVLND---VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID--------GEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 TADDNQLRAELARFlldaDTIARPvgtLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDL---DSIRQLTQALTQYRG 497
Cdd:cd03229 81 VFQDFALFPHLTVL----ENIALG---LSGGQQQRVALARALAMDPD--VLLLDEPTSALDPitrREVRALLKSLQAQLG 151
|
170
....*....|....*..
gi 1863768389 498 -ALLVASHDDAFLSELG 513
Cdd:cd03229 152 iTVVLVTHDLDEAARLA 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
353-520 |
7.14e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.85 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 353 LHIRGPERVGLVGPNGSGKTTLIDTIRGEI---------------------EPR--SGTV-------------------- 389
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdPPRnvEGTVydfvaegieeqaeylkryhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 390 -SLRVpyrllpqrlqLLDDRDSVLAAVSRLAPTAD-------DNQLRAELARFLLDADTiarPVGTLSGGERFRATLAAL 461
Cdd:PRK11147 104 iSHLV----------ETDPSEKNLNELAKLQEQLDhhnlwqlENRINEVLAQLGLDPDA---ALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 462 LLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFLSELGlTYRIDL 520
Cdd:PRK11147 171 LVSNP--DVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMA-TRIVDL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-199 |
1.39e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 79.75 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 12 FAWPSGEL-AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQH---LVLQSD-----RT 81
Cdd:COG1116 17 FPTGGGGVtALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPdrgVVFQEPallpwLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 82 VAD--VLGIEAvlaalatidagQGQPADfevvgdqwDLPDRSIAMLARFGFADLDLRRPiGTLSGGE---VillALAAQF 156
Cdd:COG1116 97 VLDnvALGLEL-----------RGVPKA--------ERRERARELLELVGLAGFEDAYP-HQLSGGMrqrV---AIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1863768389 157 LSEPDLLLLDEPTNNLDSGARARLYAALTS-WR--GQAIV-VSHDRD 199
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRlWQetGKTVLfVTHDVD 200
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-219 |
1.74e-16 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 82.49 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 15 PSGELAIAGLTCAFPD----------------QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPER--- 66
Cdd:COG4618 327 PKGRLSVENLTVVPPGskrpilrgvsfslepgEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwDREElgr 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 67 -VGYLPQHLVLqSDRTVADVlgI--------EAVLAAlatidagqgqpadfevvgdqwdlpdrsiAMLArfGFADLDLRR 137
Cdd:COG4618 407 hIGYLPQDVEL-FDGTIAEN--IarfgdadpEKVVAA----------------------------AKLA--GVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 138 P------IG----TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ---AIVVSHDRDLLDLV 204
Cdd:COG4618 454 PdgydtrIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgatVVVITHRPSLLAAV 533
|
250
....*....|....*
gi 1863768389 205 QHMAEMRAGGITFFG 219
Cdd:COG4618 534 DKLLVLRDGRVQAFG 548
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
1.83e-16 |
|
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: 82.12 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 2 PSSVVCSDLWFAWP-SGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPER 66
Cdd:COG4987 331 GPSLELEDVSFRYPgAGRPVLDGLSLTLpPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdldedDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 67 VGYLPQHLVLQSDrTVADVLgieavlaALATIDAGqgqpadfevvgdqwdlPDRSIAMLARFGFADLDLRRPIG------ 140
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENL-------RLARPDAT----------------DEELWAALERVGLGDWLAALPDGldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 141 ----TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA--IVVSHDRDLLDLVQHMAEMRAGG 214
Cdd:COG4987 467 eggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRtvLLITHRLAGLERMDRILVLEDGR 546
|
..
gi 1863768389 215 IT 216
Cdd:COG4987 547 IV 548
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
34-216 |
2.32e-16 |
|
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: 78.24 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------------RPERVGYlpqhlVLQSDRTVADVLGIEAVLAALa 96
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldedararlRARHVGF-----VFQSFQLLPTLTALENVMLPL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 97 tidagqgqpadfEVVGDQwDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGA 176
Cdd:COG4181 116 ------------ELAGRR-DARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1863768389 177 RAR---LYAALTSWRGQAIV-VSHDRDLLDLVQHMAEMRAGGIT 216
Cdd:COG4181 182 GEQiidLLFELNRERGTTLVlVTHDPALAARCDRVLRLRAGRLV 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
341-509 |
2.53e-16 |
|
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: 82.19 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD----------S 410
Cdd:COG2274 487 SPPVLDN---ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI--------------DGIDlrqidpaslrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLAAV---SRL------------APTADDNQLR--AELARflLDADTIARPVG----------TLSGGERFRATLAALLL 463
Cdd:COG2274 550 QIGVVlqdVFLfsgtirenitlgDPDATDEEIIeaARLAG--LHDFIEALPMGydtvvgeggsNLSGGQRQRLAIARALL 627
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 464 SEPPpqLLILDEPTNNLDLDSIRQLTQALTQYRG--ALLVASHDDAFL 509
Cdd:COG2274 628 RNPR--ILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI 673
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-505 |
2.62e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 343 LVLRNGAV------VSLHIRGPERVGLVGPNGSGKTTLIDTIRGeIEPRSGTVSLRVPYRLLPQRLQLLDDR------DS 410
Cdd:PRK03695 1 MQLNDVAVstrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRaylsqqQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLAAV----------SRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLL-----SEPPPQLLILDE 475
Cdd:PRK03695 80 PPFAMpvfqyltlhqPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAGQLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1863768389 476 PTNNLD------LDsirQLTQALTQYRGALLVASHD 505
Cdd:PRK03695 160 PMNSLDvaqqaaLD---RLLSELCQQGIAVVMSSHD 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-208 |
5.67e-16 |
|
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: 76.87 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpervgylpqhLVLQSDrtVADVLGIEAVLAALatIDAGQGQPA---- 106
Cdd:cd03268 27 EIYGFLGPNGAGKTTTMKIILGLIKPDSGEI------------TFDGKS--YQKNIEALRRIGAL--IEAPGFYPNltar 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 107 -DFEVVGDQWDLPDRSI-AMLARFGFADLDlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAAL 184
Cdd:cd03268 91 eNLRLLARLLGIRKKRIdEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180
....*....|....*....|....*..
gi 1863768389 185 TSWRGQAIVV---SHdrdLLDLVQHMA 208
Cdd:cd03268 170 LSLRDQGITVlisSH---LLSEIQKVA 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-169 |
5.76e-16 |
|
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: 77.09 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLPQH--------LVLQSDR-----TVADVLgieaVLAALA 96
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRDITGLPPHeraragigYVPEGRRifpelTVEENL----LLGAYA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 97 TIDAgqgqpadfevvGDQWDLpDRSIAMlarfgFADLD--LRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPT 169
Cdd:cd03224 103 RRRA-----------KRKARL-ERVYEL-----FPRLKerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
343-517 |
5.96e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 343 LVLRNGAV------VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIePRSGTVSLrvpyrllpqrlqllDDRD------S 410
Cdd:COG4138 1 LQLNDVAVagrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL--------------NGRPlsdwsaA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLA------------------------AVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLL--- 463
Cdd:COG4138 66 ELArhraylsqqqsppfampvfqylalHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvw 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 464 --SEPPPQLLILDEPTNNLDldsIRQ------LTQALTQYRGALLVASHDdaflseLGLTYR 517
Cdd:COG4138 146 ptINPEGQLLLLDEPMNSLD---VAQqaaldrLLRELCQQGITVVMSSHD------LNHTLR 198
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
340-505 |
7.11e-16 |
|
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: 76.76 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSVLAAVSRLA 419
Cdd:cd03255 15 EKVQALKG---VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV--------------DGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 P-------------------TADDN------------QLRAELARFLLD----ADTIARPVGTLSGGERFRATLAALLLS 464
Cdd:cd03255 78 AfrrrhigfvfqsfnllpdlTALENvelplllagvpkKERRERAEELLErvglGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1863768389 465 EPPpqLLILDEPTNNLDLDS---IRQLTQALTQYRG-ALLVASHD 505
Cdd:cd03255 158 DPK--IILADEPTGNLDSETgkeVMELLRELNKEAGtTIVVVTHD 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-507 |
7.72e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSlRVPYRLLPQRLQLLDDRDSVLAAVSRLA----------- 419
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-RAGGARVAYVPQRSEVPDSLPLTVRDLVamgrwarrglw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 --PTADDNQLRAE-LARFLLdADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYR 496
Cdd:NF040873 90 rrLTRDDRAAVDDaLERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQE--ADLLLLDEPTTGLDAESRERIIALLAEEH 166
|
170
....*....|....
gi 1863768389 497 G---ALLVASHDDA 507
Cdd:NF040873 167 ArgaTVVVVTHDLE 180
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-510 |
8.18e-16 |
|
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: 76.47 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---------------RVPYRLLPQRLQL 404
Cdd:cd03245 15 QEIPALDN---VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlrrNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 405 LDDRDSVLAAvsrlAPTADDNQL-----RAELARFL-LDADTIARPVG----TLSGGERFRATLAALLLSEPPpqLLILD 474
Cdd:cd03245 92 GTLRDNITLG----APLADDERIlraaeLAGVTDFVnKHPNGLDLQIGergrGLSGGQRQAVALARALLNDPP--ILLLD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 475 EPTNNLDLDSIRQLTQALTQYRG--ALLVASHDDAFLS 510
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
34-219 |
1.08e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERV--------GYLPQHLVLQSDRTVADVLGI--EAVLAALATIdagqg 103
Cdd:COG1134 56 GIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsallelgaGFHPELTGRENIYLNGRLLGLsrKEIDEKFDEI----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 104 qpADFEVVGDQWDLPDR--SIAMLARFGFadldlrrpigtlsggevillALAAQFlsEPDLLLLDEptnNL---DSGARA 178
Cdd:COG1134 131 --VEFAELGDFIDQPVKtySSGMRARLAF--------------------AVATAV--DPDILLVDE---VLavgDAAFQK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 179 RLYAALTSWRGQA---IVVSHDrdlLDLVQHMAE----MRAGGITFFG 219
Cdd:COG1134 184 KCLARIRELRESGrtvIFVSHS---MGAVRRLCDraiwLEKGRLVMDG 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
35-206 |
1.47e-15 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 75.75 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSV----------------SRPERVGYLPQHLVLQSDRTVADVLgieavlaALATI 98
Cdd:TIGR02673 33 LTGPSGAGKTTLLKLLYGALTPSRGQVriagedvnrlrgrqlpLLRRRIGVVFQDFRLLPDRTVYENV-------ALPLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 DAGQGQPADFEVVGD---QWDLPDRsiamlarfgfadldLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:TIGR02673 106 VRGKKEREIQRRVGAalrQVGLEHK--------------ADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPD 171
|
170 180 190
....*....|....*....|....*....|....
gi 1863768389 176 ARARLYAALTSW--RGQAIVV-SHDRDLLDLVQH 206
Cdd:TIGR02673 172 LSERILDLLKRLnkRGTTVIVaTHDLSLVDRVAH 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-209 |
1.51e-15 |
|
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: 75.39 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV---------SRPERVGYLPQHLVLQSDRTVADVLGIEAVLAALATIDAG 101
Cdd:cd03269 27 EIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkpldiAARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 QgqpadfEVvgDQWdlpdrsiamLARFGFADLDLRRpIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLY 181
Cdd:cd03269 107 R------RI--DEW---------LERLELSEYANKR-VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
170 180 190
....*....|....*....|....*....|
gi 1863768389 182 AALTSWR--GQAIVVSHDRdlLDLVQHMAE 209
Cdd:cd03269 169 DVIRELAraGKTVILSTHQ--MELVEELCD 196
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
29-219 |
2.28e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 78.93 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRP-------------ERVGYLPQhlvlqsdrtvadvlGIEAVLAAL 95
Cdd:TIGR01842 343 AGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDgadlkqwdretfgKHIGYLPQ--------------DVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 ATIDAGQGQPADfevvgdqwdlPDRSIAMLARFGFADLDLRRPIG----------TLSGGEVILLALAAQFLSEPDLLLL 165
Cdd:TIGR01842 409 AENIARFGENAD----------PEKIIEAAKLAGVHELILRLPDGydtvigpggaTLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 166 DEPTNNLDSGARARLYAALTSWRGQ---AIVVSHDRDLLDLVQHMAEMRAGGITFFG 219
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARgitVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-518 |
2.31e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------------SRPERVGYLPQHLVLQSDRTVAD--VLGIEAVLAA 94
Cdd:COG1129 31 EVHALLGENGAGKSTLMKILSGVYQPDSGEIlldgepvrfrsprdAQAAGIAIIHQELNLVPNLSVAEniFLGREPRRGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LatIDAGQgqpadfevvgdqwdLPDRSIAMLARFGFaDLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDS 174
Cdd:COG1129 111 L--IDWRA--------------MRRRARELLARLGL-DIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 175 GARARLYA---ALTSwRGQAIV-VSHdrdlldlvqHMAEMRAggitfFGGNFTAFTDALAVEQEAAArgvraaesdlkrq 250
Cdd:COG1129 174 REVERLFRiirRLKA-QGVAIIyISH---------RLDEVFE-----IADRVTVLRDGRLVGTGPVA------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 251 qrELAEARIkldrrqrfarsqagnVPKIVagakkgtaevsagklrgGHqadvadarrrleeaeervrdddSIEVDLSRTS 330
Cdd:COG1129 226 --ELTEDEL---------------VRLMV-----------------GR----------------------ELEDLFPKRA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 331 VPPGRDIVVTENLVLRNG-AVVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR----------------- 392
Cdd:COG1129 250 AAPGEVVLEVEGLSVGGVvRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkpvrirsprdairagi 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 393 --VPyrllpqrlqllDDRDS-------------VLAAVSRLA--PTADDNQLRAELARFL--LD--ADTIARPVGTLSGG 451
Cdd:COG1129 330 ayVP-----------EDRKGeglvldlsireniTLASLDRLSrgGLLDRRRERALAEEYIkrLRikTPSPEQPVGNLSGG 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 452 ERFRATLAALLLSEPppQLLILDEPTNNLD-------LDSIRQLTQaltqyRG-ALLVASHDdafLSE-LGLTYRI 518
Cdd:COG1129 399 NQQKVVLAKWLATDP--KVLILDEPTRGIDvgakaeiYRLIRELAA-----EGkAVIVISSE---LPElLGLSDRI 464
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-204 |
2.56e-15 |
|
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: 75.52 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRP-ERVGYLPQHLVLQSDRTVADVlgieavlaaLATIDAGQGQPADFE 109
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIElDTVSYKPQYIKADYEGTVRDL---------LSSITKDFYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 110 VvgdqwdlpdrsiAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW-- 187
Cdd:cd03237 97 T------------EIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFae 163
|
170
....*....|....*....
gi 1863768389 188 --RGQAIVVSHDRDLLDLV 204
Cdd:cd03237 164 nnEKTAFVVEHDIIMIDYL 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
29-197 |
2.96e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---RP----------ERVGYLPQHLVLQSDRTVADVLgieavlaAL 95
Cdd:PRK13548 27 PGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngRPladwspaelaRRRAVLPQHSSLSFPFTVEEVV-------AM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 ATIDAGQGQPADFEVVGdqwdlpdrsiAMLARFGFADLdLRRPIGTLSGGEVILLALA---AQfLSEPD----LLLLDEP 168
Cdd:PRK13548 100 GRAPHGLSRAEDDALVA----------AALAQVDLAHL-AGRDYPQLSGGEQQRVQLArvlAQ-LWEPDgpprWLLLDEP 167
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 169 TNNLDSG---ARARLYAALTSWRGQA-IVVSHD 197
Cdd:PRK13548 168 TSALDLAhqhHVLRLARQLAHERGLAvIVVLHD 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-219 |
3.23e-15 |
|
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: 78.02 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE------RVGYLPQHLVLQSD--RTVADVLGieavl 92
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklSRRSlrelrrRVQMVFQDPYSSLNprMTVGDIIA----- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 93 aalatidagqgQPADFEVVGDQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNL 172
Cdd:COG1123 367 -----------EPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 173 DSGARARLYAALTSWRGQA----IVVSHDrdlLDLVQHMAE----MRAGGITFFG 219
Cdd:COG1123 436 DVSVQAQILNLLRDLQRELgltyLFISHD---LAVVRYIADrvavMYDGRIVEDG 487
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-504 |
3.78e-15 |
|
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: 75.12 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 335 RDIVVT--ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSG-TVSL---------------RVPYR 396
Cdd:COG1119 7 RNVTVRrgGKTILDD---ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrggedvwelrkRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 397 LLPQRLQLLDD---RDSVLA---AVSRLAPTADDNQLraELARFLLD----ADTIARPVGTLSGGERFRATLAALLLSEP 466
Cdd:COG1119 84 SPALQLRFPRDetvLDVVLSgffDSIGLYREPTDEQR--ERARELLEllglAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1863768389 467 PpqLLILDEPTNNLDLDSIRQLTQALTQYRG----ALLVASH 504
Cdd:COG1119 162 E--LLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
4.08e-15 |
|
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: 78.10 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 2 PSSVVCSDLWFAWPSGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERV 67
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRPALRPVSFTVpPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadadSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 68 GYLPQHLVLQSDrTVADVLgieavlaALATIDAGqgqpadfevvgdqwdlPDRSIAMLARFGFADLDLRRPIGT------ 141
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENI-------RLARPDAS----------------DAEIREALERAGLDEFVAALPQGLdtpige 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 142 ----LSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA--IVVSHDRDLLDLVQH 206
Cdd:TIGR02857 455 ggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRLALAALADR 525
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
351-522 |
4.35e-15 |
|
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: 74.07 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--------RVPYRLLPQRLQLLDDRDSVLAAVSRL---A 419
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfqRDSIARGLLYLGHAPGIKTTLSVLENLrfwH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 PTADDNQLRAELARFLLDADTiARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQYR--- 496
Cdd:cd03231 99 ADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRP--LWILDEPTTALDKAGVARFAEAMAGHCarg 175
|
170 180
....*....|....*....|....*.
gi 1863768389 497 GALLVASHDDAFLSELGLTyRIDLGA 522
Cdd:cd03231 176 GMVVLTTHQDLGLSEAGAR-ELDLGF 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-233 |
6.48e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 8 SDLWFAWpSGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpervgyLPQHLVLQSDRTvadvl 86
Cdd:PRK13638 5 SDLWFRY-QDEPVLKGLNLDFsLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV--------LWQGKPLDYSKR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 87 GIEAVLAALATIDAGQGQPADFEVVgdqwdlpDRSIAM-LARFGFADLDLRR-----------------PIGTLSGGEVI 148
Cdd:PRK13638 71 GLLALRQQVATVFQDPEQQIFYTDI-------DSDIAFsLRNLGVPEAEITRrvdealtlvdaqhfrhqPIQCLSHGQKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 149 LLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLL-DLVQHMAEMRAGGITFFGGNFTA 224
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGnhvIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
....*....
gi 1863768389 225 FTDALAVEQ 233
Cdd:PRK13638 224 FACTEAMEQ 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
351-505 |
7.30e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD-------------SVLAAVSR 417
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL--------------NGRPladwspaelarrrAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 418 LA-------------------PTADDNQLRAELARflLDADTIA-RPVGTLSGGERFRATLAALLL----SEPPPQLLIL 473
Cdd:PRK13548 87 LSfpftveevvamgraphglsRAEDDALVAAALAQ--VDLAHLAgRDYPQLSGGEQQRVQLARVLAqlwePDGPPRWLLL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1863768389 474 DEPTNNLDL---DSIRQLTQALTQYRG-ALLVASHD 505
Cdd:PRK13548 165 DEPTSALDLahqHHVLRLARQLAHERGlAVIVVLHD 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
351-512 |
1.08e-14 |
|
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: 72.78 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--------RVPYRLLPQRLQLLDDRDSVLAAVSRL---A 419
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtplaeqRDEPHENILYLGHLPGLKPELSALENLhfwA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 PTADDNQLRAELARFLLDADTIA-RPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQY--- 495
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAVGLTGFEdLPAAQLSAGQQRRLALARLWLSRRP--LWILDEPTTALDKAGVALLAGLLRAHlar 176
|
170
....*....|....*..
gi 1863768389 496 RGALLVASHDDAFLSEL 512
Cdd:TIGR01189 177 GGIVLLTTHQDLGLVEA 193
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
351-505 |
1.15e-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: 73.31 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvPYRLLPQRLQLLDDRDSVLAAV-----SRLAPT---- 421
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-GKDLLKLSRRLRKIRRKEIQMVfqdpmSSLNPRmtig 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 422 ------------ADDNQLRAE-----LARFLLDADTIARPVGTLSGGERFRATLA-ALLLSeppPQLLILDEPTNNLD-- 481
Cdd:cd03257 103 eqiaeplrihgkLSKKEARKEavlllLVGVGLPEEVLNRYPHELSGGQRQRVAIArALALN---PKLLIADEPTSALDvs 179
|
170 180
....*....|....*....|....*....
gi 1863768389 482 -----LDSIRQLTQaltQYRGALLVASHD 505
Cdd:cd03257 180 vqaqiLDLLKKLQE---ELGLTLLFITHD 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-201 |
1.40e-14 |
|
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: 73.24 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 20 AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLP-------------QHLVLQSDRTVAD 84
Cdd:cd03219 15 ALDDVSFSVRPgEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGEDITGLPpheiarlgigrtfQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 85 VLgieaVLAALAtidAGQGQPADFEVVGDQWDLPDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLL 164
Cdd:cd03219 95 NV----MVAAQA---RTGSGLLLARARREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1863768389 165 LDEPTNNLDSGARARLYAALTSWRGQAI---VVSHDRDLL 201
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGItvlLVEHDMDVV 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-518 |
1.52e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaVSRLAP- 420
Cdd:COG2884 15 REALSD---VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV--------------NGQD-----LSRLKRr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 ----------------------TADDN---QLRA---------ELARFLLD----ADTIARPVGTLSGGERFRATLA-AL 461
Cdd:COG2884 73 eipylrrrigvvfqdfrllpdrTVYENvalPLRVtgksrkeirRRVREVLDlvglSDKAKALPHELSGGEQQRVAIArAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 462 LLSeppPQLLILDEPTNNLDLDSIRQLTQALTQY--RG-ALLVASHDDAFLSELGltYRI 518
Cdd:COG2884 153 VNR---PELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMP--KRV 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
35-219 |
1.97e-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: 72.75 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPER--VGYLPQHLVLQSDRTVADVL--GIEAVLAALATIDAg 101
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEKrdISYVPQNYALFPHMTVYKNIayGLKKRKVDKKEIER- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 qgqpadfevvgdqwdlpdRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLY 181
Cdd:cd03299 109 ------------------KVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 182 AALTSWRGQ----AIVVSHD-RDLLDLVQHMAEMRAGGITFFG 219
Cdd:cd03299 170 EELKKIRKEfgvtVLHVTHDfEEAWALADKVAIMLNGKLIQVG 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
337-509 |
2.20e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 75.98 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 337 IVVTENLVLRNGAVVSLH-----IRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVS----------------LRVP- 394
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDnatatINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawvnqetpaLPQPa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 395 ----------YRLLPQRLQLLDDRDS--VLAAVSRLAPTADDNQLRAELARFL----LDADTIARPVGTLSGGERFRATL 458
Cdd:PRK10636 81 leyvidgdreYRQLEAQLHDANERNDghAIATIHGKLDAIDAWTIRSRAASLLhglgFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 459 AALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFL 509
Cdd:PRK10636 161 AQALICRS--DLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFL 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
316-507 |
2.77e-14 |
|
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: 75.40 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 316 VRDDDSIEVDLSRTSVP-PGRDIVVTEnlvlrngavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvp 394
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAyPGRRPALRP---------VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV--- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 395 yRLLPQRLQLLDDRDSVLAAVS--------------RLA-PTADDNQLRAELARFLLDADTIARPVGT----------LS 449
Cdd:TIGR02857 382 -NGVPLADADADSWRDQIAWVPqhpflfagtiaeniRLArPDASDAEIREALERAGLDEFVAALPQGLdtpigeggagLS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 450 GGERFRATLAALLLSepPPQLLILDEPTNNLDLDSIRQLTQALTQYRG--ALLVASHDDA 507
Cdd:TIGR02857 461 GGQAQRLALARAFLR--DAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA 518
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
334-505 |
2.80e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 72.76 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 334 GRDIVVTENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL----------------- 391
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLvavddVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditglpphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 392 --------------------RVPYRLLPqrlqllddRDSVLAAVSRLAPTADDNQLRAELARFLLD----ADTIARPVGT 447
Cdd:COG0411 81 iartfqnprlfpeltvlenvLVAAHARL--------GRGLLAALLRLPRARREEREARERAEELLErvglADRADEPAGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 448 LSGGERFRATLAALLLSEppPQLLILDEPT---NNLDLDSIRQLTQALTQYRG-ALLVASHD 505
Cdd:COG0411 153 LSYGQQRRLEIARALATE--PKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHD 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
351-504 |
2.84e-14 |
|
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: 72.02 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL------RVPYRLLPQRLQLLD-----DRDSVLAAV---S 416
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdgfdvvKEPAEARRRLGFVSDstglyDRLTARENLeyfA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 RLAPTADDNQLRA--ELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:cd03266 104 GLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP--VLLLDEPTTGLDVMATRALREFIRQ 181
|
170
....*....|...
gi 1863768389 495 YRG---ALLVASH 504
Cdd:cd03266 182 LRAlgkCILFSTH 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-169 |
2.88e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 72.32 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPER-----VGYLPQhlvlqsDR------TVADVLgiea 90
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglPPHRiarlgIGYVPE------GRrifpslTVEENL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 91 vLAALATIDAGQGQPADFEVVgdqWDL-PDrsiamLARFgfadldLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPT 169
Cdd:COG0410 100 -LLGAYARRDRAEVRADLERV---YELfPR-----LKER------RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
34-219 |
3.13e-14 |
|
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: 71.79 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERV--------GYLPQHLVLQSDRTVADVLG-----IEAVLAALatida 100
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllglggGFNPELTGRENIYLNGRLLGlsrkeIDEKIDEI----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 101 gqgqpADFEVVGDQWDLPDR--SIAMLARFGFadldlrrpigtlsggevillALAAQFlsEPDLLLLDEPTNNLDSGARA 178
Cdd:cd03220 127 -----IEFSELGDFIDLPVKtySSGMKARLAF--------------------AIATAL--EPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1863768389 179 RLYAALTSWRGQA---IVVSHDRDLL-DLVQHMAEMRAGGITFFG 219
Cdd:cd03220 180 KCQRRLRELLKQGktvILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-488 |
3.17e-14 |
|
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: 70.80 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpQRLQLLDDRDSVLAAVSRLap 420
Cdd:cd03247 14 EQQVLKN---LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL--------DGVPVSDLEKALSSLISVL-- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 421 taddNQlraelaRFLLDADTIARPVGT-LSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQL 488
Cdd:cd03247 81 ----NQ------RPYLFDTTLRNNLGRrFSGGERQRLALARILLQDAP--IVLLDEPTVGLDPITERQL 137
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
351-512 |
3.44e-14 |
|
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: 74.94 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIePRSGTVSLRVPYRLLPQRLQLLDDRDSVLAAV-----SRLAPTADDN 425
Cdd:COG1123 25 VSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISGEVLLDGRDLLELSEALRGRRIGMVfqdpmTQLNPVTVGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 426 QLRAELARFLLDADTI-----------------ARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD------- 481
Cdd:COG1123 104 QIAEALENLGLSRAEArarvlelleavglerrlDRYPHQLSGGQRQRVAIAMALALD--PDLLIADEPTTALDvttqaei 181
|
170 180 190
....*....|....*....|....*....|.
gi 1863768389 482 LDSIRQLTQaltQYRGALLVASHDDAFLSEL 512
Cdd:COG1123 182 LDLLRELQR---ERGTTVLLITHDLGVVAEI 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
29-200 |
5.71e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 71.99 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLP-------------QHLVLQSDRTVADVLgieaVLAA 94
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfDGRDITGLPphriarlgiartfQNPRLFPELTVLENV----LVAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LATIDAG--QGQPADFEVVGDQWDLPDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPT--- 169
Cdd:COG0411 105 HARLGRGllAALLRLPRARREEREARERAEELLERVGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAagl 183
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 170 NNLDSGARARLYAALTSWRGQAIV-VSHDRDL 200
Cdd:COG0411 184 NPEETEELAELIRRLRDERGITILlIEHDMDL 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-173 |
6.99e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---RP------ERVGYLPQHLVLQSDRTVADVLgieAVLAALAtidag 101
Cdd:COG4152 28 EIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgEPldpedrRRIGYLPEERGLYPKMKVGEQL---VYLARLK----- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 102 qGQPADfevvgdqwDLPDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:COG4152 100 -GLSKA--------EAKRRADEWLERLGLGDR-ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
32-215 |
7.00e-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: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 32 VTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------------SRPERVGYLPQH--LVLQSDRTVADVLgIEAVLA 93
Cdd:cd03257 33 TLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlrkIRRKEIQMVFQDpmSSLNPRMTIGEQI-AEPLRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 94 ALATIDagqgqpadfevvgdQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGE----VILLALAAQflsePDLLLLDEPT 169
Cdd:cd03257 112 HGKLSK--------------KEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQrqrvAIARALALN----PKLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 170 NNLDSGARA---RLYAALTSWRGQAIV-VSHDrdlLDLVQHMAE----MRAGGI 215
Cdd:cd03257 174 SALDVSVQAqilDLLKKLQEELGLTLLfITHD---LGVVAKIADrvavMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
351-507 |
7.02e-14 |
|
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: 70.63 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaVSRLAP---------- 420
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI--------------DGRD-----VTGVPPerrnigmvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 --------TADDN-------------QLRA---ELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEP 476
Cdd:cd03259 80 dyalfphlTVAENiafglklrgvpkaEIRArvrELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS--LLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1863768389 477 TNNLDL---DSIRQLTQALTQYRGA-LLVASHDDA 507
Cdd:cd03259 158 LSALDAklrEELREELKELQRELGItTIYVTHDQE 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
37-210 |
7.25e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 37 GRNGVGKSTLLKIIAGELMPTRGSV---------SRPER----VGYLPQHLVLQSDrTVADVLGIEavlaalatidagqg 103
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPTSGTLlfegedistLKPEIyrqqVSYCAQTPTLFGD-TVYDNLIFP-------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 104 qpadFEVVGDQWDlPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAA--QFLsePDLLLLDEPTNNLDSGARARLY 181
Cdd:PRK10247 105 ----WQIRNQQPD-PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRnlQFM--PKVLLLDEITSALDESNKHNVN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1863768389 182 AALTSW-RGQAIV---VSHDRD-------LLDLVQHMAEM 210
Cdd:PRK10247 178 EIIHRYvREQNIAvlwVTHDKDeinhadkVITLQPHAGEM 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-203 |
7.48e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 71.63 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPT-----------------RGS----------------VSRPERVGYLPQhlv 75
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwdeildefRGSelqnyftkllegdvkvIVKPQYVDLIPK--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 76 lQSDRTVADVLGieavlaalATIDAGQgqpadFEVVGDQWDLpdRSIamlarfgfadldLRRPIGTLSGGEVILLALAAQ 155
Cdd:cd03236 102 -AVKGKVGELLK--------KKDERGK-----LDELVDQLEL--RHV------------LDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 156 FLSEPDLLLLDEPTNNLDSGAR---ARLYAALTSWRGQAIVVSHDRDLLDL 203
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRlnaARLIRELAEDDNYVLVVEHDLAVLDY 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
352-522 |
8.92e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 352 SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqRLQLLDDRDSV-------------------- 411
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--------GEPIRRQRDEYhqdllylghqpgikteltal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 --LAAVSRLAPTADDNQLRAELARFLL----DAdtiarPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSI 485
Cdd:PRK13538 93 enLRFYQRLHGPGDDEALWEALAQVGLagfeDV-----PVRQLSAGQQRRVALARLWLTRAP--LWILDEPFTAIDKQGV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1863768389 486 RQLTQALTQYR---GALLVASHDDAFLSELGLTyRIDLGA 522
Cdd:PRK13538 166 ARLEALLAQHAeqgGMVILTTHQDLPVASDKVR-KLRLGQ 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-219 |
9.11e-14 |
|
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: 72.83 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 32 VTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------------RPE--RVGYLPQ------HLvlqsdrTVADVLgi 88
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflPPHrrRIGYVFQearlfpHL------SVRGNL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 89 eavLAALATIDAGQGQPAdfevvgdqwdlPDRSIAMLarfGFADLdLRRPIGTLSGGE---VillALAAQFLSEPDLLLL 165
Cdd:COG4148 99 ---LYGRKRAPRAERRIS-----------FDEVVELL---GIGHL-LDRRPATLSGGErqrV---AIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 166 DEPTNNLDSGARARLYAALTSWRGQA---IV-VSHDRD-LLDLVQHMAEMRAGGITFFG 219
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELdipILyVSHSLDeVARLADHVVLLEQGRVVASG 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
340-498 |
1.00e-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: 69.17 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllddrDSvlAAVSRLA 419
Cdd:cd03246 13 AEPPVLRN---VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-----------------DG--ADISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 PtaddNQLRAELARFLLD----ADTIARPVgtLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQY 495
Cdd:cd03246 71 P----NELGDHVGYLPQDdelfSGSIAENI--LSGGQRQRLGLARALYGN--PRILVLDEPNSHLDVEGERALNQAIAAL 142
|
...
gi 1863768389 496 RGA 498
Cdd:cd03246 143 KAA 145
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
340-505 |
1.23e-13 |
|
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: 70.54 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD----- 409
Cdd:cd03219 3 VRGLTKRFGGLvalddVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF--------------DGEDitglp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ----------------------SVL-----AAVSRLAPTADDNQLRAEL------ARFLLD----ADTIARPVGTLSGGE 452
Cdd:cd03219 69 pheiarlgigrtfqiprlfpelTVLenvmvAAQARTGSGLLLARARREErearerAEELLErvglADLADRPAGELSYGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 453 RFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYRG---ALLVASHD 505
Cdd:cd03219 149 QRRLEIARALATDP--KLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEHD 202
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-197 |
1.62e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 27 AFPDQVTGLVGRNGVGKSTLLKIIAGeLMPTRGSV----------SRPE---RVGYLPQHLVLQSDRTVADVLgieavla 93
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIllngrplsdwSAAElarHRAYLSQQQSPPFAMPVFQYL------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 94 ALatidaGQGQPADFEVVgdqwdlpDRSIAMLA-RFGFADLdLRRPIGTLSGGEVILLALAAQFL-------SEPDLLLL 165
Cdd:COG4138 91 AL-----HQPAGASSEAV-------EQLLAQLAeALGLEDK-LSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1863768389 166 DEPTNNLDSGARA---RLYAALTSwRGQAIVVS-HD 197
Cdd:COG4138 158 DEPMNSLDVAQQAaldRLLRELCQ-QGITVVMSsHD 192
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
351-505 |
1.92e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV----SLRVPYRLLPQRLqllddrDSVLA-AVSR---LAPTA 422
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrngKLRIGYVPQKLYL------DTTLPlTVNRflrLRPGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 423 DDNQLRAELARF----LLDAdtiarPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYRG- 497
Cdd:PRK09544 97 KKEDILPALKRVqaghLIDA-----PMQKLSGGETQRVLLARALLNR--PQLLVLDEPTQGVDVNGQVALYDLIDQLRRe 169
|
170
....*....|.
gi 1863768389 498 ---ALLVASHD 505
Cdd:PRK09544 170 ldcAVLMVSHD 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
341-492 |
2.16e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD-------SVLA 413
Cdd:COG1132 352 DRPVLKD---ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI--------------DGVDirdltleSLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 414 AVS-----------------RLA-PTADDNQLR--AELARFlldADTIAR-------PVG----TLSGGERFRATLAALL 462
Cdd:COG1132 415 QIGvvpqdtflfsgtireniRYGrPDATDEEVEeaAKAAQA---HEFIEAlpdgydtVVGergvNLSGGQRQRIAIARAL 491
|
170 180 190
....*....|....*....|....*....|
gi 1863768389 463 LSEPPpqLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:COG1132 492 LKDPP--ILILDEATSALDTETEALIQEAL 519
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-184 |
2.22e-13 |
|
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: 69.67 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 20 AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpeRV-GYLPqhlvlqSDRTVADVLGIEAVLAALAT 97
Cdd:cd03267 36 ALKGISFTIEKgEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV----RVaGLVP------WKRRKKFLRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 98 IdagqgqpadfevvgdQWDLPDR-SIAMLARF-------------GFAD-LDLRR----PIGTLSGGEVILLALAAQFLS 158
Cdd:cd03267 106 L---------------WWDLPVIdSFYLLAAIydlpparfkkrldELSElLDLEElldtPVRQLSLGQRMRAEIAAALLH 170
|
170 180
....*....|....*....|....*.
gi 1863768389 159 EPDLLLLDEPTNNLDSGARARLYAAL 184
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFL 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-512 |
2.64e-13 |
|
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: 72.14 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAG--ELMPTRGS-------------VSRPERVG--------------------------- 68
Cdd:TIGR03269 27 EVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRiiyhvalcekcgyVERPSKVGepcpvcggtlepeevdfwnlsdklrrr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 69 -------YLPQHLVLQSDRTVadvlgIEAVLAALATIdagqGQPADfEVVGDQWDLPD-----RSIAMLARfgfadldlr 136
Cdd:TIGR03269 107 irkriaiMLQRTFALYGDDTV-----LDNVLEALEEI----GYEGK-EAVGRAVDLIEmvqlsHRITHIAR--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 137 rpigTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALtswrgQAIVVSHDRDLLdLVQHMAEMRAggit 216
Cdd:TIGR03269 168 ----DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNAL-----EEAVKASGISMV-LTSHWPEVIE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 217 ffggnftaftdalaveqeaaargvraaesdlkrqqrELAEARIKLDRrqrfarsqaGNVPKIvagakkGTA-EVSAGKLR 295
Cdd:TIGR03269 234 ------------------------------------DLSDKAIWLEN---------GEIKEE------GTPdEVVAVFME 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 296 GghqadvadarrrleeaEERVRDDDSIEVdlsrtsvppGRDIVVTENL----------VLRNGAVVSLHIRGPERVGLVG 365
Cdd:TIGR03269 263 G----------------VSEVEKECEVEV---------GEPIIKVRNVskryisvdrgVVKAVDNVSLEVKEGEIFGIVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 366 PNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSV------LAAVSRLAP--TADDN-------QLRAE 430
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAkryigiLHQEYDLYPhrTVLDNlteaiglELPDE 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 431 LARflLDADTIARPVG---------------TLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQY 495
Cdd:TIGR03269 398 LAR--MKAVITLKMVGfdeekaeeildkypdELSEGERHRVALAQVLIKE--PRIVILDEPTGTMDPITKVDVTHSILKA 473
|
570 580
....*....|....*....|.
gi 1863768389 496 RGAL----LVASHDDAFLSEL 512
Cdd:TIGR03269 474 REEMeqtfIIVSHDMDFVLDV 494
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
342-482 |
2.81e-13 |
|
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: 69.29 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrLLPQRLQLLDDRD------------ 409
Cdd:cd03299 12 EFKLKN---VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN----GKDITNLPPEKRDisyvpqnyalfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 --SVLAAVS-----RLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDL 482
Cdd:cd03299 85 hmTVYKNIAyglkkRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN--PKILLLDEPFSALDV 162
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-196 |
2.89e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.12 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 4 SVVCSDLWFAWPSGELAIAGLT-CAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGY 69
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISlTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdltleSLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 70 LPQHLVLQSDrTVADVLGI-------EAVLAALATIDAG---QGQPADFE-VVGDQwdlpdrsiamlarfGfadldlrrp 138
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYgrpdatdEEVEEAAKAAQAHefiEALPDGYDtVVGER--------------G--------- 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 139 iGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ--AIVVSH 196
Cdd:COG1132 475 -VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
29-201 |
2.96e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPE--RVGYLPQHLVLqsDRTVAdvLGIEAVLAALATIDAGQGQPA 106
Cdd:PRK09544 29 PGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKLYL--DTTLP--LTVNRFLRLRPGTKKEDILPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 107 dfevvgdqwdlpdrsiamLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTS 186
Cdd:PRK09544 105 ------------------LKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQ 165
|
170
....*....|....*....
gi 1863768389 187 WRGQ----AIVVSHDRDLL 201
Cdd:PRK09544 166 LRREldcaVLMVSHDLHLV 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-196 |
3.40e-13 |
|
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: 68.67 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 24 LTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPER-VGYLPQhlvlqSDRTVADVLGIEAVLAALA---TI 98
Cdd:cd03298 17 FDLTFAQgEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdVTAAPP-----ADRPVSMLFQENNLFAHLTveqNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 DAGQGQPADFEVVGDQwdlpdRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:cd03298 92 GLGLSPGLKLTAEDRQ-----AIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180
....*....|....*....|..
gi 1863768389 179 RLYAALTSWRGQ----AIVVSH 196
Cdd:cd03298 166 EMLDLVLDLHAEtkmtVLMVTH 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-215 |
3.76e-13 |
|
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: 71.76 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------------SRPER-VGYLPQHLVLQSDRTVADVLgIEA 90
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpdgrGRAKRyIGILHQEYDLYPHRTVLDNL-TEA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 91 VlaalatidagqgqpadfevvgdQWDLPD-----RSIAMLARFGFADLD----LRRPIGTLSGGEVILLALAAQFLSEPD 161
Cdd:TIGR03269 390 I----------------------GLELPDelarmKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 162 LLLLDEPTNNLDSGARARLYAALTSWR---GQA-IVVSHDRD-LLDLVQHMAEMRAGGI 215
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAReemEQTfIIVSHDMDfVLDVCDRAALMRDGKI 506
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
35-214 |
3.87e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGeLMP-TRGSVSRP--ERVGYLPQH--LVLQSDRTV------ADVLGIEAVLAALatidagqg 103
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAG-LWPyGSGRIARPagARVLFLPQRpyLPLGTLREAllypatAEAFSDAELREAL-------- 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 104 qpadfEVVGdqwdLPDrsiamLArfgfADLDLRRPIG-TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYA 182
Cdd:COG4178 465 -----EAVG----LGH-----LA----ERLDEEADWDqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
170 180 190
....*....|....*....|....*....|....
gi 1863768389 183 ALTSWRGQAIVVS--HDRDLLDLVQHMAEMRAGG 214
Cdd:COG4178 527 LLREELPGTTVISvgHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
341-505 |
5.19e-13 |
|
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: 68.30 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqRLQLLDDRDSVLAAV----- 415
Cdd:cd03263 14 TKPAVDD---LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--------GYSIRTDRKAARQSLgycpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 -----------------SRL--APTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEP 476
Cdd:cd03263 83 fdalfdeltvrehlrfyARLkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS--VLLLDEP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1863768389 477 TNNLDLDSIRQLTQALTQYRG--ALLVASHD 505
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-209 |
5.22e-13 |
|
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: 68.17 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGS--------VSRP----ERVGYLPQHLVLQSDRTVADVLGIEAVLAala 96
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPrevrRRIGIVFQDLSVDDELTGWENLYIHARLY--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 97 tidagqgqpadfevvGDQWDLPDRSIAMLARFgFADLDLR-RPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:cd03265 102 ---------------GVPGAERRERIDELLDF-VGLLEAAdRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190
....*....|....*....|....*....|....
gi 1863768389 176 ARARLYAALtswrgQAIVVSHDRDLLDLVQHMAE 209
Cdd:cd03265 166 TRAHVWEYI-----EKLKEEFGMTILLTTHYMEE 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-219 |
6.18e-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: 68.07 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 14 WPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMP---TRGSV-------SR---PERVGYLPQHLVLQSD 79
Cdd:cd03234 16 WNKYARILNDVSLHVESgQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIlfngqprKPdqfQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 80 RTVADVLGIEAVLAALATIDAGQGQPADfevvgdqwdlPDRSIAMLArfgfaDLDLRRP-IGTLSGGEVILLALAAQFLS 158
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAIRKKRV----------EDVLLRDLA-----LTRIGGNlVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 159 EPDLLLLDEPTNNLDSGARARLYAAL--TSWRGQAIVVS-HD--RDLLDLVQHMAEMRAGGITFFG 219
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLsqLARRNRIVILTiHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-219 |
6.81e-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: 68.36 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 14 WPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------RPER-----VGYLPQHLVL 76
Cdd:cd03256 10 YPNGKKALKDVSLSINPgEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgKALRqlrrqIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 77 QSDRTVadvlgIEAVL-AALATIDAGQGQPADFEVVGDQwdlpdRSIAMLARFGFADLDLRRpIGTLSGGEVILLALAAQ 155
Cdd:cd03256 90 IERLSV-----LENVLsGRLGRRSTWRSLFGLFPKEEKQ-----RALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 156 FLSEPDLLLLDEPTNNLD---SGARARLYAALTSWRGQAIVVS-HDRDL-LDLVQHMAEMRAGGITFFG 219
Cdd:cd03256 159 LMQQPKLILADEPVASLDpasSRQVMDLLKRINREEGITVIVSlHQVDLaREYADRIVGLKDGRIVFDG 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
351-504 |
1.14e-12 |
|
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: 70.08 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllPQRLQLLDDRDSVLAAVS-------------- 416
Cdd:TIGR02868 354 VSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL-------DGVPVSSLDQDEVRRRVSvcaqdahlfdttvr 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 ---RLA-PTADDNQLRAELARFLLDADTIARPVG----------TLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDL 482
Cdd:TIGR02868 427 enlRLArPDATDEELWAALERVGLADWLRALPDGldtvlgeggaRLSGGERQRLALARALLADAP--ILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*
gi 1863768389 483 DSIRQLTQAL---TQYRGALLVASH 504
Cdd:TIGR02868 505 ETADELLEDLlaaLSGRTVVLITHH 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-195 |
1.23e-12 |
|
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: 67.39 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 19 LAIAGLT-CAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGS--------VSRP----ERVGYLPQHLVLQSDRTVADV 85
Cdd:cd03266 19 QAVDGVSfTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdvVKEPaearRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIEAVLAALatidAGQGQPADFEVVGDqwdlpdrsiamlaRFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLL 165
Cdd:cd03266 99 LEYFAGLYGL----KGDELTARLEELAD-------------RLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 166 DEPTNNLDSGARARLYAALTSWR--GQAIVVS 195
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRalGKCILFS 192
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
339-504 |
1.26e-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: 66.78 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 339 VTENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRG--EIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaVS 416
Cdd:cd03217 10 VGGKEILKG---VNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILF--------------KGED-----IT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 RLAPTaddnqLRAELARFLLDADTIA----------RPVG-TLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSI 485
Cdd:cd03217 68 DLPPE-----ERARLGIFLAFQYPPEipgvknadflRYVNeGFSGGEKKRNEILQLLLLEP--DLAILDEPDSGLDIDAL 140
|
170 180
....*....|....*....|..
gi 1863768389 486 RQLTQALTQYRG---ALLVASH 504
Cdd:cd03217 141 RLVAEVINKLREegkSVLIITH 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-215 |
1.33e-12 |
|
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: 66.09 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQHLVLQSDrTVADVLgieavlaal 95
Cdd:cd03246 27 PGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwdpnELGDHVGYLPQDDELFSG-SIAENI--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 atidagqgqpadfevvgdqwdlpdrsiamlarfgfadldlrrpigtLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:cd03246 97 ----------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 176 ARARLYAALTSWRGQ---AIVVSHDRDLLDLVQHMAEMRAGGI 215
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
344-512 |
1.46e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDD---RDSVLAAVSRLAp 420
Cdd:COG2401 45 VLRD---LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAigrKGDFKDAVELLN- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 taddnqlRAELArfllDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSI----RQLTQALTQYR 496
Cdd:COG2401 121 -------AVGLS----DAVLWLRRFKELSTGQKFRFRLALLLAER--PKLLVIDEFCSHLDRQTAkrvaRNLQKLARRAG 187
|
170
....*....|....*.
gi 1863768389 497 GALLVASHDDAFLSEL 512
Cdd:COG2401 188 ITLVVATHHYDVIDDL 203
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-219 |
1.64e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 68.99 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 32 VTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------------RPE--RVGYLPQHLVLQSDRTVADVL--GIEAVL 92
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgiflPPEkrRIGYVFQEARLFPHLSVRGNLryGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 93 AALATIDagqgqpadfevvgdqwdlPDRSIAMLarfGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNL 172
Cdd:TIGR02142 105 PSERRIS------------------FERVIELL---GIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 173 DSGARARLYAALTSWRGQ----AIVVSHDrdlLDLVQHMAE----MRAGGITFFG 219
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEfgipILYVSHS---LQEVLRLADrvvvLEDGRVAAAG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
351-506 |
1.65e-12 |
|
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: 66.66 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL-----------RVPYRLLPQRLQLLDDR--------DSV 411
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVngqdvsdlrgrAIPYLRRKIGVVFQDFRllpdrnvyENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 LAA--VSRLAPTADDNQLRAELARFLLDADTIARPVGtLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLT 489
Cdd:cd03292 100 AFAleVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIM 176
|
170 180
....*....|....*....|
gi 1863768389 490 QALTQY--RGA-LLVASHDD 506
Cdd:cd03292 177 NLLKKInkAGTtVVVATHAK 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-206 |
1.65e-12 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 66.48 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIageLMPTRGSVSRPERVGylpQHLvlqsdrtvADVLGIEAVLAA--LATIDAGQGqp 105
Cdd:cd03240 20 FFSPLTLIVGQNGAGKTTIIEAL---KYALTGELPPNSKGG---AHD--------PKLIREGEVRAQvkLAFENANGK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 106 aDFEVVgdqwdlpdRSIAML-----ARFGFADLDLRRPIGTLSGGEVIL------LALAAQFLSEPDLLLLDEPTNNLDS 174
Cdd:cd03240 84 -KYTIT--------RSLAILenvifCHQGESNWPLLDMRGRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1863768389 175 GAR----ARLYAALTSWRG-QAIVVSHDRDLLDLVQH 206
Cdd:cd03240 155 ENIeeslAEIIEERKSQKNfQLIVITHDEELVDAADH 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
362-481 |
2.48e-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: 66.06 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 362 GLVGPNGSGKTTLIDTIRGEIEPRSGTV------------SLR-----VPYRLLPQRLQLLDDRDSVLAAVSRLAPTADD 424
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlkqpqKLRrrigyLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVK 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 425 NQLRAELARFLLdADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:cd03264 109 ARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD--PSILIVDEPTAGLD 162
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
344-510 |
2.69e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 66.22 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD------SVLAAVSR 417
Cdd:COG1136 23 ALRG---VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI--------------DGQDisslseRELARLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 418 -----------LAP--TADDN------------QLRAELARFLLD----ADTIARPVGTLSGGERFRATLAALLLSEPPp 468
Cdd:COG1136 86 rhigfvfqffnLLPelTALENvalplllagvsrKERRERARELLErvglGDRLDHRPSQLSGGQQQRVAIARALVNRPK- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1863768389 469 qLLILDEPTNNLDLDS----IRQLTQALTQYRGALLVASHDDAFLS 510
Cdd:COG1136 165 -LILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAA 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
341-515 |
2.77e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENL-VLRNGAVV----SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrlqLLDDRDSVLAAV 415
Cdd:PRK13539 6 EDLaCVRGGRVLfsglSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD-----------GGDIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 SRLAPTAD----------------------DNQLRAELARFLLdADTIARPVGTLSGGERFRATLAALLLSEPPpqLLIL 473
Cdd:PRK13539 75 CHYLGHRNamkpaltvaenlefwaaflggeELDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRP--IWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1863768389 474 DEPTNNLDLDSIRQLTQALTQYR---GALLVASHddaflSELGLT 515
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLaqgGIVIAATH-----IPLGLP 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
351-494 |
3.27e-12 |
|
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: 66.44 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLD---------------DRDSVLAAV 415
Cdd:cd03256 20 VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqigmifqqfnliERLSVLENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 --SRLA------------PTADDNQLRAELARFLLdADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:cd03256 100 lsGRLGrrstwrslfglfPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQ--PKLILADEPVASLD 176
|
170
....*....|...
gi 1863768389 482 LDSIRQLTQALTQ 494
Cdd:cd03256 177 PASSRQVMDLLKR 189
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-204 |
3.42e-12 |
|
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: 65.92 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGELaiagltcafpdqvTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---------------------R 63
Cdd:COG4778 25 PVLDGVSFSVAAGEC-------------VALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqaspreilalR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 64 PERVGYLPQHLvlqsdRTVADVLGIEAVLAALatIDAGQGQPADFEvvgdqwdlpdRSIAMLARFGfadLDLRR---PIG 140
Cdd:COG4778 92 RRTIGYVSQFL-----RVIPRVSALDVVAEPL--LERGVDREEARA----------RARELLARLN---LPERLwdlPPA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 141 TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARAR---LYAALTSwRGQAIV-VSHDRDLLDLV 204
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvveLIEEAKA-RGTAIIgIFHDEEVREAV 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-505 |
3.64e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSrpervgyLPQHLVLQSDRTVADVLGIEAV---------LAALATI 98
Cdd:PRK15439 35 HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE-------IGGNPCARLTPAKAHQLGIYLVpqepllfpnLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 DAGQGQPADFEvvgdqwdlpDRSIAMLARFGfADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:PRK15439 108 LFGLPKRQASM---------QKMKQLLAALG-CQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 179 RLYAALTSWR--GQAIV-VSHD-RDLLDLVQHMAEMRAGGITFFGGNFTAFTDALAveqEAAARGVRAAEsdlkrqqrel 254
Cdd:PRK15439 178 RLFSRIRELLaqGVGIVfISHKlPEIRQLADRISVMRDGTIALSGKTADLSTDDII---QAITPAAREKS---------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 255 aearikLDRRQRFARSQAGNvpkivagakkgtaevsagklrgghqadvadarrrleeaeervrdddsievdlsRTSVPPG 334
Cdd:PRK15439 245 ------LSASQKLWLELPGN-----------------------------------------------------RRQQAAG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 335 RDIVVTENLVLRNGAVVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLD-------- 406
Cdd:PRK15439 266 APVLTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvylpe 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 407 DR-------DSVLA------AVSRLAPTADDNQLRAELARF-------LLDADtiaRPVGTLSGGERFRATLAALLlsEP 466
Cdd:PRK15439 346 DRqssglylDAPLAwnvcalTHNRRGFWIKPARENAVLERYrralnikFNHAE---QAARTLSGGNQQKVLIAKCL--EA 420
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1863768389 467 PPQLLILDEPTNNLDLDS---IRQLTQALTQYRGALLVASHD 505
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSD 462
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-506 |
3.80e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 36 VGRNGVGKSTLLKIIAGELMPTRG----SVSRPERVGYLP-QHLVLQS-DRTVADVLGIEavlaalatidagqgqPADF- 108
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGerqsQFSHITRLSFEQlQKLVSDEwQRNNTDMLSPG---------------EDDTg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 109 ----EVVGDQWDLPDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAAL 184
Cdd:PRK10938 100 rttaEIIQDEVKDPARCEQLAQQFGITAL-LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 185 TSW--RGQAIVVSHDR--DLLDLVQHMAEMRAGGITFFGGNFTAFTDALaVEQEA---AARGVRAAESDLKRQQRELAEa 257
Cdd:PRK10938 179 ASLhqSGITLVLVLNRfdEIPDFVQFAGVLADCTLAETGEREEILQQAL-VAQLAhseQLEGVQLPEPDEPSARHALPA- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 258 rikldrrqrfarsqagNVPKIVagakkgtaevsagkLRGGhqadvadarrrleeaeeRVR-DDDSIEVDLSRTsVPPGrd 336
Cdd:PRK10938 257 ----------------NEPRIV--------------LNNG-----------------VVSyNDRPILHNLSWQ-VNPG-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 337 ivvtenlvlrngavvslhirgpERVGLVGPNGSGKTTLIDTIRG------------------------EIEPRSGTVS-- 390
Cdd:PRK10938 287 ----------------------EHWQIVGPNGAGKSTLLSLITGdhpqgysndltlfgrrrgsgetiwDIKKHIGYVSss 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 391 ----LRVPYRLLPQRLQLLDDRDSVLAAVSrlaptaDDNQLRAE--LARFLLDADTIARPVGTLSGGERFRATLAALLLS 464
Cdd:PRK10938 345 lhldYRVSTSVRNVILSGFFDSIGIYQAVS------DRQQKLAQqwLDILGIDKRTADAPFHSLSWGQQRLALIVRALVK 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1863768389 465 EPPpqLLILDEPTNNLD-LDsiRQLT-----QALTQYRGALLVASHDD 506
Cdd:PRK10938 419 HPT--LLILDEPLQGLDpLN--RQLVrrfvdVLISEGETQLLFVSHHA 462
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
355-481 |
4.32e-12 |
|
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: 66.28 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 355 IRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSVLAAVSRLAPTA-DDNQLRAELAR 433
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFyTHPYFKTEIAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1863768389 434 FLLDADTIARPVGTLSGGERFRATLAALLLSepPPQLLILDEPTNNLD 481
Cdd:cd03237 102 PLQIEQILDREVPELSGGELQRVAIAACLSK--DADIYLLDEPSAYLD 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
31-512 |
4.65e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---RPER-----------VGYLPQHLVLQSDRTVAD--VLGIEAVLAA 94
Cdd:COG3845 32 EIHALLGENGAGKSTLMKILYGLYQPDSGEILidgKPVRirsprdaialgIGMVHQHFMLVPNLTVAEniVLGLEPTKGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LATIDAgqgqpadfevvgdqwdLPDRSIAMLARFGFaDLDLRRPIGTLSGGE---V-ILLALaaqfLSEPDLLLLDEPTN 170
Cdd:COG3845 112 RLDRKA----------------ARARIRELSERYGL-DVDPDAKVEDLSVGEqqrVeILKAL----YRGARILILDEPTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 171 NLDSGARARLYAALTSWR--GQAIV-VSHDrdlLDLVQHMAE----MRAGgitffggnftaftdalaveqEAAARGVRAA 243
Cdd:COG3845 171 VLTPQEADELFEILRRLAaeGKSIIfITHK---LREVMAIADrvtvLRRG--------------------KVVGTVDTAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 244 ESdlkrqQRELAEARIkldrrqrfarsqagnvpkivagakkgtaevsagklrgGHqadvadarrrleeaeervrdddSIE 323
Cdd:COG3845 228 TS-----EEELAELMV-------------------------------------GR----------------------EVL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 324 VDLSRTSVPPGRDIVVTENLVLRN--GAV----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL------ 391
Cdd:COG3845 244 LRVEKAPAEPGEVVLEVENLSVRDdrGVPalkdVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdgedit 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 392 -------------RVPyrllpqrlqllDDRDSVlAAVSRLapTADDN-----QLRAELAR-FLLDADTIAR--------- 443
Cdd:COG3845 324 glsprerrrlgvaYIP-----------EDRLGR-GLVPDM--SVAENlilgrYRRPPFSRgGFLDRKAIRAfaeelieef 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 444 ---------PVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYR---GALLVASHDdafLSE 511
Cdd:COG3845 390 dvrtpgpdtPARSLSGGNQQKVILARELSRD--PKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLISED---LDE 464
|
.
gi 1863768389 512 L 512
Cdd:COG3845 465 I 465
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-204 |
5.28e-12 |
|
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: 68.89 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 15 PSGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV------------SRPERVGYLPQHLVLQSDRT 81
Cdd:TIGR01257 940 PSGRPAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnldAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 82 VADVLGIEAVLAalatidagqgqpadfevvGDQWDlpDRSIAMLARFGFADLDLRR--PIGTLSGGEVILLALAAQFLSE 159
Cdd:TIGR01257 1020 VAEHILFYAQLK------------------GRSWE--EAQLEMEAMLEDTGLHHKRneEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1863768389 160 PDLLLLDEPTNNLDSGARARLYAALTSWR-GQAIVVS-HDRDLLDLV 204
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRsGRTIIMStHHMDEADLL 1126
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
29-199 |
5.96e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.09 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS------------RPERVGYLPQHLVLQSDRTVAD--VLGIEAVLAA 94
Cdd:COG1118 27 SGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlppRERRVGFVFQHYALFPHMTVAEniAFGLRVRPPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LATIDAgqgqpadfeVVgDQWdlpdrsiamLARFGFADLDLRRPiGTLSGGE---VILL-ALAAqflsEPDLLLLDEPTN 170
Cdd:COG1118 107 KAEIRA---------RV-EEL---------LELVQLEGLADRYP-SQLSGGQrqrVALArALAV----EPEVLLLDEPFG 162
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 171 NLDSGARARLYAALTS----WRGQAIVVSHDRD 199
Cdd:COG1118 163 ALDAKVRKELRRWLRRlhdeLGGTTVFVTHDQE 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
360-509 |
6.07e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 360 RVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL----RVPYRLlpqrlqllddRD-------SVLAAV------------- 415
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpneRLGKLR----------QDqfafeefTVLDTVimghtelwevkqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 -----SRLAPTADDNQLRAEL-ARF---------------LLDADTiarPV----GTLSG---GERFRATLAALLLSEPp 467
Cdd:PRK15064 99 rdriyALPEMSEEDGMKVADLeVKFaemdgytaearagelLLGVGI---PEeqhyGLMSEvapGWKLRVLLAQALFSNP- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1863768389 468 pQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFL 509
Cdd:PRK15064 175 -DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
351-505 |
6.07e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV---------------SLRVPYRLLPQRLQLLDDRDSVLAA- 414
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvealsaraaSRRVASVPQDTSLSFEFDVRQVVEMg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 415 ----VSRLAPTADDNQLRAELARFLLDADTIA-RPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLD-SIR-- 486
Cdd:PRK09536 102 rtphRSRFDTWTETDRAAVERAMERTGVAQFAdRPVTSLSGGERQRVLLARALAQATP--VLLLDEPTASLDINhQVRtl 179
|
170
....*....|....*....
gi 1863768389 487 QLTQALTQYRGALLVASHD 505
Cdd:PRK09536 180 ELVRRLVDDGKTAVAAIHD 198
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
351-495 |
6.52e-12 |
|
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: 65.37 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEpRSGTVSLRVPYRLLPQRLQLLDDRDSVL------------------ 412
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSGQILFNGQPRKPDQFQKCVAYVrqddillpgltvretlty 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 413 AAVSRLAPTADDNQLRAELARFLLD--ADTIARP--VGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQL 488
Cdd:cd03234 105 TAILRLPRKSSDAIRKKRVEDVLLRdlALTRIGGnlVKGISGGERRRVSIAVQLLWD--PKVLILDEPTSGLDSFTALNL 182
|
....*..
gi 1863768389 489 TQALTQY 495
Cdd:cd03234 183 VSTLSQL 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
31-213 |
8.94e-12 |
|
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: 63.75 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-------------RPER--VGYLPQHLVLQSDRTVADvlgieavlaal 95
Cdd:cd03229 27 EIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltdledelPPLRrrIGMVFQDFALFPHLTVLE----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 atidagqgqpadfevvgdqwdlpdrSIAMLarfgfadldlrrpigtLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:cd03229 96 -------------------------NIALG----------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1863768389 176 ARARLYAALTSWRGQA----IVVSHDrdlLDLVQHMAE----MRAG 213
Cdd:cd03229 135 TRREVRALLKSLQAQLgitvVLVTHD---LDEAARLADrvvvLRDG 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-512 |
9.15e-12 |
|
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: 64.62 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 359 ERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--RVPYRLLPQRLQLLDDR------------------DSVLAAVSRL 418
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngTVLFDSRKKINLPPQQRkiglvfqqyalfphlnvrENLAFGLKRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 APTADDNQLRAELARFLLDaDTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD----LDSIRQLTQALTQ 494
Cdd:cd03297 104 RNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQ--PELLLLDEPFSALDralrLQLLPELKQIKKN 180
|
170
....*....|....*...
gi 1863768389 495 YRGALLVASHDdafLSEL 512
Cdd:cd03297 181 LNIPVIFVTHD---LSEA 195
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-199 |
9.91e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 66.27 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPER--VGYLPQHLVLQSDRTVAD--VLGIEAvlaalatidag 101
Cdd:COG3842 36 LLGPSGCGKTTLLRMIAGFETPDSGRILldgrdvtglPPEKrnVGMVFQDYALFPHLTVAEnvAFGLRM----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 QGQPADfevvgdqwDLPDRSIAMLARFGFADLDLRRPiGTLSGGE---VillALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:COG3842 105 RGVPKA--------EIRARVAELLELVGLEGLADRYP-HQLSGGQqqrV---ALARALAPEPRVLLLDEPLSALDAKLRE 172
|
170 180
....*....|....*....|....*
gi 1863768389 179 RLYAALTSWRGQ----AIVVSHDRD 199
Cdd:COG3842 173 EMREELRRLQRElgitFIYVTHDQE 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-173 |
1.08e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVsrpeRV-GYLPQhlvlqsDRTVADVLGIEAVLaalatidaGQGQ-------P 105
Cdd:COG4586 52 GFIGPNGAGKSTTIKMLTGILVPTSGEV----RVlGYVPF------KRRKEFARRIGVVF--------GQRSqlwwdlpA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 106 AD-FEVVGDQWDLPD----RSIAMLA-RFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:COG4586 114 IDsFRLLKAIYRIPDaeykKRLDELVeLLDLGEL-LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-477 |
1.09e-11 |
|
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: 64.38 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaVSRLAP--- 420
Cdd:cd03224 15 ILFG---VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF--------------DGRD-----ITGLPPher 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 ------------------TADDNQLRAELARFLLDADTI---------------ARPVGTLSGGERFRATLAALLLSEpp 467
Cdd:cd03224 73 aragigyvpegrrifpelTVEENLLLGAYARRRAKRKARlervyelfprlkerrKQLAGTLSGGEQQMLAIARALMSR-- 150
|
170
....*....|
gi 1863768389 468 PQLLILDEPT 477
Cdd:cd03224 151 PKLLLLDEPS 160
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
363-518 |
1.10e-11 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 64.17 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIR----GEIEPRSgtvslrvpyrllpqrlQLLDDRDSVLAAVSRLA--------PTADDNQLRAE 430
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNS----------------KGGAHDPKLIREGEVRAqvklafenANGKKYTITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 431 LARFLL-------DADT-IARPVGTLSGGERFRATLA-ALLLSE---PPPQLLILDEPTNNLDLDSIR-QLTQALTQYRG 497
Cdd:cd03240 91 LAILENvifchqgESNWpLLDMRGRCSGGEKVLASLIiRLALAEtfgSNCGILALDEPTTNLDEENIEeSLAEIIEERKS 170
|
170 180
....*....|....*....|....*
gi 1863768389 498 A----LLVASHDDAFLSELGLTYRI 518
Cdd:cd03240 171 QknfqLIVITHDEELVDAADHIYRV 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-196 |
1.15e-11 |
|
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: 63.22 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpervgylpqhlvlqsdrtvadvlgieavlaalaTIDagqGQPADFEV 110
Cdd:cd03216 27 EVHALLGENGAGKSTLMKILSGLYKPDSGEI-----------------------------------LVD---GKEVSFAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 111 VGDQWDLPdrsIAMlarfgfadldlrrpIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWR-- 188
Cdd:cd03216 69 PRDARRAG---IAM--------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaq 131
|
....*....
gi 1863768389 189 GQAIV-VSH 196
Cdd:cd03216 132 GVAVIfISH 140
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
29-199 |
1.15e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMP---TRGSV-----------SRPERVGYLPQHLVLQSDRTVADVLGieavLAA 94
Cdd:COG4136 26 PGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVllngrrltalpAEQRRIGILFQDDLLFPHLSVGENLA----FAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LATIDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDS 174
Cdd:COG4136 102 PPTIGRAQRR--------------ARVEQALEEAGLAGFADRDP-ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*....
gi 1863768389 175 GARARL----YAALTSWRGQAIVVSHDRD 199
Cdd:COG4136 167 ALRAQFrefvFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
338-488 |
1.40e-11 |
|
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: 62.83 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 338 VVTENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRdsvl 412
Cdd:cd03216 1 LELRGITKRFGGVkaldgVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------DGK---- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 413 aAVSRLAPtaddnqlraelarflldADTIARPVGT---LSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQL 488
Cdd:cd03216 63 -EVSFASP-----------------RDARRAGIAMvyqLSVGERQMVEIARALARN--ARLLILDEPTAALTPAEVERL 121
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
340-502 |
1.65e-11 |
|
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: 64.17 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVLAAVSRL- 418
Cdd:cd03251 13 DGPPVLRD---ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-----------DGHDVRDYTLASLRRQi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 ---------------------APTADDNQLR--AELA-------RFLLDADTIARPVG-TLSGGERFRATLAALLLSEPP 467
Cdd:cd03251 79 glvsqdvflfndtvaeniaygRPGATREEVEeaARAAnahefimELPEGYDTVIGERGvKLSGGQRQRIAIARALLKDPP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 468 pqLLILDEPTNNLDLDSIRQLTQA---LTQYRGALLVA 502
Cdd:cd03251 159 --ILILDEATSALDTESERLVQAAlerLMKNRTTFVIA 194
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
344-505 |
2.25e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSVLAAVSR---LAP 420
Cdd:PRK11629 24 VLHN---VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQfhhLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 --TADDN---------------QLRAE--LARFLLDADTIARPvGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLD 481
Cdd:PRK11629 101 dfTALENvamplligkkkpaeiNSRALemLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNP--RLVLADEPTGNLD 177
|
170 180
....*....|....*....|....*...
gi 1863768389 482 L---DSIRQLTQALTQYRG-ALLVASHD 505
Cdd:PRK11629 178 ArnaDSIFQLLGELNRLQGtAFLVVTHD 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
340-504 |
2.25e-11 |
|
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: 63.45 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR---VPYRLLPQRLQLLDDR--- 408
Cdd:cd03269 3 VENVTKRFGRVtalddISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkpLDIAARNRIGYLPEERgly 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 409 ------DSV--LAAVSRLAPTADDNQLRAELARFLLdADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNL 480
Cdd:cd03269 83 pkmkviDQLvyLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDP--ELLILDEPFSGL 159
|
170 180
....*....|....*....|....*..
gi 1863768389 481 DLDSIRQLTQALTQYRGA---LLVASH 504
Cdd:cd03269 160 DPVNVELLKDVIRELARAgktVILSTH 186
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
338-488 |
2.46e-11 |
|
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: 63.54 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 338 VVTENLVLRNG---AV--VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVS------LRVPYRLLPQRLQLLD 406
Cdd:cd03265 1 IEVENLVKKYGdfeAVrgVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 407 DR--DSVLAAVSRLA--------PTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEP 476
Cdd:cd03265 81 DLsvDDELTGWENLYiharlygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR--PEVLFLDEP 158
|
170
....*....|..
gi 1863768389 477 TNNLDLDSIRQL 488
Cdd:cd03265 159 TIGLDPQTRAHV 170
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
351-504 |
3.19e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 63.45 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD--------------------- 409
Cdd:TIGR04406 20 VSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI--------------DGQDithlpmherarlgigylpqea 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ------SV---LAAVSRLAPTADDNQlRAELARFLLDADTIAR----PVGTLSGGERFRATLAALLLSEppPQLLILDEP 476
Cdd:TIGR04406 86 sifrklTVeenIMAVLEIRKDLDRAE-REERLEALLEEFQISHlrdnKAMSLSGGERRRVEIARALATN--PKFILLDEP 162
|
170 180 190
....*....|....*....|....*....|.
gi 1863768389 477 TNNLD---LDSIRQLTQALTQYRGALLVASH 504
Cdd:TIGR04406 163 FAGVDpiaVGDIKKIIKHLKERGIGVLITDH 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-197 |
3.20e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGeLMPTRGSV----------SRPE---RVGYLPQHlvlqsDRTVADVlgieAVLAALATIDAG 101
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIqfagqpleawSAAElarHRAYLSQQ-----QTPPFAM----PVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 QGQPADFEVVGDQwdlpdrsiaMLARFGFADLdLRRPIGTLSGGEVILLALAAQFL-----SEPD--LLLLDEPTNNLDS 174
Cdd:PRK03695 97 KTRTEAVASALNE---------VAEALGLDDK-LGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 1863768389 175 GARARLYAALTSWRGQAIVV---SHD 197
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVvmsSHD 192
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
23-219 |
4.53e-11 |
|
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: 62.90 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 23 GLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE------RVGYLPQHLVLQSDRTVADV 85
Cdd:cd03261 18 GVDLDVRRgEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglSEAElyrlrrRMGMLFQSGALFDSLTVFEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIeavlaalatidagqgqPADFEVVGDQWDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLL 165
Cdd:cd03261 98 VAF----------------PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 166 DEPTNNLD---SGARARLYA------ALTSwrgqaIVVSHDRD-LLDLVQHMAEMRAGGITFFG 219
Cdd:cd03261 161 DEPTAGLDpiaSGVIDDLIRslkkelGLTS-----IMVTHDLDtAFAIADRIAVLYDGKIVAEG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-216 |
4.84e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.91 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------------RPERVGYLPQ--HLVlqsdrtvADVLGIE 89
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpmsklssaakaelRNQKLGFIYQfhHLL-------PDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 90 AVLAALATidaGQGQPADFEvvgdqwdlpDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPT 169
Cdd:PRK11629 107 NVAMPLLI---GKKKPAEIN---------SRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 170 NNLD---SGARARLYAALTSWRGQA-IVVSHDRDLLDLVQHMAEMRAGGIT 216
Cdd:PRK11629 174 GNLDarnADSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-175 |
5.51e-11 |
|
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: 61.80 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 27 AFPDQVTGLVGRNGVGKSTLLKIIAGELMP--TRGSV---SRPE-------RVGYLPQHLVLQSDRTVADVLGIEAVLaa 94
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlinGRPLdkrsfrkIIGYVPQDDILHPTLTVRETLMFAAKL-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 latidagqgqpadfevvgdqwdlpdRSIamlarfgfadldlrrpigtlSGGEVILLALAAQFLSEPDLLLLDEPTNNLDS 174
Cdd:cd03213 110 -------------------------RGL--------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
.
gi 1863768389 175 G 175
Cdd:cd03213 145 S 145
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-491 |
6.15e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.59 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 337 IVVTENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpQRLQLLDDRD-- 409
Cdd:COG4152 1 MLELKGLTKRFGDKtavddVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-------GEPLDPEDRRri 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 -------------SVLAAVSRLA------PTADDNQLRAELARFLLdADTIARPVGTLSGGERFRATLAALLLSEppPQL 470
Cdd:COG4152 74 gylpeerglypkmKVGEQLVYLArlkglsKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHD--PEL 150
|
170 180
....*....|....*....|....*...
gi 1863768389 471 LILDEPTNNLD-------LDSIRQLTQA 491
Cdd:COG4152 151 LILDEPFSGLDpvnvellKDVIRELAAK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-197 |
6.67e-11 |
|
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: 62.20 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 20 AIAGLTCAFP-DQVTGLVGRNGVGKSTLLKIIAG-----ELMPTRGSVSRPERVGYLPQHLVLQSDRTVADVLGIEAVLA 93
Cdd:cd03260 15 ALKDISLDIPkGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 94 A--LATIDAG---QGqpadfevVGDQWDLPDRSIAMLARFGFADLDLRRPIGT-LSGGEVILLALAAQFLSEPDLLLLDE 167
Cdd:cd03260 95 GsiYDNVAYGlrlHG-------IKLKEELDERVEEALRKAALWDEVKDRLHALgLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 168 PTNNLDSGARARLYAALTSWRGQ--AIVVSHD 197
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKEytIVIVTHN 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
316-481 |
7.48e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.70 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 316 VRDDDSIEVDLSRTSVPPGRDIVVTEnlvlrngavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVS-LRVP 394
Cdd:PRK13536 34 PGSMSTVAIDLAGVSKSYGDKAVVNG---------LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 395 YRLLPQRLQLlddRDSVLAAVSRLAP--TADDN-------------QLRA------ELARFLLDADTiarPVGTLSGGER 453
Cdd:PRK13536 105 VPARARLARA---RIGVVPQFDNLDLefTVRENllvfgryfgmstrEIEAvipsllEFARLESKADA---RVSDLSGGMK 178
|
170 180
....*....|....*....|....*...
gi 1863768389 454 FRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:PRK13536 179 RRLTLARALIND--PQLLILDEPTTGLD 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-195 |
7.88e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSR-----PE-------RVGYLPQHLVLQSDRTVADVLGIEAVLAAL 95
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvPSrarharqRVGVVPQFDNLDPDFTVRENLLVFGRYFGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 ATIDAGQGQPADFEvvgdqwdlpdrsiamlarfgFADLDLRR--PIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:PRK13537 111 SAAAARALVPPLLE--------------------FAKLENKAdaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180
....*....|....*....|....
gi 1863768389 174 SGARARLYAALTSW--RGQAIVVS 195
Cdd:PRK13537 171 PQARHLMWERLRSLlaRGKTILLT 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-210 |
8.59e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.63 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGeLMP-TRGSVSRPERVG--YLPQH--LVLQSDRtvadvlgiEAVLAAlatidagqgqpadfe 109
Cdd:cd03223 32 ITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDllFLPQRpyLPLGTLR--------EQLIYP--------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 110 vvgdqWDLpdrsiamlarfgfadldlrrpigTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSwRG 189
Cdd:cd03223 88 -----WDD-----------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE-LG 138
|
170 180
....*....|....*....|..
gi 1863768389 190 QAIV-VSHDRDLLDLVQHMAEM 210
Cdd:cd03223 139 ITVIsVGHRPSLWKFHDRVLDL 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-173 |
1.36e-10 |
|
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: 61.44 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------------RPER--VGYLPQHLVLQSDRTVADVLgieavl 92
Cdd:cd03258 30 KGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKARrrIGMIFQHFNLLSSRTVFENV------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 93 aALAtidagqgqpadFEVVG-DQWDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNN 171
Cdd:cd03258 104 -ALP-----------LEIAGvPKAEIEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
..
gi 1863768389 172 LD 173
Cdd:cd03258 171 LD 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-503 |
1.46e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSrpervgyLPQHLVLQSDRTVADVLGIEAVLAALATIDAGQGQPAD 107
Cdd:PRK09700 29 YPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-------INNINYNKLDHKLAAQLGIGIIYQELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 108 F-------EVVG----DQWDLPDRSIAMLARFGFaDLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGA 176
Cdd:PRK09700 102 YigrhltkKVCGvniiDWREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 177 RARLYAALTSWR--GQAIV-VSHdrdlldlvqHMAEMRAggitfFGGNFTAFTDALAVeqeaAARGVRAAESDlkrqqrE 253
Cdd:PRK09700 181 VDYLFLIMNQLRkeGTAIVyISH---------KLAEIRR-----ICDRYTVMKDGSSV----CSGMVSDVSND------D 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 254 LAEARIKLDRRQRFarsqAGNVPKIVAGAKKGTAEVsagklrgghqadvadarrrleeaeervrdddsievdlsrtsvpp 333
Cdd:PRK09700 237 IVRLMVGRELQNRF----NAMKENVSNLAHETVFEV-------------------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 334 gRDIVVTENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL-------RVPYRLLPQRLQLLD 406
Cdd:PRK09700 269 -RNVTSRDRKKVRD---ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLngkdispRSPLDAVKKGMAYIT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 407 D--RDSVL---------AAVSRLAPTA-----------DDNQLRAELARFLLD--ADTIARPVGTLSGGERFRATLAALL 462
Cdd:PRK09700 345 EsrRDNGFfpnfsiaqnMAISRSLKDGgykgamglfheVDEQRTAENQRELLAlkCHSVNQNITELSGGNQQKVLISKWL 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1863768389 463 LSEppPQLLILDEPTNNLDLDS-------IRQLTQaltQYRGALLVAS 503
Cdd:PRK09700 425 CCC--PEVIIFDEPTRGIDVGAkaeiykvMRQLAD---DGKVILMVSS 467
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-216 |
2.62e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.80 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 21 IAGLTCAFP-DQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV---SRP----------ERVGYLPQHLVLQSDRTVADVL 86
Cdd:PRK11231 18 LNDLSLSLPtGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgDKPismlssrqlaRRLALLPQHHLTPEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 87 --GIEAVLAALatidaGQGQPADFEVVgdQWDLPDRSIAMLArfgfadldlRRPIGTLSGGE---VILLALAAQflsEPD 161
Cdd:PRK11231 98 ayGRSPWLSLW-----GRLSAEDNARV--NQAMEQTRINHLA---------DRRLTDLSGGQrqrAFLAMVLAQ---DTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 162 LLLLDEPTNNLDsgararlyaaltswrgqaivVSHDRDLLDLvqhMAEMRAGGIT 216
Cdd:PRK11231 159 VVLLDEPTTYLD--------------------INHQVELMRL---MRELNTQGKT 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
339-504 |
2.82e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 339 VTENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRG--EIEPRSGTVSLrvpyrllpqrlqllDDRD------- 409
Cdd:COG0396 10 VEGKEILKG---VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILL--------------DGEDilelspd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ---------------------------SVLAAVSRLAPTADD--NQLRAELARFLLDADTIARPV-GTLSGGERFRATLA 459
Cdd:COG0396 73 eraragiflafqypveipgvsvsnflrTALNARRGEELSAREflKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 460 ALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYRG---ALLVASH 504
Cdd:COG0396 153 QMLLLE--PKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITH 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
35-186 |
3.07e-10 |
|
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: 59.68 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSDRTVADVLGIEAVLAALATID--AGQGQPADFEVvg 112
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHfwAAIHGGAQRTI-- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 113 dqWDLpdrsiamLARFGFADLDlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTS 186
Cdd:TIGR01189 109 --EDA-------LAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
320-494 |
3.27e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 320 DSIEVDLSRTSVPPGRDIVVtENLVLR--NGAV----VSLHIRGPERVGLVGPNGSGKTTLIDTI-------RGEIE-PR 385
Cdd:COG4178 346 DALPEAASRIETSEDGALAL-EDLTLRtpDGRPlledLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGRIArPA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 386 SGTVSL--RVPYRLLpqrlqllddrDSVLAAVS--RLAPTADDNQLRAELARFLLDA-----DTIARPVGTLSGGERFRA 456
Cdd:COG4178 425 GARVLFlpQRPYLPL----------GTLREALLypATAEAFSDAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 457 TLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:COG4178 495 AFARLLLHK--PDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
344-477 |
3.33e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 60.38 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-------------------VPyrllpqrlql 404
Cdd:COG0410 18 VLHG---VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgeditglpphriarlgigyVP---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 405 lDDRD-----SV-----LAAVSRLAPTADDNQLRAELARF--LldADTIARPVGTLSGGER-----FRAtlaalLLSEpp 467
Cdd:COG0410 85 -EGRRifpslTVeenllLGAYARRDRAEVRADLERVYELFprL--KERRRQRAGTLSGGEQqmlaiGRA-----LMSR-- 154
|
170
....*....|
gi 1863768389 468 PQLLILDEPT 477
Cdd:COG0410 155 PKLLLLDEPS 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
344-476 |
3.73e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.43 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD-------------- 409
Cdd:COG1137 18 VVKD---VSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL--------------DGEDithlpmhkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 -------SV----------LAAVSRLAPTADDNQLRAE--LARFLLD--ADTIArpvGTLSGGERFRATLAALLLSEppP 468
Cdd:COG1137 81 gylpqeaSIfrkltvedniLAVLELRKLSKKEREERLEelLEEFGIThlRKSKA---YSLSGGERRRVEIARALATN--P 155
|
....*...
gi 1863768389 469 QLLILDEP 476
Cdd:COG1137 156 KFILLDEP 163
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
351-505 |
3.89e-10 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 59.95 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpQRLQLLDDRDSVLAAVSR------------L 418
Cdd:TIGR02673 21 VSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI--------AGEDVNRLRGRQLPLLRRrigvvfqdfrllP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 APTADDN-QLRAELARflLDADTIARPVG-----------------TLSGGERFRATLAALLLSEPPpqLLILDEPTNNL 480
Cdd:TIGR02673 93 DRTVYENvALPLEVRG--KKEREIQRRVGaalrqvglehkadafpeQLSGGEQQRVAIARAIVNSPP--LLLADEPTGNL 168
|
170 180
....*....|....*....|....*...
gi 1863768389 481 DLD---SIRQLTQALTQYRGALLVASHD 505
Cdd:TIGR02673 169 DPDlseRILDLLKRLNKRGTTVIVATHD 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-180 |
4.21e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.50 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 17 GELAIAGLT-CAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS----------RPERVGYLPQHLVLQSDRTVADV 85
Cdd:PRK13539 14 GRVLFSGLSfTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddpdVAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIEAvlaalATIDAGQGQPAdfevvgdqwdlpdrsiAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLL 165
Cdd:PRK13539 94 LEFWA-----AFLGGEELDIA----------------AALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170
....*....|....*
gi 1863768389 166 DEPTNNLDSGARARL 180
Cdd:PRK13539 152 DEPTAALDAAAVALF 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-219 |
4.28e-10 |
|
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: 60.05 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGELaiagltcafpdqvTGLVGRNGVGKSTLLKIIAGELMPTRGSV-----------SRPERVGYLPQHLVLQ 77
Cdd:cd03296 20 DVSLDIPSGEL-------------VALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdvpVQERNVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 78 SDRTVADvlgieAVLAALATIDAGQGQPADfevvgdqwDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFL 157
Cdd:cd03296 87 RHMTVFD-----NVAFGLRVKPRSERPPEA--------EIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 158 SEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ----AIVVSHDR-DLLDLVQHMAEMRAGGITFFG 219
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhvtTVFVTHDQeEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
35-213 |
4.38e-10 |
|
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: 59.43 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSDRTVADVLGIEAVLAALATIdagqgqpadfevvgdQ 114
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL---------------R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 115 WDLPDRSIAM----LARFGFADLDlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW--R 188
Cdd:cd03231 96 FWHADHSDEQveeaLARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcaR 174
|
170 180
....*....|....*....|....*
gi 1863768389 189 GQAIVVSHDRDLLDLVQHMAEMRAG 213
Cdd:cd03231 175 GGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-492 |
4.49e-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: 59.10 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTI--RGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVLAAVSRLAPt 421
Cdd:cd03213 24 LLKN---VSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLI-----------NGRPLDKRSFRKIIGYVP- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 422 aDDNQLRAEL--ARFLLDAdtiARPVGtLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:cd03213 89 -QDDILHPTLtvRETLMFA---AKLRG-LSGGERKRVSIALELVSNPS--LLFLDEPTSGLDSSSALQVMSLL 154
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-196 |
4.57e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGELAIAGLTCAFPDQ-VTGLVGRNGVGKSTLLKIIAGELMPTRGSV---SRPerVGYLpQHLVLQSDrtVAD 84
Cdd:PRK10790 345 NVSFAYRDDNLVLQNINLSVPSRgFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldGRP--LSSL-SHSVLRQG--VAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 85 VLGIEAVLAALATIDAGQGQPADFEVVgdqWD-LPDRSIAMLARfGFADlDLRRPIG----TLSGGEVILLALAAQFLSE 159
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQV---WQaLETVQLAELAR-SLPD-GLYTPLGeqgnNLSVGQKQLLALARVLVQT 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 1863768389 160 PDLLLLDEPTNNLDSGARARLYAALTSWRGQA--IVVSH 196
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAH 533
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
351-494 |
5.70e-10 |
|
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: 59.48 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD--------------------- 409
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL--------------DGQDitklpmhkrarlgigylpqea 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ------SV---LAAVSRLAPtaDDNQLRAELARFLLDADTIA----RPVGTLSGGERFRATLAALLLSEppPQLLILDEP 476
Cdd:cd03218 85 sifrklTVeenILAVLEIRG--LSKKEREEKLEELLEEFHIThlrkSKASSLSGGERRRVEIARALATN--PKFLLLDEP 160
|
170 180
....*....|....*....|.
gi 1863768389 477 TNNLD---LDSIRQLTQALTQ 494
Cdd:cd03218 161 FAGVDpiaVQDIQKIIKILKD 181
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-216 |
6.48e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 24 LTCAFP-DQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV---SRP----------ERVGYLPQHLVLQSDRTVADVLGIE 89
Cdd:PRK10575 30 LSLTFPaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPleswsskafaRKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 90 AV--LAALatidaGQGQPADFEVVgdqwdlpDRSIAMLARFGFAdldlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDE 167
Cdd:PRK10575 110 RYpwHGAL-----GRFGAADREKV-------EEAISLVGLKPLA----HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1863768389 168 PTNNLDsgararlyaaltswrgqaivVSHDRDLLDLVQHMAEMRagGIT 216
Cdd:PRK10575 174 PTSALD--------------------IAHQVDVLALVHRLSQER--GLT 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
343-521 |
7.96e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.10 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 343 LVLRNGAVVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYrllpqrlqllddrDSVLAAVSRLapta 422
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFS-------------RNKLIFIDQL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 423 ddnqlraelaRFLLDAD----TIARPVGTLSGGERFRATLAALLLSEPPPQLLILDEPTNNLDLDSIRQLTQALTQYRG- 497
Cdd:cd03238 69 ----------QFLIDVGlgylTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDl 138
|
170 180
....*....|....*....|....*.
gi 1863768389 498 --ALLVASHDDAFLSElgLTYRIDLG 521
Cdd:cd03238 139 gnTVILIEHNLDVLSS--ADWIIDFG 162
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
31-173 |
8.97e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.33 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-------------RPERVGYLPQHLVLQSDRTVADVLGIeavlaalat 97
Cdd:COG4604 28 GITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvattpsreLAKRLAILRQENHINSRLTVRELVAF--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 98 idaG-----QGQP--ADFEVVgdqwdlpDRSIAMLarfgfaDL-DLR-RPIGTLSGGE--------VIllalaAQflsEP 160
Cdd:COG4604 99 ---GrfpysKGRLtaEDREII-------DEAIAYL------DLeDLAdRYLDELSGGQrqrafiamVL-----AQ---DT 154
|
170
....*....|...
gi 1863768389 161 DLLLLDEPTNNLD 173
Cdd:COG4604 155 DYVLLDEPLNNLD 167
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-481 |
1.04e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---RVPYRLLPQRLqllddRDSVLAAVSRLAP--TADDN 425
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgePVPSRARHARQ-----RVGVVPQFDNLDPdfTVREN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 426 -------------QLRA------ELARFLLDADTiarPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:PRK13537 101 llvfgryfglsaaAARAlvppllEFAKLENKADA---KVGELSGGMKRRLTLARALVND--PDVLVLDEPTTGLD 170
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-201 |
1.06e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 13 AWPSGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRG-------SVSR---------PERVGYLPQHLV 75
Cdd:PRK10908 10 AYLGGRQALQGVTFHMrPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghDITRlknrevpflRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 76 LQSDRTVADVLGIEAVLAalatidagqGQPADfevvgdqwDLPDRSIAMLARFGFADLDLRRPIgTLSGGEVILLALAAQ 155
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIA---------GASGD--------DIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1863768389 156 FLSEPDLLLLDEPTNNLD---SGARARLYAALTSWRGQAIVVSHDRDLL 201
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-197 |
1.14e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.61 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-------------RPerVGYLPQ------HLvlqsdrTVAD--VLGIE 89
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltalppaeRP--VSMLFQennlfpHL------TVAQniGLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 90 AVLaalaTIDAGQGQpadfevvgdqwdlpdRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPT 169
Cdd:COG3840 98 PGL----KLTAEQRA---------------QVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 170 NNLDSGARA---RLYAALTSWRGQAIV-VSHD 197
Cdd:COG3840 158 SALDPALRQemlDLVDELCRERGLTVLmVTHD 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
341-482 |
1.16e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.11 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaV 415
Cdd:COG3842 9 ENVSKRYGDVtalddVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL--------------DGRD-----V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 SRLAP------------------TADDN------------QLRAELARFLLD-------ADtiaRPVGTLSGGERFRATL 458
Cdd:COG3842 70 TGLPPekrnvgmvfqdyalfphlTVAENvafglrmrgvpkAEIRARVAELLElvgleglAD---RYPHQLSGGQQQRVAL 146
|
170 180
....*....|....*....|....*
gi 1863768389 459 A-ALLLSeppPQLLILDEPTNNLDL 482
Cdd:COG3842 147 ArALAPE---PRVLLLDEPLSALDA 168
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
351-495 |
1.29e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRG----------------EIEPRS----------------GTVslrvpyrll 398
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingielrELDPESwrkhlswvgqnpqlphGTL--------- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 399 pqrlqllddRDSVLAAvsrlAPTADDNQLRAELAR-----FLLD-ADTIARPVG----TLSGGERFRATLAALLLSepPP 468
Cdd:PRK11174 440 ---------RDNVLLG----NPDASDEQLQQALENawvseFLPLlPQGLDTPIGdqaaGLSVGQAQRLALARALLQ--PC 504
|
170 180
....*....|....*....|....*..
gi 1863768389 469 QLLILDEPTNNLDLDSIRQLTQALTQY 495
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAA 531
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
352-507 |
1.31e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 352 SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSVLAAVSR-------------- 417
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL--------------NGQDHTTTPPSRrpvsmlfqennlfs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 418 -----------LAP----TADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLD- 481
Cdd:PRK10771 85 hltvaqniglgLNPglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP--ILLLDEPFSALDp 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1863768389 482 ---------LDSI---RQLTqaltqyrgaLLVASH--DDA 507
Cdd:PRK10771 163 alrqemltlVSQVcqeRQLT---------LLMVSHslEDA 193
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
362-508 |
1.32e-09 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 58.05 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 362 GLVGPNGSGKTTLIDTIrgeieprsgTVSLrvpYRLLPQRLQLLDDRdSVLAAVSRLAPTADDNQLRAELAR----FLLD 437
Cdd:cd03279 32 LICGPTGAGKSTILDAI---------TYAL---YGKTPRYGRQENLR-SVFAPGEDTAEVSFTFQLGGKKYRversRGLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 438 ADT---------------IARPVGTLSGGERFRATLA-ALLLSE-------PPPQLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:cd03279 99 YDQftrivllpqgefdrfLARPVSTLSGGETFLASLSlALALSEvlqnrggARLEALFIDEGFGTLDPEALEAVATALEL 178
|
170
....*....|....*..
gi 1863768389 495 YRG---ALLVASHDDAF 508
Cdd:cd03279 179 IRTenrMVGVISHVEEL 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
352-507 |
1.37e-09 |
|
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: 58.27 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 352 SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPQRLQLLD--------------DRDSVLAAVS 416
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgVDVTAAPPADRPVSmlfqennlfahltvEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 RLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLD---LDSIRQLTQALT 493
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP--VLLLDEPFAALDpalRAEMLDLVLDLH 175
|
170
....*....|....*..
gi 1863768389 494 QYRG-ALLVASH--DDA 507
Cdd:cd03298 176 AETKmTVLMVTHqpEDA 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
31-219 |
1.40e-09 |
|
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: 58.45 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE------RVGYLPQHLVLQSDRTVadvlgieavlaa 94
Cdd:COG1127 32 EILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglSEKElyelrrRIGMLFQGGALFDSLTV------------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 latidagqgqpadFEVVG----DQWDLPDRSIAMLARF--------GFADLdlrRPiGTLSGGEV----ILLALAAqfls 158
Cdd:COG1127 100 -------------FENVAfplrEHTDLSEAEIRELVLEklelvglpGAADK---MP-SELSGGMRkrvaLARALAL---- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 159 EPDLLLLDEPTNNLD---SGARARLYAALTSWRGQ-AIVVSHDRD-LLDLVQHMAEMRAGGITFFG 219
Cdd:COG1127 159 DPEILLYDEPTAGLDpitSAVIDELIRELRDELGLtSVVVTHDLDsAFAIADRVAVLADGKIIAEG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
142-505 |
1.41e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 142 LSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ----AIVVSHDrdlLDLVQHMAE----MRAG 213
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnmgLLFITHN---LSIVRKLADrvavMQNG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 214 GitffggnftaftdalAVEQEAAARGVRAAESDLKRQQrelaearikLDrrqrfARSQAGNVPkivagakkgtAEVSAGK 293
Cdd:PRK15134 234 R---------------CVEQNRAATLFSAPTHPYTQKL---------LN-----SEPSGDPVP----------LPEPASP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 294 LrgghqadvadarrrleeaeervrdddsIEVDLSRTSVPPGRDI---VVTENLVLRNgavVSLHIRGPERVGLVGPNGSG 370
Cdd:PRK15134 275 L---------------------------LDVEQLQVAFPIRKGIlkrTVDHNVVVKN---ISFTLRPGETLGLVGESGSG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 371 KTT-------LIDTiRGEI----EP-------------RSGTVSLRVPYRLLpqrlqllDDRDSVLAAVS--------RL 418
Cdd:PRK15134 325 KSTtglallrLINS-QGEIwfdgQPlhnlnrrqllpvrHRIQVVFQDPNSSL-------NPRLNVLQIIEeglrvhqpTL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 APTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLA-ALLLSeppPQLLILDEPTNNLDLD---SIRQLTQALTQ 494
Cdd:PRK15134 397 SAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIArALILK---PSLIILDEPTSSLDKTvqaQILALLKSLQQ 473
|
410
....*....|..
gi 1863768389 495 -YRGALLVASHD 505
Cdd:PRK15134 474 kHQLAYLFISHD 485
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-184 |
1.68e-09 |
|
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: 60.07 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 4 SVVCSDLWFAWPSGELAIAGLTC-AFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPervGYLPQHLVLQSDRTV 82
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLdLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD---GVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 83 ADVLGIEAVLAA---LATIDAGQGQPADFEVvgdqwdlpdrsIAMLARFGFADLDLRRPIG----------TLSGGEVIL 149
Cdd:TIGR02868 411 VSVCAQDAHLFDttvRENLRLARPDATDEEL-----------WAALERVGLADWLRALPDGldtvlgeggaRLSGGERQR 479
|
170 180 190
....*....|....*....|....*....|....*
gi 1863768389 150 LALAAQFLSEPDLLLLDEPTNNLDSGARARLYAAL 184
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
351-526 |
1.89e-09 |
|
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: 58.21 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllPQRLQLLDDRDSvLAAVSR-----------LA 419
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL-------AGQDLFALDEDA-RARLRArhvgfvfqsfqLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 P--TADDN---------------QLRAELARFLLDADTIARPvGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDL 482
Cdd:COG4181 103 PtlTALENvmlplelagrrdaraRARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPA--ILFADEPTGNLDA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 483 ---DSIRQLTQALTQYRGA-LLVASHDDAFLSELGLTYRIDLGAVADP 526
Cdd:COG4181 180 atgEQIIDLLFELNRERGTtLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
341-481 |
2.14e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.18 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrlLPQRLQLLDDRdsvlaAV----S 416
Cdd:COG1116 23 GVTALDD---VSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-----GKPVTGPGPDR-----GVvfqeP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 RLAP--TADDN------------QLRAELARFLLD-------ADtiARPvGTLSGGERFRATLA-ALLLSeppPQLLILD 474
Cdd:COG1116 90 ALLPwlTVLDNvalglelrgvpkAERRERARELLElvglagfED--AYP-HQLSGGMRQRVAIArALAND---PEVLLMD 163
|
....*..
gi 1863768389 475 EPTNNLD 481
Cdd:COG1116 164 EPFGALD 170
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
351-505 |
2.44e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---------------RVPYRLLPQRLQLLDDRDSVLAAV 415
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFegedistlkpeiyrqQVSYCAQTPTLFGDTVYDNLIFPW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 SRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLlsEPPPQLLILDEPTNNLDLDSIRQLTQALTQY 495
Cdd:PRK10247 106 QIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVLLLDEITSALDESNKHNVNEIIHRY 183
|
170
....*....|....
gi 1863768389 496 ----RGALLVASHD 505
Cdd:PRK10247 184 vreqNIAVLWVTHD 197
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
344-505 |
2.52e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.16 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPQRLQLLDDRDSVLA---AVSRLA 419
Cdd:PRK10419 27 VLNN---VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgEPLAKLNRAQRKAFRRDIQMVfqdSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 PTADDNQLRAELARFLLDADTIARPV--------------------GTLSGGERFRATLAALLLSEppPQLLILDEPTNN 479
Cdd:PRK10419 104 PRKTVREIIREPLRHLLSLDKAERLArasemlravdlddsvldkrpPQLSGGQLQRVCLARALAVE--PKLLILDEAVSN 181
|
170 180 190
....*....|....*....|....*....|
gi 1863768389 480 LDL---DSIRQLTQALTQYRG-ALLVASHD 505
Cdd:PRK10419 182 LDLvlqAGVIRLLKKLQQQFGtACLFITHD 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
341-495 |
2.86e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.45 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD----------S 410
Cdd:PRK11160 352 PQPVLKG---LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL--------------NGQPiadyseaalrQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLAAVS--------------RLA-PTADDNQLRAELARF----LLDADT--------IARPvgtLSGGERFRATLAALLL 463
Cdd:PRK11160 415 AISVVSqrvhlfsatlrdnlLLAaPNASDEALIEVLQQVglekLLEDDKglnawlgeGGRQ---LSGGEQRRLGIARALL 491
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 464 SEPPpqLLILDEPTNNLDLDSIRQLTQALTQY 495
Cdd:PRK11160 492 HDAP--LLLLDEPTEGLDAETERQILELLAEH 521
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
31-173 |
3.10e-09 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 57.67 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------SRP--ER----VGYLPQHLVLQSDRTVADvlGIEAVLAALA 96
Cdd:TIGR04406 28 EIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqditHLPmhERarlgIGYLPQEASIFRKLTVEE--NIMAVLEIRK 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 97 TIDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:TIGR04406 106 DLDRAERE--------------ERLEALLEEFQISHL-RDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
340-492 |
3.38e-09 |
|
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: 57.24 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV-------------SLR-----VPyrllpqr 401
Cdd:cd03253 12 PGRPVLKD---VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevtldSLRraigvVP------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 402 lqllddRDSVL------AAVSRLAPTADDNQLR--AELA-------RFLLDADTIARPVGT-LSGGERFRATLAALLLSE 465
Cdd:cd03253 82 ------QDTVLfndtigYNIRYGRPDATDEEVIeaAKAAqihdkimRFPDGYDTIVGERGLkLSGGEKQRVAIARAILKN 155
|
170 180
....*....|....*....|....*..
gi 1863768389 466 PPpqLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:cd03253 156 PP--ILLLDEATSALDTHTEREIQAAL 180
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
323-510 |
3.67e-09 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 59.28 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 323 EVDLSRTS-VPPGrdivvTENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllPQR 401
Cdd:TIGR01842 316 HLSVENVTiVPPG-----GKKPTLRG---ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-------DGA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 402 LQLLDDRD------------------SVLAAVSRLAPTADDNQL--RAELA-------RFLLDADTIARPVG-TLSGGER 453
Cdd:TIGR01842 381 DLKQWDREtfgkhigylpqdvelfpgTVAENIARFGENADPEKIieAAKLAgvhelilRLPDGYDTVIGPGGaTLSGGQR 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 454 FRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYR---GALLVASHDDAFLS 510
Cdd:TIGR01842 461 QRIALARALYGDP--KLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLG 518
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-215 |
3.97e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERvgylpqhlvlqsDRTVADVLGI-EAVLAALATIDAG--QGQ 104
Cdd:PRK11701 30 YPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------------DGQLRDLYALsEAERRRLLRTEWGfvHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 105 PAD---------------FEVVGDQW--DLPDRSIAMLARfgfADLDLRR----PiGTLSGGEVILLALAAQFLSEPDLL 163
Cdd:PRK11701 98 PRDglrmqvsaggnigerLMAVGARHygDIRATAGDWLER---VEIDAARiddlP-TTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 164 LLDEPTNNLDSGARARLYAALtswRG-------QAIVVSHDRDLLDLVQH-MAEMRAGGI 215
Cdd:PRK11701 174 FMDEPTGGLDVSVQARLLDLL---RGlvrelglAVVIVTHDLAVARLLAHrLLVMKQGRV 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-392 |
4.27e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 56.77 E-value: 4.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR 392
Cdd:cd03220 34 EFWALKD---VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
340-481 |
4.30e-09 |
|
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: 56.71 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrLQLLDDRDSVLAAV---S 416
Cdd:cd03293 15 GAVTALED---ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD---------GEPVTGPGPDRGYVfqqD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 RLAP--TADDN------------QLRAELARFLLD-------ADtiARPvGTLSGGERFRATLAALLLSEppPQLLILDE 475
Cdd:cd03293 83 ALLPwlTVLDNvalglelqgvpkAEARERAEELLElvglsgfEN--AYP-HQLSGGMRQRVALARALAVD--PDVLLLDE 157
|
....*.
gi 1863768389 476 PTNNLD 481
Cdd:cd03293 158 PFSALD 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
120-505 |
5.50e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.54 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 120 RSIAMLARFGFADLdlRRPIGT----LSGGE----VILLALAaqflSEPDLLLLDEPTNNLDSGARAR---LYAALTSWR 188
Cdd:COG4172 133 RALELLERVGIPDP--ERRLDAyphqLSGGQrqrvMIAMALA----NEPDLLIADEPTTALDVTVQAQildLLKDLQREL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 189 GQAIV-VSHDrdlLDLVQHMAE----MRAGGItffggnftaftdalaVEQEAAARGVRAAESDLKRQqreLAEARikldr 263
Cdd:COG4172 207 GMALLlITHD---LGVVRRFADrvavMRQGEI---------------VEQGPTAELFAAPQHPYTRK---LLAAE----- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 264 rqrfarsqagnvPKIVAGAKKGTAEV--SAGKLRgghqadvadarrrleeaeervrdddsIEVDLSRTSVPPGRDIVVte 341
Cdd:COG4172 261 ------------PRGDPRPVPPDAPPllEARDLK--------------------------VWFPIKRGLFRRTVGHVK-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 nlvlrngAV--VSLHIRGPERVGLVGPNGSGKTT-------LIDTiRGEIE---------PRSGTVSLR-----V---PY 395
Cdd:COG4172 301 -------AVdgVSLTLRRGETLGLVGESGSGKSTlglallrLIPS-EGEIRfdgqdldglSRRALRPLRrrmqvVfqdPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 396 rllpqrlQLLDDRDSVLAAVSR----LAPTADDNQLRAELARFL----LDADTIARPVGTLSGGERFRATLA-ALLLSep 466
Cdd:COG4172 373 -------GSLSPRMTVGQIIAEglrvHGPGLSAAERRARVAEALeevgLDPAARHRYPHEFSGGQRQRIAIArALILE-- 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1863768389 467 pPQLLILDEPTNNLDLdSIR----QLTQALTQYRG-ALLVASHD 505
Cdd:COG4172 444 -PKLLVLDEPTSALDV-SVQaqilDLLRDLQREHGlAYLFISHD 485
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
341-504 |
5.70e-09 |
|
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: 56.46 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV-------------SLR-----VPyrllpqrl 402
Cdd:cd03254 15 KKPVLKD---INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrkSLRsmigvVL-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 403 qlLDD---RDSVLA--AVSRLAPTADDNQLRAELARFLL-------DADTIARPVG-TLSGGERFRATLAALLLSEPPpq 469
Cdd:cd03254 84 --QDTflfSGTIMEniRLGRPNATDEEVIEAAKEAGAHDfimklpnGYDTVLGENGgNLSQGERQLLAIARAMLRDPK-- 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 470 LLILDEPTNNLDLDS---IRQLTQALTQYRGALLVASH 504
Cdd:cd03254 160 ILILDEATSNIDTETeklIQEALEKLMKGRTSIIIAHR 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
352-494 |
6.56e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 352 SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSG--TVSLRVP---------------YRLLPQRLQLLDDRDSVLAA 414
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerQSQFSHItrlsfeqlqklvsdeWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 415 VSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP--DLLILDEPFDGLDVASRQQLAELLAS 180
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
329-511 |
6.57e-09 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 58.22 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 329 TSVPPGrdivvTENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDr 408
Cdd:COG4618 337 TVVPPG-----SKRPILRG---VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL--------------DG- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 409 dsvlAAVSRLAptaddnqlRAELARF---------LLD---ADTIAR-------------------------------PV 445
Cdd:COG4618 394 ----ADLSQWD--------REELGRHigylpqdveLFDgtiAENIARfgdadpekvvaaaklagvhemilrlpdgydtRI 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 446 G----TLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQYR---GALLVASHDDAFLSE 511
Cdd:COG4618 462 GeggaRLSGGQRQRIGLARALYGDPR--LVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLLAA 532
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-219 |
6.62e-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: 58.87 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGsvsrpervgylpqhlvlqsDRTVADvlgiEAVLAALATIDAGQGQPADF 108
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-------------------DATVAG----KSILTNISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 109 EVVGDQWD-------------LPDRSIAMLARFGFADLDLR----RPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNN 171
Cdd:TIGR01257 2021 DAIDDLLTgrehlylyarlrgVPAEEIEKVANWSIQSLGLSlyadRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 172 LDSGARARLYAALTSW--RGQAIVV-SHDRDLLD-LVQHMAEMRAGGITFFG 219
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIirEGRAVVLtSHSMEECEaLCTRLAIMVKGAFQCLG 2152
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-518 |
6.70e-09 |
|
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: 58.30 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAG-------------ELMPTRGS-VSRPERVGY--LPQHLVLQSDRTVAD--VLGIEA 90
Cdd:TIGR02633 26 PGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPLKASnIRDTERAGIviIHQELTLVPELSVAEniFLGNEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 91 VLAALATIDAgqgqpadfevvgdqwDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTn 170
Cdd:TIGR02633 106 TLPGGRMAYN---------------AMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 171 nldsgararlyAALTSWRGQAivvshdrdLLDLVQhmaEMRAGG-----ITFFGGNFTAFTDALAVEQEAAARGVRAAES 245
Cdd:TIGR02633 170 -----------SSLTEKETEI--------LLDIIR---DLKAHGvacvyISHKLNEVKAVCDTICVIRDGQHVATKDMST 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 246 dlkrqqreLAEARIKLDRRQRFARSQAGNVPKIVAGAKKGTAEVSAGKLRGGHQADVADarrrleeaeervrdddsievd 325
Cdd:TIGR02633 228 --------MSEDDIITMMVGREITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVDD--------------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 326 lsrtsvppgrdivvtenlvlrngavVSLHIRGPERVGLVGPNGSGKTTLIDTI--------RGEIEPRSGTVSLRVPYRL 397
Cdd:TIGR02633 279 -------------------------VSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfEGNVFINGKPVDIRNPAQA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 398 LPQRLQLL-DDRD----------------SVL---AAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRAT 457
Cdd:TIGR02633 334 IRAGIAMVpEDRKrhgivpilgvgknitlSVLksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 458 LAALLLSEppPQLLILDEPTNNLDLDS---IRQLTQALTQYRGALLVASHDdafLSE-LGLTYRI 518
Cdd:TIGR02633 414 LAKMLLTN--PRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSE---LAEvLGLSDRV 473
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-173 |
6.74e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 32 VTgLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLPQHlvlQSDRTVADV-----------LGIEAVLaALAtid 99
Cdd:COG1101 35 VT-VIGSNGAGKSTLLNAIAGSLPPDSGSILiDGKDVTKLPEY---KRAKYIGRVfqdpmmgtapsMTIEENL-ALA--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 100 AGQGQPADFevvgdQWDLPDRSIAM----LARFGFaDLD--LRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:COG1101 107 YRRGKRRGL-----RRGLTKKRRELfrelLATLGL-GLEnrLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
351-482 |
7.14e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 58.60 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR------------------VPYRLLPQRLQLLDD----- 407
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslkdidrhtlrqfinyLPQEPYIFSGSILENlllga 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 408 -----RDSVLAAVsRLAptaddnQLRAELARFLLDADT-IARPVGTLSGGERFRATLAALLLSepPPQLLILDEPTNNLD 481
Cdd:TIGR01193 573 kenvsQDEIWAAC-EIA------EIKDDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLT--DSKVLILDESTSNLD 643
|
.
gi 1863768389 482 L 482
Cdd:TIGR01193 644 T 644
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
338-481 |
7.22e-09 |
|
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: 56.11 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 338 VVTENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---RVPYRLLPqrlqlldDRD 409
Cdd:cd03301 1 VELENVTKRFGNVtalddLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrDVTDLPPK-------DRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 svLAAV---------------------SRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEppP 468
Cdd:cd03301 74 --IAMVfqnyalyphmtvydniafglkLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE--P 149
|
170
....*....|...
gi 1863768389 469 QLLILDEPTNNLD 481
Cdd:cd03301 150 KVFLMDEPLSNLD 162
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
344-482 |
8.05e-09 |
|
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: 56.79 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV--SLRVPYRLLPQRLQLLDDRDSVLAAVS----R 417
Cdd:cd03291 52 VLKN---INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhSGRISFSSQFSWIMPGTIKENIIFGVSydeyR 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 418 LAPTADDNQLRAELARFLLDADTIARPVG-TLSGGERFRATLAALLLSEppPQLLILDEPTNNLDL 482
Cdd:cd03291 129 YKSVVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKD--ADLYLLDSPFGYLDV 192
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
344-505 |
8.80e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 56.74 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPQRLQLLDDRDSVLA---AVSRLA 419
Cdd:TIGR02769 26 VLTN---VSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDLYQLDRKQRRAFRRDVQLVfqdSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 PTADDNQLRAELARFLLDADTIARPVGT--------------------LSGGERFRATLAALLLSEPppQLLILDEPTNN 479
Cdd:TIGR02769 103 PRMTVRQIIGEPLRHLTSLDESEQKARIaelldmvglrsedadklprqLSGGQLQRINIARALAVKP--KLIVLDEAVSN 180
|
170 180 190
....*....|....*....|....*....|
gi 1863768389 480 LDL---DSIRQLTQALTQYRG-ALLVASHD 505
Cdd:TIGR02769 181 LDMvlqAVILELLRKLQQAFGtAYLFITHD 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
344-492 |
9.25e-09 |
|
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: 55.97 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPQRLQLLDDR------------DS 410
Cdd:cd03261 15 VLKG---VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgEDISGLSEAELYRLRRrmgmlfqsgalfDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 --VLAAV-------SRLAPTADDNQLRAELARFLLDADTIARPvGTLSGGERFRATLA-ALLLSeppPQLLILDEPTNNL 480
Cdd:cd03261 92 ltVFENVafplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALArALALD---PELLLYDEPTAGL 167
|
170
....*....|....*....
gi 1863768389 481 D-------LDSIRQLTQAL 492
Cdd:cd03261 168 DpiasgviDDLIRSLKKEL 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-505 |
1.01e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.09 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrlqLLDDRDSVLAAVS-------------- 416
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYR-----------MRDGQLRDLYALSeaerrrllrtewgf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 ---------RLAPTADDN--------------QLRAE----LARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQ 469
Cdd:PRK11701 94 vhqhprdglRMQVSAGGNigerlmavgarhygDIRATagdwLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTH--PR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1863768389 470 LLILDEPTNNLD-------LDSIRQLTQALtqyRGALLVASHD 505
Cdd:PRK11701 172 LVFMDEPTGGLDvsvqarlLDLLRGLVREL---GLAVVIVTHD 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-199 |
1.02e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 55.93 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVSR---------PERVGYLpQHLVLQSDRTVAD--VLGIEAVLAALATidagqg 103
Cdd:TIGR01184 16 LIGHSGCGKSTLLNLISGLAQPTSGGVILegkqitepgPDRMVVF-QNYSLLPWLTVREniALAVDRVLPDLSK------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 104 qpadfevvGDQWDLPDRSIAMLARFGFADldlrRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAA 183
Cdd:TIGR01184 89 --------SERRAIVEEHIALVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180
....*....|....*....|
gi 1863768389 184 LTS-W---RGQAIVVSHDRD 199
Cdd:TIGR01184 157 LMQiWeehRVTVLMVTHDVD 176
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
351-481 |
1.04e-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: 55.81 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaaVSRLAP---------- 420
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF--------------GGED-----ATDVPVqernvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 --------TADDN---QLRAELARFLLDADTIARPV-----------------GTLSGGERFRATLAALLLSEppPQLLI 472
Cdd:cd03296 82 hyalfrhmTVFDNvafGLRVKPRSERPPEAEIRAKVhellklvqldwladrypAQLSGGQRQRVALARALAVE--PKVLL 159
|
....*....
gi 1863768389 473 LDEPTNNLD 481
Cdd:cd03296 160 LDEPFGALD 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-202 |
1.07e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 137 RPIGTLSGGEVILLALAAQF-LS-----EPDLLLLDEPTNNLDSGARARLYAALTSWR---GQAIVVSHDRDLLD 202
Cdd:PRK03918 784 RPLTFLSGGERIALGLAFRLaLSlylagNIPLLILDEPTPFLDEERRRKLVDIMERYLrkiPQVIIVSHDEELKD 858
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
341-511 |
1.43e-08 |
|
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: 55.23 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllPQRLQLLDDRD----------- 409
Cdd:cd03262 12 DFHVLKG---IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-------DGLKLTDDKKNinelrqkvgmv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ----------SVLAAVSrLAPTADDNQLRAE---LARFLLD----ADTIARPVGTLSGGERFRATLAALLLSEPPpqLLI 472
Cdd:cd03262 82 fqqfnlfphlTVLENIT-LAPIKVKGMSKAEaeeRALELLEkvglADKADAYPAQLSGGQQQRVAIARALAMNPK--VML 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1863768389 473 LDEPTNNLD-------LDSIRQLTQaltqyRG-ALLVASHDDAFLSE 511
Cdd:cd03262 159 FDEPTSALDpelvgevLDVMKDLAE-----EGmTMVVVTHEMGFARE 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
351-492 |
1.46e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVLAAVSR-LA---------- 419
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-----------DGTDIRTVTRASLRRnIAvvfqdaglfn 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 -----------PTADDNQLRAELAR-----FLLDA----DTIARPVG-TLSGGERFRATLAALLLSEPPpqLLILDEPTN 478
Cdd:PRK13657 423 rsiednirvgrPDATDEEMRAAAERaqahdFIERKpdgyDTVVGERGrQLSGGERQRLAIARALLKDPP--ILILDEATS 500
|
170
....*....|....
gi 1863768389 479 NLDLDSIRQLTQAL 492
Cdd:PRK13657 501 ALDVETEAKVKAAL 514
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-219 |
1.58e-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: 55.38 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 12 FAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------SRPE-----RVGYLPQHLVLQ 77
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKgEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPvelrrKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 78 SDRTVADvlGIEAVLAALATIDAGQGQPAD--FEVVGdqwdLPDRSiamlarfgFADldlRRPiGTLSGGEV----ILLA 151
Cdd:cd03295 88 PHMTVEE--NIALVPKLLKWPKEKIRERADelLALVG----LDPAE--------FAD---RYP-HELSGGQQqrvgVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 152 LAAqflsEPDLLLLDEPTNNLDSGARARL---YAALTSWRGQAIV-VSHDRD-LLDLVQHMAEMRAGGITFFG 219
Cdd:cd03295 150 LAA----DPPLLLMDEPFGALDPITRDQLqeeFKRLQQELGKTIVfVTHDIDeAFRLADRIAIMKNGEIVQVG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-200 |
1.67e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.17 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------------RPERVGYlpqhlVLQSDRTVADVLGIEAV 91
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeearaklRAKHVGF-----VFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 92 -LAALAtidagQGQpadfevvgDQWDLPDRSIAMLARFGFADlDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTN 170
Cdd:PRK10584 110 eLPALL-----RGE--------SSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|....
gi 1863768389 171 NLDSGARARLYAALTSW-RGQA---IVVSHDRDL 200
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLnREHGttlILVTHDLQL 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
33-215 |
1.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 33 TGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERV---GYLPQHLvlqsdRTVADVLGI-----EAVL---AALATIDAG 101
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitaGKKNKKL-----KPLRKKVGIvfqfpEHQLfeeTVEKDICFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 qgqPADFEVVGDqwDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARL- 180
Cdd:PRK13634 111 ---PMNFGVSEE--DAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMm 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1863768389 181 --YAALTSWRGQAIV-VSHD-RDLLDLVQHMAEMRAGGI 215
Cdd:PRK13634 186 emFYKLHKEKGLTTVlVTHSmEDAARYADQIVVMHKGTV 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-237 |
1.89e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 12 FAWPSGEL-AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSDRTVADVL--- 86
Cdd:TIGR00957 644 FTWARDLPpTLNGITFSIPEgALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILfgk 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 87 -----GIEAVLAALATIdagqgqpADFEVV--GDQWDLPDRSIamlarfgfadldlrrpigTLSGGEVILLALAAQFLSE 159
Cdd:TIGR00957 724 alnekYYQQVLEACALL-------PDLEILpsGDRTEIGEKGV------------------NLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 160 PDLLLLDEPTNNLDSGARARLYAALTSWRG-----QAIVVSHDRDLLDLVQHMAEMRAGGITFFG---------GNFTAF 225
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknkTRILVTHGISYLPQVDVIIVMSGGKISEMGsyqellqrdGAFAEF 858
|
250
....*....|...
gi 1863768389 226 TDALA-VEQEAAA 237
Cdd:TIGR00957 859 LRTYApDEQQGHL 871
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.90e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.62 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 1 MPSSVV-CSDLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPER-VGYLPQHLVlq 77
Cdd:PRK13636 1 MEDYILkVEELNYNYSDGTHALKGININIKKgEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKGLM-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 78 sdrTVADVLGIEAVLAALATIDAGQGQPADFEVVGDQwdLPDRSIA-----MLARFGFADLDlRRPIGTLSGGEVILLAL 152
Cdd:PRK13636 79 ---KLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLK--LPEDEVRkrvdnALKRTGIEHLK-DKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 153 AAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA----IVVSHDRDLLDL-VQHMAEMRAGGITFFGGNFTAFTD 227
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgltiIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-200 |
1.97e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELmpTRGSVSRPERVgylPQHLVLQSDRTVAdvlgIEAV-LAALATIDAGQGQPA- 106
Cdd:PRK13547 26 PGRVTALLGRNGAGKSTLLKALAGDL--TGGGAPRGARV---TGDVTLNGEPLAA----IDAPrLARLRAVLPQAAQPAf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 107 ---DFEVV----------GDQWDLPDRSIA--MLARFGFADLDlRRPIGTLSGGEVILLALA---AQF------LSEPDL 162
Cdd:PRK13547 97 afsAREIVllgrypharrAGALTHRDGEIAwqALALAGATALV-GRDVTTLSGGELARVQFArvlAQLwpphdaAQPPRY 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1863768389 163 LLLDEPTNNLDSGARARLYAALTS----WRGQAIVVSHDRDL 200
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPNL 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
320-392 |
2.37e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.09 E-value: 2.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 320 DSIEVDLSRTSVPPGRDIVVtenlvLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR 392
Cdd:COG1134 22 RSLKELLLRRRRTRREEFWA-----LKD---VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-196 |
2.61e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---RPER-----------VGYLPQHLVLQSDRTVADVLgieaVLAALa 96
Cdd:PRK11288 31 QVHALMGENGAGKSTLLKILSGNYQPDAGSILidgQEMRfasttaalaagVAIIYQELHLVPEMTVAENL----YLGQL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 97 tidagqgqPADFEVVgDQWDLPDRSIAMLARFGFaDLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGA 176
Cdd:PRK11288 106 --------PHKGGIV-NRRLLNYEAREQLEHLGV-DIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180
....*....|....*....|...
gi 1863768389 177 RARLYAALTSWR--GQAIV-VSH 196
Cdd:PRK11288 176 IEQLFRVIRELRaeGRVILyVSH 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-173 |
2.70e-08 |
|
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: 53.47 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 8 SDLWFAWP-SGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpervgYLPQHLVLQSDRTVADV 85
Cdd:cd03247 4 NNVSFSYPeQEQQVLKNLSLELkQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-------TLDGVPVSDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGieaVLaalatidagQGQPADFevvgdqwdlpdrsiamlarfgfaDLDLRRPIGT-LSGGEVILLALAAQFLSEPDLLL 164
Cdd:cd03247 77 IS---VL---------NQRPYLF-----------------------DTTLRNNLGRrFSGGERQRLALARILLQDAPIVL 121
|
....*....
gi 1863768389 165 LDEPTNNLD 173
Cdd:cd03247 122 LDEPTVGLD 130
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
344-492 |
2.79e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.70 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD-------------S 410
Cdd:COG4604 16 VLDD---VSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV--------------DGLDvattpsrelakrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VL----AAVSRL----------------APTADDNQLRAELARFLlDADTIA-RPVGTLSGGERFRATLAALLLSEPPpq 469
Cdd:COG4604 79 ILrqenHINSRLtvrelvafgrfpyskgRLTAEDREIIDEAIAYL-DLEDLAdRYLDELSGGQRQRAFIAMVLAQDTD-- 155
|
170 180
....*....|....*....|...
gi 1863768389 470 LLILDEPTNNLDLDSIRQLTQAL 492
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLL 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-213 |
2.82e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 54.01 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 12 FAWPSGE----LAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSDrTVAD-V 85
Cdd:cd03250 8 FTWDSGEqetsFTLKDINLEVPKgELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG-TIREnI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIEAVLAAL--ATIDAGQGQPaDFEVV--GDQWDLPDRSIamlarfgfadldlrrpigTLSGGEVILLALAAQFLSEPD 161
Cdd:cd03250 87 LFGKPFDEERyeKVIKACALEP-DLEILpdGDLTEIGEKGI------------------NLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 162 LLLLDEPTNNLDSGARARLY--AALTSWRGQA--IVVSHDRDLLDLVQHMAEMRAG 213
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFenCILGLLLNNKtrILVTHQLQLLPHADQIVVLDNG 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
341-505 |
3.10e-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: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSVLAAVSRLAP 420
Cdd:COG1127 17 DRVVLDG---VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--------------DGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 ------------------TADDN-------------QLRAELARFLLDA----DTIARPVGTLSGGERFRATLA-ALLLS 464
Cdd:COG1127 80 lrrrigmlfqggalfdslTVFENvafplrehtdlseAEIRELVLEKLELvglpGAADKMPSELSGGMRKRVALArALALD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1863768389 465 eppPQLLILDEPTNNLD------LDS-IRQLTQALtqyrGA-LLVASHD 505
Cdd:COG1127 160 ---PEILLYDEPTAGLDpitsavIDElIRELRDEL----GLtSVVVTHD 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-173 |
3.17e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQHLVLQSDRTVADV--LGIEAVLAALATI 98
Cdd:PRK09536 33 GLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvealsarAASRRVASVPQDTSLSFEFDVRQVveMGRTPHRSRFDTW 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 99 DagqgqPADFEVVgdqwdlpDRSIAMLARFGFADldlrRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:PRK09536 113 T-----ETDRAAV-------ERAMERTGVAQFAD----RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-206 |
3.66e-08 |
|
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: 54.01 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWP--SGELAIAGLTCAF-PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSdrtVADV 85
Cdd:cd03248 16 NVTFAYPtrPDTLVLQDVSFTLhPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS---KVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIEAVLAALA---TIDAGQGQPADFEVVGDQWDLPDRSIAMLARFGFaDLDLRRPIGTLSGGEVILLALAAQFLSEPDL 162
Cdd:cd03248 93 VGQEPVLFARSlqdNIAYGLQSCSFECVKEAAQKAHAHSFISELASGY-DTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1863768389 163 LLLDEPTNNLDSGARARLYAALTSW--RGQAIVVSHDrdlLDLVQH 206
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHR---LSTVER 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
33-209 |
3.84e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 33 TGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpeRVGylpqHLVLQSD------RTVADVLGI-----EAVLAALATIDAG 101
Cdd:PRK13643 35 TALIGHTGSGKSTLLQHLNGLLQPTEGKV----TVG----DIVVSSTskqkeiKPVRKKVGVvfqfpESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 QGQPADFEVVGDQWDlpDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLY 181
Cdd:PRK13643 107 AFGPQNFGIPKEKAE--KIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190
....*....|....*....|....*....|.
gi 1863768389 182 AALTSWR--GQAIV-VSHdrdLLDLVQHMAE 209
Cdd:PRK13643 185 QLFESIHqsGQTVVlVTH---LMDDVADYAD 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
34-209 |
4.06e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 54.43 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLPQHLVLQSDRTVADVL--GIEAVlAALATIDAGQGQPADFEV 110
Cdd:TIGR02769 41 GLLGRSGCGKSTLARLLLGLEKPAQGTVSfRGQDLYQLDRKQRRAFRRDVQLVFqdSPSAV-NPRMTVRQIIGEPLRHLT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 111 VGDQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ 190
Cdd:TIGR02769 120 SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQA 199
|
170 180
....*....|....*....|...
gi 1863768389 191 A----IVVSHDrdlLDLVQHMAE 209
Cdd:TIGR02769 200 FgtayLFITHD---LRLVQSFCQ 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-504 |
4.10e-08 |
|
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: 52.93 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNGavvSLHIRGPERVGLVGPNGSGKTTLIDTIrGEIEP-RSGTVSL----------RVPYrllpqrlqllddrds 410
Cdd:cd03223 14 RVLLKDL---SFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMpegedllflpQRPY--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 vLAAVSrlaptaddnqLRaelarflldaDTIARPVG-TLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLT 489
Cdd:cd03223 75 -LPLGT----------LR----------EQLIYPWDdVLSGGEQQRLAFARLLLHK--PKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*
gi 1863768389 490 QALTQYRGALLVASH 504
Cdd:cd03223 132 QLLKELGITVISVGH 146
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-200 |
4.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLPQHLvLQSDRTVA--- 83
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKgEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLiKGEPIKYDKKSL-LEVRKTVGivf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 84 ----DVLGIEAVLAALATIDAGQGQPADfevvgdqwDLPDRSIAMLARFGFADLDlRRPIGTLSGGEVILLALAAQFLSE 159
Cdd:PRK13639 85 qnpdDQLFAPTVEEDVAFGPLNLGLSKE--------EVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1863768389 160 PDLLLLDEPTNNLDS-GARA--RLYAALTSwRGQAIVVS-HDRDL 200
Cdd:PRK13639 156 PEIIVLDEPTSGLDPmGASQimKLLYDLNK-EGITIIIStHDVDL 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
251-510 |
4.75e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 251 QRELA--EARIKLDRRQRFARSQAgNVPKIVAgAKKGTAEVSAGKLRGGHQADVADARRrleeaeervrDDDSIEVDlsr 328
Cdd:PLN03073 124 ERDLAkiERRKRKEERQREVQYQA-HVAEMEA-AKAGMPGVYVNHDGNGGGPAIKDIHM----------ENFSISVG--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 329 tsvppGRDIVVTENLVLRNGavvslhirgpERVGLVGPNGSGKTTL--------IDTI---------------------- 378
Cdd:PLN03073 189 -----GRDLIVDASVTLAFG----------RHYGLVGRNGTGKTTFlrymamhaIDGIpkncqilhveqevvgddttalq 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 379 ---------------RGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSVLAAVSRL-----APTADDNQLRAE--LARFLL 436
Cdd:PLN03073 254 cvlntdiertqlleeEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIykrleLIDAYTAEARAAsiLAGLSF 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 437 DADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASHDDAFLS 510
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEP--DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-196 |
5.28e-08 |
|
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: 53.77 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYL 70
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAgKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 71 PQHLVLQSDR----------TVADVLGIEAVLAAlatidagqgqpadfevvgdqwDLPDRSIAMlaRFGFADLDLRRpiG 140
Cdd:cd03253 81 PQDTVLFNDTigynirygrpDATDEEVIEAAKAA---------------------QIHDKIMRF--PDGYDTIVGER--G 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 141 T-LSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQ--AIVVSH 196
Cdd:cd03253 136 LkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-195 |
5.40e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGElaiagltCafpdqvTGLVGRNGVGKSTLLKIIAGELMPTRGSVS---RPE---------RVGYLPQ 72
Cdd:PRK13536 55 AVVNGLSFTVASGE-------C------FGLLGPNGAGKSTIARMILGMTSPDAGKITvlgVPVpararlaraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 73 HLVLQSDRTVADVLgieavlaalatidagqgqpadfEVVGDQWDLPDRSI--AMLARFGFADLDLRR--PIGTLSGGEVI 148
Cdd:PRK13536 122 FDNLDLEFTVRENL----------------------LVFGRYFGMSTREIeaVIPSLLEFARLESKAdaRVSDLSGGMKR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1863768389 149 LLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW--RGQAIVVS 195
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILLT 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
31-173 |
5.56e-08 |
|
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: 53.70 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------SRP--ER----VGYLPQHLVLQSDRTVADVLgieavLAALA 96
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditKLPmhKRarlgIGYLPQEASIFRKLTVEENI-----LAVLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 97 TidagqgqpadFEVVGDQWDlpDRSIAMLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:cd03218 102 I----------RGLSKKERE--EKLEELLEEFHITHL-RKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-496 |
6.75e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSVLAAVSRLAPT--------- 421
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRmtveenlam 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 422 ----ADDNQLRAELAR----FLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALT 493
Cdd:PRK11614 104 ggffAERDQFQERIKWvyelFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ--PRLLLLDEPSLGLAPIIIQQIFDTIE 181
|
...
gi 1863768389 494 QYR 496
Cdd:PRK11614 182 QLR 184
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
109-202 |
6.95e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 54.32 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 109 EVVGDQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLS---EPDLLLLDEPTNNLDSGARARLY---A 182
Cdd:pfam13304 204 EGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLellK 283
|
90 100
....*....|....*....|
gi 1863768389 183 ALTSWRGQAIVVSHDRDLLD 202
Cdd:pfam13304 284 ELSRNGAQLILTTHSPLLLD 303
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-177 |
1.02e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 13 AWPSGELAIA--GLTCAFP-----DQVT---------GLVGRNGVGKSTLLKIIAGELMPTRGSVS---RP--------- 64
Cdd:NF033858 259 ADDDDEPAIEarGLTMRFGdftavDHVSfrirrgeifGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgQPvdagdiatr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 65 ERVGYLPQHLVLQSDRTVADVLGIEAVLaalatidagqgqpadFEVVGDQWdlPDRSIAMLARFGFADLDLRRPiGTLSG 144
Cdd:NF033858 339 RRVGYMSQAFSLYGELTVRQNLELHARL---------------FHLPAAEI--AARVAEMLERFDLADVADALP-DSLPL 400
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 145 GEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR 177
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
31-168 |
1.07e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.72 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------SRP--ER----VGYLPQH------LvlqsdrTVADvlGIEA 90
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfldgeditHLPmhKRarlgIGYLPQEasifrkL------TVED--NILA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 91 VLaALATIDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLdLRRPIGTLSGGE---V-ILLALAAqflsEPDLLLLD 166
Cdd:COG1137 102 VL-ELRKLSKKERE--------------ERLEELLEEFGITHL-RKSKAYSLSGGErrrVeIARALAT----NPKFILLD 161
|
..
gi 1863768389 167 EP 168
Cdd:COG1137 162 EP 163
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-180 |
1.14e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.94 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQhlvlqSDRTVadVLGIEAVLAALATID--------A 100
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRGV--VFQKDALLPWLNVLDnvafglrlR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 101 GQGQPADFEVVGDqwdlpdrsiaMLARFGFADLDlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARL 180
Cdd:COG4525 105 GVPKAERRARAEE----------LLALVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
344-482 |
1.17e-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: 54.92 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV--SLRVPYRLLPQRLQLLDDRDSVLAAVS----R 417
Cdd:TIGR01271 441 VLKN---ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhSGRISFSPQTSWIMPGTIKDNIIFGLSydeyR 517
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 418 LAPTADDNQLRAELARFLLDADTIARPVG-TLSGGERFRATLAALLLSEppPQLLILDEPTNNLDL 482
Cdd:TIGR01271 518 YTSVIKACQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKD--ADLYLLDSPFTHLDV 581
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-200 |
1.18e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpeRVgyLPQHLVLQSDRTVADVLG 87
Cdd:PRK13647 9 DLHFRYKDGTKALKGLSLSIPEgSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV----KV--MGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 88 I------EAVLAALATIDAGQGqPADFEVVGDQwdLPDRSIAMLARFGFADLDLRRPIgTLSGGEVILLALAAQFLSEPD 161
Cdd:PRK13647 83 LvfqdpdDQVFSSTVWDDVAFG-PVNMGLDKDE--VERRVEEALKAVRMWDFRDKPPY-HLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1863768389 162 LLLLDEPTNNLDSGARARLYAALT--SWRGQAIVVS-HDRDL 200
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDrlHNQGKTVIVAtHDVDL 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
31-199 |
1.28e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.55 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------RPERVGYLPQHLVLQSDRTVADvlGIEAVLAALATID 99
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlhaRDRKVGFVFQHYALFRHMTVFD--NIAFGLTVLPRRE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 100 AGQGQPADFEVVgdqwdlpdrsiAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARAR 179
Cdd:PRK10851 107 RPNAAAIKAKVT-----------QLLEMVQLAHLADRYP-AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180
....*....|....*....|....*...
gi 1863768389 180 lyaaLTSWRGQ--------AIVVSHDRD 199
Cdd:PRK10851 175 ----LRRWLRQlheelkftSVFVTHDQE 198
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-204 |
1.65e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.42 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRP-ERVGYLPQHLvlqsdrtvadvlgieavlaalatidagqgqpadfe 109
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDgITPVYKPQYI----------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 110 vvgdqwdlpdrsiamlarfgfadldlrrpigTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSgaRARLYAALTSWR- 188
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAIRRl 117
|
170 180
....*....|....*....|.
gi 1863768389 189 -----GQAIVVSHDRDLLDLV 204
Cdd:cd03222 118 seegkKTALVVEHDLAVLDYL 138
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
343-504 |
1.65e-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: 52.09 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 343 LVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---------------RVPYRLLPQRLQLLDD 407
Cdd:cd03248 28 LVLQD---VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehkylhsKVSLVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 408 RDSV--------LAAVSRLAPTADDNQLRAELArflLDADTIARPVGT-LSGGERFRATLAALLLSEPPpqLLILDEPTN 478
Cdd:cd03248 105 QDNIayglqscsFECVKEAAQKAHAHSFISELA---SGYDTEVGEKGSqLSGGQKQRVAIARALIRNPQ--VLILDEATS 179
|
170 180
....*....|....*....|....*...
gi 1863768389 479 NLDLDSIRQLTQALTQY--RGALLVASH 504
Cdd:cd03248 180 ALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
358-519 |
1.68e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 358 PERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVslrvpyrllpqrlqllddrdsVLAAVSRLaptaddnqlrAELARFLLD 437
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------IYIDGEDI----------LEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 438 ADTIARPVGTLSGGERFRATLAalLLSEPPPQLLILDEPTNNLD---------LDSIRQLTQALTQYRGALLVASHDDAF 508
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALA--LARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKD 128
|
170
....*....|.
gi 1863768389 509 LSELGLTYRID 519
Cdd:smart00382 129 LGPALLRRRFD 139
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
363-491 |
1.75e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.32 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPqrlqllddrDSVLA----------------AVSRL-----AP 420
Cdd:PRK11231 33 LIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPISMLS---------SRQLArrlallpqhhltpegiTVRELvaygrSP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 -------TADDNQLRAELARFLLDADTIA-RPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDL-------DSI 485
Cdd:PRK11231 104 wlslwgrLSAEDNARVNQAMEQTRINHLAdRRLTDLSGGQRQRAFLAMVLAQDTP--VVLLDEPTTYLDInhqvelmRLM 181
|
....*.
gi 1863768389 486 RQLTQA 491
Cdd:PRK11231 182 RELNTQ 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-195 |
1.92e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 1 MPSSVVCSDLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS----------RPERVGY 69
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGgSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqalQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 70 LPQHL-------VLQSDRTVADVLGIEAVLAalatidagQGQPADFEVVGdqwdlpdrsiAMLARFGFADLDLRRpIGTL 142
Cdd:PRK15056 83 VPQSEevdwsfpVLVEDVVMMGRYGHMGWLR--------RAKKRDRQIVT----------AALARVDMVEFRHRQ-IGEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 143 SGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWR--GQAIVVS 195
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdeGKTMLVS 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-202 |
1.96e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGEL--MPTRGSVSRPErvgylpqhlvLQSDRtvaDVLGIEAVLAALATIDAgqgqpa 106
Cdd:COG2401 55 PGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD----------NQFGR---EASLIDAIGRKGDFKDA------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 107 dfevvgdqwdlpdrsIAMLARFGFADLDL-RRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD-SGARARLYAAL 184
Cdd:COG2401 116 ---------------VELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrQTAKRVARNLQ 180
|
170 180
....*....|....*....|.
gi 1863768389 185 TSWR---GQAIVVSHDRDLLD 202
Cdd:COG2401 181 KLARragITLVVATHHYDVID 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
344-505 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRG-----EIEPRSGTVSLRvpyrllpqRLQLLDDRDSVLAAVSRL 418
Cdd:cd03260 15 ALKD---ISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLD--------GKDIYDLDVDVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 A-----PTA------------------DDNQLRAELARFLLDADTIARPV------GTLSGGERFRATLA-ALLLsepPP 468
Cdd:cd03260 84 GmvfqkPNPfpgsiydnvayglrlhgiKLKEELDERVEEALRKAALWDEVkdrlhaLGLSGGQQQRLCLArALAN---EP 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1863768389 469 QLLILDEPTNNLDLDSIRQLTQALTQYRG--ALLVASHD 505
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
351-505 |
2.04e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.84 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvlaAVSRLAP---------- 420
Cdd:COG1118 21 VSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL--------------NGRD----LFTNLPPrerrvgfvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 --------TADDN-------------QLRAELARFL--LDADTIA-RPVGTLSGGERFRATLAALLLSEppPQLLILDEP 476
Cdd:COG1118 83 hyalfphmTVAENiafglrvrppskaEIRARVEELLelVQLEGLAdRYPSQLSGGQRQRVALARALAVE--PEVLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 477 TNNLDL---DSIRQ-LTQALTQYRGALLVASHD 505
Cdd:COG1118 161 FGALDAkvrKELRRwLRRLHDELGGTTVFVTHD 193
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
363-518 |
2.07e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIrgeieprsgtvSLRVPYRLLPQRLQLLDDRDSVLAAVSrlaptaddnqlrAELARFLLdadtia 442
Cdd:cd03227 26 ITGPNGSGKSTILDAI-----------GLALGGAQSATRRRSGVKAGCIVAAVS------------AELIFTRL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 443 rpvgTLSGGERFRATLAALL--LSEPPPQLLILDEPTNNLDLDSIRQLTQALTQYRGA---LLVASHDDAFLSELGLTYR 517
Cdd:cd03227 77 ----QLSGGEKELSALALILalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLPELAELADKLIH 152
|
.
gi 1863768389 518 I 518
Cdd:cd03227 153 I 153
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
34-215 |
2.40e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.38 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLPQHLVLQSDRTVADVL--GIEAVlAALATIDAGQGQPADFEV 110
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAFRRDIQMVFqdSISAV-NPRKTVREIIREPLRHLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 111 VGDQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA---RLYAALTSW 187
Cdd:PRK10419 121 SLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAgviRLLKKLQQQ 200
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 188 RGQAIV-VSHDrdlLDLVQHMAE----MRAGGI 215
Cdd:PRK10419 201 FGTACLfITHD---LRLVERFCQrvmvMDNGQI 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
35-205 |
2.46e-07 |
|
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: 51.37 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAG--ELMPTRGSVsrpervgylpqhlVLQSDrtvaDVLGIEAVLAALATIDAGQGQPADFEVVg 112
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpKYEVTEGEI-------------LFKGE----DITDLPPEERARLGIFLAFQYPPEIPGV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 113 dqwdlpdrSIAMLARF---GFadldlrrpigtlSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRG 189
Cdd:cd03217 93 --------KNADFLRYvneGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE 152
|
170
....*....|....*....
gi 1863768389 190 Q---AIVVSHDRDLLDLVQ 205
Cdd:cd03217 153 EgksVLIITHYQRLLDYIK 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-180 |
3.52e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 37 GRNGVGKSTLLKIIAGELMPTRGSVSrpervgYLPQHLVLQSDRTVADVL------GIEAVLAALA--TIDAGQGQPADf 108
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDAGEVL------WQGEPIRRQRDEYHQDLLylghqpGIKTELTALEnlRFYQRLHGPGD- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 109 evvgdqwdlPDRSIAMLARFG---FADLdlrrPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARL 180
Cdd:PRK13538 107 ---------DEALWEALAQVGlagFEDV----PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
36-197 |
3.86e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 36 VGRNGVGKSTLLKIIAGELMPTRGS----------VSRPER-VGYLPQHLVLQSDRTVADVL--GIEAVLAALATIDAGQ 102
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDlfigekrmndVPPAERgVGMVFQSYALYPHLSVAENMsfGLKLAGAKKEEINQRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 103 GQPADfevvgdqwdlpdrsIAMLARFgfadLDlRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR----- 177
Cdd:PRK11000 115 NQVAE--------------VLQLAHL----LD-RKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmri 174
|
170 180
....*....|....*....|..
gi 1863768389 178 --ARLYAALTSwrgQAIVVSHD 197
Cdd:PRK11000 175 eiSRLHKRLGR---TMIYVTHD 193
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
351-504 |
4.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.59 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvPYRLLPQRLQLLDDRDSV------------------- 411
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-GVDITDKKVKLSDIRKKVglvfqypeyqlfeetiekd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 LA-AVSRLAPTADD--NQLRAELARFLLDADTIA-RPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD------ 481
Cdd:PRK13637 105 IAfGPINLGLSEEEieNRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAME--PKILILDEPTAGLDpkgrde 182
|
170 180
....*....|....*....|....
gi 1863768389 482 -LDSIRQLTQaltQYRGALLVASH 504
Cdd:PRK13637 183 iLNKIKELHK---EYNMTIILVSH 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
338-481 |
5.05e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 51.61 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 338 VVTENLVLRNGAV-----VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDsvl 412
Cdd:COG3839 4 LELENVSKSYGGVealkdIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI--------------GGRD--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 413 aaVSRLAP------------------TADDN-----QLR-----------AELARFL-----LDadtiaRPVGTLSGGER 453
Cdd:COG3839 67 --VTDLPPkdrniamvfqsyalyphmTVYENiafplKLRkvpkaeidrrvREAAELLgledlLD-----RKPKQLSGGQR 139
|
170 180
....*....|....*....|....*....
gi 1863768389 454 FRATLA-ALLLsepPPQLLILDEPTNNLD 481
Cdd:COG3839 140 QRVALGrALVR---EPKVFLLDEPLSNLD 165
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-195 |
5.59e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 21 IAGLTCafPDQVTGLVGRNGVGKSTLLKIIAGEL---------MPTRGSVSRP--ERVGYLPQHLVLQSDRTVADVLGIE 89
Cdd:PLN03211 87 VTGMAS--PGEILAVLGPSGSGKSTLLNALAGRIqgnnftgtiLANNRKPTKQilKRTGFVTQDDILYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 90 AVLAALATidagqgqpadfevvgdqwdLPDRSIAMLARFGFADLDLRRPIGT---------LSGGEVILLALAAQFLSEP 160
Cdd:PLN03211 165 SLLRLPKS-------------------LTKQEKILVAESVISELGLTKCENTiignsfirgISGGERKRVSIAHEMLINP 225
|
170 180 190
....*....|....*....|....*....|....*..
gi 1863768389 161 DLLLLDEPTNNLDSGARARLYAALTSW--RGQAIVVS 195
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLaqKGKTIVTS 262
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-502 |
6.26e-07 |
|
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: 50.56 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV-------------SLR--VPYRLLPQRLQLL 405
Cdd:cd03252 14 GPVILDN---ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpaWLRrqVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 406 DDRDSVlaAVSRLAPTADDNQLRAELA---RFLLDA----DTIARPVGT-LSGGERFRATLAALLLSEppPQLLILDEPT 477
Cdd:cd03252 91 SIRDNI--ALADPGMSMERVIEAAKLAgahDFISELpegyDTIVGEQGAgLSGGQRQRIAIARALIHN--PRILIFDEAT 166
|
170 180
....*....|....*....|....*...
gi 1863768389 478 NNLDLDS---IRQLTQALTQYRGALLVA 502
Cdd:cd03252 167 SALDYESehaIMRNMHDICAGRTVIIIA 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
35-217 |
6.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.93 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS---------------RP--ERVGylpqhLVLQ--SDRTVADVLGIEAVLAal 95
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyiRPvrKRIG-----MVFQfpESQLFEDTVEREIIFG-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 atidagqgqPADFEVVGDQwdLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:PRK13646 111 ---------PKNFKMNLDE--VKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1863768389 176 AR---ARLYAALTSWRGQAIV-VSHDRDllDLVQHMAE---MRAGGITF 217
Cdd:PRK13646 180 SKrqvMRLLKSLQTDENKTIIlVSHDMN--EVARYADEvivMKEGSIVS 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
31-173 |
8.48e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 50.38 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGS-------VSRPE--------RVGYLPQHLVLQSDRTVadvlgIEAVLAAL 95
Cdd:COG1126 28 EVVVIIGPSGSGKSTLLRCINLLEEPDSGTitvdgedLTDSKkdinklrrKVGMVFQQFNLFPHLTV-----LENVTLAP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 ATIdagQGQPADfEVVgdqwdlpDRSIAMLARFGFADLDLRRPiGTLSGGE---V-ILLALAAqflsEPDLLLLDEPTNN 171
Cdd:COG1126 103 IKV---KKMSKA-EAE-------ERAMELLERVGLADKADAYP-AQLSGGQqqrVaIARALAM----EPKVMLFDEPTSA 166
|
..
gi 1863768389 172 LD 173
Cdd:COG1126 167 LD 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
351-494 |
8.51e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRLLPQRLQLLDDRDSVLAAVSRLAPTADDNQL-- 427
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGLQLag 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 428 -----RAELARFLLD----ADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:PRK11248 100 vekmqRLEIAHQMLKkvglEGAEKRYIWQLSGGQRQRVGIARALAAN--PQLLLLDEPFGALDAFTREQMQTLLLK 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
35-197 |
8.96e-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: 49.95 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS-RPERVGYLP----------QHLVLQSDRTVAD--VLGIEAVLAALATIDAG 101
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEEPTSGRIYiGGRDVTDLPpkdrdiamvfQNYALYPHMTVYDniAFGLKLRKVPKDEIDER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 QgqpadfevvgdqwdlpdRSIAMLARFGfADLDlRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLY 181
Cdd:cd03301 111 V-----------------REVAELLQIE-HLLD-RKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180
....*....|....*....|
gi 1863768389 182 AALTSWRGQ----AIVVSHD 197
Cdd:cd03301 171 AELKRLQQRlgttTIYVTHD 190
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
351-492 |
9.32e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEP---RSGTVSLR-----VPYRLLPQRLQLLDD---------RDSVLA 413
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNgmpidAKEMRAISAYVQQDDlfiptltvrEHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 414 AVSRL--APTADDNQLRAE---LARFLLD-ADTI---ARPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDS 484
Cdd:TIGR00955 124 AHLRMprRVTKKEKRERVDevlQALGLRKcANTRigvPGRVKGLSGGERKRLAFASELLTDPP--LLFCDEPTSGLDSFM 201
|
....*...
gi 1863768389 485 IRQLTQAL 492
Cdd:TIGR00955 202 AYSVVQVL 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
35-219 |
1.07e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSV-SRPERVgylpqhlVLQSDRTVADVLGI------EAVLAALATIDAGQGqPAD 107
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVlIRGEPI-------TKENIREVRKFVGLvfqnpdDQIFSPTVEQDIAFG-PIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 108 FEVvgDQWDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYA---AL 184
Cdd:PRK13652 107 LGL--DEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDflnDL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1863768389 185 TSWRGQAIVVSHDRdlLDLVQHMAE----MRAGGITFFG 219
Cdd:PRK13652 184 PETYGMTVIFSTHQ--LDLVPEMADyiyvMDKGRIVAYG 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
416-518 |
1.08e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 416 SRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDS---IRQLTQAL 492
Cdd:PRK13549 374 SRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLN--PKILILDEPTRGIDVGAkyeIYKLINQL 451
|
90 100
....*....|....*....|....*..
gi 1863768389 493 TQYRGALLVASHDdafLSE-LGLTYRI 518
Cdd:PRK13549 452 VQQGVAIIVISSE---LPEvLGLSDRV 475
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
351-482 |
1.14e-06 |
|
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: 50.87 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--RVPYRLLPQRLQLLDDRD--------------SV--- 411
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggEVLQDSARGIFLPPHRRRigyvfqearlfphlSVrgn 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 412 LAAVSRLAPTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLA-ALLLSeppPQLLILDEPTNNLDL 482
Cdd:COG4148 98 LLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGrALLSS---PRLLLMDEPLAALDL 166
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
360-488 |
1.19e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 360 RVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpQRLQLLDDRDSVLAAVSRLAPTADDNQLRAELARFL---- 435
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-------GEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIafgp 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 436 ----LDADTIARPVGT-----------------LSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQL 488
Cdd:PRK13652 105 inlgLDEETVAHRVSSalhmlgleelrdrvphhLSGGEKKRVAIAGVIAMEP--QVLVLDEPTAGLDPQGVKEL 176
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-219 |
1.53e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 32 VTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGY-------LPQHL-----VLQSDR-----TVADVL--GIEAVL 92
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgicLPPEKrrigyVFQDARlfphyKVRGNLryGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 93 aalatidagqgqPADFevvgdqwdlpDRSIAMLarfGFADLDLRRPIgTLSGGEVILLALAAQFLSEPDLLLLDEPTNNL 172
Cdd:PRK11144 106 ------------VAQF----------DKIVALL---GIEPLLDRYPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 173 DSGARARLYAALTSWRGQA----IVVSHDRD-LLDLVQHMAEMRAGGITFFG 219
Cdd:PRK11144 160 DLPRKRELLPYLERLAREInipiLYVSHSLDeILRLADRVVVLEQGKVKAFG 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-173 |
1.58e-06 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 50.89 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 3 SSVVCSDLWFAWPSGELAIAGLTCAFP-DQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------------RpERV 67
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNILSDISLTIKmNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlngfslkdidrhtlR-QFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 68 GYLPQ-----------HLVLQSDRTVADVLGIEAVlaALATIDAgqgqpaDFEvvgdqwDLPdrsiamlarFGFaDLDLR 136
Cdd:TIGR01193 551 NYLPQepyifsgsileNLLLGAKENVSQDEIWAAC--EIAEIKD------DIE------NMP---------LGY-QTELS 606
|
170 180 190
....*....|....*....|....*....|....*..
gi 1863768389 137 RPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:TIGR01193 607 EEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
344-493 |
1.65e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 48.95 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSVLAAVSRLA---- 419
Cdd:cd03369 23 VLKN---VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI--------------DGIDISTIPLEDLRsslt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 -----PTADDNQLRAELARF-------LLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDS--- 484
Cdd:cd03369 86 iipqdPTLFSGTIRSNLDPFdeysdeeIYGALRVSEGGLNLSQGQRQLLCLARALLKR--PRVLVLDEATASIDYATdal 163
|
170
....*....|...
gi 1863768389 485 ----IRQLTQALT 493
Cdd:cd03369 164 iqktIREEFTNST 176
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-181 |
1.86e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPeRVGYLPQHLVLQSDRTVADVLGIEA-VLAALAT 97
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniAKP-YCTYIGHNLGLKLEMTVFENLKFWSeIYNSAET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 98 IDAGqgqpadfevvgdqwdlpdrsiamLARFGFADLdLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR 177
Cdd:PRK13541 104 LYAA-----------------------IHYFKLHDL-LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
....
gi 1863768389 178 ARLY 181
Cdd:PRK13541 160 DLLN 163
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-215 |
2.04e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 13 AWPSGELAIAGLT----CAFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGS-------VS----------RPERVGYLP 71
Cdd:PRK10535 13 SYPSGEEQVEVLKgislDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVAtldadalaqlRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 72 QHLVLQSDRTVADVLGIEAVLAALATIDAGQgqpadfevvgdqwdlpdRSIAMLARFGFADLDLRRPiGTLSGGEVILLA 151
Cdd:PRK10535 93 QRYHLLSHLTAAQNVEVPAVYAGLERKQRLL-----------------RAQELLQRLGLEDRVEYQP-SQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 152 LAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLLDLVQHMAEMRAGGI 215
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGhtvIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
341-506 |
2.04e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL--------RVPYRLLPQRLQLLDD----- 407
Cdd:PRK13540 13 DQPLLQQ---ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqsikkdLCTYQKQLCFVGHRSGinpyl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 408 --RDSVLAAVSrlapTADDNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSI 485
Cdd:PRK13540 90 tlRENCLYDIH----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSK--AKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|....
gi 1863768389 486 RQLTQALTQYR---GALLVASHDD 506
Cdd:PRK13540 164 LTIITKIQEHRakgGAVLLTSHQD 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
35-173 |
2.16e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 49.69 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS---------RPER--VGYLPQHLVLQSDRTVAD-------VLGIEAvlaalA 96
Cdd:COG3839 34 LLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdvtdlPPKDrnIAMVFQSYALYPHMTVYEniafplkLRKVPK-----A 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 97 TIDAgqgqpadfevvgdqwdlpdRSIAMLARFGFADLDLRRPiGTLSGGE---VillALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:COG3839 109 EIDR-------------------RVREAAELLGLEDLLDRKP-KQLSGGQrqrV---ALGRALVREPKVFLLDEPLSNLD 165
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
321-481 |
2.28e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.70 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 321 SIEVDlsRTSVPPGRDIVVTEnlvlrngavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpq 400
Cdd:PRK10851 2 SIEIA--NIKKSFGRTQVLND---------ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 401 rlqlldDRDsvlaaVSRLapTADDNQL-----RAELARFLLDADTIA----------RPVGT------------------ 447
Cdd:PRK10851 63 ------GTD-----VSRL--HARDRKVgfvfqHYALFRHMTVFDNIAfgltvlprreRPNAAaikakvtqllemvqlahl 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1863768389 448 -------LSGGERFRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:PRK10851 130 adrypaqLSGGQKQRVALARALAVE--PQILLLDEPFGALD 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
354-504 |
2.53e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 354 HIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPqrlqlldDRDSVLAAVSRLAPTADD--------- 424
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-------DRSRFMAYLGHLPGLKADlstlenlhf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 425 -NQLRAELARFLLD-----------ADTIARpvgTLSGGERFRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:PRK13543 106 lCGLHGRRAKQMPGsalaivglagyEDTLVR---QLSAGQKKRLALARLWLSPAP--LWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 1863768389 493 TQY---RGALLVASH 504
Cdd:PRK13543 181 SAHlrgGGAALVTTH 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
33-227 |
2.60e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 33 TGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPERVGYLPQH--LVLQSDRTVadvLGIEAVLAALATida 100
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstSKNKDIKQIRKKvgLVFQFPESQ---LFEETVLKDVAF--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 101 gqgQPADFEVvgDQWDLPDRSIAMLARFGFA-DLDLRRPIgTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARAR 179
Cdd:PRK13649 110 ---GPQNFGV--SQEEAEALAREKLALVGISeSLFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 180 LYAALTSWR--GQAIV-VSHdrdLLDLVQHMAE----MRAGGITFFGGNFTAFTD 227
Cdd:PRK13649 184 LMTLFKKLHqsGMTIVlVTH---LMDDVANYADfvyvLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
351-505 |
2.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.92 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR---VPYrllpqrlqlldDRDSVLAAVSRL--------- 418
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepIKY-----------DKKSLLEVRKTVgivfqnpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 ---APTADDNQL---------RAELARFLLDA-------DTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNN 479
Cdd:PRK13639 90 qlfAPTVEEDVAfgplnlglsKEEVEKRVKEAlkavgmeGFENKPPHHLSGGQKKRVAIAGILAMK--PEIIVLDEPTSG 167
|
170 180
....*....|....*....|....*....
gi 1863768389 480 LD---LDSIRQLTQALTQYRGALLVASHD 505
Cdd:PRK13639 168 LDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
340-504 |
2.76e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIrgPER--VGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDR------DSV 411
Cdd:PRK10790 352 DDNLVLQN---INLSV--PSRgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--------------DGRplsslsHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 L----AAVSR----LAPTADDN-------------------QLrAELARFLldADTIARPVG----TLSGGERFRATLAA 460
Cdd:PRK10790 413 LrqgvAMVQQdpvvLADTFLANvtlgrdiseeqvwqaletvQL-AELARSL--PDGLYTPLGeqgnNLSVGQKQLLALAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1863768389 461 LLLSepPPQLLILDEPTNNLDLDSIRQLTQALTQYR--GALLVASH 504
Cdd:PRK10790 490 VLVQ--TPQILILDEATANIDSGTEQAIQQALAAVRehTTLVVIAH 533
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
54-210 |
3.00e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 54 LMPTRGSVSRPERVG--YLPQHL-VLQSDRTVADVLGIEAVLAALATIDagqgQPADFEvvgdqwdlpdrSIAMLARFGF 130
Cdd:PRK00635 734 TTDNRTSIPCPSCLGkrFLPQVLeVRYKGKNIADILEMTAYEAEKFFLD----EPSIHE-----------KIHALCSLGL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 131 ADLDLRRPIGTLSGGEVILLALAAQFLS---EPDLLLLDEPTNNL---DSGARARLYAALTSWRGQAIVVSHDRDLLDLV 204
Cdd:PRK00635 799 DYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVA 878
|
....*.
gi 1863768389 205 QHMAEM 210
Cdd:PRK00635 879 DYVLEL 884
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
334-518 |
3.19e-06 |
|
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: 47.81 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 334 GRDIVVTENLVLRnGAV--VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYRllpqrlqllddRDS 410
Cdd:cd03215 1 GEPVLEVRGLSVK-GAVrdVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVT-----------RRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLAAVSR-LAPTADDNQLRAELARFLLDADTIARPVgtLSGGERFRATLAALLLSEPppQLLILDEPTNNLDL---DSIR 486
Cdd:cd03215 69 PRDAIRAgIAYVPEDRKREGLVLDLSVAENIALSSL--LSGGNQQKVVLARWLARDP--RVLILDEPTRGVDVgakAEIY 144
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 487 QLTQALTQYRGALLVASHDDAFLseLGLTYRI 518
Cdd:cd03215 145 RLIRELADAGKAVLLISSELDEL--LGLCDRI 174
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
341-492 |
3.42e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 48.26 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD----------S 410
Cdd:cd03244 16 LPPVLKN---ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI--------------DGVDiskiglhdlrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLAAV------------SRLAP--TADDNQLRAELARFLLDADTIARPVG----------TLSGGERFRATLAALLLSEP 466
Cdd:cd03244 79 RISIIpqdpvlfsgtirSNLDPfgEYSDEELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKS 158
|
170 180
....*....|....*....|....*.
gi 1863768389 467 PpqLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:cd03244 159 K--ILVLDEATASVDPETDALIQKTI 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-173 |
3.71e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 37 GRNGVGKSTLLKIIAGELMPTRG-------SVSRPER---VGYLPQHLVLQSDRTvadvlgieaVLAALATIDAGQGQPA 106
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGqiqidgkTATRGDRsrfMAYLGHLPGLKADLS---------TLENLHFLCGLHGRRA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 107 DfevvgdqwDLPDRSIAMLARFGFADLDLRRpigtLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:PRK13543 115 K--------QMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-199 |
3.96e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.67 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVsrpERVGYlpqHLVLQSD--------RTVADVLGI-EAVL---AALATIDAGq 102
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSSGTI---TIAGY---HITPETGnknlkklrKKVSLVFQFpEAQLfenTVLKDVEFG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 103 gqPADFEVVGDQwdLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYA 182
Cdd:PRK13641 111 --PKNFGFSEDE--AKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ 186
|
170 180
....*....|....*....|
gi 1863768389 183 ALTSWRGQA---IVVSHDRD 199
Cdd:PRK13641 187 LFKDYQKAGhtvILVTHNMD 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-173 |
3.97e-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: 48.25 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQHLVLQSdRTVADvlgieavlaAL 95
Cdd:cd03252 27 PGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpaWLRRQVGVVLQENVLFN-RSIRD---------NI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 96 ATIDAGqgqpADFEVVGDQWDLPD-RSIAMLARFGFADLDLRRPIGtLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:cd03252 97 ALADPG----MSMERVIEAAKLAGaHDFISELPEGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-179 |
5.81e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 19 LAIAGLTCAFP-DQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------RPE---RVGYLPQHL--VLQSDRT 81
Cdd:NF033858 15 VALDDVSLDIPaGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhRRAvcpRIAYMPQGLgkNLYPTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 82 VADVLGIEAVLAalatidaGQGQPADfevvgdqwdlpDRSIAMLAR----FGFADldlrRPIGTLSGGEVILLALAAQFL 157
Cdd:NF033858 95 VFENLDFFGRLF-------GQDAAER-----------RRRIDELLRatglAPFAD----RPAGKLSGGMKQKLGLCCALI 152
|
170 180
....*....|....*....|..
gi 1863768389 158 SEPDLLLLDEPTNNLDSGARAR 179
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQ 174
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-215 |
5.92e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGeLMPTRGSV-------------SRPERVGYLPQ--HLVLQSDR---TVADV-LGIEAV 91
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLG-FLPYQGSLkingielreldpeSWRKHLSWVGQnpQLPHGTLRdnvLLGNPdASDEQL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 92 LAALAtidagQGQPADFevvgdqwdlpdrsIAMLArfgfadLDLRRPIG----TLSGGEVILLALAAQFLSEPDLLLLDE 167
Cdd:PRK11174 456 QQALE-----NAWVSEF-------------LPLLP------QGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1863768389 168 PTNNLDSGARARLYAALTS-WRGQ-AIVVSHDRDLLDLVQHMAEMRAGGI 215
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAaSRRQtTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
31-173 |
6.46e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 48.26 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----------SRPE------RVGYLPQHLVLQSDRTVADVLGIEAVLAa 94
Cdd:PRK11153 32 EIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltalSEKElrkarrQIGMIFQHFNLLSSRTVFDNVALPLELA- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 latidagqGQPADfevvgdqwDLPDRSIAMLARFGFADLDLRRPiGTLSGGE----VILLALAaqflSEPDLLLLDEPTN 170
Cdd:PRK11153 111 --------GTPKA--------EIKARVTELLELVGLSDKADRYP-AQLSGGQkqrvAIARALA----SNPKVLLCDEATS 169
|
...
gi 1863768389 171 NLD 173
Cdd:PRK11153 170 ALD 172
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-197 |
7.04e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.77 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGS-------VSRP--ERvGYLPQHLVLQSDRTVAD--VLGIEavlaaLAT 97
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgkpVEGPgaER-GVVFQNEGLLPWRNVQDnvAFGLQ-----LAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 98 IDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLDlRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR 177
Cdd:PRK11248 100 VEKMQRL--------------EIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180
....*....|....*....|....
gi 1863768389 178 ARLYA-ALTSWRG---QAIVVSHD 197
Cdd:PRK11248 165 EQMQTlLLKLWQEtgkQVLLITHD 188
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
406-514 |
7.05e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 48.39 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 406 DDRDSVLAAVSRLAPTADDNQLRA-ELARFLLD--ADTIARPV-------GTLsggeRFRATLAALLLSEPPPqLLILDE 475
Cdd:COG4637 212 ERFERILEALRDAFPGFEDIEVEPdEDGRVLLEfrEKGLDRPFparelsdGTL----RFLALLAALLSPRPPP-LLCIEE 286
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1863768389 476 PTNNLDLDSIRQLTQALTQY--RGALLVASHDDAFLSELGL 514
Cdd:COG4637 287 PENGLHPDLLPALAELLREAseRTQVIVTTHSPALLDALEP 327
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-173 |
7.75e-06 |
|
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: 47.14 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV---------SRPE------RVGYLPQHLVLQSDRTVadvlgIEAVLAAL 95
Cdd:cd03262 27 EVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltdDKKNinelrqKVGMVFQQFNLFPHLTV-----LENITLAP 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 96 ATIdagQGQPADfEVVgdqwdlpDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:cd03262 102 IKV---KGMSKA-EAE-------ERALELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-180 |
7.98e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.60 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 3 SSVVCSDLWFAWPSGELaIAGLTCAFPDQ-VTGLVGRNGVGKSTLLKIIAG--ELMPTrgsvSRPERVGYLPQHLVLQSD 79
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEV-LDGVNLEIPDNtITALMGPSGSGKSTLLRVFNRliELYPE----ARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 80 -----RTVADVLGIEAVLAALATIDAGQGQPADFEVVGDQWDLPDRSIAMLARFGFADL---DLRRPIGTLSGGEVILLA 151
Cdd:PRK14247 77 vielrRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEvkdRLDAPAGKLSGGQQQRLC 156
|
170 180
....*....|....*....|....*....
gi 1863768389 152 LAAQFLSEPDLLLLDEPTNNLDSGARARL 180
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKI 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
31-169 |
8.30e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------------RPERVGYLPQHLVLQSDRTVADVLGIEAVLAala 96
Cdd:PRK11614 32 EIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkditdwqtakiMREAVAIVPEGRRVFSRMTVEENLAMGGFFA--- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 97 tiDAGQGQpadfEVVGDQWDLpdrsiamlarfgFADLDLRRP--IGTLSGGEVILLALAAQFLSEPDLLLLDEPT 169
Cdd:PRK11614 109 --ERDQFQ----ERIKWVYEL------------FPRLHERRIqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-195 |
9.12e-06 |
|
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: 46.47 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIA---------GELM----PTRGSVSRpeRVGYLPQHLVLQSDRTVADVLGIEAVLAAL 95
Cdd:cd03232 32 PGTLTALMGESGAGKTTLLDVLAgrktagvitGEILingrPLDKNFQR--STGYVEQQDVHSPNLTVREALRFSALLRGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 ATIDagqgqpadfevvgdqwdlpdrsiamlarfgfadldlRRpigtlsggeviLLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:cd03232 110 SVEQ------------------------------------RK-----------RLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|..
gi 1863768389 176 ARARLYAAL--TSWRGQAIVVS 195
Cdd:cd03232 143 AAYNIVRFLkkLADSGQAILCT 164
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
436-505 |
9.68e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 9.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 436 LDADTIARPVGTLSGGERFRATLAALLLS-EPPPQLLILDEPTNNLDLDSIRQLT---QALTQYRGALLVASHD 505
Cdd:PRK00635 798 LDYLPLGRPLSSLSGGEIQRLKLAYELLApSKKPTLYVLDEPTTGLHTHDIKALIyvlQSLTHQGHTVVIIEHN 871
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
34-239 |
9.86e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSVSRPER--VGYLPQH-----LVLQSDRTVAD--VLGIEA----VLAALATIDA 100
Cdd:PRK10762 282 GVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangIVYISEDRKRDglVLGMSVkenmSLTALRYFSR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 101 GQGQ---PADFEVVGDQWDLpdrsiamlarFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGAR 177
Cdd:PRK10762 362 AGGSlkhADEQQAVSDFIRL----------FNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 178 ARLYAALTSWRGQA---IVVSHDR-DLLDLVQHMAEMRAGGITffgGNFTAfTDAlavEQE---AAARG 239
Cdd:PRK10762 432 KEIYQLINQFKAEGlsiILVSSEMpEVLGMSDRILVMHEGRIS---GEFTR-EQA---TQEklmAAAVG 493
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
341-492 |
9.93e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 47.15 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVLAAVSRL-- 418
Cdd:cd03249 15 DVPILKG---LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL-----------DGVDIRDLNLRWLRSQig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 --------------------APTADDNQLR-----AELARFLLDA----DTIARPVGT-LSGGERFRATLAALLLSEPPp 468
Cdd:cd03249 81 lvsqepvlfdgtiaenirygKPDATDEEVEeaakkANIHDFIMSLpdgyDTLVGERGSqLSGGQKQRIAIARALLRNPK- 159
|
170 180
....*....|....*....|....
gi 1863768389 469 qLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:cd03249 160 -ILLLDEATSALDAESEKLVQEAL 182
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
363-505 |
1.23e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIR----GEIEPRS-------------GTVSL---------RVPYRLLPQRLQLLDDRDSVLAAVS 416
Cdd:COG0419 28 IVGPNGAGKSTILEAIRyalyGKARSRSklrsdlinvgseeASVELefehggkryRIERRQGEFAEFLEAKPSERKEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 RLAPT-------ADDNQLRAELARFLLDADTIAR-------------PVGTLSGGERFRATLAALLlsepppqLLILDep 476
Cdd:COG0419 108 RLLGLeiyeelkERLKELEEALESALEELAELQKlkqeilaqlsgldPIETLSGGERLRLALADLL-------SLILD-- 178
|
170 180
....*....|....*....|....*....
gi 1863768389 477 TNNLDLDSIRQLTQALTQyrgaLLVASHD 505
Cdd:COG0419 179 FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
31-180 |
1.34e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.52 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPerVGYLPQHLVLQSDRTVAdvlgieavlaalat 97
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlshvppyQRP--INMMFQSYALFPHMTVE-------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 98 idagqgQPADFEVVGDQW---DLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDS 174
Cdd:PRK11607 110 ------QNIAFGLKQDKLpkaEIASRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
....*.
gi 1863768389 175 GARARL 180
Cdd:PRK11607 183 KLRDRM 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
443-506 |
1.56e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 443 RPVGTLSGGER------FRATLAALLLSEPPpqLLILDEPTNNLDLDSIRQLTQALTQYRGAL---LVASHDD 506
Cdd:PRK03918 784 RPLTFLSGGERialglaFRLALSLYLAGNIP--LLILDEPTPFLDEERRRKLVDIMERYLRKIpqvIIVSHDE 854
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
122-210 |
1.64e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 122 IAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPD--LLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSH 196
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGntvLVVEH 197
|
90
....*....|....
gi 1863768389 197 DRDLLDLVQHMAEM 210
Cdd:cd03270 198 DEDTIRAADHVIDI 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
115-209 |
1.65e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 115 WDLPDRSIAMLARF----GFADLDLRRPIGTLSGG--EVILLA--LAAqflsEPDLLLLDEPTNNLDSGARARLYAALTS 186
Cdd:PRK15439 373 WIKPARENAVLERYrralNIKFNHAEQAARTLSGGnqQKVLIAkcLEA----SPQLLIVDEPTRGVDVSARNDIYQLIRS 448
|
90 100
....*....|....*....|....*.
gi 1863768389 187 WRGQAIVV---SHDrdlLDLVQHMAE 209
Cdd:PRK15439 449 IAAQNVAVlfiSSD---LEEIEQMAD 471
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
31-197 |
1.70e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.59 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpeRVGYLPQH-------LVLQSDR-----TVADVLGIeavlaalati 98
Cdd:PRK11247 39 QFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----LAGTAPLAearedtrLMFQDARllpwkKVIDNVGL---------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 99 dagqgqpadfevvGDQWDLPDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARA 178
Cdd:PRK11247 105 -------------GLKGQWRDAALQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180
....*....|....*....|...
gi 1863768389 179 RLYAALTS-WRGQA---IVVSHD 197
Cdd:PRK11247 171 EMQDLIESlWQQHGftvLLVTHD 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
351-505 |
1.75e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.76 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV---------SLRVPYRLLPQRLQLLDDRDSVLAAVS----- 416
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLMKLRESVGMVFQDPDNQLFSASvyqdv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 417 -----RLAPTADDNQLRAELArflLDADTIA----RPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLD---LDS 484
Cdd:PRK13636 105 sfgavNLKLPEDEVRKRVDNA---LKRTGIEhlkdKPTHCLSFGQKKRVAIAGVLVMEP--KVLVLDEPTAGLDpmgVSE 179
|
170 180
....*....|....*....|..
gi 1863768389 485 IRQLTQALTQYRG-ALLVASHD 505
Cdd:PRK13636 180 IMKLLVEMQKELGlTIIIATHD 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
322-504 |
1.76e-05 |
|
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: 46.04 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 322 IEV-DLSRTSVPPGRDIVVTENlvlrngavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpq 400
Cdd:cd03258 2 IELkNVSKVFGDTGGKVTALKD--------VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 401 rlqllDDRDsvlaaVSRLAPTaddnQLRAELARF--------LLDADT----IARP---------------------VG- 446
Cdd:cd03258 65 -----DGTD-----LTLLSGK----ELRKARRRIgmifqhfnLLSSRTvfenVALPleiagvpkaeieervlellelVGl 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 447 ---------TLSGGERFRATLAALLLSEppPQLLILDEPTNNLD---LDSIRQLTQALTQYRG-ALLVASH 504
Cdd:cd03258 131 edkadaypaQLSGGQKQRVGIARALANN--PKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITH 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
351-481 |
1.86e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.62 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL----RVPYRLLPQRLQLLDD------------------- 407
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdEKNKKKTKEKEKVLEKlviqktrfkkikkikeirr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 408 -------------------RDSVLAAVSRLAPTADDNQLRAELARFL-LDADTIARPVGTLSGGERFRATLAALLLSEpp 467
Cdd:PRK13651 106 rvgvvfqfaeyqlfeqtieKDIIFGPVSMGVSKEEAKKRAAKYIELVgLDESYLQRSPFELSGGQKRRVALAGILAME-- 183
|
170
....*....|....
gi 1863768389 468 PQLLILDEPTNNLD 481
Cdd:PRK13651 184 PDFLVFDEPTAGLD 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
340-391 |
1.98e-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: 45.54 E-value: 1.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL 391
Cdd:cd03250 16 ETSFTLKD---INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV 64
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
351-490 |
2.21e-05 |
|
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: 45.69 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD--------------------- 409
Cdd:cd03300 19 VSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL--------------DGKDitnlpphkrpvntvfqnyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 ---SVLAAVS---RLAPTaDDNQLRAELARFL----LDaDTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNN 479
Cdd:cd03300 85 phlTVFENIAfglRLKKL-PKAEIKERVAEALdlvqLE-GYANRKPSQLSGGQQQRVAIARALVNE--PKVLLLDEPLGA 160
|
170
....*....|.
gi 1863768389 480 LDLdSIRQLTQ 490
Cdd:cd03300 161 LDL-KLRKDMQ 170
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-173 |
2.30e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 45.77 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 24 LTCaFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS----------RP---------ERVGYLPQHLVLQSDRTVAD 84
Cdd:COG4161 23 LEC-PSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdfsqKPsekairllrQKVGMVFQQYNLWPHLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 85 VLgIEAVLAALatidagqGQPADfevvgdqwDLPDRSIAMLARFGFADLDLRRPIgTLSGGEVILLALAAQFLSEPDLLL 164
Cdd:COG4161 102 NL-IEAPCKVL-------GLSKE--------QAREKAMKLLARLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQVLL 164
|
....*....
gi 1863768389 165 LDEPTNNLD 173
Cdd:COG4161 165 FDEPTAALD 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
351-505 |
2.47e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 46.16 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---------------RV------PyrllpqrlqlldDRD 409
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlseetvwdvrrQVgmvfqnP------------DNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 SVLAAVsrlaptADD------NQ--LRAELARFLLDA-------DTIARPVGTLSGGERFRATLAALLLSEppPQLLILD 474
Cdd:PRK13635 94 FVGATV------QDDvafgleNIgvPREEMVERVDQAlrqvgmeDFLNREPHRLSGGQKQRVAIAGVLALQ--PDIIILD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 475 EPTNNLD-------LDSIRQLTQaltQYRGALLVASHD 505
Cdd:PRK13635 166 EATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
341-502 |
2.68e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.94 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlQLLDDRDSVL-------A 413
Cdd:PRK11176 355 EVPALRN---INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-----------DGHDLRDYTLaslrnqvA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 414 AVSR------------LAPTADDNQLRAELARFLLDA-------------DTIARPVGT-LSGGERFRATLAALLLSEPP 467
Cdd:PRK11176 421 LVSQnvhlfndtiannIAYARTEQYSREQIEEAARMAyamdfinkmdnglDTVIGENGVlLSGGQRQRIAIARALLRDSP 500
|
170 180 190
....*....|....*....|....*....|....*...
gi 1863768389 468 pqLLILDEPTNNLDLDSIRQLTQALTQY---RGALLVA 502
Cdd:PRK11176 501 --ILILDEATSALDTESERAIQAALDELqknRTSLVIA 536
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-233 |
3.26e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.81 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 34 GLVGRNGVGKSTLLKIIAGELMPTRGSV---------------SRPERVGYL---PQHLVLQSdrTVA-DV------LGI 88
Cdd:PRK13637 37 GLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvklsDIRKKVGLVfqyPEYQLFEE--TIEkDIafgpinLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 89 EA------VLAALatidagqgqpadfEVVG-DQWDLPDRSiamlarfgfadldlrrPIgTLSGGEVILLALAAQFLSEPD 161
Cdd:PRK13637 115 SEeeienrVKRAM-------------NIVGlDYEDYKDKS----------------PF-ELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 162 LLLLDEPTNNLDSGARARLYAALTSWRGQ----AIVVSHD-RDLLDLVQHMAEMRAGGITFFGGNFTAFTDALAVEQ 233
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEynmtIILVSHSmEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
362-505 |
3.27e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 362 GLVGPNGSGKTTLIDTIRGEIEPRSGTVSL---------------RVPYRLLPQRLQLLDDRDSVLA--------AVSRL 418
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLdaqpleswsskafarKVAYLPQQLPAAEGMTVRELVAigrypwhgALGRF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 419 AptADDNQlRAELARFLLDADTIA-RPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLD---SIRQLTQALTQ 494
Cdd:PRK10575 121 G--AADRE-KVEEAISLVGLKPLAhRLVDSLSGGERQRAWIAMLVAQD--SRCLLLDEPTSALDIAhqvDVLALVHRLSQ 195
|
170
....*....|..
gi 1863768389 495 YRGALLVAS-HD 505
Cdd:PRK10575 196 ERGLTVIAVlHD 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
362-512 |
3.48e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.77 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 362 GLVGPNGSGKTTLIDTIRGEIEPRSGTV---------------SLRVPYRLLPQRLQLL---DDRDSVLA-AVSRLAPTA 422
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgllALRQQVATVFQDPEQQifyTDIDSDIAfSLRNLGVPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 423 DDNQLRAELARFLLDADTI-ARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYRGA--- 498
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFrHQPIQCLSHGQKKRVAIAGALVLQ--ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnh 188
|
170
....*....|....
gi 1863768389 499 LLVASHDDAFLSEL 512
Cdd:PRK13638 189 VIISSHDIDLIYEI 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
136-194 |
3.48e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 3.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 136 RRPIGTLSGG---EVILlalaAQFLSEP-DLLLLDEPTNNLDSGARARLYAAL--TSWRGQAIVV 194
Cdd:PRK11288 391 EQLIMNLSGGnqqKAIL----GRWLSEDmKVILLDEPTRGIDVGAKHEIYNVIyeLAAQGVAVLF 451
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-184 |
3.66e-05 |
|
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: 45.30 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQHLVLQSDrTVADVLGI-------EA 90
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrdytlaSLRRQIGLVSQDVFLFND-TVAENIAYgrpgatrEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 91 VLAALATIDAgqgqpADFEVvgdqwDLPDRSIAMLARFGfadldlrrpiGTLSGGEVILLALAAQFLSEPDLLLLDEPTN 170
Cdd:cd03251 108 VEEAARAANA-----HEFIM-----ELPEGYDTVIGERG----------VKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170
....*....|....
gi 1863768389 171 NLDSGARARLYAAL 184
Cdd:cd03251 168 ALDTESERLVQAAL 181
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
139-201 |
3.67e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 3.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 139 IGTLSGGEVILLALA-----AQFL-SEPDLLLLDEPTNNLDSGARARLYAAL------TSWRGQAIVVSHDRDLL 201
Cdd:PRK01156 799 IDSLSGGEKTAVAFAlrvavAQFLnNDKSLLIMDEPTAFLDEDRRTNLKDIIeyslkdSSDIPQVIMISHHRELL 873
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
35-199 |
4.23e-05 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 45.33 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS-----------------RPERVGYLPQHLVLQSDRTVAD--VLGIEAvlaal 95
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamsrkelrelRRKKISMVFQSFALLPHRTVLEnvAFGLEV----- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 96 atidagQGQPADFEVvgdqwdlpDRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSG 175
Cdd:cd03294 130 ------QGVPRAERE--------ERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180
....*....|....*....|....*...
gi 1863768389 176 ARARL---YAALTSWRGQAIV-VSHDRD 199
Cdd:cd03294 195 IRREMqdeLLRLQAELQKTIVfITHDLD 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-219 |
4.25e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.19 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 27 AFPDQVTGLVGRNGVGKSTLLKIIAGELMP-TRGSVSR------------PERVGYLPQ------------HLVLQS--- 78
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVllngmpidakemRAISAYVQQddlfiptltvreHLMFQAhlr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 79 -DRTVAD---VLGIEAVLAALATIDAGQgqpadfEVVGDqwdlPDRsiamlarfgfadldlrrpIGTLSGGEVILLALAA 154
Cdd:TIGR00955 128 mPRRVTKkekRERVDEVLQALGLRKCAN------TRIGV----PGR------------------VKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 155 QFLSEPDLLLLDEPTNNLDSGARARLYAALT--SWRGQAIVVS-HD--RDLLDLVQHMAEMRAGGITFFG 219
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKglAQKGKTIICTiHQpsSELFELFDKIILMAEGRVAYLG 249
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-204 |
4.28e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV------SRPERVGYLPQHLVLQSDRTVADVLG-------IEAVLAA 94
Cdd:COG3593 21 LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKfdeedfYLGDDPDLPEIEIELTFGSLLSRLLRlllkeedKEELEEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 95 LATIDA--------------------GQGQPADFEVVGDQWDLPDRSIamlaRFGFADlDLRRPIGTLSGGE--VILLAL 152
Cdd:COG3593 101 LEELNEelkealkalnellseylkelLDGLDLELELSLDELEDLLKSL----SLRIED-GKELPLDRLGSGFqrLILLAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 153 AAQFL-----SEPDLLLLDEPTNNLDSGARARLYAAL---TSWRGQAIVVSHDRDLLDLV 204
Cdd:COG3593 176 LSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLkelSEKPNQVIITTHSPHLLSEV 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
133-202 |
4.62e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 4.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 133 LDLRRPIGTLSGGEVILLALAAQFLSEPD--LLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLLD 202
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGntvILIEHNLDVLS 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-224 |
4.66e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 133 LDLRRPIGTLSGGEVILLALAAQFLSEPD--LLLLDEPTNNLDSGARARLYAALTSWRGQA---IVVSHDRDLLDLVQHM 207
Cdd:TIGR00630 480 LSLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGntlIVVEHDEDTIRAADYV 559
|
90
....*....|....*...
gi 1863768389 208 AEMRAG-GItfFGGNFTA 224
Cdd:TIGR00630 560 IDIGPGaGE--HGGEVVA 575
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-197 |
4.72e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.96 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 32 VTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPE--------------------------RVGYLPQHLVLQSDRTVadv 85
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQHFNLWSHMTV--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 lgIEAVLAAlatidagqgqpaDFEVVG-DQWDLPDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLL 164
Cdd:PRK10619 110 --LENVMEA------------PIQVLGlSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1863768389 165 LDEPTNNLDS---GARARLYAALTSWRGQAIVVSHD 197
Cdd:PRK10619 176 FDEPTSALDPelvGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
31-173 |
4.86e-05 |
|
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: 46.44 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSDrTVAD--VLGIE-AVLAALATIDAGQGQPad 107
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPG-TIKDniIFGLSyDEYRYTSVIKACQLEE-- 529
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 108 fevvgDQWDLPDRSIAMLARFGFadldlrrpigTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:TIGR01271 530 -----DIALFPEKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
30-200 |
5.74e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.57 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 30 DQVTGLVGRNGVGKSTLLKIIAGELMptrGSVSRPERVGYLPQHLVLQSDRTvadvlgiEAVLaalaTIDAGQGQPADFE 109
Cdd:cd03279 28 NGLFLICGPTGAGKSTILDAITYALY---GKTPRYGRQENLRSVFAPGEDTA-------EVSF----TFQLGGKKYRVER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 110 VVG---DQWdlpdRSIAMLARFGFADLdLRRPIGTLSGGEVILLALA-AQFLSEP---------DLLLLDEPTNNLDSGA 176
Cdd:cd03279 94 SRGldyDQF----TRIVLLPQGEFDRF-LARPVSTLSGGETFLASLSlALALSEVlqnrggarlEALFIDEGFGTLDPEA 168
|
170 180
....*....|....*....|....*..
gi 1863768389 177 RARLYAALTSWRGQ---AIVVSHDRDL 200
Cdd:cd03279 169 LEAVATALELIRTEnrmVGVISHVEEL 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-196 |
5.85e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 28 FPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV--------------SRPERVGYLPQHLVLQSDRTVAD--VLGIEAV 91
Cdd:PRK10762 28 YPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlylgkevtfngpksSQEAGIGIIHQELNLIPQLTIAEniFLGREFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 92 lAALATIDagqgqpadfevvgdqWD-LPDRSIAMLARFGFaDLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTN 170
Cdd:PRK10762 108 -NRFGRID---------------WKkMYAEADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180
....*....|....*....|....*....
gi 1863768389 171 NLDSGARARLYAALTSWRGQ--AIV-VSH 196
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQgrGIVyISH 199
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
359-503 |
6.18e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 359 ERVGLVGPNGSGKTTLIDTIRGEIEPRS--GTVSL--RVPYRLLPQRL--QLLDD--------RDS-VLAAVSRLaPTAD 423
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILAnnRKPTKQILKRTgfVTQDDilyphltvRETlVFCSLLRL-PKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 424 DNQLRAELARFLLDADTIARPVGT---------LSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENTiignsfirgISGGERKRVSIAHEMLINP--SLLILDEPTSGLDATAAYRLVLTLGS 251
|
170
....*....|.
gi 1863768389 495 --YRGALLVAS 503
Cdd:PLN03211 252 laQKGKTIVTS 262
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
351-506 |
6.61e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.82 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDD-----------------RDSVLA 413
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkkvslvfqfpeaqlfENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 414 AVS----RLAPTADDNQLRAE--LARFLLDADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQ 487
Cdd:PRK13641 106 DVEfgpkNFGFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEP--EILCLDEPAAGLDPEGRKE 183
|
170 180
....*....|....*....|....
gi 1863768389 488 LTQALTQYRGA---LLVASH--DD 506
Cdd:PRK13641 184 MMQLFKDYQKAghtVILVTHnmDD 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
31-173 |
7.88e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 44.68 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS--------------RPER--VGYLPQHLVLQSDRTVAD-Vlgieavla 93
Cdd:COG1135 32 EIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalserelRAARrkIGMIFQHFNLLSSRTVAEnV-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 94 ALAtidagqgqpadFEVVGdqwdLPDRSIA-----MLARFGFADLDLRRPiGTLSGGE---V-ILLALAaqflSEPDLLL 164
Cdd:COG1135 104 ALP-----------LEIAG----VPKAEIRkrvaeLLELVGLSDKADAYP-SQLSGGQkqrVgIARALA----NNPKVLL 163
|
....*....
gi 1863768389 165 LDEPTNNLD 173
Cdd:COG1135 164 CDEATSALD 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
351-481 |
8.04e-05 |
|
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: 44.21 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrlqLLDDRDSVLAAVSR----------LAP 420
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-----------GEDIREQDPVELRRkigyviqqigLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 --TADDN---------------QLRA-ELARFL-LDADTIA-RPVGTLSGGERFRATLAALLLSEPPpqLLILDEPTNNL 480
Cdd:cd03295 89 hmTVEENialvpkllkwpkekiRERAdELLALVgLDPAEFAdRYPHELSGGQQQRVGVARALAADPP--LLLMDEPFGAL 166
|
.
gi 1863768389 481 D 481
Cdd:cd03295 167 D 167
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
31-173 |
8.29e-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: 44.46 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSRPERVGYLPQHLVLQSDrTVAD--VLGIE-AVLAALATIDAGQGQPad 107
Cdd:cd03291 64 EMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG-TIKEniIFGVSyDEYRYKSVVKACQLEE-- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 108 fevvgDQWDLPDRSIAMLARFGFadldlrrpigTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:cd03291 141 -----DITKFPEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-518 |
8.32e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTV-----------SLRVPYRLLPQRLQLLD-----DR---DSV 411
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlkNREVPFLRRQIGMIFQDhhllmDRtvyDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 412 LAAVSRLAPTADDNQLR--AELARFLLDADTIARPVgTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD---LDSIR 486
Cdd:PRK10908 101 AIPLIIAGASGDDIRRRvsAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNK--PAVLLADEPTGNLDdalSEGIL 177
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 487 QLTQALTQYRGALLVASHDDAFLSElgLTYRI 518
Cdd:PRK10908 178 RLFEEFNRVGVTVLMATHDIGLISR--RSYRM 207
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-513 |
8.72e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 44.34 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRD--------------------------------- 409
Cdd:COG4674 41 IIGPNGAGKTTLMDVITGKTRPDSGSVLF--------------GGTDltgldeheiarlgigrkfqkptvfeeltvfenl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 --------SVLAAVSRLAPTADDNQLRAELARFLLDADTiARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:COG4674 107 elalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKA-DRLAGLLSHGQKQWLEIGMLLAQD--PKLLLLDEPVAGMT 183
|
170 180 190
....*....|....*....|....*....|....
gi 1863768389 482 LDSIRQLTQALTQYRG--ALLVASHDDAFLSELG 513
Cdd:COG4674 184 DAETERTAELLKSLAGkhSVVVVEHDMEFVRQIA 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
342-505 |
1.03e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.05 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEI----EPRSGTVS--------------------LRVPYRL 397
Cdd:PRK13547 14 RAILRD---LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVTgdvtlngeplaaidaprlarLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 398 LPQRLQLLDDRDSVLAA----VSRLAPTADDNQLRAELARFLLDADTI-ARPVGTLSGGERFRATLAALLL-------SE 465
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALvGRDVTTLSGGELARVQFARVLAqlwpphdAA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1863768389 466 PPPQLLILDEPTNNLD-------LDSIRQLTQaltQYRGALLVASHD 505
Cdd:PRK13547 171 QPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
138-194 |
1.06e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 1.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 138 PIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLY---AALTSwRGQAIVV 194
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYkliNQLVQ-QGVAIIV 460
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
440-492 |
1.21e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 440 TIARPVGTLSGGERFRATLAALLLS-EPPPQLLILDEPTNNLDLDSIRQLTQAL 492
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKrSTGRTLYILDEPTTGLHFDDIKKLLEVL 875
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-505 |
1.33e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.82 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDdRDSVLAavsRLAPTADDNQLRAELARFLL------ 436
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR-RIGLLA---QNATTPGDITVQELVARGRYphqplf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 437 ------DADTIARP-------------VGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLD---SIRQLTQALTQ 494
Cdd:PRK10253 114 trwrkeDEEAVTKAmqatgithladqsVDTLSGGQRQRAWIAMVLAQE--TAIMLLDEPTTWLDIShqiDLLELLSELNR 191
|
170
....*....|..
gi 1863768389 495 YRGALLVAS-HD 505
Cdd:PRK10253 192 EKGYTLAAVlHD 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
436-529 |
1.43e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.76 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 436 LDADTIARPVGTLSGGERFRATLAA-LLLSEPPPQLLILDEPTNNLDLDSIRQLT---QALTQYRGALLVASHDdaflse 511
Cdd:cd03271 158 LGYIKLGQPATTLSGGEAQRIKLAKeLSKRSTGKTLYILDEPTTGLHFHDVKKLLevlQRLVDKGNTVVVIEHN------ 231
|
90
....*....|....*...
gi 1863768389 512 lgltyrIDLGAVADPLLD 529
Cdd:cd03271 232 ------LDVIKCADWIID 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
351-490 |
1.46e-04 |
|
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: 44.43 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGeIEPRsGTVSLRVPYRLLPQRLQLLDDRDSV--------LAAVSRLA--- 419
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPH-GTWDGEIYWSGSPLKASNIRDTERAgiviihqeLTLVPELSvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 420 ------------PTADDNQ--LRAE--LARFLLDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD-- 481
Cdd:TIGR02633 98 niflgneitlpgGRMAYNAmyLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ--ARLLILDEPSSSLTek 175
|
170
....*....|....
gi 1863768389 482 -----LDSIRQLTQ 490
Cdd:TIGR02633 176 eteilLDIIRDLKA 189
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-477 |
1.48e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGT-------VSLRVPyrllpqrlqllddRDS------------- 410
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEilidgkpVRIRSP-------------RDAialgigmvhqhfm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 -----------VLAAVSRLAPTADDNQLRAELARFL------LDADtiaRPVGTLSGGERFRA-TLAALLLSeppPQLLI 472
Cdd:COG3845 91 lvpnltvaeniVLGLEPTKGGRLDRKAARARIRELSerygldVDPD---AKVEDLSVGEQQRVeILKALYRG---ARILI 164
|
....*
gi 1863768389 473 LDEPT 477
Cdd:COG3845 165 LDEPT 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-505 |
1.54e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.34 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqllDDRDSVL-----------------A 413
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII--------------DDEDISLlplhararrgigylpqeA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 414 AVSRLAPTADD------------NQLRAELARFLLDADTIAR---PVG-TLSGGERFRATLAALLLSEppPQLLILDEPT 477
Cdd:PRK10895 88 SIFRRLSVYDNlmavlqirddlsAEQREDRANELMEEFHIEHlrdSMGqSLSGGERRRVEIARALAAN--PKFILLDEPF 165
|
170 180 190
....*....|....*....|....*....|.
gi 1863768389 478 NNLDLDS---IRQLTQALTQYRGALLVASHD 505
Cdd:PRK10895 166 AGVDPISvidIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-63 |
1.54e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 1.54e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1863768389 27 AFPDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSVSR 63
Cdd:PRK13546 47 AYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR 83
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-488 |
1.69e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.24 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 342 NLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR-VPYrllpqrlqlldDRDSVLAAVSR--- 417
Cdd:COG1129 17 VKALDG---VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPV-----------RFRSPRDAQAAgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 418 -------LAPT------------------ADDNQLRAE----LARFLLDADTiARPVGTLSGGER-----FRAtlaalLL 463
Cdd:COG1129 83 iihqelnLVPNlsvaeniflgreprrgglIDWRAMRRRarelLARLGLDIDP-DTPVGDLSVAQQqlveiARA-----LS 156
|
170 180 190
....*....|....*....|....*....|..
gi 1863768389 464 SEppPQLLILDEPTNNLD-------LDSIRQL 488
Cdd:COG1129 157 RD--ARVLILDEPTASLTereverlFRIIRRL 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
341-392 |
1.82e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.44 E-value: 1.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 341 ENLVLRNG---AV--VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR 392
Cdd:PRK11300 9 SGLMMRFGgllAVnnVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR 65
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-173 |
2.01e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 42.70 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 5 VVCSDLWFAWPSGELAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV----SRPER------------- 66
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTgQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEpsfeatrsrnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 67 VGYLPQHLVLQsDRTVADVLGIEAVLAAL---ATIDAGQGQP-ADFEVVGDQWDLPDRSIamlarfgfadldlrrpigTL 142
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITFGSPFNKQrykAVTDACSLQPdIDLLPFGDQTEIGERGI------------------NL 141
|
170 180 190
....*....|....*....|....*....|.
gi 1863768389 143 SGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:cd03290 142 SGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-173 |
2.06e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.08 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 24 LTCAFPDQVTgLVGRNGVGKSTLLKIIAGELMPTRGSVS-----------------RPER--VGYLPQHLVLQSDRTVAD 84
Cdd:PRK11124 23 LDCPQGETLV-LLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdfsktpsdkaiRELRrnVGMVFQQYNLWPHLTVQQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 85 VLgIEA---VLAaLATIDAGQgqpadfevvgdqwdlpdRSIAMLARFGFADLDLRRPIgTLSGGEVILLALAAQFLSEPD 161
Cdd:PRK11124 102 NL-IEApcrVLG-LSKDQALA-----------------RAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQ 161
|
170
....*....|..
gi 1863768389 162 LLLLDEPTNNLD 173
Cdd:PRK11124 162 VLLFDEPTAALD 173
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-61 |
2.06e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 2.06e-04
10 20 30
....*....|....*....|....*....|...
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV 61
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
443-508 |
2.45e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 443 RPVGTLSGGERFRATLA-ALLLSEPPP-------QLLILDEPTNNLDLDSIRQLTQALTQYRGA---LLVASHDDAF 508
Cdd:TIGR00618 946 RPSATLSGGETFLASLSlALALADLLStsggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIREGskmIGIISHVPEF 1022
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
433-521 |
2.53e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 433 RFLLDAD----TIARPVGTLSGGERFRATLAALLLSEPPPQLLILDEPTNNLDLDSIRQLTQALTQYR---GALLVASHD 505
Cdd:TIGR00630 470 GFLIDVGldylSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRdlgNTLIVVEHD 549
|
90
....*....|....*.
gi 1863768389 506 DAFLSElgLTYRIDLG 521
Cdd:TIGR00630 550 EDTIRA--ADYVIDIG 563
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
134-206 |
2.53e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 134 DLRRPIGTLSGGEVIL----LALA-AQFLSEP-----DLLLLDEPTNNLDSGARARLYAALTSWR--GQAI-VVSHDRDL 200
Cdd:TIGR00618 943 GSVRPSATLSGGETFLaslsLALAlADLLSTSggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIRegSKMIgIISHVPEF 1022
|
....*.
gi 1863768389 201 LDLVQH 206
Cdd:TIGR00618 1023 RERIPH 1028
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
336-508 |
2.54e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.17 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 336 DIVVTENLVLRNGAVV-----SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyRLLPQRLQLLDDRD- 409
Cdd:PRK11432 5 NFVVLKNITKRFGSNTvidnlNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI----DGEDVTHRSIQQRDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 -----------------SVLAAVSRLAPTADDNQLRAELARFLLDADTIA-RPVGTLSGGERFRATLA-ALLLSeppPQL 470
Cdd:PRK11432 81 cmvfqsyalfphmslgeNVGYGLKMLGVPKEERKQRVKEALELVDLAGFEdRYVDQISGGQQQRVALArALILK---PKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1863768389 471 LILDEPTNNLDL-------DSIRQLTQaltQYRGALLVASHD--DAF 508
Cdd:PRK11432 158 LLFDEPLSNLDAnlrrsmrEKIRELQQ---QFNITSLYVTHDqsEAF 201
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-215 |
2.64e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 136 RRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW----RGQAIVVSHDRDLL---DLVQHMA 208
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakkdKGIIIISSEMPELLgitDRILVMS 465
|
....*..
gi 1863768389 209 EMRAGGI 215
Cdd:PRK10982 466 NGLVAGI 472
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-215 |
2.70e-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: 43.12 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGeLMPTRGSVS---------------------RPERVGYLPQhlvlqsD--------RT 81
Cdd:COG0444 32 ETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedllklsekelrkiRGREIQMIFQ------DpmtslnpvMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 82 VADVLgIEAVLAalatidagqgqpadFEVVGDQwDLPDRSIAMLARFGFAD----LDlRRPiGTLSGGE----VILLALA 153
Cdd:COG0444 105 VGDQI-AEPLRI--------------HGGLSKA-EARERAIELLERVGLPDperrLD-RYP-HELSGGMrqrvMIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 154 aqflSEPDLLLLDEPTNNLDSGARA---RLYAALTSWRGQAIV-VSHDrdlLDLVQHMAE----MRAGGI 215
Cdd:COG0444 167 ----LEPKLLIADEPTTALDVTIQAqilNLLKDLQRELGLAILfITHD---LGVVAEIADrvavMYAGRI 229
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-167 |
2.98e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGEL--AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVsrpervgylpqhlvlqsdrtvaDV 85
Cdd:PRK13545 26 DLFFRSKDGEYhyALNNISFEVPEgEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------------------DI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 86 LGIEAVLAALATIDAGQGQPADFEVVGDQWDLPDRSIAMLAR--FGFADLD--LRRPIGTLSGGEVILLALAAQFLSEPD 161
Cdd:PRK13545 84 KGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPeiIEFADIGkfIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
....*.
gi 1863768389 162 LLLLDE 167
Cdd:PRK13545 164 ILVIDE 169
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
13-51 |
3.23e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 42.45 E-value: 3.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1863768389 13 AWPSGELAIAGL-TCAFPDQVTGLVGRNGVGKSTLLKIIA 51
Cdd:COG3910 19 AYPFNLPAVRNLeGLEFHPPVTFFVGENGSGKSTLLEAIA 58
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
407-519 |
3.69e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 407 DRDSVLAAVSRLAPTADDNQLRAELARFLLDADTI---------------ARPVGTLSGGER------FRATLAALLLSE 465
Cdd:PRK01156 746 DKSGVPAMIRKSASQAMTSLTRKYLFEFNLDFDDIdvdqdfnitvsrggmVEGIDSLSGGEKtavafaLRVAVAQFLNND 825
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 466 PppQLLILDEPTNNLDLDSIRQLTQ----ALTQYRG--ALLVASHDDAFLSELGLTYRID 519
Cdd:PRK01156 826 K--SLLIMDEPTAFLDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSVADVAYEVK 883
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
351-481 |
4.40e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 42.31 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrlqllddrDSVLAAVSR---LAPTAD---- 423
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG----------------ERVITAGKKnkkLKPLRKkvgi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 424 -----DNQLRAE----------------------LARFL-----LDADTIARPVGTLSGGERFRATLAALLLSEPppQLL 471
Cdd:PRK13634 90 vfqfpEHQLFEEtvekdicfgpmnfgvseedakqKAREMielvgLPEELLARSPFELSGGQMRRVAIAGVLAMEP--EVL 167
|
170
....*....|
gi 1863768389 472 ILDEPTNNLD 481
Cdd:PRK13634 168 VLDEPTAGLD 177
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
131-184 |
4.84e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.14 E-value: 4.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 131 ADLDLRRPIGTLSGGE-------VILLALAAQFLSE------PDLLLLDEPTNNLDSGARARLYAAL 184
Cdd:pfam13558 22 SEVETYRRSGGLSGGEkqllaylPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-173 |
5.18e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.80 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPER-VGYLPQHLVLQSDRTVADvlGIEAVLAALA 96
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhARARRgIGYLPQEASIFRRLSVYD--NLMAVLQIRD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 97 TIDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLdlRRPIG-TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD 173
Cdd:PRK10895 108 DLSAEQRE--------------DRANELMEEFHIEHL--RDSMGqSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
440-524 |
5.75e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 440 TIARPVGTLSGGERFRATLAALLLSEPPPQLLILDEPTNNL---DLDSIRQLTQALTQYRGALLVASHDDAFLSelgLTY 516
Cdd:PRK00635 469 TPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQMIS---LAD 545
|
....*....
gi 1863768389 517 R-IDLGAVA 524
Cdd:PRK00635 546 RiIDIGPGA 554
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
341-391 |
6.48e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.51 E-value: 6.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL 391
Cdd:PRK13632 21 ENNALKN---VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI 68
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
365-488 |
7.20e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 365 GPNGSGKTTLIDTIRGEIEPRSGTVSL--RVPYRLLPQRLQLLDDR-------DSvlaavsRLAP------------TAD 423
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLngRVLFDAEKGICLPPEKRrigyvfqDA------RLFPhykvrgnlrygmAKS 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 424 DNQLRAELARFLLDADTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQL 488
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAP--ELLLMDEPLASLDLPRKREL 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
344-512 |
8.16e-04 |
|
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: 42.10 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 344 VLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRG--EIEPRSGTVSLRVPYRLLPQRLQL----------------- 404
Cdd:TIGR03269 15 VLKN---ISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCEKCGYVERpskvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 405 -------------------------------LDDR--DSVLAAVSRLAPTADDNQLRA-ELARFLLDADTIARPVGTLSG 450
Cdd:TIGR03269 92 eevdfwnlsdklrrrirkriaimlqrtfalyGDDTvlDNVLEALEEIGYEGKEAVGRAvDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863768389 451 GERFRATLAALLLSEppPQLLILDEPTNNLDLDSIR----QLTQALTQYRGALLVASHDDAFLSEL 512
Cdd:TIGR03269 172 GEKQRVVLARQLAKE--PFLFLADEPTGTLDPQTAKlvhnALEEAVKASGISMVLTSHWPEVIEDL 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-505 |
9.14e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.19 E-value: 9.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 439 DTIARPVGTLSGGERFRATLA-ALLLSeppPQLLILDEPTNNLDLDSIRQLTQALTQYRG--ALLVASHD 505
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIArALALK---PKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
351-528 |
9.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.32 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSVlaAVSRLAPtadDNQL--- 427
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKV--GIVFQNP---DNQFvga 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 428 ----------------RAELARFLLDA-------DTIARPVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLD--- 481
Cdd:PRK13640 101 tvgddvafglenravpRPEMIKIVRDVladvgmlDYIDSEPANLSGGQKQRVAIAGILAVEP--KIIILDESTSMLDpag 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 482 ----LDSIRQLTQaltqyrgallvashdDAFLSELGLTYRIDLGAVADPLL 528
Cdd:PRK13640 179 keqiLKLIRKLKK---------------KNNLTVISITHDIDEANMADQVL 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
31-197 |
1.02e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 31 QVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-SRPERVGYLPQHLVLQSDRTVADVLGIEAVLAALATidagqgqpadFE 109
Cdd:PRK11831 34 KITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNV----------FD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 110 VVG----DQWDLPD---RSIAML-----ARFGFADLdlrRPiGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDS--- 174
Cdd:PRK11831 104 NVAyplrEHTQLPApllHSTVMMkleavGLRGAAKL---MP-SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPitm 179
|
170 180
....*....|....*....|....
gi 1863768389 175 GARARLYAALTSWRG-QAIVVSHD 197
Cdd:PRK11831 180 GVLVKLISELNSALGvTCVVVSHD 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-218 |
1.02e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 138 PIG-TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWRGQAivvshDRDLLDLVQHMAEM-RAGGI 215
Cdd:PTZ00265 1354 PYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA-----DKTIITIAHRIASIkRSDKI 1428
|
...
gi 1863768389 216 TFF 218
Cdd:PTZ00265 1429 VVF 1431
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
338-508 |
1.12e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 40.89 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 338 VVTENLVLR-NGAVV----SLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVslRVPYRLLPQRLQLLDDRDSVL 412
Cdd:PRK11264 4 IEVKNLVKKfHGQTVlhgiDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITIDTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 413 AAVSR---------LAP--TADDNQL------------------RAELARFLLDADTIARPvGTLSGGERFRATLAALLL 463
Cdd:PRK11264 82 QLRQHvgfvfqnfnLFPhrTVLENIIegpvivkgepkeeataraRELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1863768389 464 SEppPQLLILDEPTNNLD-------LDSIRQLTQAltqyRGALLVASHDDAF 508
Cdd:PRK11264 161 MR--PEVILFDEPTSALDpelvgevLNTIRQLAQE----KRTMVIVTHEMSF 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-173 |
1.15e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 40.89 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV---------SRP------------ERVGYLPQHLVLQSDRTVADVLg 87
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtARSlsqqkglirqlrQHVGFVFQNFNLFPHRTVLENI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 88 IEAVLAAlatidagQGQPADFEVVgdqwdlpdRSIAMLARFGFADLDLRRPiGTLSGGEVILLALAAQFLSEPDLLLLDE 167
Cdd:PRK11264 107 IEGPVIV-------KGEPKEEATA--------RARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
....*.
gi 1863768389 168 PTNNLD 173
Cdd:PRK11264 171 PTSALD 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
328-505 |
1.21e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 41.63 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 328 RTSVPPGRDIVVtenlVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTvslrvpYRLLPQRLQLLDD 407
Cdd:PRK10535 11 RRSYPSGEEQVE----VLKG---ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT------YRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 408 RDsvLAAVSR-----------LAP--TADDN------------QLRAELARFLLD----ADTIARPVGTLSGGERFRATL 458
Cdd:PRK10535 78 DA--LAQLRRehfgfifqryhLLShlTAAQNvevpavyaglerKQRLLRAQELLQrlglEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1863768389 459 AALLLSepPPQLLILDEPTNNLDLDSIRQLTQALTQYRG---ALLVASHD 505
Cdd:PRK10535 156 ARALMN--GGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHD 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
433-505 |
1.24e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 433 RFLLDAD----TIARPVGTLSGGERFRATLAALLLSEPPPQLLILDEPTNNLDLDSIRQLTQALTQYRGA---LLVASHD 505
Cdd:cd03270 119 GFLVDVGlgylTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLgntVLVVEHD 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-481 |
1.33e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.85 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 318 DDDSIEvdlsRTSVPPGRDIVVTenlvLRNGAVV----------SLHIRGPE--RVGLVGPNGSGKTTLIDTIRGEIEPR 385
Cdd:TIGR00957 620 EPDSIE----RRTIKPGEGNSIT----VHNATFTwardlpptlnGITFSIPEgaLVAVVGQVGCGKSSLLSALLAEMDKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 386 SGTVSLR--VPYRLLPQRLQLLDDRDSVLaavsrLAPTADDNQLRAELARFLLDADTIARPVG----------TLSGGER 453
Cdd:TIGR00957 692 EGHVHMKgsVAYVPQQAWIQNDSLRENIL-----FGKALNEKYYQQVLEACALLPDLEILPSGdrteigekgvNLSGGQK 766
|
170 180
....*....|....*....|....*...
gi 1863768389 454 FRATLAALLLSEppPQLLILDEPTNNLD 481
Cdd:TIGR00957 767 QRVSLARAVYSN--ADIYLFDDPLSAVD 792
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
443-494 |
1.36e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.98 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863768389 443 RPVGTLSGGERFRATLAALLLS-----------EPPPQLLILDEPTNNLDLDSIRQLTQALTQ 494
Cdd:pfam13558 28 RRSGGLSGGEKQLLAYLPLAAAlaaqygsaegrPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-196 |
1.51e-03 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 40.22 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKSTLLKIIAGELMPTRGSV-------------SRPERVGYLPQHLVL------------QSDRTVA 83
Cdd:cd03249 28 PGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLfdgtiaenirygKPDATDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 84 DVlgIEAvlAALATIDagqgqpaDFEVvgdqwDLPDRSIAMLARFGFadldlrrpigTLSGGEVILLALAAQFLSEPDLL 163
Cdd:cd03249 108 EV--EEA--AKKANIH-------DFIM-----SLPDGYDTLVGERGS----------QLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1863768389 164 LLDEPTNNLDSGARARLYAALTSWRG--QAIVVSH 196
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
316-504 |
1.56e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.27 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 316 VRDDDSIEVDLSRTSVPPGR-DIVVTEN--------LVLRNGAVV--SLHIRGPE--RVGLVGPNGSGKTTLIDTIrGEI 382
Cdd:TIGR00954 423 VEEIESGREGGRNSNLVPGRgIVEYQDNgikfenipLVTPNGDVLieSLSFEVPSgnNLLICGPNGCGKSSLFRIL-GEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 383 EP-RSGTVSL----------RVPYRLLPQRlqllddRDSVLAAVSrlaptADDNQLR----AELARFL--LDADTI-ARP 444
Cdd:TIGR00954 502 WPvYGGRLTKpakgklfyvpQRPYMTLGTL------RDQIIYPDS-----SEDMKRRglsdKDLEQILdnVQLTHIlERE 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863768389 445 VG---------TLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQLTQALTQYRGALLVASH 504
Cdd:TIGR00954 571 GGwsavqdwmdVLSGGEKQRIAMARLFYHK--PQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-518 |
1.61e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.92 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrLQLLDDRDSVLAA---------------- 414
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN---------NINYNKLDHKLAAqlgigiiyqelsvide 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 415 --------VSRL-------APTADDNQLRAELARFLL------DADTIarpVGTLSGGERFRATLAALLLSEppPQLLIL 473
Cdd:PRK09700 95 ltvlenlyIGRHltkkvcgVNIIDWREMRVRAAMMLLrvglkvDLDEK---VANLSISHKQMLEIAKTLMLD--AKVIIM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1863768389 474 DEPTNNLDLDSIRQLTQALTQYRG---ALLVASHDDAFLSELGLTYRI 518
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTV 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
359-512 |
1.63e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 359 ERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLrvpyrllpqrlqlldDRDSVLAAVSRLaptaddnqlraelarfllda 438
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---------------DGITPVYKPQYI-------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 439 dtiarpvgTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD----LDSIRQLTQALTQYRGALLVASHDDAFLSEL 512
Cdd:cd03222 71 --------DLSGGELQRVAIAAALLRN--ATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYL 138
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
351-391 |
1.68e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.94 E-value: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSL 391
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
129-204 |
1.73e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 129 GFADLDLRrpiGTLSGGE------VILLALAAQFLSEPDLLLLDEPTNNLD-------SGARARLYAALTSWRG-QAIVV 194
Cdd:TIGR00606 1190 GDTALDMR---GRCSAGQkvlaslIIRLALAETFCLNCGIIALDEPTTNLDrenieslAHALVEIIKSRSQQRNfQLLVI 1266
|
90
....*....|
gi 1863768389 195 SHDRDLLDLV 204
Cdd:TIGR00606 1267 THDEDFVELL 1276
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
329-492 |
1.97e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 329 TSVPPGRDIVVT------ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPR---SGTVSLR-VPYRLL 398
Cdd:cd03233 1 ASTLSWRNISFTtgkgrsKIPILKD---FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNgIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 399 PQRLqlldDRDSVLAAvsrlaptADDNQLR----AELARFLLD--ADTIARPVgtlSGGERFRATLAALLLSepPPQLLI 472
Cdd:cd03233 78 AEKY----PGEIIYVS-------EEDVHFPtltvRETLDFALRckGNEFVRGI---SGGERKRVSIAEALVS--RASVLC 141
|
170 180
....*....|....*....|....*..
gi 1863768389 473 LDEPTNNLD-------LDSIRQLTQAL 492
Cdd:cd03233 142 WDNSTRGLDsstaleiLKCIRTMADVL 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
333-518 |
2.13e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 333 PGRDIVVTENLV-LRNGAV--VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyrllpqrLQLLDDRD 409
Cdd:PRK10982 246 PGEVILEVRNLTsLRQPSIrdVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLH---------GKKINNHN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 410 SVLAAVSRLAPTADD--------------NQLRAELARFL------------------LDADTIARP-----VGTLSGGE 452
Cdd:PRK10982 317 ANEAINHGFALVTEErrstgiyayldigfNSLISNIRNYKnkvglldnsrmksdtqwvIDSMRVKTPghrtqIGSLSGGN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863768389 453 RFRATLAALLLSEPppQLLILDEPTNNLDLDS---IRQLTQALTQY-RGALLVASHddafLSE-LGLTYRI 518
Cdd:PRK10982 397 QQKVIIGRWLLTQP--EILMLDEPTRGIDVGAkfeIYQLIAELAKKdKGIIIISSE----MPElLGITDRI 461
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
341-505 |
2.32e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 40.05 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 341 ENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVslrvpyrllpqrlqllddrdsvLAAVSRLAP 420
Cdd:PRK11247 24 ERTVLNQ---LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------------------LAGTAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 421 TADDNQLRAELARFL------------------------LDADTIARPVG----TLSGGERFRATLAALLLSEPppQLLI 472
Cdd:PRK11247 79 AREDTRLMFQDARLLpwkkvidnvglglkgqwrdaalqaLAAVGLADRANewpaALSGGQKQRVALARALIHRP--GLLL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1863768389 473 LDEPTNNLD-LDSI--RQLTQALTQYRG-ALLVASHD 505
Cdd:PRK11247 157 LDEPLGALDaLTRIemQDLIESLWQQHGfTVLLVTHD 193
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-173 |
2.56e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.58 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 35 LVGRNGVGKSTLLKIIAGELMPTRGSVS---RP----------ERVGYLPQHLVLQSDrTVADVLgieaVLAALATIDag 101
Cdd:PRK11160 371 LLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPiadyseaalrQAISVVSQRVHLFSA-TLRDNL----LLAAPNASD-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 102 qgqpadfevvgdqwdlpDRSIAMLARFGFADL------------DLRRPigtLSGGEVILLALAAQFLSEPDLLLLDEPT 169
Cdd:PRK11160 444 -----------------EALIEVLQQVGLEKLleddkglnawlgEGGRQ---LSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
....
gi 1863768389 170 NNLD 173
Cdd:PRK11160 504 EGLD 507
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
142-194 |
2.56e-03 |
|
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: 38.95 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1863768389 142 LSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSWR--GQAIVV 194
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdaGKAVLL 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
351-518 |
2.67e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.71 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRvpyRLLPQRLQLLDDR--------------------DS 410
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID---GDLLTEENVWDIRhkigmvfqnpdnqfvgatveDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 411 VLAAVSRLAPTADDNQLRAELARFLLD-ADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLD----LDSI 485
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGmQDFKEREPARLSGGQKQRVAIAGAVAMR--PKIIILDEATSMLDpegrLELI 180
|
170 180 190
....*....|....*....|....*....|...
gi 1863768389 486 RQLTQALTQYRGALLVASHDdafLSELGLTYRI 518
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHD---LDEVALSDRV 210
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
139-216 |
3.28e-03 |
|
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: 38.49 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 139 IGTLSGGEVILLALAAQF----LSEPDLLLLDEPTNNLDSGARARLYAALTSWRG---QAIVVSHDRDL---LDLVQHMA 208
Cdd:cd03227 75 RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkgaQVIVITHLPELaelADKLIHIK 154
|
....*...
gi 1863768389 209 EMRAGGIT 216
Cdd:cd03227 155 KVITGVYK 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-484 |
3.65e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 3.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1863768389 439 DTIARPVG-TLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDS 484
Cdd:PTZ00265 1349 DTNVGPYGkSLSGGQKQRIAIARALLRE--PKILLLDEATSSLDSNS 1393
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-179 |
4.05e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.25 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 20 AIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAG--ELMP---TRGSV-------SRPE--------RVGYLPQH----- 73
Cdd:COG1117 26 ALKDINLDIPEnKVTALIGPSGCGKSTLLRCLNRmnDLIPgarVEGEIlldgediYDPDvdvvelrrRVGMVFQKpnpfp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 74 ----------LVLQ--SDRTVADVLgIEAVL--AALatidagqgqpadfevvgdqWD-LPDRsiamlarfgfadldLRRP 138
Cdd:COG1117 106 ksiydnvaygLRLHgiKSKSELDEI-VEESLrkAAL-------------------WDeVKDR--------------LKKS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1863768389 139 IGTLSGGE----VILLALAAqflsEPDLLLLDEPTNNLDSGARAR 179
Cdd:COG1117 152 ALGLSGGQqqrlCIARALAV----EPEVLLMDEPTSALDPISTAK 192
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-62 |
4.11e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 39.20 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 8 SDLWFAWPSGE-LAIAGLTCAFPD-QVTGLVGRNGVGKSTLLKIIAGELMPTRGSVS 62
Cdd:PRK13632 11 ENVSFSYPNSEnNALKNVSFEINEgEYVAILGHNGSGKSTISKILTGLLKPQSGEIK 67
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
163-207 |
4.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1863768389 163 LLLDEPTNNLDSGARARLYAALTSWR----GQAIVVSHDRDLLDLVQHM 207
Cdd:PRK02224 815 LILDEPTVFLDSGHVSQLVDLVESMRrlgvEQIVVVSHDDELVGAADDL 863
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
142-197 |
4.65e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 38.92 E-value: 4.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1863768389 142 LSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSW--RGQAIVVSHD 197
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
340-488 |
5.03e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 340 TENLVLRNgavVSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEP-RSGTVSLR--VPYRLLPQRLQLLDDRDSVLAAV- 415
Cdd:PLN03232 628 TSKPTLSD---INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRgsVAYVPQVSWIFNATVRENILFGSd 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863768389 416 ---SRLAPTADDNQLRAELARFL-LDADTIARPVGTLSGGERFRATLAALLLSEppPQLLILDEPTNNLDLDSIRQL 488
Cdd:PLN03232 705 fesERYWRAIDVTALQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSN--SDIYIFDDPLSALDAHVAHQV 779
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
363-488 |
5.53e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.80 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 363 LVGPNGSGKTTLIDTIRG--EIEP------RSGTVSLrvpYRLLPQRLQLLDDRDSVLAAVSRL-----APTADDNQLRA 429
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLllQSNFiylpaeRSGPARL---YPSLVRELSDLGSRGEYTADFLAElenleILDDKSKELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 430 ELARFL-----------LDADTIARPVGTLSGGERFRATLA------------ALLLSEPPPQLLILDEPTNNLDLDSIR 486
Cdd:COG4938 102 QVEEWLekifpgkvevdASSDLVRLVFRPSGNGKRIPLSNVgsgvsellpillALLSAAKPGSLLIIEEPEAHLHPKAQS 181
|
..
gi 1863768389 487 QL 488
Cdd:COG4938 182 AL 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
361-389 |
6.45e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 6.45e-03
10 20
....*....|....*....|....*....
gi 1863768389 361 VGLVGPNGSGKTTLIDTIRGEIEPRSGTV 389
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-244 |
6.61e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 39.17 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 9 DLWFAWPSGELAIAGLT-CAFPDQVTGLVGRNGVGKSTLLKIIagelmptrgsvsrpERVgYLPQHLVLQSDRTVADVLG 87
Cdd:PRK13657 339 DVSFSYDNSRQGVEDVSfEAKPGQTVAIVGPTGAGKSTLINLL--------------QRV-FDPQSGRILIDGTDIRTVT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 88 IEAVLAALATI--DAGqgqpadfevvgdqwdLPDRSIAMLARFGFAD---------------LD--LRRPIG-------- 140
Cdd:PRK13657 404 RASLRRNIAVVfqDAG---------------LFNRSIEDNIRVGRPDatdeemraaaeraqaHDfiERKPDGydtvvger 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 141 --TLSGGEVILLALAAQFLSEPDLLLLDEPTNNLDSGARARLYAALTSwrgqaivVSHDRDLLDLVQHMAEMR-AGGITF 217
Cdd:PRK13657 469 grQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGRTTFIIAHRLSTVRnADRILV 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1863768389 218 F-----------------GGNFTAFTDALAVEQEAAARGVRAAE 244
Cdd:PRK13657 542 FdngrvvesgsfdelvarGGRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
125-227 |
6.66e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 38.68 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 125 LARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNNLD-SGARARLYAALTSWRGQ--AIVVSHDRD-L 200
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpKGEHEMMQLILDAKANNktVFVITHTMEhV 239
|
90 100
....*....|....*....|....*..
gi 1863768389 201 LDLVQHMAEMRAGGITFFGGNFTAFTD 227
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
351-392 |
7.28e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 7.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLR 392
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-197 |
7.56e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.92 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 29 PDQVTGLVGRNGVGKST----LLKIIA--GEL----MPTRGsVSRPERVGYLPQHLVLQSDRTVA-----DVLGI--EAV 91
Cdd:PRK15134 311 PGETLGLVGESGSGKSTtglaLLRLINsqGEIwfdgQPLHN-LNRRQLLPVRHRIQVVFQDPNSSlnprlNVLQIieEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 92 LAALATIDAGQGQpadfevvgdqwdlpDRSIAMLARFGFADLDLRRPIGTLSGGEVILLALAAQFLSEPDLLLLDEPTNN 171
Cdd:PRK15134 390 RVHQPTLSAAQRE--------------QQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190
....*....|....*....|....*....|
gi 1863768389 172 LDSGARARLYAALTSWRGQA----IVVSHD 197
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHqlayLFISHD 485
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
357-492 |
8.12e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.48 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 357 GPERVGLVGPNGSGKTTLIDTIRGEIEPRSG-TVSLRVPYRLLPQRLQLLDDRDSVLAAVSRLAPTADDNQLRAElarfl 435
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGyFLRGKCDENLPYSPLLEALTREGLLRQLLDELESSLLEAWRAA----- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 436 LDADTIARPVGTLSGGERFRATLAALLLSEPPPQ---LLILDeptnnlDLDSIRQLTQAL 492
Cdd:pfam13191 98 LLEALAPVPELPGDLAERLLDLLLRLLDLLARGErplVLVLD------DLQWADEASLQL 151
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
444-503 |
8.15e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.83 E-value: 8.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863768389 444 PVGTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDLDSIRQLTQALTQYRGA----LLVAS 503
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRP--KVLILDEPTRGVDVGAKKEIYQLINQFKAEglsiILVSS 453
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
351-506 |
9.39e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 37.84 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 351 VSLHIRGPERVGLVGPNGSGKTTLIDTIRGEIEPRSGTVSLRVPYRLLPQRLQLLDDRDSVLAAVSR---LAPT------ 421
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQsfmLIPTlnalen 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863768389 422 ---------ADDNQLRAElARFLLDADTIARPV----GTLSGGERFRATLAALLLSEPppQLLILDEPTNNLDL---DSI 485
Cdd:PRK10584 109 velpallrgESSRQSRNG-AKALLEQLGLGKRLdhlpAQLSGGEQQRVALARAFNGRP--DVLFADEPTGNLDRqtgDKI 185
|
170 180
....*....|....*....|..
gi 1863768389 486 RQLTQALTQ-YRGALLVASHDD 506
Cdd:PRK10584 186 ADLLFSLNReHGTTLILVTHDL 207
|
|
| |
