|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-547 |
5.07e-102 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 319.03 E-value: 5.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 1 MKEYKRILLPLQKEKLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLI-QRELKAAYVYIALFAGSRLLMWVNNLSFDYVS 79
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLaGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 80 SKASQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFIL 159
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 160 WVTPFLFFSAMVPMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQH 239
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 240 CIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLD------ 313
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDeppeip 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 314 -KRGADSKVERAMGMTITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE- 391
Cdd:COG1132 326 dPPGAVPLPPVRGEIEFENVSFSYPGDRPV-LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDi 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 ---------ARMTTVWQEPRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKR 461
Cdd:COG1132 405 rdltleslrRQIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
....*.
gi 446589027 542 HSFLQR 547
Cdd:COG1132 565 GGLYAR 570
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-540 |
8.42e-84 |
|
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: 275.17 E-value: 8.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 5 KRILLPLQKEKLLVIAAVCSGCFAAILNLSRPLFMGLIVDN-LIQRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKAS 83
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRvLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 84 QRILRKKRIYVLRHFFLLPFEESEKIKQGELeTLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVTP 163
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDL-ASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 164 FLFFSAMVPMLMGKKVRNIASIAQN----NQSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQH 239
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEasakRQSLLVETLR----GIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 240 CIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLDK----- 314
Cdd:COG2274 380 LLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLppere 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 315 --RGADSKVERAMGMTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA 392
Cdd:COG2274 460 egRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 R----------MTTVWQEPRFFRTTVKENVHFGEEYL-ENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKR 461
Cdd:COG2274 540 RqidpaslrrqIGVVLQDVFLFSGTIRENITLGDPDAtDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-542 |
1.08e-66 |
|
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: 225.79 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 1 MKEYKRILLPLQKE-KLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRE--LKAAYVYIALFAGSRLLMWVNNLSFDY 77
Cdd:COG4988 1 QKPLDKRLKRLARGaRRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGapLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 78 VSSKASQRI---LRKKriyVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQ--FIGAFIALQH 152
Cdd:COG4988 81 AAFRAAARVkrrLRRR---LLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVplLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 153 IDMKFILWVT-PFL-FFsamvPMLMGKKVrniASIAQNNQSSVVEMVSQF---VKGVQDLRSLQKEKWAIRLFKGVtAQS 227
Cdd:COG4988 158 WLSGLILLVTaPLIpLF----MILVGKGA---AKASRRQWRALARLSGHFldrLRGLTTLKLFGRAKAEAERIAEA-SED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 228 YKtevKKTMmqhciGV------VGTVIETGAYI----VVLIIGAQkIMKGEMEVGALVAVLATIEMLFFPVRYVGdllmm 297
Cdd:COG4988 230 FR---KRTM-----KVlrvaflSSAVLEFFASLsialVAVYIGFR-LLGGSLTLFAALFVLLLAPEFFLPLRDLG----- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 298 TQV-----AAASANRVFSFLDKRGADSK-------VERAMGMTITNVSFQeSDGEKCRIHNIDLQIHPGELVIIVGESGA 365
Cdd:COG4988 296 SFYharanGIAAAEKIFALLDAPEPAAPagtaplpAAGPPSIELEDVSFS-YPGGRPALDGLSLTIPPGERVALVGPSGA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 366 GKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQEPRFFRTTVKENVHFGE-EYLENQLEKNIELVNVKP 434
Cdd:COG4988 375 GKSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 435 IIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEK 514
Cdd:COG4988 455 FVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLAL 534
|
570 580
....*....|....*....|....*...
gi 446589027 515 AILADRVVIMKEGRIVAGGSPEKLINSH 542
Cdd:COG4988 535 LAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
77-548 |
7.77e-64 |
|
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: 218.48 E-value: 7.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 77 YVSSKASQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPN----WVRLYGSILIeyihAIAQFIGAFIALQH 152
Cdd:COG4987 77 LVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAldnlYLRVLLPLLV----ALLVILAAVAFLAF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 153 IDMKFILWVTPFLFFSAMV-PMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTE 231
Cdd:COG4987 153 FSPALALVLALGLLLAGLLlPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 232 VKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEvGALVAVLATIEM-LFFPVRYVGDLLMMTQVAAASANRVFS 310
Cdd:COG4987 233 RRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALaLFEALAPLPAAAQHLGRVRAAARRLNE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 311 FLDKR------GADSKVERAMGMTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGS 384
Cdd:COG4987 312 LLDAPpavtepAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 385 IVYYGNE----------ARMTTVWQEPRFFRTTVKENVHFGEEYL-ENQLEKNIELVNVKPIIRDLSEGIETELHKSGVE 453
Cdd:COG4987 392 ITLGGVDlrdldeddlrRRIAVVPQRPHLFDTTLRENLRLARPDAtDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 454 FSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGG 533
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*
gi 446589027 534 SPEKLINSHSFLQRY 548
Cdd:COG4987 552 THEELLAQNGRYRQL 566
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
329-547 |
1.81e-52 |
|
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: 178.29 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW---------- 398
Cdd:COG1122 3 LENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelrrkvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPR--FFRTTVKENVHFGeeyLENQ-LEKNielvNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:COG1122 82 QNPDdqLFAPTVEEDVAFG---PENLgLPRE----EIRERVEEALElvGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-539 |
2.82e-52 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 187.23 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 4 YKRILLPLQKEKLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRELKAAYVYIALF-AGSRLLMWVNNLSFDYVSSKA 82
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVvIGLAVLRGICSFVSTYLLSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 83 SQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVT 162
Cdd:TIGR02203 82 SNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 163 PFLFFSAMVPMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTA----QSYKTEVKKTMMQ 238
Cdd:TIGR02203 162 VMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNrnrrLAMKMTSAGSISS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 239 HCIGVVGTVietgAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLD----K 314
Cdd:TIGR02203 242 PITQLIASL----ALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDsppeK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 315 RGADSKVERAMG-MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-- 391
Cdd:TIGR02203 318 DTGTRAIERARGdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDla 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 --------ARMTTVWQEPRFFRTTVKENVHFGE--EYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKR 461
Cdd:TIGR02203 398 dytlaslrRQVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQR 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
329-528 |
3.62e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.10 E-value: 3.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVW 398
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPR--FFRTTVKENVHFGeeyLENQLEKNIElvnVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNL 474
Cdd:cd03225 82 QNPDdqFFGPTVEEEVAFG---LENLGLPEEE---IEERVEEALElvGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 475 IILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGR 528
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-542 |
1.02e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.01 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARMTTVWQEPRFFRT-TV 408
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrRRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFGEEYlenqleKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDP 486
Cdd:COG1131 91 RENLRFFARL------YGLPRKEARERIDELLElfGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 487 SNQETVWNMIEGLGRE-VTRIVVTH---DVEKaiLADRVVIMKEGRIVAGGSPEKLINSH 542
Cdd:COG1131 165 EARRELWELLRELAAEgKTVLLSTHyleEAER--LCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
327-528 |
1.61e-47 |
|
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: 162.94 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTT 396
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFRTTVKENVhfgeeylenqleknielvnvkpiirdlsegietelhksgveFSGGERKRLALLRAIVSNPNLII 476
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGR 528
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
329-548 |
2.73e-45 |
|
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: 159.59 E-value: 2.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARMT 395
Cdd:cd03261 3 LRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 396 TVWQEPRFFRT-TVKENVHFGeeylenqLEKNIELvnVKPIIRDLSE------GIETELHKSGVEFSGGERKRLALLRAI 468
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFP-------LREHTRL--SEEEIREIVLekleavGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 469 VSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS-HSF 544
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTPEELRASdDPL 231
|
....
gi 446589027 545 LQRY 548
Cdd:cd03261 232 VRQF 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
40-524 |
4.72e-45 |
|
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: 166.69 E-value: 4.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 40 GLIVDNLIQRELKAAYVYIALFAGSR-LLMWVNnlsfDYVSSKASQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLV 118
Cdd:TIGR02857 32 GLISAGEPLAELLPALGALALVLLLRaLLGWLQ----ERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 119 ---VSDIPNWVRLY--GSILIEYIHAIaqfIGAFIALQHIDMKFILWVTPFLFFSAMvpMLMGKKVrniASIAQNNQSSV 193
Cdd:TIGR02857 108 legVEALDGYFARYlpQLVLAVIVPLA---ILAAVFPQDWISGLILLLTAPLIPIFM--ILIGWAA---QAAARKQWAAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 194 VEMVSQF---VKGVQDLRSLQKEKWAI-RLFKgvTAQSYKtevKKTMmqhciGVV------GTVIETGAYIVVLIIGAQ- 262
Cdd:TIGR02857 180 SRLSGHFldrLRGLPTLKLFGRAKAQAaAIRR--SSEEYR---ERTM-----RVLriaflsSAVLELFATLSVALVAVYi 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 263 --KIMKGEME-VGALVAVLATIEmLFFPVRYVGDLLMMTQVAAASANRVFSFLDKRG------ADSKVERAMGMTITNVS 333
Cdd:TIGR02857 250 gfRLLAGDLDlATGLFVLLLAPE-FYLPLRQLGAQYHARADGVAAAEALFAVLDAAPrplagkAPVTAAPASSLEFSGVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 334 FQeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQEPRF 403
Cdd:TIGR02857 329 VA-YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrDQIAWVPQHPFL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 404 FRTTVKENVHFGEEYL-ENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:TIGR02857 408 FAGTIAENIRLARPDAsDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446589027 483 GLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIM 524
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
190-539 |
5.23e-45 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 168.89 E-value: 5.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 190 QSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEM 269
Cdd:TIGR03375 324 NAVLVESLS----GLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 270 EVGALVAV----------LATIEMLFfpVRYVG--------DLLMMTQVAAASANRVFSFLDKRGadsKVEramgmtITN 331
Cdd:TIGR03375 400 TMGGLIACvmlsgralapLGQLAGLL--TRYQQaktalqslDELMQLPVERPEGTRFLHRPRLQG---EIE------FRN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 332 VSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQEP 401
Cdd:TIGR03375 469 VSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqidpadlrrnIGYVPQDP 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RFFRTTVKENVHFGEEYLENQ-LEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:TIGR03375 549 RLFYGTLRDNIALGAPYADDEeILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 481 TAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
329-548 |
1.55e-44 |
|
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: 157.45 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARMT 395
Cdd:COG1127 8 VRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsekelyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 396 TVWQEPRFFRT-TVKENVHFGEEYLENQLEKNI-ELVNVKpiirdLSE-GIETELHKSGVEFSGGERKRLALLRAIVSNP 472
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPLREHTDLSEAEIrELVLEK-----LELvGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 473 NLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS-HSFLQRY 548
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVTHDLDSAFaIADRVAVLADGKIIAEGTPEELLASdDPWVRQF 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
331-533 |
8.68e-44 |
|
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: 155.05 E-value: 8.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQE 400
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqldpadlrrnIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PRFFRTTVKENVHFGEEYLENQ-LEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:cd03245 87 VTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGG 533
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
344-529 |
1.21e-42 |
|
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: 151.87 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG------NEARMT--------TVWQE----PRFfr 405
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklSEKELAafrrrhigFVFQSfnllPDL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 tTVKENVHFGEEYLENQLEKNIElvnvkpIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:cd03255 98 -TALENVELPLLLAGVPKKERRE------RAEELLErvGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446589027 484 LDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRI 529
Cdd:cd03255 171 LDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-542 |
1.35e-42 |
|
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: 151.99 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFqESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQE 400
Cdd:cd03254 7 NVNF-SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdisrkslrsmIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PRFFRTTVKENVHFGEEYLENQLEKNI-ELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:cd03254 86 TFLFSGTIMENIRLGRPNATDEEVIEAaKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSH 542
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
329-546 |
1.35e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 153.35 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG----NEARMTT-------V 397
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtlDEENLWEirkkvgmV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEP--RFFRTTVKENVHFGeeyLENQlekNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:TIGR04520 83 FQNPdnQFVGATVEDDVAFG---LENL---GVPREEMRKRVDEALKlvGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQ 546
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEegITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVELLK 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
328-529 |
9.06e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.20 E-value: 9.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFQesDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvYYGNEARMT---TVW------ 398
Cdd:COG4619 2 ELEGLSFR--VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-YLDGKPLSAmppPEWrrqvay 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 --QEPRFFRTTVKEnvHFGEEYLENQLEKNIELVnvkpiIRDLSE-GIETE-LHKSGVEFSGGERKRLALLRAIVSNPNL 474
Cdd:COG4619 79 vpQEPALWGGTVRD--NLPFPFQLRERKFDRERA-----LELLERlGLPPDiLDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 475 IILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRI 529
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-541 |
9.66e-42 |
|
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: 156.99 E-value: 9.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARMTTVWQEPR--FF-RTT 407
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslrelrRRVQMVFQDPYssLNpRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGeeyLENQLEKNIElvNVKPIIRDLSE--GIETE-LHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:COG1123 361 VGDIIAEP---LRLHGLLSRA--ERRERVAELLErvGLPPDlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 485 DPSNQETVWNMIEGLGRE--VTRIVVTHD---VEKaiLADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG1123 436 DVSVQAQILNLLRDLQRElgLTYLFISHDlavVRY--IADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
329-546 |
6.85e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 148.60 E-value: 6.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT----------VW 398
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlkeirkkigiIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEP--RFFRTTVKENVHFGeeyLENqleKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNL 474
Cdd:PRK13632 90 QNPdnQFIGATVEDDIAFG---LEN---KKVPPKKMKDIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 475 IILDEPTAGLDPSNQETVWNMIEGLGREVTR--IVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQ 546
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKtlISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILE 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
328-538 |
2.23e-40 |
|
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: 146.54 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSI-------VYYGNEAR--MTTVW 398
Cdd:COG4555 3 EVENLSK--KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvRKEPREARrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPRFF-RTTVKENVHFGEEYLENQLEKNIELVNVkpIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIIL 477
Cdd:COG4555 81 DERGLYdRLTVRENIRYFAELYGLFDEELKKRIEE--LIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGREVTRIVVT----HDVEKaiLADRVVIMKEGRIVAGGSPEKL 538
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSshimQEVEA--LCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
331-530 |
2.84e-40 |
|
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: 145.73 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARMTTV 397
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkirrKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRF---FRTTVKEnvHFGEEYLENQLEKNIELVNVkpIIRDLSEGI---ETELHKSGVEFSGGERKRLALLRAIVSN 471
Cdd:cd03257 88 FQDPMSslnPRMTIGE--QIAEPLRIHGKLSKKEARKE--AVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRIV 530
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGvVAKIADRVAVMYAGKIV 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
327-531 |
5.33e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.80 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG------NEARMTT-- 396
Cdd:COG1136 5 LELRNLTksYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 ------VWQeprFF----RTTVKENVHFGEEYlenqleKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLAL 464
Cdd:COG1136 85 rrhigfVFQ---FFnllpELTALENVALPLLL------AGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 465 LRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVA 531
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
344-529 |
5.74e-40 |
|
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: 142.92 E-value: 5.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA---------RMTTVWQEPRFFRT-TVKENVh 413
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 fgeeylenqleknielvnvkpiirdlsegietelhksgvEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 446589027 494 NMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:cd03230 136 ELLRELKKEgKTILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
331-548 |
1.07e-39 |
|
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: 144.30 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQE 400
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdytlaslrrqIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:cd03251 85 VFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQRY 548
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
327-541 |
1.26e-39 |
|
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: 144.80 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------AR-MTT 396
Cdd:COG1120 2 LEAENLSV--GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelARrIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRF-FRTTVKENVHFG-----------EEYLENQLEKNIELVNvkpiIRDLSEGIETELhksgvefSGGERKRLAL 464
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGryphlglfgrpSAEDREAVEEALERTG----LEHLADRPVDEL-------SGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 465 LRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAArYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-543 |
1.81e-39 |
|
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: 144.18 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQE 400
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafrRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 ------PRFfrtTVKENVhfgEEYLENQLEKNIElvnvKPIIRDLSE-GIETEL-----HksgvEFSGGERKRLALLRAI 468
Cdd:COG1124 88 pyaslhPRH---TVDRIL---AEPLRIHGLPDRE----ERIAELLEQvGLPPSFldrypH----QLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 469 VSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEK-AILADRVVIMKEGRIVAGGSPEKLINSHS 543
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
329-528 |
6.15e-39 |
|
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: 141.07 E-value: 6.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKC---RIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGneaRMTTVWQEPRFFR 405
Cdd:cd03250 3 VEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---SIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 TTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:cd03250 80 GTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446589027 486 PSNQETVW-NMIEGLGREV-TRIVVTHDVEKAILADRVVIMKEGR 528
Cdd:cd03250 160 AHVGRHIFeNCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
331-548 |
7.93e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 143.36 E-value: 7.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDG---EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG------NEARMTTVWQ-- 399
Cdd:TIGR04521 5 NVSYIYQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditakKKKKLKDLRKkv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 400 -------EPRFFRTTVKENVHFG-------EEYLENQLEKNIELVNvkpiirdLSEGIeteLHKSGVEFSGGERKRLALL 465
Cdd:TIGR04521 85 glvfqfpEHQLFEETVYKDIAFGpknlglsEEEAEERVKEALELVG-------LDEEY---LERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 466 RAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSH 542
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkgLTVILVTHSMEDVAeYADRVIVMHKGKIVLDGTPREVFSDV 234
|
....*.
gi 446589027 543 SFLQRY 548
Cdd:TIGR04521 235 DELEKI 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
327-531 |
9.26e-39 |
|
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: 141.46 E-value: 9.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-----ARMTTVWQ 399
Cdd:cd03293 1 LEVRNVSktYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtgpgPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 400 EPRFF--RtTVKENVHFGeeyLENQLEKNIELvnvKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLI 475
Cdd:cd03293 81 QDALLpwL-TVLDNVALG---LELQGVPKAEA---RERAEELLElvGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKE--GRIVA 531
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTHDIDEAVfLADRVVVLSArpGRIVA 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
329-538 |
1.23e-38 |
|
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: 141.16 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYK-----PSNGSIVYYGNE------------ 391
Cdd:cd03260 3 LRDLNV--YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 ARMTTVWQEPRFFRTTVKENVHFGeeyLENQLEKNIElvNVKPIIRDLSEGI----ETELHKSGVEFSGGERKRLALLRA 467
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYG---LRLHGIKLKE--ELDERVEEALRKAalwdEVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-538 |
1.53e-38 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 150.26 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 6 RILLPLQKEKLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLIQR----ELKAAYVYIALF-AGSRLLMWVNNLSFDYVSS 80
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDkgppALASAIFFMCLLsIASSVSAGLRGGSFNYTMA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 81 KASQRILRKKRIYVLRH---FFLlpfeeseKIKQGELETLVVSD---IPNWVRLYGSILIEYIhaiAQFIGAFIalqhid 154
Cdd:TIGR00958 231 RINLRIREDLFRSLLRQdlgFFD-------ENKTGELTSRLSSDtqtMSRSLSLNVNVLLRNL---VMLLGLLG------ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 155 mkFILWV-----------TPFLFFSAMVpmlMGKKVRNIA-----SIAQNNQssVVEMVsqfVKGVQDLRSLQKEKWAIR 218
Cdd:TIGR00958 295 --FMLWLsprltmvtlinLPLVFLAEKV---FGKRYQLLSeelqeAVAKANQ--VAEEA---LSGMRTVRSFAAEEGEAS 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 219 LFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLL--M 296
Cdd:TIGR00958 365 RFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYsgM 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 297 MTQVAAASanRVFSFLDKR------------GADSKVEramgmtITNVSFQ-ESDGEKCRIHNIDLQIHPGELVIIVGES 363
Cdd:TIGR00958 445 MQAVGASE--KVFEYLDRKpnipltgtlaplNLEGLIE------FQDVSFSyPNRPDVPVLKGLTFTLHPGEVVALVGPS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 364 GAGKTTLLKLMTGLYKPSNGSI------------VYYGNEARMttVWQEPRFFRTTVKENVHFGEEYLEN-QLEKNIELV 430
Cdd:TIGR00958 517 GSGKSTVAALLQNLYQPTGGQVlldgvplvqydhHYLHRQVAL--VGQEPVLFSGSVRENIAYGLTDTPDeEIMAAAKAA 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 431 NVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVtrIVVTH 510
Cdd:TIGR00958 595 NAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTV--LLIAH 672
|
570 580
....*....|....*....|....*...
gi 446589027 511 DVEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:TIGR00958 673 RLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-531 |
4.05e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 140.61 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 323 RAMGMTITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-----ARMT 395
Cdd:COG1116 4 AAPALELRGVSkrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 396 TVWQEPRFF--RtTVKENVHFG--------EEYLEnQLEKNIELV------NVKPiirdlsegieTELhksgvefSGGER 459
Cdd:COG1116 84 VVFQEPALLpwL-TVLDNVALGlelrgvpkAERRE-RARELLELVglagfeDAYP----------HQL-------SGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 460 KRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKE--GRIVA 531
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHDVDEAVfLADRVVVLSArpGRIVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
328-546 |
7.13e-38 |
|
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: 146.20 E-value: 7.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPS---NGSIVYYGNE----------ARM 394
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDllelsealrgRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 TTVWQEPR--FFRTTVKENVHFGeeyLENQLEKNIElvnVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVS 470
Cdd:COG1123 86 GMVFQDPMtqLNPVTVGDQIAEA---LENLGLSRAE---ARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 471 NPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQ 546
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAeIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
327-544 |
7.42e-38 |
|
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: 139.54 E-value: 7.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTT 396
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlaladpawlrRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFRTTVKENVHFGEEYLEnqLEKNIE---LVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMS--MERVIEaakLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSF 544
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
328-528 |
9.97e-38 |
|
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: 136.22 E-value: 9.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarmttVWQEPRFfrtt 407
Cdd:cd00267 1 EIENLSF--RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD-----IAKLPLE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 vkenvhfgeeylenQLEKNIELVnvkpiirdlsegietelhksgVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:cd00267 70 --------------ELRRRIGYV---------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446589027 488 NQETVWNMIEGLGRE-VTRIVVTHDVE-KAILADRVVIMKEGR 528
Cdd:cd00267 115 SRERLLELLRELAEEgRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
346-533 |
2.96e-37 |
|
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: 136.88 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYygNEARMTT----------VWQEPRFFRT-TVKENVHF 414
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI--DGRDVTGvpperrnigmVFQDYALFPHlTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 GeeyLENQLEKNIELV-NVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:cd03259 96 G---LKLRGVPKAEIRaRVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446589027 494 NMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGG 533
Cdd:cd03259 171 EELKELQRElgITTIYVTHDQEEALaLADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
328-530 |
4.29e-37 |
|
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: 136.23 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFQESDGEKcRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA----RMTTVW---QE 400
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakeRRKSIGyvmQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PR--FFRTTVKENVHFGEEYLENQLEKnielvnVKPIIRDLSEGIETELHKsgVEFSGGERKRLALLRAIVSNPNLIILD 478
Cdd:cd03226 80 VDyqLFTDSVREELLLGLKELDAGNEQ------AETVLKDLDLYALKERHP--LSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 479 EPTAGLDPSNQETVWNMIEGL-GREVTRIVVTHDVEKAIL-ADRVVIMKEGRIV 530
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-511 |
4.78e-37 |
|
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: 144.04 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 5 KRILLPLQKEKLLVIAAV----CSGCFAAILN------LSRPLFMGLIVDnliqreLKAAYVYIALFAGSR-LLMWVNNL 73
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVllgaLALGSAVALLgvsawlISRAAEMPPVLY------LSVAAVAVRAFGIGRaVFRYLERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 74 sfdyVSSKASQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPN----WVRLY---GSILIEYIHAIAqFIGA 146
Cdd:TIGR02868 76 ----VGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDAlqdlYVRVIvpaGVALVVGAAAVA-AIAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 147 FIALQHIDMKFILWVTPFLffsamVPMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQ 226
Cdd:TIGR02868 151 LSVPAALILAAGLLLAGFV-----APLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 227 SYKTEVKKTMMQHcIGVVGTVIETGAYIV-VLIIGAQKIMKGEMEvGALVAVLATIEM-LFFPVRYVGDLLMMTQVAAAS 304
Cdd:TIGR02868 226 LTRAERRAAAATA-LGAALTLLAAGLAVLgALWAGGPAVADGRLA-PVTLAVLVLLPLaAFEAFAALPAAAQQLTRVRAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 305 ANRVFSFLDKRG--ADSKVERA-------MGMTITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMT 375
Cdd:TIGR02868 304 AERIVEVLDAAGpvAEGSAPAAgavglgkPTLELRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 376 GLYKPSNGSIV--------YYGNEARMTTVW--QEPRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIE 444
Cdd:TIGR02868 383 GLLDPLQGEVTldgvpvssLDQDEVRRRVSVcaQDAHLFDTTVRENLRLArPDATDEELWAALERVGLADWLRALPDGLD 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 445 TELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHD 511
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-547 |
7.42e-37 |
|
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: 145.27 E-value: 7.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 11 LQKEKLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRELKAAYVYIAL-FAGSRLLMWVNNLSFDYVSSKASQRILRK 89
Cdd:TIGR01193 151 ITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIgLIIAYIIQQILSYIQIFLLNVLGQRLSID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 90 KRIYVLRHFFLLPFEESEKIKQGELeTLVVSDIPNWVRLYGSILIEYI--HAIAQFIGAFIALQHIDMkFILWVTPFLFF 167
Cdd:TIGR01193 231 IILSYIKHLFELPMSFFSTRRTGEI-VSRFTDASSIIDALASTILSLFldMWILVIVGLFLVRQNMLL-FLLSLLSIPVY 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 168 SAMVPMLMGKKVRNIASIAQNN---QSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVV 244
Cdd:TIGR01193 309 AVIIILFKRTFNKLNHDAMQANavlNSSIIEDLN----GIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 245 GTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDL---LMMTQVAAASANRVF----SFLDKRGA 317
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLqpkLQAARVANNRLNEVYlvdsEFINKKKR 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 318 DSKVERAMGMTITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG-------- 389
Cdd:TIGR01193 465 TELNNLNGDIVINDVSYSYGYGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidr 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 390 NEAR--MTTVWQEPRFFRTTVKENVHFG--EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALL 465
Cdd:TIGR01193 544 HTLRqfINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 466 RAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLgREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFL 545
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
|
..
gi 446589027 546 QR 547
Cdd:TIGR01193 703 AS 704
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
346-541 |
9.84e-37 |
|
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: 136.31 E-value: 9.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYygNEARMTTVWQEPR-----------FFRTTVKENVHF 414
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL--NGKDITNLPPEKRdisyvpqnyalFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 GeeyLENQLEKNIEL-VNVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:cd03299 95 G---LKKRKVDKKEIeRKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 494 NMIEGLGRE--VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:cd03299 170 EELKKIRKEfgVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
328-533 |
1.70e-36 |
|
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: 133.71 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------AR-MTTV 397
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelARkIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQeprffrttvkenvhfgeeylenqlekNIELVNvkpiIRDLSEGIETELhksgvefSGGERKRLALLRAIVSNPNLIIL 477
Cdd:cd03214 79 PQ--------------------------ALELLG----LAHLADRPFNEL-------SGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAIL-ADRVVIMKEGRIVAGG 533
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-548 |
2.92e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.22 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGM----TITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARmtTVWQE 400
Cdd:COG1121 1 MMMmpaiELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--RARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 ----------PRFFRTTVKENV------HFG-------EEYleNQLEKNIELVNVKPI----IRDLSegietelhksgve 453
Cdd:COG1121 77 igyvpqraevDWDFPITVRDVVlmgrygRRGlfrrpsrADR--EAVDEALERVGLEDLadrpIGELS------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 454 fsGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKeGRIVA 531
Cdd:COG1121 142 --GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVReYFDRVLLLN-RGLVA 218
|
250
....*....|....*..
gi 446589027 532 GGSPEKLINSHSFLQRY 548
Cdd:COG1121 219 HGPPEEVLTPENLSRAY 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
328-538 |
3.98e-36 |
|
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: 134.62 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFQESDGEKcRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARM 394
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 TTVWQEPRFF-RTTVKENVHFGeeylenqleknieLVNVKPIIRDLSE-----------------GIETELHKSGVEFSG 456
Cdd:cd03256 81 GMIFQQFNLIeRLSVLENVLSG-------------RLGRRSTWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 457 GERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGG 533
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAReYADRIVGLKDGRIVFDG 227
|
....*
gi 446589027 534 SPEKL 538
Cdd:cd03256 228 PPAEL 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
331-543 |
4.76e-36 |
|
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: 134.28 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT----------VWQE 400
Cdd:cd03253 5 NVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslrraigvVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:cd03253 84 TVLFNDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHS 543
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-547 |
1.24e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW---------- 398
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvrrqvgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEP--RFFRTTVKENVHFGeeyLENQLEKNIELVN-VKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLI 475
Cdd:PRK13635 88 QNPdnQFVGATVQDDVAFG---LENIGVPREEMVErVDQALRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-535 |
1.99e-35 |
|
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: 132.23 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQE 400
Cdd:cd03244 7 NVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglhdlrSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PRFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:cd03244 87 PVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 481 TAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSP 535
Cdd:cd03244 167 TASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
325-538 |
2.60e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 135.61 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGM---TITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-------EAR- 393
Cdd:COG3842 1 MAMpalELENVSK--RYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppEKRn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 MTTVWQEPRFF-RTTVKENVHFG-------EEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALL 465
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlrmrgvpKAEIRARVAELLELV-----------GLEGLADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 466 RAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHDQEEALaLADRIAVMNDGRIEQVGTPEEI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
331-530 |
1.33e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG-NEARMT------------TV 397
Cdd:COG2884 6 NVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLSRLKrreipylrrrigVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRF-FRTTVKENVHF-------GEEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIV 469
Cdd:COG2884 85 FQDFRLlPDRTVYENVALplrvtgkSRKEIRRRVREVLDLV-----------GLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDveKAILAD---RVVIMKEGRIV 530
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHD--LELVDRmpkRVLELEDGRLV 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-540 |
1.49e-34 |
|
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: 129.86 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-ARMTT----------VWQEPRFFRT-TVKEN 411
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPheraragigyVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 VHFGEEYLENQLEKNI--ELVNVKPIIRDLsegieteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQ 489
Cdd:cd03224 96 LLLGAYARRRAKRKARleRVYELFPRLKER-------RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446589027 490 ETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:cd03224 169 EEIFEAIRELRDEgVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
329-529 |
1.92e-34 |
|
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: 128.10 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMT----------TVW 398
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdpnelgdhvgYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPRFFRTTVKENVhfgeeylenqleknielvnvkpiirdlsegietelhksgveFSGGERKRLALLRAIVSNPNLIILD 478
Cdd:cd03246 83 QDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446589027 479 EPTAGLDPSNQETVWNMIEGL-GREVTRIVVTHDVEKAILADRVVIMKEGRI 529
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
344-482 |
3.47e-34 |
|
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: 126.61 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQEPRFF-RTTVKENV 412
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 413 HFG-------EEYLENQLEKNIELVnvkpiirDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
329-538 |
5.44e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.02 E-value: 5.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARMT 395
Cdd:COG3638 5 LRNLSKR-YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgralrrlrRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 396 TVWQEPRFF-RTTVKENV----------------HFGEEYLENQLEkNIELVnvkpiirdlseGIETELHKSGVEFSGGE 458
Cdd:COG3638 84 MIFQQFNLVpRLSVLTNVlagrlgrtstwrsllgLFPPEDRERALE-ALERV-----------GLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 459 RKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSP 535
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdgITVVVNLHQVDLARrYADRIIGLRDGRVVFDGPP 231
|
...
gi 446589027 536 EKL 538
Cdd:COG3638 232 AEL 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
327-533 |
1.21e-33 |
|
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: 125.89 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA---------RMTTV 397
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsdlekalssLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRFFRTTVKENVhfgeeylenqleknielvnvkpiirdlsegietelhksGVEFSGGERKRLALLRAIVSNPNLIIL 477
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGG 533
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
329-538 |
1.37e-33 |
|
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: 127.24 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR--MTTVWQE----PR 402
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdRKAARQSlgycPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 403 F---FRT-TVKENVHF-----GeeylenqLEKNIELVNVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:cd03263 83 FdalFDElTVREHLRFyarlkG-------LPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKL 538
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
331-531 |
2.33e-33 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 126.70 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarMTTVWQEPR-FFRttvk 409
Cdd:TIGR02211 8 GKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQS--LSKLSSNERaKLR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 eNVHFGEEY-----------LEN----QLEKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNP 472
Cdd:TIGR02211 82 -NKKLGFIYqfhhllpdftaLENvampLLIGKKSVKEAKERAYEMLEkvGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 473 NLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVA 531
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRElnTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
327-528 |
2.93e-33 |
|
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: 124.99 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQEsdGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG------------NEARM 394
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 TTVWQEPR-FFRTTVKENVHFGeeylenqleknielvnvkpiirdlsegietelhksgveFSGGERKRLALLRAIVSNPN 473
Cdd:cd03229 79 GMVFQDFAlFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGR 528
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
328-541 |
1.13e-32 |
|
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: 125.11 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTV 397
Cdd:cd03295 2 EFENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdpvelrrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRFF-RTTVKENV-------HFGEEYLENQLEKNIELVNVKPiirdlsegiETELHKSGVEFSGGERKRLALLRAIV 469
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkllKWPKEKIRERADELLALVGLDP---------AEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 470 SNPNLIILDEPTAGLDP----SNQETVWNMIEGLGRevTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:cd03295 152 ADPPLLLMDEPFGALDPitrdQLQEEFKRLQQELGK--TIVFVTHDIDEAFrLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-308 |
1.47e-32 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 126.51 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRELKAAYVYIAL-FAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVLR 96
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALlLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 97 HFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPFLFFSAMVpm 173
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKltlVALLLLPLYVLILRY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 174 lMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAY 253
Cdd:cd07346 159 -FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 254 IVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
346-538 |
1.49e-32 |
|
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: 124.40 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARmttvwQEPRFFRTTVkeNVHFGEEYLENQLE- 424
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-----REPREVRRRI--GIVFQDLSVDDELTg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 425 -KNIE----LVNVKPIIRDlsEGIETEL---------HKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQE 490
Cdd:cd03265 91 wENLYiharLYGVPGAERR--ERIDELLdfvglleaaDRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 491 TVWNMIEGLGRE--VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKL 538
Cdd:cd03265 169 HVWEYIEKLKEEfgMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
325-540 |
3.32e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.16 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSF---QESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------- 391
Cdd:PRK13637 1 MSIKIENLTHiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklsd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 --ARMTTVWQEPRF--FRTTVKENVHFG-------EEYLENQLEKNIELVNVKpiirdlsegIETELHKSGVEFSGGERK 460
Cdd:PRK13637 81 irKKVGLVFQYPEYqlFEETIEKDIAFGpinlglsEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 461 RLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEK-AILADRVVIMKEGRIVAGGSPEK 537
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEynMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPRE 231
|
...
gi 446589027 538 LIN 540
Cdd:PRK13637 232 VFK 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
344-540 |
3.90e-32 |
|
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: 123.50 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------NEARMTTVWQEPRFF-RTTVKENVHF 414
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlppHKRPVNTVFQNYALFpHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 G-------EEYLENQLEKNIELVNVkpiirdlsEGIEtelHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:cd03300 96 GlrlkklpKAEIKERVAEALDLVQL--------EGYA---NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 488 NQETVWNMIEGLGREV--TRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:cd03300 165 LRKDMQLELKRLQKELgiTFVFVTHDQEEALtMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
344-548 |
6.98e-32 |
|
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: 122.78 E-value: 6.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-ARMTT----------VWQEPRFFRT-TVKEN 411
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDiTGLPPhriarlgigyVPEGRRIFPSlTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 VHFGEEYL--ENQLEKNIELV-NVKPIIRDLsegieteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSN 488
Cdd:COG0410 99 LLLGAYARrdRAEVRADLERVyELFPRLKER-------RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 489 QETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQRY 548
Cdd:COG0410 172 VEEIFEIIRRLNREgVTILLVEQNARFALeIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
329-541 |
8.17e-32 |
|
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: 123.27 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQEsdGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVY-YGNEARMTTVWQ-------- 399
Cdd:COG1119 6 LRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlFGERRGGEDVWElrkriglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 400 ----EPRFFR-TTVKENV---HFG-----EEYLENQLEKNIELvnvkpiIRDLseGIETELHKSGVEFSGGERKRLALLR 466
Cdd:COG1119 84 spalQLRFPRdETVLDVVlsgFFDsiglyREPTDEQRERAREL------LELL--GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 467 AIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEkAILA--DRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE-EIPPgiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
325-541 |
9.25e-32 |
|
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: 122.83 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFQEsdGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-------- 396
Cdd:cd03296 1 MSIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqernvgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFR-TTVKENVHFGEEylenqleknielvnVKPIIRDLSEG-IETELHK-------SGV------EFSGGERKR 461
Cdd:cd03296 79 VFQHYALFRhMTVFDNVAFGLR--------------VKPRSERPPEAeIRAKVHEllklvqlDWLadrypaQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhVTTVFVTHDQEEALeVADRVVVMNKGRIEQVGTPDEV 224
|
...
gi 446589027 539 INS 541
Cdd:cd03296 225 YDH 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
345-522 |
1.20e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.43 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARMTTVWQEPRFFRT-TVKENVHF 414
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrRRLAYLGHADGLKPElTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 -----GEEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQ 489
Cdd:COG4133 99 waalyGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180 190
....*....|....*....|....*....|....
gi 446589027 490 ETVWNMIEG-LGREVTRIVVTHDvEKAILADRVV 522
Cdd:COG4133 168 ALLAELIAAhLARGGAVLLTTHQ-PLELAAARVL 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
344-538 |
1.47e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvYYGNEaRMTTVwqEPR-------------FFRTTVKE 410
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-LIGGR-DVTDL--PPKdrniamvfqsyalYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFGeeyLENQLEKNIElvnVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPsn 488
Cdd:COG3839 95 NIAFP---LKLRKVPKAE---IDRRVREAAEllGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA-- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 489 qETVWNM---IEGLGRE--VTRIVVTHD-VEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:COG3839 167 -KLRVEMraeIKRLHRRlgTTTIYVTHDqVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
346-539 |
1.50e-31 |
|
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: 121.88 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQEPRFFRTTVKENVHFG 415
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlnlrwlrsqIGLVSQEPVLFDGTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 EEYL-ENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWN 494
Cdd:cd03249 101 KPDAtDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446589027 495 MIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:cd03249 181 ALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
346-541 |
2.57e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 121.39 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARM--TTVWQEPR-FFRTTVKENVH 413
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitglppheiARLgiGRTFQIPRlFPELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGeeyLENQLEKNIELVNVKPIIRDLSE---------GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:cd03219 98 VA---AQARTGSGLLLARARREEREAREraeellervGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 485 DPSNQETVWNMIEGLGRE-VTRIVVTHDVeKAI--LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:cd03219 175 NPEETEELAELIRELRERgITVLLVEHDM-DVVmsLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
339-530 |
3.45e-31 |
|
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: 120.44 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNeaRMTTVWQEPR-----------FFRTT 407
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPKDRdiamvfqnyalYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGEEyLENQLEKNIElVNVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:cd03301 89 VYDNIAFGLK-LRKVPKDEID-ERVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 488 NQETVWNMIEGLGRE--VTRIVVTHD-VEKAILADRVVIMKEGRIV 530
Cdd:cd03301 165 LRVQMRAELKRLQQRlgTTTIYVTHDqVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
344-548 |
4.63e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 120.87 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------ARMTTVWQEPRFF-RTTVK 409
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrgkklrklrRRIGMIFQHYNLIeRLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENVHFGEEYLENQLEKNIELVNVKPIIRDLSE----GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:TIGR02315 98 ENVLHGRLGYKPTWRSLLGRFSEEDKERALSAlervGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 486 PSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLiNSHSFLQRY 548
Cdd:TIGR02315 178 PKTSKQVMDYLKRINKEdgITVIINLHQVDLAKkYADRIVGLKAGEIVFDGAPSEL-DDEVLRHIY 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
329-540 |
6.49e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.38 E-value: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT----------VW 398
Cdd:PRK13647 7 VEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrskvglVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEP--RFFRTTVKENVHFG-------EEYLENQLEKNIELVNVKpiirDLSegietelHKSGVEFSGGERKRLALLRAIV 469
Cdd:PRK13647 86 QDPddQVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMW----DFR-------DKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAeWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-536 |
6.87e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 120.65 E-value: 6.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPRF-----------FRTTVKENV 412
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRravlpqhsslsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFGEEYLENQLEKNIELVnvkpiirdlsegiETELHKSGV---------EFSGGERKRLALLRAIV------SNPNLIIL 477
Cdd:PRK13548 98 AMGRAPHGLSRAEDDALV-------------AAALAQVDLahlagrdypQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAIL-ADRVVIMKEGRIVAGGSPE 536
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPA 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
254-536 |
7.49e-31 |
|
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: 126.40 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 254 IVVLIIGAQKIMKGEMEVGALVA-------VLATIEMLffpvryVGDLLMMTQvAAASANRVFSFLDKRGADskvERAMG 326
Cdd:COG4618 254 SAVLGLGAYLVIQGEITPGAMIAasilmgrALAPIEQA------IGGWKQFVS-ARQAYRRLNELLAAVPAE---PERMP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 M-------TITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMttvW- 398
Cdd:COG4618 324 LprpkgrlSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---Wd 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 ------------QEPRFFRTTVKENV-HFGEEylenQLEKNIE---LVNVKPIIRDLSEGIETELHKSGVEFSGGERKRL 462
Cdd:COG4618 401 reelgrhigylpQDVELFDGTIAENIaRFGDA----DPEKVVAaakLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRI 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 463 ALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGL-GREVTRIVVTHDVekAIL--ADRVVIMKEGRIVAGGSPE 536
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRP--SLLaaVDKLLVLRDGRVQAFGPRD 551
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
344-533 |
8.92e-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: 119.18 E-value: 8.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-----VWQEPRF---FRTTVKENV--- 412
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyVPQRRSIdrdFPISVRDVVlmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 ---HFGEEYLENQLEKNIelvnvkpIIRDLSEGIETELHKSGV-EFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSN 488
Cdd:cd03235 95 lygHKGLFRRLSKADKAK-------VDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 489 QETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKeGRIVAGG 533
Cdd:cd03235 168 QEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLN-RTVVASG 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
345-531 |
1.02e-30 |
|
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: 119.46 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarMTTVWQEPR---------F-FRT-------T 407
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALDEDARarlrarhvgFvFQSfqllptlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVhfgeeylenQLEknIELVNVkpiiRDLSEGIETELHKSGV---------EFSGGERKRLALLRAIVSNPNLIILD 478
Cdd:COG4181 107 ALENV---------MLP--LELAGR----RDARARARALLERVGLghrldhypaQLSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 479 EPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVA 531
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
78-547 |
1.05e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.09 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 78 VSSKASQRILRKKRIYVLRHffLLPFEESE--KIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHID- 154
Cdd:PRK11160 83 VSHDATFRVLTHLRVFTFSK--LLPLSPAGlaRYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDl 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 155 ---------MKFILWVTPFLFFSAmvpmlmGKKVrniaSIAQNNQSSvvEMVSQFVKGVQDL----------RSLQK-EK 214
Cdd:PRK11160 161 tlaltlggiLLLLLLLLPLLFYRL------GKKP----GQDLTHLRA--QYRVQLTEWLQGQaeltlfgaedRYRQQlEQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 215 WAIRLFKGVTAQSYKTEVKKTMMQHCIGVvgtvietgAYIVVLIIGAQKImKGEMEVGALVA-----VLATIEMLFfPVr 289
Cdd:PRK11160 229 TEQQWLAAQRRQANLTGLSQALMILANGL--------TVVLMLWLAAGGV-GGNAQPGALIAlfvfaALAAFEALM-PV- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 290 yVGDLLMMTQVAAaSANRVFSFLDKR-----GADSKVERAMG-MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGES 363
Cdd:PRK11160 298 -AGAFQHLGQVIA-SARRINEITEQKpevtfPTTSTAAADQVsLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 364 GAGKTTLLKLMTGLYKPSNGSIVYYG------NE----ARMTTVWQEPRFFRTTVKENVHFG-----EEYLENQLEKnIE 428
Cdd:PRK11160 376 GCGKSTLLQLLTRAWDPQQGEILLNGqpiadySEaalrQAISVVSQRVHLFSATLRDNLLLAapnasDEALIEVLQQ-VG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 429 LVNvkpiIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVV 508
Cdd:PRK11160 455 LEK----LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446589027 509 THDVEKAILADRVVIMKEGRIVAGGSPEKLINSH----SFLQR 547
Cdd:PRK11160 531 THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQgryyQLKQR 573
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
344-536 |
1.83e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 119.37 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARM----TtvWQEPRFFRT-TVK 409
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitglpphriARLgiarT--FQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENV------HFGEEYLENqleknieLVNVKPIIRDLSE------------GIETELHKSGVEFSGGERKRLALLRAIVSN 471
Cdd:COG0411 98 ENVlvaahaRLGRGLLAA-------LLRLPRARREEREareraeellervGLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVeKAI--LADRVVIMKEGRIVAGGSPE 536
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDM-DLVmgLADRIVVLDFGRVIAEGTPA 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
345-538 |
2.00e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.79 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEArmtTVWQEPR-------F-----FR-TTVKEN 411
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---FTNLPPRerrvgfvFqhyalFPhMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 VHFG-------EEYLENQLEKNIELVNVkpiirdlsEGIE----TELhksgvefSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:COG1118 96 IAFGlrvrppsKAEIRARVEELLELVQL--------EGLAdrypSQL-------SGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 481 TAGLDPSNQETVW----NMIEGLGreVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:COG1118 161 FGALDAKVRKELRrwlrRLHDELG--GTTVFVTHDQEEALeLADRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
267-549 |
2.93e-30 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 124.83 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 267 GEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLDKR----GADSKVERAMGMTITNVSFQESDGEKC 342
Cdd:PRK10790 277 GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPrqqyGNDDRPLQSGRIDIDNVSFAYRDDNLV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 rIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQEPRFFRTTVKENV 412
Cdd:PRK10790 357 -LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslshsvlrqgVAMVQQDPVVLADTFLANV 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETV 492
Cdd:PRK10790 436 TLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI 515
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 493 WNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHS-FLQRYE 549
Cdd:PRK10790 516 QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGrYWQMYQ 573
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-541 |
4.73e-30 |
|
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: 117.64 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARMTTVW--QEPRFFRT- 406
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrARLGIGYlpQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 TVKENV-------HFGEEYLENQLEKNIELVNVKPIirdlsegieteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:cd03218 91 TVEENIlavleirGLSKKEREEKLEELLEEFHITHL-----------RKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIVVT-HDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLsITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
246-539 |
5.41e-30 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 124.16 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 246 TVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLDKR-----GADSK 320
Cdd:COG5265 270 ALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPpevadAPDAP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 321 VERAMGMTIT--NVSFQeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-- 396
Cdd:COG5265 350 PLVVGGGEVRfeNVSFG-YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTqa 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 --------VWQEPRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRA 467
Cdd:COG5265 429 slraaigiVPQDTVLFNDTIAYNIAYGrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIART 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
325-548 |
6.71e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.73 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFQESDG---EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEP 401
Cdd:PRK13646 1 MTIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RFFRTTVKENVHFGEEYL-ENQLEKNIE---------LVNVKPIIRDL--SEGIETE-LHKSGVEFSGGERKRLALLRAI 468
Cdd:PRK13646 81 RPVRKRIGMVFQFPESQLfEDTVEREIIfgpknfkmnLDEVKNYAHRLlmDLGFSRDvMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 469 VSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDV-EKAILADRVVIMKEGRIVAGGSPEKLINSHSFL 545
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
...
gi 446589027 546 QRY 548
Cdd:PRK13646 241 ADW 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
330-538 |
8.42e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.27 E-value: 8.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 330 TNVSFQ----ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG-------------NEA 392
Cdd:PRK13633 8 KNVSYKyesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 RMttVWQEP--RFFRTTVKENVHFGEEYLenqleknielvNVKPiiRDLSEGIETELHKSGV-EF--------SGGERKR 461
Cdd:PRK13633 88 GM--VFQNPdnQIVATIVEEDVAFGPENL-----------GIPP--EEIRERVDESLKKVGMyEYrrhaphllSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
329-535 |
1.34e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.05 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSfqESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-------EAR-MTTVWQE 400
Cdd:PRK09452 17 LRGIS--KSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaENRhVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 PRFF-RTTVKENVHFGeeyLENQLEKNIElvnVKPIIRD------LSEGIETELHksgvEFSGGERKRLALLRAIVSNPN 473
Cdd:PRK09452 95 YALFpHMTVFENVAFG---LRMQKTPAAE---ITPRVMEalrmvqLEEFAQRKPH----QLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSP 535
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGTP 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
325-538 |
1.94e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.43 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFQESDG---EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSiVYYGNEA--------- 392
Cdd:PRK13634 1 MDITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT-VTIGERVitagkknkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 ------RMTTVWQ--EPRFFRTTVKENVHFG-------EEYLENQLEKNIELVNvkpiirdLSEGIeteLHKSGVEFSGG 457
Cdd:PRK13634 80 lkplrkKVGIVFQfpEHQLFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVG-------LPEEL---LARSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 458 ERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGS 534
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkgLTTVLVTHSMEDAArYADQIVVMHKGTVFLQGT 229
|
....
gi 446589027 535 PEKL 538
Cdd:PRK13634 230 PREI 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
344-541 |
1.96e-29 |
|
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: 116.97 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE--------------ARMTTVWQEPRFF-RTTV 408
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkelrelrrKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFG-------EEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELV-----------GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 482 AGLDP----SNQETVWNMIEGLGRevTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:cd03294 189 SALDPlirrEMQDELLRLQAELQK--TIVFITHDLDEALrLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
345-533 |
2.41e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 116.56 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-----------EAR----MTTVW----QEPR-FF 404
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalsEAErrrlLRTEWgfvhQHPRdGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKE--NV----------HFGEeyLENQLEKNIELVNVKPI-IRDLSEgietelhksgvEFSGGERKRLALLRAIVSN 471
Cdd:PRK11701 103 RMQVSAggNIgerlmavgarHYGD--IRATAGDWLERVEIDAArIDDLPT-----------TFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGG 533
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRElgLAVVIVTHDLAVArLLAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
331-538 |
2.60e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.72 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN----------EARMTT--VW 398
Cdd:PRK13639 6 DLKYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllEVRKTVgiVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEP--RFFRTTVKENVHFG-------EEYLENQLEKNIELVNVkpiirdlsEGIEtelHKSGVEFSGGERKRLALLRAIV 469
Cdd:PRK13639 85 QNPddQLFAPTVEEDVAFGplnlglsKEEVEKRVKEALKAVGM--------EGFE---NKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
344-546 |
4.97e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------------NEARMttVWQEPRFF-RTTV 408
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvderlirQEAGM--VFQQFYLFpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFGEEYLENQLEKNIElvnvkPIIRDL--SEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDP 486
Cdd:PRK09493 95 LENVMFGPLRVRGASKEEAE-----KQARELlaKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 487 SNQETVWNMIEGLGRE-VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKLINS------HSFLQ 546
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEgMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIKNppsqrlQEFLQ 237
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
347-538 |
5.21e-29 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 116.72 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA---------RMTTVWQEPRFFRT-TVKENVH-FG 415
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvreprkvrrSIGIVPQYASVDEDlTGRENLEmMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 EEY--LENQLEKNIElvnvkpiirDLSEGIE-TELHKSGVE-FSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQET 491
Cdd:TIGR01188 92 RLYglPKDEAEERAE---------ELLELFElGEAADRPVGtYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446589027 492 VWNMIEGLGRE-VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKL 538
Cdd:TIGR01188 163 IWDYIRALKEEgVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
346-531 |
7.92e-29 |
|
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: 112.14 E-value: 7.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWqeprffrttvkenvhfgeeylenqlek 425
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 426 nielvnvkpiirdlsegietELHKSGVEF----SGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGR 501
Cdd:cd03216 71 --------------------DARRAGIAMvyqlSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA 130
|
170 180 190
....*....|....*....|....*....|..
gi 446589027 502 E-VTRIVVTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:cd03216 131 QgVAVIFISHRLDEVFeIADRVTVLRDGRVVG 162
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
329-533 |
8.19e-29 |
|
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: 113.44 E-value: 8.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFqeSDGEKCRIHNIDLQIHPGELVIiVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW---------Q 399
Cdd:cd03264 3 LENLTK--RYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrrigylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 400 EPRFF-RTTVkenvhfgEEYLENQ-LEKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLI 475
Cdd:cd03264 80 EFGVYpNFTV-------REFLDYIaWLKGIPSKEVKARVDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEK-AILADRVVIMKEGRIVAGG 533
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDvESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
327-546 |
1.07e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.85 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYygNEARMTT---------- 396
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY--NNQAITDdnfeklrkhi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 --VWQEP--RFFRTTVKENVHFGeeyLENQL---EKNIELVNVKPIIRDLSEGIETELHksgvEFSGGERKRLALLRAIV 469
Cdd:PRK13648 86 giVFQNPdnQFVGSIVKYDVAFG---LENHAvpyDEMHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQ 546
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
337-536 |
1.08e-28 |
|
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: 113.01 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 337 SDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGL--YKPSNGSIVYYGNE---------ARM--TTVWQEPrf 403
Cdd:cd03217 9 SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeerARLgiFLAFQYP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 404 frttvkenvhfgEEylenqleknIELVNVKPIIRDLSEGietelhksgveFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:cd03217 87 ------------PE---------IPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 484 LDPSNQETVWNMIEGLGRE-VTRIVVTH--DVEKAILADRVVIMKEGRIVAGGSPE 536
Cdd:cd03217 135 LDIDALRLVAEVINKLREEgKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
327-541 |
1.36e-28 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 113.93 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLK---LMTGLYKPSN--GSIVYYGNE---------- 391
Cdd:TIGR00972 2 IEIENLNL--FYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnRMNDLVPGVRieGKVLFDGQDiydkkidvve 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 --ARMTTVWQEPRFFRTTVKENVHFG------------EEYLENQLEKnielvnvkpiiRDLSEGIETELHKSGVEFSGG 457
Cdd:TIGR00972 80 lrRRVGMVFQKPNPFPMSIYDNIAYGprlhgikdkkelDEIVEESLKK-----------AALWDEVKDRLHDSALGLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 458 ERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPE 536
Cdd:TIGR00972 149 QQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAArISDRTAFFYDGELVEYGPTE 228
|
....*
gi 446589027 537 KLINS 541
Cdd:TIGR00972 229 QIFTN 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
174-540 |
1.82e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 119.35 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 174 LMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAY 253
Cdd:PRK11176 184 VVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLAL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 254 IVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLD----KRGADSKVERAMG-MT 328
Cdd:PRK11176 264 AFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDleqeKDEGKRVIERAKGdIE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT----------VW 398
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaslrnqvalVS 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPRFFRTTVKENVHF--GEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLII 476
Cdd:PRK11176 424 QNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTH---DVEKailADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEK---ADEILVVEDGEIVERGTHAELLA 567
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
328-540 |
2.06e-28 |
|
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: 113.06 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------------A 392
Cdd:cd03258 3 ELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsgkelrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 RMTTVWQEPRFF-RTTVKENV-------HFGEEYLENQLEKNIELVNVKpiirDLSEGIETELhksgvefSGGERKRLAL 464
Cdd:cd03258 83 RIGMIFQHFNLLsSRTVFENValpleiaGVPKAEIEERVLELLELVGLE----DKADAYPAQL-------SGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 465 LRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTH--DVEKAIlADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHemEVVKRI-CDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
327-547 |
2.31e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKP---SNGSIVYYGNEARMTTVW----- 398
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 -----QEP--RFFRTTVKENVHFGeeyLENQLEKNIELVNvkpIIRD-LSEGIETELHKSG-VEFSGGERKRLALLRAIV 469
Cdd:PRK13640 86 vgivfQNPdnQFVGATVGDDVAFG---LENRAVPRPEMIK---IVRDvLADVGMLDYIDSEpANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
250-541 |
3.17e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 118.91 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 250 TGAYIVVLIIGAQKIMKGEMEVGALVAV--LAT--IEMLFFPVRYVGDLLMmtqvAAASANRVFSFLD------KRGADS 319
Cdd:PRK13657 251 TITMLAILVLGAALVQKGQLRVGEVVAFvgFATllIGRLDQVVAFINQVFM----AAPKLEEFFEVEDavpdvrDPPGAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 320 KVERAMG-MTITNVSFqESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----- 393
Cdd:PRK13657 327 DLGRVKGaVEFDDVSF-SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvtra 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 -----MTTVWQEPRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRA 467
Cdd:PRK13657 406 slrrnIAVVFQDAGLFNRSIEDNIRVGrPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
329-544 |
4.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.54 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA-----------RMTTV 397
Cdd:PRK13644 4 LENVSYSYPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirkLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEP--RFFRTTVKENVHFGEeylENQLEKNIELvnVKPIIRDLSE-GIETELHKSGVEFSGGERKRLALLRAIVSNPNL 474
Cdd:PRK13644 83 FQNPetQFVGRTVEEDLAFGP---ENLCLPPIEI--RKRVDRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 475 IILDEPTAGLDPSNQETVWNMIEGLGREVTRIV-VTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSF 544
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-536 |
4.65e-28 |
|
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: 117.98 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 7 ILLPLQKEKLLVIAAVCSGCFAAILNlsrplfMGLIVdnLIQRELKAAYV----YIALFAGSRLLMWVNNLSFDYVSSKA 82
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLAN------AGLIA--LINQALNATGAalarLLLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 83 SQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPNwVRLYGSILIEYIHAIAQFIGAFIalqhidmkFILWVT 162
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRT-ISQAFVRLPELLQSVALVLGCLA--------YLAWLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 163 PFLFFSAMVPMLMG--------KKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRsLQKEKwAIRLFKGV---TAQSYKTE 231
Cdd:COG4615 147 PPLFLLTLVLLGLGvagyrllvRRARRHLRRAREAEDRLFKHFRALLEGFKELK-LNRRR-RRAFFDEDlqpTAERYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 232 VKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKImkGEMEVGALVAVLATIEMLFFPVRYVGD---LLMMTQVAAASANRV 308
Cdd:COG4615 225 RIRADTIFALANNWGNLLFFALIGLILFLLPAL--GWADPAVLSGFVLVLLFLRGPLSQLVGalpTLSRANVALRKIEEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 309 FSFLDKRGADSKVERAMGM-----TIT--NVSFQ---ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLY 378
Cdd:COG4615 303 ELALAAAEPAAADAAAPPApadfqTLElrGVTYRypgEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 379 KPSNGSIVYYGNEARMTTvWQEPRFFRTTVKENVHFGEEYLenQLEKNIELVNVKPIIRDLsegietEL-HK-------- 449
Cdd:COG4615 383 RPESGEILLDGQPVTADN-REAYRQLFSAVFSDFHLFDRLL--GLDGEADPARARELLERL------ELdHKvsvedgrf 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 450 SGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNqetvwnmieglgREV--------------TRIVVTHDVEKA 515
Cdd:COG4615 454 STTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF------------RRVfytellpelkargkTVIAISHDDRYF 521
|
570 580
....*....|....*....|.
gi 446589027 516 ILADRVVIMKEGRIVAGGSPE 536
Cdd:COG4615 522 DLADRVLKMDYGKLVELTGPA 542
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
346-533 |
6.55e-28 |
|
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: 111.23 E-value: 6.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIhPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGnearmtTVWQEPR---------------------FF 404
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG------TVLFDSRkkinlppqqrkiglvfqqyalFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKENVHFGEEYLEN-----QLEKNIELVNVKPIirdlsegieteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:cd03297 89 HLNVRENLAFGLKRKRNredriSVDELLDLLGLDHL-----------LNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKA-ILADRVVIMKEGRIVAGG 533
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-547 |
8.43e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 117.64 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGlYKPSNGSIVYYGNEAR---MTT-------VWQEPRFFRTTVKENVHFG 415
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELReldPESwrkhlswVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 EEYL-ENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWN 494
Cdd:PRK11174 447 NPDAsDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446589027 495 MIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT 579
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
344-529 |
1.06e-27 |
|
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: 111.02 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN----------EARMTTVWQEPRFFRTTVKENVH 413
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylHSKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLEnqLEKNIELV---NVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQE 490
Cdd:cd03248 110 YGLQSCS--FECVKEAAqkaHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 446589027 491 TVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRI 529
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
332-538 |
1.38e-27 |
|
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: 113.67 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 332 VSFQESDGEKCRihNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------------NEARMTTV 397
Cdd:TIGR02142 3 ARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRFF-RTTVKENVHFG-----EEYLENQLEKNIELVNVKPIIRDLSEgietelhksgvEFSGGERKRLALLRAIVSN 471
Cdd:TIGR02142 81 FQEARLFpHLSVRGNLRYGmkrarPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDV-EKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLHAEfgIPILYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
347-515 |
2.13e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 109.05 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE------------ARMTTVWQEP--RFFRTTVKENV 412
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDPddQLFAADVDQDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFG-------EEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:TIGR01166 91 AFGplnlglsEAEVERRVREALTAV-----------GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 446589027 486 PSNQETVWNMIEGLGREVTRIVV-THDVEKA 515
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVIsTHDVDLA 190
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
346-548 |
2.50e-27 |
|
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: 110.06 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARMTTVW--QEPRFFRT-TVKENVH 413
Cdd:TIGR04406 19 DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDithlpmherARLGIGYlpQEASIFRKlTVEENIM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLENQLEKNIELvnvkpIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQET 491
Cdd:TIGR04406 99 AVLEIRKDLDRAEREE-----RLEALLEefQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 492 VWNMIEGLGREVTRIVVT-HDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQRY 548
Cdd:TIGR04406 174 IKKIIKHLKERGIGVLITdHNVRETLdICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
344-529 |
2.65e-27 |
|
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: 109.42 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA-------------RMTTVWQEPRFFRT-TVK 409
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraipylrrKIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENVHFGEEYLE-------NQLEKNIELVNVKPIIRDLSEgietelhksgvEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 483 GLDPSNQETVWNMIEGLG-REVTRIVVTHDveKAILAD---RVVIMKEGRI 529
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINkAGTTVVVATHA--KELVDTtrhRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
344-527 |
2.86e-27 |
|
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: 109.86 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA------RMTtVWQEPRFFR-TTVKENV---- 412
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdRMV-VFQNYSLLPwLTVRENIalav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 -----HFGEEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDP- 486
Cdd:TIGR01184 80 drvlpDLSKSERRAIVEEHIALV-----------GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAl 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446589027 487 ---SNQETVWNMIEglGREVTRIVVTHDVEKAI-LADRVVIMKEG 527
Cdd:TIGR01184 149 trgNLQEELMQIWE--EHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
346-541 |
3.02e-27 |
|
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: 112.89 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG----NEARMTT----------VWQEPRFF-RTTVKE 410
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqDSARGIFlpphrrrigyVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFGEEYLEN-----QLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:COG4148 97 NLLYGRKRAPRaerriSFDEVVELL-----------GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 486 -PSNQEtVWNMIEGLGREV-TRIV-VTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG4148 166 lARKAE-ILPYLERLRDELdIPILyVSHSLDEVArLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
327-538 |
3.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.98 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQ-ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW------- 398
Cdd:PRK13650 5 IEVKNLTFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWdirhkig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 ---QEP--RFFRTTVKENVHFGeeyLENQ---LEKNIELVNVKPIIRDLSEGIETELHKsgveFSGGERKRLALLRAIVS 470
Cdd:PRK13650 85 mvfQNPdnQFVGATVEDDVAFG---LENKgipHEEMKERVNEALELVGMQDFKEREPAR----LSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 471 NPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
150-548 |
4.63e-27 |
|
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: 116.58 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 150 LQHIDMKFILWVT--PFL-----FFSAMVPM--LMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLR------SLQKEK 214
Cdd:TIGR00957 443 LQVILALYFLWLNlgPSVlagvaVMVLMVPLnaVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKlyawelAFLDKV 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 215 WAIRL--FKGVTAQSYKTEVKkTMMQHCIGVVGTVIETGAYIVV---LIIGAQKimkgemevgALVAvLATIEMLFFPVR 289
Cdd:TIGR00957 523 EGIRQeeLKVLKKSAYLHAVG-TFTWVCTPFLVALITFAVYVTVdenNILDAEK---------AFVS-LALFNILRFPLN 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 290 YVGDLLMMTQVAAASANRVFSFLDKRGAD-SKVER-------AMGMTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVG 361
Cdd:TIGR00957 592 ILPMVISSIVQASVSLKRLRIFLSHEELEpDSIERrtikpgeGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVG 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 362 ESGAGKTTLLKLMTGLYKPSNGSIVYYGNEArmtTVWQEPRFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSE 441
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDKVEGHVHMKGSVA---YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPS 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 442 GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMI---EGLGREVTRIVVTHDVEKAILA 518
Cdd:TIGR00957 749 GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQV 828
|
410 420 430
....*....|....*....|....*....|....
gi 446589027 519 DRVVIMKEGRIVAGGSPEKLINSH----SFLQRY 548
Cdd:TIGR00957 829 DVIIVMSGGKISEMGSYQELLQRDgafaEFLRTY 862
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-541 |
5.12e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.05 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN---------EARMTTVWQ----EPRFfr 405
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarhaRQRVGVVPQfdnlDPDF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 tTVKENVHFGEEYLENQLEKNIELVnvkPIIRDLSEgIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:PRK13537 96 -TVRENLLVFGRYFGLSAAAARALV---PPLLEFAK-LENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 486 PSNQETVWNMIEGL-GREVTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:PRK13537 171 PQARHLMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
339-529 |
5.16e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.77 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYyGN----EARMTT--VWQEPRFFR-TTVKEN 411
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTaplaEAREDTrlMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 VHFG--EEYLENQLEKnIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQ 489
Cdd:PRK11247 102 VGLGlkGQWRDAALQA-LAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446589027 490 ETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:PRK11247 170 IEMQDLIESLWQQhgFTVLLVTHDVSEAVaMADRVLLIEEGKI 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
325-538 |
2.13e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.56 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSfqESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN--------EARMTT 396
Cdd:PRK10851 1 MSIEIANIK--KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlharDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFR-TTVKENVHFGEEYLENQLEKNIELVNVKpiIRDLSEGIETElHKSG---VEFSGGERKRLALLRAIVSNP 472
Cdd:PRK10851 79 VFQHYALFRhMTVFDNIAFGLTVLPRRERPNAAAIKAK--VTQLLEMVQLA-HLADrypAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 473 NLIILDEPTAGLDPSNQETVWNMIEGLGREV--TRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMeVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
327-549 |
2.53e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.94 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSF---QESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVY--YGNEARMTT----- 396
Cdd:PRK13645 7 IILDNVSYtyaKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANLKKikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 --------VWQEPRF--FRTTVKENVHFGEEYLENQLEKNIELVnvkPIIRDLSEGIETELHKSGVEFSGGERKRLALLR 466
Cdd:PRK13645 87 rlrkeiglVFQFPEYqlFQETIEKDIAFGPVNLGENKQEAYKKV---PELLKLVQLPEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 467 AIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTR--IVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHS 543
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKriIMVTHNMDQVLrIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
....*.
gi 446589027 544 FLQRYE 549
Cdd:PRK13645 244 LLTKIE 249
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
346-530 |
3.44e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.05 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA-------------RMTTVWQEPrfF-----RTT 407
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgrelrplrrRMQMVFQDP--YaslnpRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVhfgEEYLENQleknielvNVKPIiRDLSEGIETELHKSGV----------EFSGGERKRLALLRAIVSNPNLIIL 477
Cdd:COG4608 114 VGDII---AEPLRIH--------GLASK-AERRERVAELLELVGLrpehadryphEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHD--VEKAIlADRVVIMKEGRIV 530
Cdd:COG4608 182 DEPVSALDVSIQAQVLNLLEDLQDElgLTYLFISHDlsVVRHI-SDRVAVMYLGKIV 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
348-533 |
3.62e-26 |
|
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: 106.04 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 348 DLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------NEARMTTVWQEPRFF-RTTVKENVHFGeey 418
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappADRPVSMLFQENNLFaHLTVEQNVGLG--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 lenqLEKNIELV-----NVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:cd03298 95 ----LSPGLKLTaedrqAIEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446589027 494 NMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGG 533
Cdd:cd03298 169 DLVLDLHAEtkMTVLMVTHQPEDAKrLAQRVVFLDNGRIAAQG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-533 |
4.62e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 105.76 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE--------ARMTTVWQEPRFF-RTTVK 409
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealRRIGALIEAPGFYpNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENVhfgeeyLENQLEKNIELVNVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQ 489
Cdd:cd03268 91 ENL------RLLARLLGIRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 490 ETVWNMIEGLGRE-VTRIVVTHDV-EKAILADRVVIMKEGRIVAGG 533
Cdd:cd03268 163 KELRELILSLRDQgITVLISSHLLsEIQKVADRIGIINKGKLIEEG 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
346-530 |
8.23e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVyYGNEARMTTVWQEPRFF-RTTVKENVHFGEEYLeNQLE 424
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-IPKGLRIGYLPQEPPLDdDLTVLDTVLDGDAEL-RALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 425 KNIELVNVKP-----IIRDLSE------------------------GIETELHKSGV-EFSGGERKRLALLRAIVSNPNL 474
Cdd:COG0488 94 AELEELEAKLaepdeDLERLAElqeefealggweaearaeeilsglGFPEEDLDRPVsELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 475 IILDEPTAGLDpsnQETV-WnmIEG--LGREVTRIVVTHDVEkaiLADRVVimkeGRIV 530
Cdd:COG0488 174 LLLDEPTNHLD---LESIeW--LEEflKNYPGTVLVVSHDRY---FLDRVA----TRIL 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
235-547 |
8.28e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 112.76 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 235 TMMQHCIGVVGTVIETGAYIvvliigaqkIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFL-- 312
Cdd:PLN03232 527 SFILNSIPVVVTLVSFGVFV---------LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLls 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 313 DKR--GADSKVERAM-GMTITNVSFQ-ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPS-NGSIVY 387
Cdd:PLN03232 598 EERilAQNPPLQPGApAISIKNGYFSwDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVI 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 388 YGNEArmtTVWQEPRFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIrDLSEGIE-TELHKSGVEFSGGERKRLALLR 466
Cdd:PLN03232 678 RGSVA---YVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDL-DLLPGRDlTEIGERGVNISGGQKQRVSMAR 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 467 AIVSNPNLIILDEPTAGLDPSNQETVWN--MIEGLgREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSF 544
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDEL-KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
...
gi 446589027 545 LQR 547
Cdd:PLN03232 833 FKK 835
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
344-541 |
9.13e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARM--TTVWQEPRFFRT-TVKEN 411
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrARLgiGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 V-------HFGEEYLENQLEkniELvnvkpiirdLSE-GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:COG1137 99 IlavlelrKLSKKEREERLE---EL---------LEEfGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 484 LDPSNQETVWNMIE-----GLGrevtrIVVT-HDVeKAILA--DRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG1137 167 VDPIAVADIQKIIRhlkerGIG-----VLITdHNV-RETLGicDRAYIISEGKVLAEGTPEEILNN 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
326-547 |
9.52e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.52 E-value: 9.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 326 GMTITNVSFQ-ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKP-SNGSIVYYGNEARMTTV-Wqepr 402
Cdd:PLN03130 614 AISIKNGYFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQVsW---- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 403 FFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:PLN03130 690 IFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 483 GLDPSNQETVWNM-IEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:PLN03130 770 ALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
345-547 |
1.04e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.46 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarMTTVWQEPRFFRT---------------TVK 409
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED--LTDSKKDINKLRRkvgmvfqqfnlfphlTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENVHFGeeylenqleknieLVNVKPIIRDLSEGI-ETELHKSGV---------EFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:COG1126 96 ENVTLA-------------PIKVKKMSKAEAEERaMELLERVGLadkadaypaQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVE--KAIlADRVVIMKEGRIVAGGSPEKLINS------HSFLQR 547
Cdd:COG1126 163 PTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGfaREV-ADRVVFMDGGRIVEEGPPEEFFENpqhertRAFLSK 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-530 |
1.05e-25 |
|
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: 107.45 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKP---SNGSIVYYGNE--------------AR 393
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklsekelrkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 MTTVWQE------PRFfrtTVKEnvHFGEEYLENQLEKNIElvnVKPIIRDLSE--GI---ETELHKSGVEFSGGERKRL 462
Cdd:COG0444 88 IQMIFQDpmtslnPVM---TVGD--QIAEPLRIHGGLSKAE---ARERAIELLErvGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 463 ALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHD---VekAILADRVVIMKEGRIV 530
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElgLAILFITHDlgvV--AEIADRVAVMYAGRIV 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
346-548 |
1.15e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.22 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------AR-MTTVWQEPRFF-RTTVKENVHFGe 416
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltalppaERpVSMLFQENNLFpHLTVAQNIGLG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 417 eylenqleknielvnVKPIIRdLSEG----IETELHKSGVE---------FSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:COG3840 96 ---------------LRPGLK-LTAEqraqVEQALERVGLAglldrlpgqLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 484 LDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHS--FLQRY 548
Cdd:COG3840 160 LDPALRQEMLDLVDELCRErgLTVLMVTHDPEDAArIADRVLLVADGRIAADGPTAALLDGEPppALAAY 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
344-524 |
1.28e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNeARMTTVWQ---EPRFFRTTVKENV---HFGEE 417
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-ARVAYVPQrseVPDSLPLTVRDLVamgRWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 418 YLENQLEKNIELVnvkpIIRDLSE-GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMI 496
Cdd:NF040873 87 GLWRRLTRDDRAA----VDDALERvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180
....*....|....*....|....*....
gi 446589027 497 -EGLGREVTRIVVTHDVEKAILADRVVIM 524
Cdd:NF040873 163 aEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
344-533 |
1.29e-25 |
|
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: 105.11 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARMTTVWQEprffRTTVKENVHF 414
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflRRIGVVFGQ----KTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 GEEYLENQLEKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETV 492
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSEllDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 493 WNMIEGLGRE--VTRIVVTH---DVEKaiLADRVVIMKEGRIVAGG 533
Cdd:cd03267 193 RNFLKEYNRErgTTVLLTSHymkDIEA--LARRVLVIDKGRLLYDG 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
338-538 |
1.51e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.38 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 338 DGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEP---------RFFRTTV 408
Cdd:PRK11607 30 DGQHA-VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPinmmfqsyaLFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFG-------EEYLENQLEKNIELVNVKpiirdlsEGIETELHksgvEFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:PRK11607 109 EQNIAFGlkqdklpKAEIASRVNEMLGLVHMQ-------EFAKRKPH----QLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 482 AGLDPS----NQETVWNMIEGLGreVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK11607 178 GALDKKlrdrMQLEVVDILERVG--VTCVMVTHDQEEAMtMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
344-528 |
1.83e-25 |
|
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: 104.44 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPR---------------FF---- 404
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPReilalrrrtigyvsqFLrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKENVhfGEEYLENQLEKNIELVNVKPIIRDLseGIETEL-HKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:COG4778 107 RVSALDVV--AEPLLERGVDREEARARARELLARL--NLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 484 LDPSNQETVWNMIEGLGREVTRIV-VTHDVE-KAILADRVVIMKEGR 528
Cdd:COG4778 183 LDAANRAVVVELIEEAKARGTAIIgIFHDEEvREAVADRVVDVTPFS 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
317-542 |
1.86e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 317 ADSKVERAMGMT-ITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG------ 389
Cdd:PRK13536 29 AKASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpar 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 390 ---NEARMTTVWQ----EPRFfrtTVKEN-VHFGEEYLENQLEknielvnVKPIIRDLSE--GIETELHKSGVEFSGGER 459
Cdd:PRK13536 109 arlARARIGVVPQfdnlDLEF---TVRENlLVFGRYFGMSTRE-------IEAVIPSLLEfaRLESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 460 KRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEG-LGREVTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEK 537
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHA 258
|
....*
gi 446589027 538 LINSH 542
Cdd:PRK13536 259 LIDEH 263
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-548 |
2.30e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-----ARMTTVWQEPRFFR 405
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgADRGVVFQKDALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 -TTVKENVHFG--------EEYLEnQLEKNIELVnvkpiirdlseGIEtELHKSGV-EFSGGERKRLALLRAIVSNPNLI 475
Cdd:COG4525 90 wLNVLDNVAFGlrlrgvpkAERRA-RAEELLALV-----------GLA-DFARRRIwQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGLGREVTRIV--VTHDVEKAI-LADRVVIMK--EGRIVAGGSPEklinshsFLQRY 548
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVflITHSVEEALfLATRLVVMSpgPGRIVERLELD-------FSRRF 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
252-527 |
2.31e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 252 AYIVVLIIGAQKIMKGEMEVGALV-AVLATIEM---LFFPVRYVGDLlmmtqvAA--ASANRVFSFLD-------KRGAD 318
Cdd:COG4178 279 AVIFPILVAAPRYFAGEITLGGLMqAASAFGQVqgaLSWFVDNYQSL------AEwrATVDRLAGFEEaleaadaLPEAA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 319 SKVERAMG--MTITNVSFQESDGEKcRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYyGNEARMTT 396
Cdd:COG4178 353 SRIETSEDgaLALEDLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-PAGARVLF 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFRTTVKENV---HFGEEYLENQLEKNIELVNVKpiirDLSEGIETELHKSGVeFSGGERKRLALLRAIVSNPN 473
Cdd:COG4178 431 LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEEADWDQV-LSLGEQQRLAFARLLLHKPD 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEG 527
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-530 |
2.66e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.17 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVS---FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-ARMTT------ 396
Cdd:COG1101 2 LELKNLSktfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTKLPEykraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 ---VWQEPR---FFRTTVKEN------------VHFGeeylenQLEKNIELVnvKPIIRDLSEGIETELH-KSGVeFSGG 457
Cdd:COG1101 82 igrVFQDPMmgtAPSMTIEENlalayrrgkrrgLRRG------LTKKRRELF--RELLATLGLGLENRLDtKVGL-LSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 458 ERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIV 530
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnnLTTLMVTHNMEQALdYGNRLIMMHEGRII 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
347-533 |
2.88e-25 |
|
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: 103.60 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarmttVWQEPR---------------FFRTTVKEN 411
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-----VVKEPAearrrlgfvsdstglYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 V-HFGEEY-LENQleknielvNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:cd03266 99 LeYFAGLYgLKGD--------ELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446589027 488 NQETVWNMIEGLGREVTRIVV-THDV-EKAILADRVVIMKEGRIVAGG 533
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFsTHIMqEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
329-529 |
2.92e-25 |
|
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: 103.76 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVsfQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE------------ARMTT 396
Cdd:cd03262 3 IKNL--HKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkninelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFF-RTTVKENVHFGeeylenqleknieLVNVKPIIRDLSE----------GIETELHKSGVEFSGGERKRLALL 465
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLA-------------PIKVKGMSKAEAEeralellekvGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 466 RAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
325-546 |
4.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFQESDG---EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT----- 396
Cdd:PRK13649 1 MGINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 ---------VWQ--EPRFFRTTVKENVHFG-------EEYLENQLEKNIELVnvkpiirdlseGIETEL-HKSGVEFSGG 457
Cdd:PRK13649 81 kqirkkvglVFQfpESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALV-----------GISESLfEKNPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 458 ERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTH---DVekAILADRVVIMKEGRIVAGG 533
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHlmdDV--ANYADFVYVLEKGKLVLSG 227
|
250
....*....|...
gi 446589027 534 SPEKLINSHSFLQ 546
Cdd:PRK13649 228 KPKDIFQDVDFLE 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
325-548 |
4.63e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFQESDG---EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------NEA- 392
Cdd:PRK13641 1 MSIKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgNKNl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 -----RMTTVWQ--EPRFFRTTVKENVHFG-------EEYLENQLEKNIELVnvkpiirdlseGIETEL-HKSGVEFSGG 457
Cdd:PRK13641 81 kklrkKVSLVFQfpEAQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKV-----------GLSEDLiSKSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 458 ERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEK-AILADRVVIMKEGRIVAGGSP 535
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASP 229
|
250
....*....|...
gi 446589027 536 EKLINSHSFLQRY 548
Cdd:PRK13641 230 KEIFSDKEWLKKH 242
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
334-529 |
5.21e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.36 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 334 FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------ARMTTVWQE------ 400
Cdd:PRK11629 15 YQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaAKAELRNQKlgfiyq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 401 -----PRFfrtTVKENVHF----GEEYLENQLEKNIELVNvkpiirdlSEGIETELHKSGVEFSGGERKRLALLRAIVSN 471
Cdd:PRK11629 95 fhhllPDF---TALENVAMplliGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRI 529
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLqgTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
327-530 |
6.49e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYyGNEARMTTVWQEPRFFRT 406
Cdd:COG0488 316 LELEGLSK--SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIGYFDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 --TVKENVhfgEEYLENQLEKNIelvnvkpiiRDLSEGI---ETELHKS-GVeFSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:COG0488 393 dkTVLDEL---RDGAPGGTEQEV---------RGYLGRFlfsGDDAFKPvGV-LSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 481 TAGLDPsnqETVWNMIEGL----GrevTRIVVTHD---VEKaiLADRVVIMKEGRIV 530
Cdd:COG0488 460 TNHLDI---ETLEALEEALddfpG---TVLLVSHDryfLDR--VATRILEFEDGGVR 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
345-531 |
7.41e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-----------VWQEPRFFRT-TVKENV 412
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdaqaagiaiIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFGEEYlenqleKNIELVNVKPIIRDLSE-----GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:COG1129 101 FLGREP------RRGGLIDWRAMRRRAREllarlGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 488 NQETVWNMIEGL-GREVTRIVVTHDVE--KAIlADRVVIMKEGRIVA 531
Cdd:COG1129 175 EVERLFRIIRRLkAQGVAIIYISHRLDevFEI-ADRVTVLRDGRLVG 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
322-522 |
8.67e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 8.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 322 ERAMGMTITNVSFQEsdGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarMTTV---- 397
Cdd:PRK10247 3 ENSPLLQLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGED--ISTLkpei 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 --------WQEPRFFRTTVKENVHFGEEYLENQLEKNIelvnvkpIIRDLS--EGIETELHKSGVEFSGGERKRLALLRA 467
Cdd:PRK10247 79 yrqqvsycAQTPTLFGDTVYDNLIFPWQIRNQQPDPAI-------FLDDLErfALPDTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVV 522
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqnIAVLWVTHDKDEINHADKVI 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
344-540 |
1.09e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.15 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE---------ARMTTV--WQEPRFFRT-TVKEN 411
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiARMGVVrtFQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 VHFGEeylENQLEKNI--ELVNVKPIIRDLSEGIE---TELHKSGV-EFSG--------GERKRLALLRAIVSNPNLIIL 477
Cdd:PRK11300 101 LLVAQ---HQQLKTGLfsGLLKTPAFRRAESEALDraaTWLERVGLlEHANrqagnlayGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
345-541 |
1.58e-24 |
|
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: 107.08 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkPSNGSIVYYGNE-------------ARMTTVWQEPrfF-----RT 406
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldglsrralrplrRRMQVVFQDP--FgslspRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 TVKE------NVHFGEEYLENQLEKNIELvnvkpiirdLSE-GIETE-LHKSGVEFSGGERKRLALLRAIVSNPNLIILD 478
Cdd:COG4172 380 TVGQiiaeglRVHGPGLSAAERRARVAEA---------LEEvGLDPAaRHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 479 EPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHD--VEKAiLADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLQREhgLAYLFISHDlaVVRA-LAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
329-538 |
1.88e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-----------EAR--MT 395
Cdd:PRK11831 10 MRGVSF--TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlyTVRkrMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 396 TVWQEPRFFR-TTVKENV--------HFGEEYLENQLEKNIELVNvkpiIRDLSEGIETELhksgvefSGGERKRLALLR 466
Cdd:PRK11831 88 MLFQSGALFTdMNVFDNVayplrehtQLPAPLLHSTVMMKLEAVG----LRGAAKLMPSEL-------SGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 467 AIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVPEVLsIADHAYIVADKKIVAHGSAQAL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
346-536 |
2.01e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-----------VWQEPRFFRT-TVKENVH 413
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprdaialgigmVHQHFMLVPNlTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGeeyLENQLEKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPsnQET 491
Cdd:COG3845 103 LG---LEPTKGGRLDRKAARARIRELSEryGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP--QEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446589027 492 --VWNMIEGLGRE-VTRIVVTHDVE--KAIlADRVVIMKEGRIVAGGSPE 536
Cdd:COG3845 178 deLFEILRRLAAEgKSIIFITHKLRevMAI-ADRVTVLRRGKVVGTVDTA 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
344-545 |
2.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVY-YGNEA------------------------------ 392
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWiFKDEKnkkktkekekvleklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 ---RMTTVWQ--EPRFFRTTVKENVHFG--------EEYLENQLeKNIELVNVKpiirdlsegiETELHKSGVEFSGGER 459
Cdd:PRK13651 103 irrRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvskEEAKKRAA-KYIELVGLD----------ESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 460 KRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEK 537
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLeWTKRTIFFKDGKIIKDGDTYD 251
|
....*...
gi 446589027 538 LINSHSFL 545
Cdd:PRK13651 252 ILSDNKFL 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
348-543 |
3.31e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 348 DLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEP---------RFFRTTVKENVHFGeey 418
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPvsmlfqennLFSHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 LENQLEKNIELvnvKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS-NQEtvwnM 495
Cdd:PRK10771 96 LNPGLKLNAAQ---REKLHAIARqmGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAlRQE----M 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 496 IEGLG-----REVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHS 543
Cdd:PRK10771 169 LTLVSqvcqeRQLTLLMVSHSLEDAArIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
339-533 |
3.65e-24 |
|
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: 100.43 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN------EARMTTVWQEPRFFR-TTVKEN 411
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaaRNRIGYLPEERGLYPkMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 -VHFGeeylenQLeKNIELVNVKPIIRDLSEGIETELHKSGV--EFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSN 488
Cdd:cd03269 91 lVYLA------QL-KGLKKEEARRRIDEWLERLELSEYANKRveELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446589027 489 QETVWNMIEGLGRE-VTRIVVTH---DVEKaiLADRVVIMKEGRIVAGG 533
Cdd:cd03269 164 VELLKDVIRELARAgKTVILSTHqmeLVEE--LCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
331-538 |
4.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVY------YGNEARMT------TVW 398
Cdd:PRK13636 10 ELNYNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFdgkpidYSRKGLMKlresvgMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEP--RFFRTTVKENVHFGEEYL---ENQLEKNIELVNVKpiirdlsEGIETELHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:PRK13636 89 QDPdnQLFSASVYQDVSFGAVNLklpEDEVRKRVDNALKR-------TGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 474 LIILDEPTAGLDPSN----QETVWNMIEGLGreVTRIVVTHDVEK-AILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK13636 162 VLVLDEPTAGLDPMGvseiMKLLVEMQKELG--LTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
344-548 |
4.99e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 100.72 E-value: 4.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarmTTVWQEPR---------------FFRTTV 408
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKimreavaivpegrrvFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFGEEYLE-NQLEKNIELVnvkpiiRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:PRK11614 98 EENLAMGGFFAErDQFQERIKWV------YELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 488 NQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQRY 548
Cdd:PRK11614 172 IIQQIFDTIEQLREQgMTIFLVEQNANQALkLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
344-527 |
1.54e-23 |
|
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: 98.94 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSiVYYGNEARMTTVW---------------QEPRFFRTTV 408
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK-VHWSNKNESEPSFeatrsrnrysvayaaQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS- 487
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446589027 488 ----NQETVWNMIEGLGRevTRIVVTHDVEKAILADRVVIMKEG 527
Cdd:cd03290 176 sdhlMQEGILKFLQDDKR--TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
346-525 |
3.46e-23 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 97.85 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPR---------------FF----RT 406
Cdd:TIGR02324 26 NVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQASPRevlevrrktigyvsqFLrvipRV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 TVKENVhfGEEYLENQLEKNIELVNVKPIIRDLSegIETEL-HKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:TIGR02324 106 SALEVV--AEPLLERGVPREAARARARELLARLN--IPERLwHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446589027 486 PSNQETVWNMI-EGLGREVTRIVVTHDVE-KAILADRVVIMK 525
Cdd:TIGR02324 182 AANRQVVVELIaEAKARGAALIGIFHDEEvRELVADRVMDVT 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-538 |
4.97e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.57 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKL---MTGLYkPSN---GSIVYYGNE--------- 391
Cdd:COG1117 12 IEVRNLNV--YYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLI-PGArveGEILLDGEDiydpdvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 ---ARMTTVWQEPRFFRTTVKENVHFGeeylenqleknIELVNVKPIiRDLSEGIET-------------ELHKSGVEFS 455
Cdd:COG1117 89 elrRRVGMVFQKPNPFPKSIYDNVAYG-----------LRLHGIKSK-SELDEIVEEslrkaalwdevkdRLKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 456 GGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGS 534
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAArVSDYTAFFYLGELVEFGP 236
|
....
gi 446589027 535 PEKL 538
Cdd:COG1117 237 TEQI 240
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
344-530 |
5.15e-23 |
|
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: 98.72 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPRFFRT----------------T 407
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDvqlvfqdspsavnprmT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGEEYLEN-----QLEKNIELVnvkpiirDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:TIGR02769 107 VRQIIGEPLRHLTSldeseQKARIAELL-------DMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 483 GLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKA-ILADRVVIMKEGRIV 530
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVqSFCQRVAVMDKGQIV 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-543 |
6.52e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.39 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGnearMTTVWQEPRFFR--TTVkenvhFG------ 415
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKEFARriGVV-----FGqrsqlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 --------------------EEYLENqLEKNIELVNVKPII----RDLSegieteLhksgvefsgGERKRLALLRAIVSN 471
Cdd:COG4586 109 wdlpaidsfrllkaiyripdAEYKKR-LDELVELLDLGELLdtpvRQLS------L---------GQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTH---DVEKaiLADRVVIMKEGRIVAGGSPEKLINSHS 543
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRErgTTILLTSHdmdDIEA--LCDRVIVIDHGRIIYDGSLEELKERFG 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
344-538 |
7.60e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIV---YYGNEARmtTVWQEPRFFRTtVKENVHF------ 414
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgdITIDTAR--SLSQQKGLIRQ-LRQHVGFvfqnfn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 ---GEEYLENQLEKNielVNVKPIIRDLSEGIETEL-HKSGVE---------FSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:PRK11264 96 lfpHRTVLENIIEGP---VIVKGEPKEEATARARELlAKVGLAgketsyprrLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 482 AGLDPSNQETVWNMIEGLGREV-TRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKAL 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
344-539 |
8.04e-23 |
|
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: 101.80 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSI-VYYGNE-ARMTtvwqEPRFF-RTTVKENVHF-GEEY- 418
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwVDMT----KPGPDgRGRAKRYIGIlHQEYd 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 -------LEN-----QLEKNIELVNVKPIIRDLSEGIETE-----LHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:TIGR03269 376 lyphrtvLDNlteaiGLELPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 482 AGLDPSNQETVWNMIEGLGREV--TRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLI 539
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
344-527 |
9.62e-23 |
|
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: 98.39 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGneaRMTTVWQEPRFFRTTVKENVHFGEEYLENQL 423
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---RISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 424 EKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW-NMIEGLGRE 502
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeSCVCKLMAN 209
|
170 180
....*....|....*....|....*
gi 446589027 503 VTRIVVTHDVEKAILADRVVIMKEG 527
Cdd:cd03291 210 KTRILVTSKMEHLKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
341-534 |
1.02e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.93 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 341 KCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVyygNEARMTTVWQEPRFFRTTVKENVHFGEEYLE 420
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---AERSIAYVPQQAWIMNATVRGNILFFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 421 NQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS-NQETVWNMIEGL 499
Cdd:PTZ00243 750 ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGA 829
|
170 180 190
....*....|....*....|....*....|....*
gi 446589027 500 GREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGS 534
Cdd:PTZ00243 830 LAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
339-536 |
1.04e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGL--YKPSNGSIVYYG--------NE-AR--MTTVWQEP---- 401
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGedilelspDErARagIFLAFQYPveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 -----RFFRTTVkeNVHFGEEY----LENQLEKNIELVNVKP--IIRDLSEGietelhksgveFSGGERKRLALLRAIVS 470
Cdd:COG0396 91 gvsvsNFLRTAL--NARRGEELsareFLKLLKEKMKELGLDEdfLDRYVNEG-----------FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 471 NPNLIILDEPTAGLDpsnqetVWNM---IEGL----GREVTRIVVTHdvEKAIL----ADRVVIMKEGRIVAGGSPE 536
Cdd:COG0396 158 EPKLAILDETDSGLD------IDALrivAEGVnklrSPDRGILIITH--YQRILdyikPDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
357-547 |
2.11e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 357 VIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------NEARMTT--VWQEP--RFFRTTVKENVHFG-------EE 417
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkeniREVRKFVglVFQNPddQIFSPTVEQDIAFGpinlgldEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 418 YLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIE 497
Cdd:PRK13652 113 TVAHRVSSALHML-----------GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446589027 498 GLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:PRK13652 182 DLPETygMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
344-538 |
2.13e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.64 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT--------VWQEPRFF-RTTVKENVHF 414
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqrdicmVFQSYALFpHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 G-------EEYLENQLEKNIELVnvkpiirDLsEGIETELHKsgvEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDP- 486
Cdd:PRK11432 102 GlkmlgvpKEERKQRVKEALELV-------DL-AGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDAn 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 487 ---SNQETVWNMIEGLGreVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK11432 171 lrrSMREKIRELQQQFN--ITSLYVTHDQSEAFaVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
328-511 |
2.49e-22 |
|
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: 92.90 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvyygnearmttvwqeprffrtT 407
Cdd:cd03221 2 ELENLSK--TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------T 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGeeYLEnQLeknielvnvkpiirdlsegietelhksgvefSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:cd03221 59 WGSTVKIG--YFE-QL-------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180
....*....|....*....|....
gi 446589027 488 NQETVWNMIEGLGREVtrIVVTHD 511
Cdd:cd03221 105 SIEALEEALKEYPGTV--ILVSHD 126
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
331-530 |
3.20e-22 |
|
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: 94.54 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCR--IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGL--YKPSNGSIVYYGNEARMTT-------VWQ 399
Cdd:cd03213 10 TVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSfrkiigyVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 400 EPRFFRT-TVKENVHFGEEylenqleknielvnvkpiIRDLSegietelhksgvefsGGERKRLALLRAIVSNPNLIILD 478
Cdd:cd03213 90 DDILHPTlTVRETLMFAAK------------------LRGLS---------------GGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 479 EPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI--LADRVVIMKEGRIV 530
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
331-549 |
4.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCR-IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSiVYYGN---------------EARM 394
Cdd:PRK13643 8 NYTYQPNSPFASRaLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK-VTVGDivvsstskqkeikpvRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 TTVWQEP--RFFRTTVKENVHFG-------EEYLENQLEKNIELVnvkpiirdlseGIETEL-HKSGVEFSGGERKRLAL 464
Cdd:PRK13643 87 GVVFQFPesQLFEETVLKDVAFGpqnfgipKEKAEKIAAEKLEMV-----------GLADEFwEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 465 LRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEK-AILADRVVIMKEGRIVAGGSPEKLINSH 542
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
....*..
gi 446589027 543 SFLQRYE 549
Cdd:PRK13643 236 DFLKAHE 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
344-540 |
4.94e-22 |
|
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: 100.86 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN--EARMTTVWQE----PR----FFRTTVKENVH 413
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdiETNLDAVRQSlgmcPQhnilFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 F-----GEEYLENQLEknielvnVKPIIRDlsEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSN 488
Cdd:TIGR01257 1026 FyaqlkGRSWEEAQLE-------MEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446589027 489 QETVWNMIEGLGREVTRIVVTHDVEKA-ILADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
325-533 |
5.23e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEP--R 402
Cdd:COG4161 1 MSIQLKNINC--FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 403 FFRTTVkeNVHFgEEY--------LENQLEKNIELVN-VKPIIRDLSEGIETELH---KSGV---EFSGGERKRLALLRA 467
Cdd:COG4161 79 LLRQKV--GMVF-QQYnlwphltvMENLIEAPCKVLGlSKEQAREKAMKLLARLRltdKADRfplHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGR-EVTRIVVTHDVEKA-ILADRVVIMKEGRIVAGG 533
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQG 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
346-544 |
8.74e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------------NEARMTTVWQEPRFF-RTTVKE 410
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppEKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFG-EEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD-PSN 488
Cdd:PRK11144 96 NLRYGmAKSMVAQFDKIVALL-----------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 489 QEtVWNMIEGLGREV-TRIV-VTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSF 544
Cdd:PRK11144 165 RE-LLPYLERLAREInIPILyVSHSLDEILrLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-530 |
1.51e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMT--GLYKPS---NGSIVYYGNE---ARMTTV---------WQEP 401
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNiysPRTDTVdlrkeigmvFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RFFRTTVKENVHFG--------EEYLENQLEKNIELVNVKPIIRDlsegietELHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:PRK14239 96 NPFPMSIYENVVYGlrlkgikdKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAI-LADRVVIMKEGRIV 530
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASrISDRTGFFLDGDLI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
344-535 |
1.77e-21 |
|
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: 92.48 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQEPRFFRTTVKENVH 413
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistipledlrSSLTIIPQDPTLFSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLENQLEKNIELvnvkpiirdlSEGietelhksGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:cd03369 104 PFDEYSDEEIYGALRV----------SEG--------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446589027 494 NMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSP 535
Cdd:cd03369 166 KTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
260-540 |
2.12e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.86 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 260 GAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRVFSFLDKR-----GADSKVERAMGMTITNVSF 334
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEApvvkdGSEPVPEGRGELDVNIRQF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 335 QESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN----------EARMTTVWQEPRFF 404
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqldswRSRLAVVSQTPFLF 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKENVHFGE-EYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:PRK10789 402 SDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 484 LDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
328-534 |
3.49e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 94.76 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-----------AR- 393
Cdd:COG1135 3 ELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltalserelraARr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 -MTTVWQEPRFFRT-TVKENVHF-------GEEYLENQLEKNIELVnvkpiirdlseGIETELHKSGVEFSGGERKRLAL 464
Cdd:COG1135 83 kIGMIFQHFNLLSSrTVAENVALpleiagvPKAEIRKRVAELLELV-----------GLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 465 LRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTH--DVEKAIlADRVVIMKEGRIVAGGS 534
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElgLTIVLITHemDVVRRI-CDRVAVLENGRIVEQGP 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
339-510 |
5.31e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARmttvwqEPRFFRT------------ 406
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------DPDVAEAchylghrnamkp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 --TVKENVHFGEEYL---ENQLEKNIELVNVKPIirdlsegieteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:PRK13539 87 alTVAENLEFWAAFLggeELDIAAALEAVGLAPL-----------AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 446589027 482 AGLDPSNQETVWNMIEG-LGREVTRIVVTH 510
Cdd:PRK13539 156 AALDAAAVALFAELIRAhLAQGGIVIAATH 185
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
339-532 |
5.89e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.47 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-ARMTTvwQEPRFFRTTVkeNVHFGEE 417
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDiTRLKN--REVPFLRRQI--GMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 418 YL--ENQLEKNIELvnvkPII------RDLSEGIETELHKSG---------VEFSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:PRK10908 89 HLlmDRTVYDNVAI----PLIiagasgDDIRRRVSAALDKVGlldkaknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 481 TAGLDPSNQETVWNMIEGLGR-EVTRIVVTHDVekAILADR---VVIMKEGRIVAG 532
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRvGVTVLMATHDI--GLISRRsyrMLTLSDGHLHGG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-541 |
5.93e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.41 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQeSDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSN-----GSIVYYG----------NEAR 393
Cdd:PRK14258 10 VNNLSFY-YDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNqniyerrvnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 --MTTVWQEPRFFRTTVKENVHFGEEYLENQLEKNIELVnVKPIIR--DLSEGIETELHKSGVEFSGGERKRLALLRAIV 469
Cdd:PRK14258 88 rqVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDI-VESALKdaDLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLG--REVTRIVVTHDVEKAI-LADRVVIMK--EGRI---VAGGSPEKLINS 541
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrLSDFTAFFKgnENRIgqlVEFGLTKKIFNS 246
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
344-527 |
7.63e-21 |
|
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: 97.29 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGneaRMTTVWQEPRFFRTTVKENVHFGEEYLENQL 423
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG---RISFSPQTSWIMPGTIKDNIIFGLSYDEYRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 424 EKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW-NMIEGLGRE 502
Cdd:TIGR01271 519 TSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeSCLCKLMSN 598
|
170 180
....*....|....*....|....*
gi 446589027 503 VTRIVVTHDVEKAILADRVVIMKEG 527
Cdd:TIGR01271 599 KTRILVTSKLEHLKKADKILLLHEG 623
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
327-538 |
8.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.46 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQ-ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW------- 398
Cdd:PRK13642 5 LEVENLVFKyEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlrrkig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 ---QEP--RFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKsgveFSGGERKRLALLRAIVSNPN 473
Cdd:PRK13642 85 mvfQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPAR----LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
326-538 |
9.09e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 326 GMTITNVSfqESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvyYGNEARMTTVWQEPR--- 402
Cdd:PRK11000 3 SVTLRNVT--KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL--FIGEKRMNDVPPAERgvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 403 -FFRT-------TVKENVHFGEEYL---ENQLEKNIElvNVKPIIRdlsegIETELHKSGVEFSGGERKRLALLRAIVSN 471
Cdd:PRK11000 79 mVFQSyalyphlSVAENMSFGLKLAgakKEEINQRVN--QVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 472 PNLIILDEPTAGLDPSNQetVWNMIE------GLGRevTRIVVTHD-VEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALR--VQMRIEisrlhkRLGR--TMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
328-548 |
9.56e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVSFQESDgeKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGneaRMTTVWQEPRFFR-- 405
Cdd:PRK10575 13 ALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA---QPLESWSSKAFARkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 ------------TTVKENV------------HFGEEYLEnQLEKNIELVNVKPIIRDLSEGIetelhksgvefSGGERKR 461
Cdd:PRK10575 88 aylpqqlpaaegMTVRELVaigrypwhgalgRFGAADRE-KVEEAISLVGLKPLAHRLVDSL-----------SGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAEL 235
|
250
....*....|
gi 446589027 539 INSHSFLQRY 548
Cdd:PRK10575 236 MRGETLEQIY 245
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-308 |
1.10e-20 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 92.49 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRELK-------AAYVYIALFAGsrLLMWVNNLSFDYVSSKASQRIlrKK 90
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRellwllaLLILGVALLRG--VFRYLQGYLAEKASQKVAYDL--RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 91 RIYvlRHFFLLPFEESEKIKQGELETLVVSDIpNWVRLY-GSILIEYIHAIAQFIGAFIALQHIDMKF---ILWVTPFLF 166
Cdd:cd18542 77 DLY--DHLQRLSFSFHDKARTGDLMSRCTSDV-DTIRRFlAFGLVELVRAVLLFIGALIIMFSINWKLtliSLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 167 FSAMVpmlMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGT 246
Cdd:cd18542 154 LFSYV---FFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 247 VIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-538 |
1.13e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQ-----EPR--FFRTTVKEN-VHFG 415
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpEERglYPKMKVGEQlVYLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 eeylenQLeKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:COG4152 97 ------RL-KGLSKAEAKRRADEWLErlGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446589027 494 NMIEGLGRE-VTRIVVTHD---VEKaiLADRVVIMKEGRIVAGGSPEKL 538
Cdd:COG4152 170 DVIRELAAKgTTVIFSSHQmelVEE--LCDRIVIINKGRKVLSGSVDEI 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
339-538 |
2.37e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLL-----KLMTGLYKpsNGSIVYYGN--EARMTT-----VWQEPRFFRT 406
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMpiDAKEMRaisayVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 -TVKENVHFGEEY-LENQLEKNIELVNVKPIIRDLSEG------IETELHKSGVefSGGERKRLALLRAIVSNPNLIILD 478
Cdd:TIGR00955 114 lTVREHLMFQAHLrMPRRVTKKEKRERVDEVLQALGLRkcantrIGVPGRVKGL--SGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 479 EPTAGLDPSNQETVWNMIEGL---GRevTRIVVTHDVEKAI--LADRVVIMKEGRIVAGGSPEKL 538
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLaqkGK--TIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
344-546 |
2.83e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSI----VYYGNEA----------------------RMTTV 397
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKnnhelitnpyskkiknfkelrrRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRF--FRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSegiETELHKSGVEFSGGERKRLALLRAIVSNPNLI 475
Cdd:PRK13631 122 FQFPEYqlFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD---DSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 476 ILDEPTAGLDPSNQETVWNMI-EGLGREVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQ 546
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLeVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
339-541 |
4.39e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.03 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMT-------TVW--QEPRFFRTTVK 409
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlKVAdkNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENV-HFG----EEYLENQLEKNIELVNV-KPIIRDLSE------GI-ETELHKSGVEFSGGERKRLALLRAIVSNPNLII 476
Cdd:PRK10619 96 MVFqHFNlwshMTVLENVMEAPIQVLGLsKQEARERAVkylakvGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
327-529 |
5.74e-20 |
|
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: 87.21 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGeKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEaRMTTVWQEPRFFRT 406
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-DLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 TVKEnvhfgeeylenQLeknielvnvkpiirdlsegieteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDP 486
Cdd:cd03223 79 TLRE-----------QL-----------------------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446589027 487 SNQETVWNMIEGLGreVTRIVVTHDVEKAILADRVVIM-KEGRI 529
Cdd:cd03223 125 ESEDRLYQLLKELG--ITVISVGHRPSLWKFHDRVLDLdGEGGW 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
346-548 |
5.99e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-----ARMTTVWQEPRFFR-TTVKENVHFGEEYL 419
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgAERGVVFQNEGLLPwRNVQDNVAFGLQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 420 ENQLEKNIELVNVKPIIRDLsEGIEtelHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGL 499
Cdd:PRK11248 99 GVEKMQRLEIAHQMLKKVGL-EGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 500 GREVTRIV--VTHDVEKAI-LADRVVIMK--EGRIVaggspEKLinSHSFLQRY 548
Cdd:PRK11248 175 WQETGKQVllITHDIEEAVfMATELVLLSpgPGRVV-----ERL--PLNFARRF 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-529 |
8.81e-20 |
|
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: 87.10 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARmttvwqeprffRTTVKENVHFGEEYL-EN 421
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT-----------RRSPRDAIRAGIAYVpED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 422 QLEKNieLVNVKPIIRDLSegietelhkSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGR 501
Cdd:cd03215 84 RKREG--LVLDLSVAENIA---------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|
gi 446589027 502 E-VTRIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:cd03215 153 AgKAVLLISSELDELLgLCDRILVMYEGRI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
325-533 |
9.47e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.53 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 325 MGMTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEP--R 402
Cdd:PRK11124 1 MSIQLNGINC--FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 403 FFRTTVkeNVHFgEEY--------LENQLEKNIELVNV-KPIIRDLSEGIETELHKSG------VEFSGGERKRLALLRA 467
Cdd:PRK11124 79 ELRRNV--GMVF-QQYnlwphltvQQNLIEAPCRVLGLsKDQALARAEKLLERLRLKPyadrfpLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGL-GREVTRIVVTHDVEKA-ILADRVVIMKEGRIVAGG 533
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELaETGITQVIVTHEVEVArKTASRVVYMENGHIVEQG 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
344-535 |
1.02e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.67 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvYYGNEaRMTTVwqEPR------FFRT-------TVKE 410
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGR-VVNEL--EPAdrdiamVFQNyalyphmSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFGeeyLEN------QLEKNIElvNVKPIIrdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:PRK11650 96 NMAYG---LKIrgmpkaEIEERVA--EAARIL-----ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 485 DPS--NQetvwnM---IEGLGRE--VTRIVVTHD-VEKAILADRVVIMKEGRIVAGGSP 535
Cdd:PRK11650 166 DAKlrVQ-----MrleIQRLHRRlkTTSLYVTHDqVEAMTLADRVVVMNGGVAEQIGTP 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
344-515 |
1.03e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYK--PS---NGSIVYYGNE------------ARMTTVWQEPRFFRT 406
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNlyapdvdpvevrRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 TVKENVHFGEEYleNQLEKNI-ELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:PRK14243 106 SIYDNIAYGARI--NGYKGDMdELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190
....*....|....*....|....*....|
gi 446589027 486 PSNQETVWNMIEGLGREVTRIVVTHDVEKA 515
Cdd:PRK14243 184 PISTLRIEELMHELKEQYTIIIVTHNMQQA 213
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
346-544 |
1.20e-19 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 88.47 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTG--LYKPSNGSIVYYG--------NE-AR--MTTVWQEP---------RF 403
Cdd:TIGR01978 18 GVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGqdllelepDErARagLFLAFQYPeeipgvsnlEF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 404 FRTTVkeNVHFGEEYLE--------NQLEKNIELVNVKP--IIRDLSEGietelhksgveFSGGERKRLALLRAIVSNPN 473
Cdd:TIGR01978 98 LRSAL--NARRSARGEEpldlldfeKLLKEKLALLDMDEefLNRSVNEG-----------FSGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLgREVTR--IVVTHDVE--KAILADRVVIMKEGRIVAGGSPE--KLINSHSF 544
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRL-REPDRsfLIITHYQRllNYIKPDYVHVLLDGRIVKSGDVElaKELEAKGY 240
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
331-529 |
1.33e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.96 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDgEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTvWQEPRFFRTTVKE 410
Cdd:PRK10522 327 NVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ-PEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFGEEYLENQ-LEKNIELVNVKPIIRDLSEGIETELHK-SGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSN 488
Cdd:PRK10522 405 DFHLFDQLLGPEgKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446589027 489 QETVWNMIEGLGREV--TRIVVTHDVEKAILADRVVIMKEGRI 529
Cdd:PRK10522 485 RREFYQVLLPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
339-524 |
1.47e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.15 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKP---SNGSIvyYGNEARMTTVWQEPR-----------FF 404
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV--LLNGRRLTALPAEQRrigilfqddllFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKENVHFGeeyLENQLEKNielvNVKPIIRD-LSE-GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:COG4136 90 HLSVGENLAFA---LPPTIGRA----QRRARVEQaLEEaGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 483 GLDPS--NQ--ETVWNMIEGLGREVtrIVVTHDVEKAILADRVVIM 524
Cdd:COG4136 163 KLDAAlrAQfrEFVFEQIRQRGIPA--LLVTHDEEDAPAAGRVLDL 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
344-530 |
1.52e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.59 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG------NEARMTT-------VWQE------PRFf 404
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklNRAQRKAfrrdiqmVFQDsisavnPRK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 rtTVKENVHFGEEYLENqLEKNIELVNVKPIIR--DLSEGIeteLHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:PRK10419 107 --TVREIIREPLRHLLS-LDKAERLARASEMLRavDLDDSV---LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446589027 483 GLDPSNQETVWNMIEGLGRE--VTRIVVTHD---VEKaiLADRVVIMKEGRIV 530
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQfgTACLFITHDlrlVER--FCQRVMVMDNGQIV 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-541 |
1.90e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 324 AMGMTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA----------R 393
Cdd:PRK09536 1 MPMIDVSDLSV--EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraasrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 MTTVWQEPRF-FRTTVKENVHFGeeylenqleKNIELVNVKPIIRDLSEGIETELHKSGV---------EFSGGERKRLA 463
Cdd:PRK09536 79 VASVPQDTSLsFEFDVRQVVEMG---------RTPHRSRFDTWTETDRAAVERAMERTGVaqfadrpvtSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 464 LLRAIVSNPNLIILDEPTAGLDPSNQ----ETVWNMIEGlGRevTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQvrtlELVRRLVDD-GK--TAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADV 226
|
...
gi 446589027 539 INS 541
Cdd:PRK09536 227 LTA 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
344-540 |
2.29e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.35 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR----------MTTVWQEPRFFRTTVKENVH 413
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgltdlrrvLSIIPQSPVLFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:PLN03232 1332 PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 494 NMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PLN03232 1412 RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-548 |
2.94e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTT----LLKLMtglykPSNGSIVYYGN-------------EARMTTVWQEP 401
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQplhnlnrrqllpvRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RFF---RTTVKE------NVH---FGEEYLENQLEKNIELVNVKPIIRdlsegietelHKSGVEFSGGERKRLALLRAIV 469
Cdd:PRK15134 372 NSSlnpRLNVLQiieeglRVHqptLSAAQREQQVIAVMEEVGLDPETR----------HRYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGL--GREVTRIVVTHD--VEKAiLADRVVIMKEGRIVAGGSPEKLINSHSfl 545
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLqqKHQLAYLFISHDlhVVRA-LCHQVIVLRQGEVVEQGDCERVFAAPQ-- 518
|
...
gi 446589027 546 QRY 548
Cdd:PRK15134 519 QEY 521
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-308 |
3.10e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 88.34 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 16 LLVIAAVCSgcfaAILNLSRPLFMGLIVDNLI-----QRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKK 90
Cdd:cd18563 3 LGFLLMLLG----TALGLVPPYLTKILIDDVLiqlgpGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 91 RIYVLRHFFLLPFEESEKIKQGELETLVVSDIpnwVRLYG---SILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPF 164
Cdd:cd18563 79 RRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDT---DRLQDflsDGLPDFLTNILMIIGIGVVLFSLNWKlalLVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 165 LFFSAMvpmLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIG-V 243
Cdd:cd18563 156 VVWGSY---FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFpL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 244 VGTVIETGAYIVvLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18563 233 LTFLTSLGTLIV-WYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
327-541 |
3.70e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.06 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQEsdGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA----------RMTT 396
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsrelakRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRF-FRTTVKENVHFG-----------------EEYLEnQLEknielvnvkpiIRDLSEGIETELhksgvefSGGE 458
Cdd:COG4604 80 LRQENHInSRLTVRELVAFGrfpyskgrltaedreiiDEAIA-YLD-----------LEDLADRYLDEL-------SGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 459 RKR--LALlrAIVSNPNLIILDEPTAGLDP--SNQ--ETVWNMIEGLGREVtrIVVTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:COG4604 141 RQRafIAM--VLAQDTDYVLLDEPLNNLDMkhSVQmmKLLRRLADELGKTV--VIVLHDINFAScYADHIVAMKDGRVVA 216
|
250
....*....|
gi 446589027 532 GGSPEKLINS 541
Cdd:COG4604 217 QGTPEEIITP 226
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
17-308 |
4.12e-19 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 87.87 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 17 LVIAAVCSgCFAAILNLSRPLFMGLIVDNLIQRELKAAYVY--IALFAGSRLLMWVNNlsfdYVSSKASQRILRKKRIYV 94
Cdd:cd18551 1 LILALLLS-LLGTAASLAQPLLVKNLIDALSAGGSSGGLLAllVALFLLQAVLSALSS----YLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 95 LRHFFLLPFEESEKIKQGELETLVVSDIpNWVR-LYGSILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPFLFFsAM 170
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDT-TLLReLITSGLPQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAFL-II 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 171 VPMlmGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIET 250
Cdd:cd18551 154 LPL--GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 251 GAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
344-543 |
4.18e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.72 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW----------QEPRFFRTTVKENVH 413
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlrkvlgiipQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:PLN03130 1335 PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 494 NMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI-NSHS 543
Cdd:PLN03130 1415 KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGS 1465
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
328-534 |
5.26e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.32 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 328 TITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarMTTV-WQEPRFF 404
Cdd:PRK11153 3 ELKNISkvFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD--LTALsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 R---------------TTVKENVHFGEEyLENQLEKNI--------ELVnvkpiirdlseGIETELHKSGVEFSGGERKR 461
Cdd:PRK11153 81 RrqigmifqhfnllssRTVFDNVALPLE-LAGTPKAEIkarvtellELV-----------GLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTH--DVEKAIlADRVVIMKEGRIVAGGS 534
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElgLTIVLITHemDVVKRI-CDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
19-308 |
6.24e-19 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 87.47 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 19 IAAVCSGCFAAILNLSRPLFMGLIVDNLIQREL--KAAYVYIALFAGSRLLMWVnnlsFDYVSSK----ASQRI---LRK 89
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLtaSQLLRYALLILLLALLIGI----FRFLWRYlifgASRRIeydLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 90 KriyVLRHFFLLPFEESEKIKQGELETLVVSDIpNWVRLY-GSILIEYIHAIAQFIGAFIALQHIDMKFILW-VTPFLFF 167
Cdd:cd18541 78 D---LFAHLLTLSPSFYQKNRTGDLMARATNDL-NAVRMAlGPGILYLVDALFLGVLVLVMMFTISPKLTLIaLLPLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 168 SAMVpMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTV 247
Cdd:cd18541 154 ALLV-YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 248 IETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18541 233 LIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-541 |
1.03e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.17 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 336 ESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG--------------NEARMTTVWQEP 401
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RFF-RTTVKENVHFGEEYL----ENQLEKNIELVNvkpiirdlSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLII 476
Cdd:PRK10070 116 ALMpHMTVLDNTAFGMELAginaEERREKALDALR--------QVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGREVTRIVV--THDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVfiSHDLDEAMrIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
327-539 |
1.14e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPRFFR- 405
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 ----------TTVKENVHFGEE-YLE--NQL-EKNIELVNV---KPIIRDLSEGIETELhksgvefSGGERKRLALLRAI 468
Cdd:PRK11231 81 lpqhhltpegITVRELVAYGRSpWLSlwGRLsAEDNARVNQameQTRINHLADRRLTDL-------SGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 469 VSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLI 539
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
347-538 |
2.58e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.30 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR-MTTV-WQEPRffrttvkenvhfgeeylenqle 424
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgMKDDeWRAVR---------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 425 KNIELV------------NVKPIIrdlSEGIET---ELHKSGV-----------------------EFSGGERKRLALLR 466
Cdd:PRK15079 98 SDIQMIfqdplaslnprmTIGEII---AEPLRTyhpKLSRQEVkdrvkammlkvgllpnlinryphEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 467 AIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHD--VEKAIlADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDlaVVKHI-SDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-308 |
2.99e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 85.28 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRELKAAYVY--IALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVL 95
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLglALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 96 RHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVT---PFLFFSAMvp 172
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLipiPFLALGAW-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 173 mLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVK--KTM-MQHciGVVGTVIE 249
Cdd:cd18778 159 -LYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRamKLWaIFH--PLMEFLTS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 250 TGaYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18778 236 LG-TVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-548 |
3.78e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 359 IVGESGAGKTTLLKLMTGLYKPSNG------------SIVYYGN----EARMTTVWQEPRFFRTTVKENVHFGEEYLENQ 422
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrSIFNYRDvlefRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 423 LEKNIELVNVKPIIR-DLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGR 501
Cdd:PRK14271 132 PRKEFRGVAQARLTEvGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446589027 502 EVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS--HSFLQRY 548
Cdd:PRK14271 212 RLTVIIVTHNLAQAArISDRAALFFDGRLVEEGPTEQLFSSpkHAETARY 261
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-508 |
3.96e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.55 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 9 LPLQKEKLLVIAAVCsgcfAAILNLSRPLFM---GLIVDNLIQRE----LKAAYVYIALFagSRLLMWVNNLSFDYVSSK 81
Cdd:PTZ00265 54 LPASHRKLLGVSFVC----ATISGGTLPFFVsvfGVIMKNMNLGEnvndIIFSLVLIGIF--QFILSFISSFCMDVVTTK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 82 asqrILRKKRIYVLRHFFLlpfeESEKIKQGELETLVVSDIPNWVRLY----GSILIEYIHAIAQFIGAFIALQHIDMKF 157
Cdd:PTZ00265 128 ----ILKTLKLEFLKSVFY----QDGQFHDNNPGSKLTSDLDFYLEQVnagiGTKFITIFTYASAFLGLYIWSLFKNARL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 158 ILWVT---PFLFFSAMVPMLMGKKVRNIASIAQNNQSSVVEmvsQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKK 234
Cdd:PTZ00265 200 TLCITcvfPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE---EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 235 TMMQHC-IGVV-GTVIETGA----YIVVLIIG--AQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASAN 306
Cdd:PTZ00265 277 NFMESLhIGMInGFILASYAfgfwYGTRIIISdlSNQQPNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 307 RVFSFLDKR------GADSKVERAMGMTITNVSFQESDGEKCRIH-NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYK 379
Cdd:PTZ00265 357 SLYEIINRKplvennDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 380 PSNGSIVYYGNE-----------ARMTTVWQEPRFFRTTVKENVHFGE------EYLENQLEKNI--------------- 427
Cdd:PTZ00265 437 PTEGDIIINDSHnlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlEALSNYYNEDGndsqenknkrnscra 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 428 -------------------------------ELVNV--KPIIRD----LSEGIETELHKSGVEFSGGERKRLALLRAIVS 470
Cdd:PTZ00265 517 kcagdlndmsnttdsneliemrknyqtikdsEVVDVskKVLIHDfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
|
570 580 590
....*....|....*....|....*....|....*...
gi 446589027 471 NPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVV 508
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
344-536 |
4.37e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 83.92 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTG--LYKPSNGSIVYYGN-------EAR----MTTVWQEP--------- 401
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGEsildlepEERahlgIFLAFQYPieipgvsna 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RFFRTTVKENVHFGE-------EYLENQLEKnIELVNVKPII--RDLSEGietelhksgveFSGGERKRLALLRAIVSNP 472
Cdd:CHL00131 103 DFLRLAYNSKRKFQGlpeldplEFLEIINEK-LKLVGMDPSFlsRNVNEG-----------FSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 473 NLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIV-VTH--DVEKAILADRVVIMKEGRIVAGGSPE 536
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
327-535 |
5.46e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPgeLVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN------------EARM 394
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllalRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 TTVWQEP--RFFRTTVKENVHF-------GEEYLENQLEKNIELVNVKPIirdlsegieteLHKSGVEFSGGERKRLALL 465
Cdd:PRK13638 80 ATVFQDPeqQIFYTDIDSDIAFslrnlgvPEAEITRRVDEALTLVDAQHF-----------RHQPIQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 466 RAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVV-THDVEKAI-LADRVVIMKEGRIVAGGSP 535
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYeISDAVYVLRQGQILTHGAP 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
346-510 |
5.90e-18 |
|
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: 82.41 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-ARMTTVWQEPRFF---------RTTVKENVHFG 415
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlAEQRDEPHENILYlghlpglkpELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 EEYL---ENQLEKNIELVNvkpiIRDLSEGIETELhksgvefSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETV 492
Cdd:TIGR01189 98 AAIHggaQRTIEDALAAVG----LTGFEDLPAAQL-------SAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 446589027 493 WNMIEG-LGREVTRIVVTH 510
Cdd:TIGR01189 167 AGLLRAhLARGGIVLLTTH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
344-548 |
8.61e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVW-----------QEPRFFRT-TVKEN 411
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHararrgigylpQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 VHFGEEYLENQLEKNIElvnvkpiirDLSEGIETELHKS------GVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:PRK10895 99 LMAVLQIRDDLSAEQRE---------DRANELMEEFHIEhlrdsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 486 PSNQETVWNMIEGLGREVTRIVVT-HDVEKAI-LADRVVIMKEGRIVAGGSPEKLINSHSFLQRY 548
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITdHNVRETLaVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
327-536 |
1.71e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSfqesdgEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkPSNGSIVYYGNE---------AR---M 394
Cdd:COG4138 1 LQLNDVA------VAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaelARhraY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 TTVWQEPRFFRTtvkenVHfgeEYLENQLEKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGE--RKRLAllrAIV- 469
Cdd:COG4138 74 LSQQQSPPFAMP-----VF---QYLALHQPAGASSEAVEQLLAQLAEalGLEDKLSRPLTQLSGGEwqRVRLA---AVLl 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 470 -----SNPN--LIILDEPTAGLDPSNQETVWNMIEGL---GREVtrIVVTHDVEKAIL-ADRVVIMKEGRIVAGGSPE 536
Cdd:COG4138 143 qvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELcqqGITV--VMSSHDLNHTLRhADRVWLLKQGKLVASGETA 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
344-540 |
2.10e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLY---KPSNGSIVYYGNearmtTVWQEPRFFRTTVKENVHFGEEY-- 418
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGR-----TVQREGRLARDIRKSRANTGYIFqq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 ---------LENQLeknIELVNVKPIIRDLSE-----------------GIETELHKSGVEFSGGERKRLALLRAIVSNP 472
Cdd:PRK09984 95 fnlvnrlsvLENVL---IGALGSTPFWRTCFSwftreqkqralqaltrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 473 NLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALrYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
347-541 |
2.46e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.77 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTV---------WQEPRFFRT----------- 406
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpadRRQLQRIRTrlgmvfqsfnl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 ----TVKENVhfgeeylenqleknIEL-VNVKPIIRDlsEGIETE---LHKSGV---------EFSGGERKRLALLRAIV 469
Cdd:COG4598 107 wshmTVLENV--------------IEApVHVLGRPKA--EAIERAealLAKVGLadkrdaypaHLSGGQQQRAAIARALA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 470 SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:COG4598 171 MEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEgRTMLVVTHEMGFARdVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
327-539 |
3.30e-17 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 81.49 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTT 396
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplhtlrSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLII 476
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
27-308 |
3.34e-17 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 82.05 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 27 FAAILNLSRPLFMGLIVDNLI---QRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVLRHFFLLPF 103
Cdd:cd18544 10 LATALELLGPLLIKRAIDDYIvpgQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 104 EESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVTPFLFFSAMVPMLMGKKVRNIA 183
Cdd:cd18544 90 SFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 184 SIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTaQSYKTEVKKTMMQHciGVVGTVIE---TGAYIVVLIIG 260
Cdd:cd18544 170 REVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEIN-QEYRKANLKSIKLF--ALFRPLVEllsSLALALVLWYG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446589027 261 AQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18544 247 GGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-533 |
3.73e-17 |
|
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: 80.78 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 334 FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGL---YKPSNGSIVYYGNEARMTTVWQEPRFFRT---- 406
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKCVAYVRQddil 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 ----TVKENVHF------GEEYLENQLEKNIE-----LVNVKPIIRDLSEGIetelhksgvefSGGERKRLALLRAIVSN 471
Cdd:cd03234 93 lpglTVRETLTYtailrlPRKSSDAIRKKRVEdvllrDLALTRIGGNLVKGI-----------SGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 472 PNLIILDEPTAGLDPSnqeTVWNMIEGLGREVTR----IVVTHDVEKAI--LADRVVIMKEGRIVAGG 533
Cdd:cd03234 162 PKVLILDEPTSGLDSF---TALNLVSTLSQLARRnrivILTIHQPRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-537 |
3.81e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.78 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 333 SFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPRFFRTtvkenv 412
Cdd:PRK10535 13 SYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFGEEYLENQL------EKNIELVNV---------KPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLI 475
Cdd:PRK10535 87 HFGFIFQRYHLlshltaAQNVEVPAVyaglerkqrLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGL-GREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEK 537
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
347-540 |
3.81e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.70 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEA-------------RMTTVWQEPrfF-----RTTV 408
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllrqKIQIVFQNP--YgslnpRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 kenvhfgEEYLENQLEKNIEL------VNVKPIIRDLseGIETEL-----HKsgveFSGGERKRLALLRAIVSNPNLIIL 477
Cdd:PRK11308 112 -------GQILEEPLLINTSLsaaerrEKALAMMAKV--GLRPEHydrypHM----FSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 478 DEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHD---VEKaiLADRVVIMKEGRIVAGGSPEKLIN 540
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQElgLSYVFISHDlsvVEH--IADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
347-538 |
5.68e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-ARMTT----------VWQEPRFF-RTTVKENVHF 414
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcARLTPakahqlgiylVPQEPLLFpNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 415 GEEYLENQLEKnielvnVKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWN 494
Cdd:PRK15439 110 GLPKRQASMQK------MKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 495 MIEGLGREVTRIV-VTHDV-EKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK15439 182 RIRELLAQGVGIVfISHKLpEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
18-308 |
7.15e-17 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 80.99 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLSRPLFMGLIVDNLIQ-RELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVLR 96
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAhGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 97 HFFLLPFEESEKIKQGELETLVVSDIpNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKF---ILWVTPFLFFSAMvpm 173
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDL-SLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLalvALASLPPLVLVAR--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 174 LMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQhciGVVGTVIET--- 250
Cdd:cd18543 157 RFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLR---ARFWPLLEAlpe 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 251 GAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
347-529 |
1.38e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.05 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarMTTVWQEPRF-FRTtvkENVHFGEEYLE----- 420
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP--LHQMDEEARAkLRA---KHVGFVFQSFMliptl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 421 NQLEkNIELvnvKPIIRDLSE--------------GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDP 486
Cdd:PRK10584 104 NALE-NVEL---PALLRGESSrqsrngakalleqlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446589027 487 SNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRI 529
Cdd:PRK10584 180 QTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
346-523 |
1.52e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYK--PSNGSIvyygnearmttvwqeprffrttvkenvhfgeEYLENQL 423
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV-------------------------------DVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 424 EKNIELVNVKPIIRDLSEGIETeLHKSGV-----------EFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETV 492
Cdd:COG2401 97 GREASLIDAIGRKGDFKDAVEL-LNAVGLsdavlwlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190
....*....|....*....|....*....|....*
gi 446589027 493 WNMIEGLGRE--VTRIVVTH--DVEKAILADRVVI 523
Cdd:COG2401 176 ARNLQKLARRagITLVVATHhyDVIDDLQPDLLIF 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
339-529 |
1.86e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.59 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarmttvWqeprffrtTVKENVHFGEEY 418
Cdd:TIGR03740 11 GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP------W--------TRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 LENQLEKNI---ELVNVKPIIRDLSEG-IETELHKSGVE---------FSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:TIGR03740 77 ESPPLYENLtarENLKVHTTLLGLPDSrIDEVLNIVDLTntgkkkakqFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 486 PSNQETVWNMIEGLGRE-VTRIVVTHDV-EKAILADRVVIMKEGRI 529
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQgITVILSSHILsEVQQLADHIGIISEGVL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
327-547 |
2.22e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVS--FQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKT-TLLKLMTGLYKPS----NGSIVYYGNEA------- 392
Cdd:PRK15134 6 LAIENLSvaFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaseqt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 -------RMTTVWQEPrffrtTVKEN-VHfgeeYLENQLEKNIEL-------VNVKPIIRDLSE-GIE---TELHKSGVE 453
Cdd:PRK15134 86 lrgvrgnKIAMIFQEP-----MVSLNpLH----TLEKQLYEVLSLhrgmrreAARGEILNCLDRvGIRqaaKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 454 FSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTR--IVVTHD---VEKaiLADRVVIMKEGR 528
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNlsiVRK--LADRVAVMQNGR 234
|
250 260
....*....|....*....|.
gi 446589027 529 IVAGGSPEKLINS--HSFLQR 547
Cdd:PRK15134 235 CVEQNRAATLFSAptHPYTQK 255
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
331-533 |
2.33e-16 |
|
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: 77.69 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDG--EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGL---YKPSNGSIVYYGNEARMTT--------- 396
Cdd:cd03233 8 NISFTTGKGrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAekypgeiiy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 VWQEPRFFRT-TVKENVHFGEEYLENQleknielvnvkpIIRdlseGIetelhksgvefSGGERKRLALLRAIVSNPNLI 475
Cdd:cd03233 88 VSEEDVHFPTlTVRETLDFALRCKGNE------------FVR----GI-----------SGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 476 ILDEPTAGLDPSnqeTVWNMIEGLgREVTRIvvTHDVEKAILA----------DRVVIMKEGRIVAGG 533
Cdd:cd03233 141 CWDNSTRGLDSS---TALEILKCI-RTMADV--LKTTTFVSLYqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
346-533 |
3.46e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-----------VWQEPRFF-RTTVKENVH 413
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklaaqlgigiIYQELSVIdELTVLENLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLENQLEKNI---ELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQE 490
Cdd:PRK09700 103 IGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446589027 491 TVWNMIEGLGREVTRIV-VTHDV-EKAILADRVVIMKEGRIVAGG 533
Cdd:PRK09700 183 YLFLIMNQLRKEGTAIVyISHKLaEIRRICDRYTVMKDGSSVCSG 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
344-539 |
3.79e-16 |
|
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: 82.30 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG-NEA---------RMTTVWQEPRFFRTTVKENVH 413
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAkiglhdlrfKITIIPQDPVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVW 493
Cdd:TIGR00957 1382 PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 494 NMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:TIGR00957 1462 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
333-533 |
4.34e-16 |
|
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: 77.57 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 333 SFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvyygnEARMTTVWQ-------EPRFfr 405
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRVSSLlglgggfNPEL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 tTVKENVHFgeeyleNQLEKNI---ELVNVKPIIRDLSEgIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:cd03220 100 -TGRENIYL------NGRLLGLsrkEIDEKIDEIIEFSE-LGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 483 GLDPSNQETVWNMIEGLGRE-VTRIVVTHDvEKAI--LADRVVIMKEGRIVAGG 533
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQgKTVILVSHD-PSSIkrLCDRALVLEKGKIRFDG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-548 |
4.65e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKL---MTGLYKPS--NGSIVYYGNEA----------RMTTVWQEPRFFRT-T 407
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIfkmdvielrrRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGEEYleNQLEKN-IEL-VNVKPIIR--DLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:PRK14247 99 IFENVALGLKL--NRLVKSkKELqERVRWALEkaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 484 LDPSNQETVWNMIEGLGREVTRIVVTH-DVEKAILADRVVIMKEGRIVAGGSPEKLINS--HSFLQRY 548
Cdd:PRK14247 177 LDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNprHELTEKY 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
327-547 |
6.15e-16 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; 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: 213256 [Multi-domain] Cd Length: 275 Bit Score: 77.97 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKpSNGSIVYYGNEARMTTV--W------ 398
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLqkWrkafgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 --QEPRFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLII 476
Cdd:cd03289 82 ipQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
327-536 |
6.48e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFqeSDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGnEARMTTVWQEPRFFRT 406
Cdd:PRK09544 5 VSLENVSV--SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-KLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 ---TVKENVhfgeeylenQLEKNIELVNVKPIIRDLSEG--IETELHKsgveFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:PRK09544 82 lplTVNRFL---------RLRPGTKKEDILPALKRVQAGhlIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 482 AGLDPSNQETVWNMIEGLGREVTRIV--VTHDVEKAILADRVVIMKEGRIVAGGSPE 536
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVlmVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
331-538 |
6.64e-16 |
|
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: 80.50 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKT----TLLKLM-TGLYKPSnGSIVYYGNE-------------- 391
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLpDPAAHPS-GSILFDGQDllglserelrrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 ARMTTVWQEPRffrT------TVkenvhfgeeylENQLEKNIEL------VNVKPIIRDLSE--GI---ETEL----Hks 450
Cdd:COG4172 92 NRIAMIFQEPM---TslnplhTI-----------GKQIAEVLRLhrglsgAAARARALELLErvGIpdpERRLdaypH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 451 gvEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHD---VEKaiLADRVVIMK 525
Cdd:COG4172 156 --QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElgMALLLITHDlgvVRR--FADRVAVMR 231
|
250
....*....|...
gi 446589027 526 EGRIVAGGSPEKL 538
Cdd:COG4172 232 QGEIVEQGPTAEL 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
343-531 |
7.17e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQ----------EPR-----FFRTT 407
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpEDRkgeglVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKEN--------------VHFGEEylENQLEKNIELVNVKPiiRDLSEGIETelhksgveFSGGERKRLALLRAIVSNPN 473
Cdd:COG1129 347 IRENitlasldrlsrgglLDRRRE--RALAEEYIKRLRIKT--PSPEQPVGN--------LSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLgLSDRILVMREGRIVG 474
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
351-523 |
9.20e-16 |
|
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: 77.06 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 351 IHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvyygnEARMTTVWQEPRF----FRTTVKENVH--FGEEYLENQLE 424
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTVSYKPQYikadYEGTVRDLLSsiTKDFYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 425 KNIelvnVKPIirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIE--GLGRE 502
Cdd:cd03237 97 TEI----AKPL------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfAENNE 166
|
170 180
....*....|....*....|..
gi 446589027 503 VTRIVVTHDVEKA-ILADRVVI 523
Cdd:cd03237 167 KTAFVVEHDIIMIdYLADRLIV 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
346-540 |
1.21e-15 |
|
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: 79.85 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGL--YKPSNGSIVYY-----------------------GNEARMTTV--W 398
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvgepcpvcGGTLEPEEVdfW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPRFFRTTVKENVH---------FGEE-YLENQLE--KNIELVNVKPIIR--DLSEGIETELHKSGV--EFSGGERKRL 462
Cdd:TIGR03269 98 NLSDKLRRRIRKRIAimlqrtfalYGDDtVLDNVLEalEEIGYEGKEAVGRavDLIEMVQLSHRITHIarDLSGGEKQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 463 ALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgISMVLTSHWPEvIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
.
gi 446589027 540 N 540
Cdd:TIGR03269 258 A 258
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-541 |
1.61e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.62 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 340 EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYK------PSNGSIVYYGNE----------ARMTTVWQEPRF 403
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDifqidaiklrKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 404 F-RTTVKENVHFGEEYLENQLEKNIELVnVKPIIRD--LSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:PRK14246 102 FpHLSIYDNIAYPLKSHGIKEKREIKKI-VEECLRKvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 481 TAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-308 |
1.80e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 77.17 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 17 LVIAAVCSGcFAAILNLSRPLFMGLIVDNLIQRE----------------------LKAAYVYIALFAGsrLLMWVNNls 74
Cdd:cd18564 1 LALALLALL-LETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdplallllAAAALVGIALLRG--LASYAGT-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 75 fdYVSSKASQRILRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHID 154
Cdd:cd18564 76 --YLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 155 MKFILW---VTPFLFFSAMVpmlMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTE 231
Cdd:cd18564 154 WQLALIalaVAPLLLLAARR---FSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 232 VKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18564 231 LRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-288 |
3.57e-15 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 75.76 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 16 LLVIAAVCSGCFAAILnlsrPLFMGLIVDNLIQ---RELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRI 92
Cdd:pfam00664 3 LAILLAILSGAISPAF----PLVLGRILDVLLPdgdPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 93 YVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVTPFLFFSAMVP 172
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 173 MLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGA 252
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 446589027 253 YIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPV 288
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
17-308 |
7.66e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 75.29 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 17 LVIAAVCSGCfaailNLSRPLFMGLIVDNLI-----QRELKAAYVYIALFAGSRLLmwvnNLSFDYVSSKASQRILRKKR 91
Cdd:cd18557 2 LLFLLISSAA-----QLLLPYLIGRLIDTIIkggdlDVLNELALILLAIYLLQSVF----TFVRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 92 IYVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVTPFLFFSAMV 171
Cdd:cd18557 73 RDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 172 PMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETG 251
Cdd:cd18557 153 SKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 252 AYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18557 233 SLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
17-308 |
8.76e-15 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 75.15 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 17 LVIAAVCSGcFAAILNLSRPLFMGLIVDNLIQRELKAAYVYIALFAGsrLLMWVNNLSF---DYVSSKASQRILRKKRIY 93
Cdd:cd18552 1 LALAILGMI-LVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAII--GLFLLRGLASylqTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 94 VLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPFLFFsam 170
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVLPLAAL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 171 vPM-LMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQhciGVVGTVIE 249
Cdd:cd18552 155 -PIrRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARAR---ALSSPLME 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 250 TGAYI---VVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18552 231 LLGAIaiaLVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
345-542 |
1.40e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvyygnEARMTTVWQ-------EPRFfrtTVKENVHFGEE 417
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRVSALlelgagfHPEL---TGRENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 418 YL---ENQLEKNIELvnvkpiIRDLSE-G--IETELhKSgveFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQET 491
Cdd:COG1134 115 LLglsRKEIDEKFDE------IVEFAElGdfIDQPV-KT---YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 492 VWNMIEGLGREVTRIV-VTHD---VEKaiLADRVVIMKEGRIVAGGSPEKLINSH 542
Cdd:COG1134 185 CLARIRELRESGRTVIfVSHSmgaVRR--LCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
339-541 |
1.45e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.87 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQEPRFF-----------RTT 407
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIgllaqnattpgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGEeYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVE-FSGGERKRLALLRAIVSNPNLIILDEPTAGLDP 486
Cdd:PRK10253 98 VQELVARGR-YPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 487 SNQETVWNMIEGLGRE--VTRIVVTHDVEKAI-LADRVVIMKEGRIVAGGSPEKLINS 541
Cdd:PRK10253 177 SHQIDLLELLSELNREkgYTLAAVLHDLNQACrYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
331-536 |
1.72e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKT-TLLKLMtGLYKPS---NGSIVYYGNE--------------A 392
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANgriGGSATFNGREilnlpekelnklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 393 RMTTVWQEPRffrTTVKENVHFGEEYLEN-QLEKNIE-----------LVNVKpiIRDLSEGIETELHksgvEFSGGERK 460
Cdd:PRK09473 98 QISMIFQDPM---TSLNPYMRVGEQLMEVlMLHKGMSkaeafeesvrmLDAVK--MPEARKRMKMYPH----EFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446589027 461 RLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRIVAGGSPE 536
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
351-538 |
2.44e-14 |
|
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: 76.59 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 351 IHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE--ARMTTVWQE----PRFfrtTVKENVHFGEE--YLENQ 422
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSilTNISDVHQNmgycPQF---DAIDDLLTGREhlYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 423 LE----KNIELVNVKPIirdLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEG 498
Cdd:TIGR01257 2039 LRgvpaEEIEKVANWSI---QSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446589027 499 LGREVTRIVVT-HDVEKA-ILADRVVIMKEGRIVAGGSPEKL 538
Cdd:TIGR01257 2116 IIREGRAVVLTsHSMEECeALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
17-308 |
2.62e-14 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 73.66 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 17 LVIAAVCSGcFAAILNLSRPLFMGLIVDNLI-QRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVL 95
Cdd:cd18545 2 LLLALLLML-LSTAASLAGPYLIKIAIDEYIpNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 96 RHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILW---VTPFLFFSAMVp 172
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVtlaVLPLLVLVVFL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 173 mlMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGA 252
Cdd:cd18545 160 --LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 253 YIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18545 238 TALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
339-485 |
2.93e-14 |
|
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: 71.76 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-EARMTTVWQEPRFF---------RTTV 408
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYlghapgiktTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 409 KENVHF-GEEYLENQLEKNIELVNVKpiirdlseGIEtelHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:cd03231 91 LENLRFwHADHSDEQVEEALARVGLN--------GFE---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
344-531 |
3.67e-14 |
|
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: 74.86 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPS--NGSIVYYGNE-----------ARMTTVWQEPRFFRT-TVK 409
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPlkasnirdterAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 410 ENVHFGEEYLEN--QLEKNIELVNVKPIIRDLSEGIETELHKSGvEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:TIGR02633 97 ENIFLGNEITLPggRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 488 NQETVWNMIEGLGRE-VTRIVVTHDVEK-AILADRVVIMKEGRIVA 531
Cdd:TIGR02633 176 ETEILLDIIRDLKAHgVACVYISHKLNEvKAVCDTICVIRDGQHVA 221
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
18-308 |
4.02e-14 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 73.21 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRE-----------LKAAYVYIALFAGSRLLMWVNNlsfdYVSSKASQRI 86
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvdfsglLRILLLLLGLYLLSALFSYLQN----RLMARVSQRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 87 LRKKRIYVLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVTPFLF 166
Cdd:cd18547 77 VYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 167 FSAMVPMLMGKKVRNIASIAQNNQSSVV----EMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKT----MMQ 238
Cdd:cd18547 157 LSLLVTKFIAKRSQKYFRKQQKALGELNgyieEMIS----GQKVVKAFNREEEAIEEFDEINEELYKASFKAQfysgLLM 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 239 HCIGVVGTVIetgaYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18547 233 PIMNFINNLG----YVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-547 |
4.23e-14 |
|
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: 75.72 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKpSNGSIVYYGNEARMTTV--W------ 398
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLqtWrkafgv 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 --QEPRFFRTTVKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLII 476
Cdd:TIGR01271 1297 ipQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 477 LDEPTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLINSHSFLQR 547
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-548 |
4.55e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPS-----NGSIVYYGNEA------------RMTTVWQEPRFF-R 405
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspdvdpievrrEVGMVFQYPNPFpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 406 TTVKENVHFGEEY-----LENQLEKNIELVNVKPIirdLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEP 480
Cdd:PRK14267 100 LTIYDNVAIGVKLnglvkSKKELDERVEWALKKAA---LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 481 TAGLDPSNQETVWNMIEGLGREVTRIVVTHD-VEKAILADRVVIMKEGRIVAGGSPEKLINS--HSFLQRY 548
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENpeHELTEKY 247
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
346-511 |
5.39e-14 |
|
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: 74.59 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGsivyygnEARM---TTVW---QEPRFFRT-TVKENVH----- 413
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPqpgIKVGylpQEPQLDPTkTVRENVEegvae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 --------------FGEE------YLENQ--LEKNIELVNVKPIIRDLSEGIE-----------TELhksgvefSGGERK 460
Cdd:TIGR03719 96 ikdaldrfneisakYAEPdadfdkLAAEQaeLQEIIDAADAWDLDSQLEIAMDalrcppwdadvTKL-------SGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 461 RLALLRAIVSNPNLIILDEPTAGLDpsnQETV-WnmIEGLGREV--TRIVVTHD 511
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD---AESVaW--LERHLQEYpgTVVAVTHD 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-531 |
5.60e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTV-----------WQE----PRFfrtTVKE 410
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaalaagvaiiYQElhlvPEM---TVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFGeeylenQLEKNIELVNVKPIIRDLSEgietELHKSGVEF---------SGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:PRK11288 99 NLYLG------QLPHKGGIVNRRLLNYEARE----QLEHLGVDIdpdtplkylSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 482 AGLDPSNQETVWNMIEGL---GREVtrIVVTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELraeGRVI--LYVSHRMEEIFaLCDAITVFKDGRYVA 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
339-485 |
7.23e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMttvwQEPRFFRT------------ 406
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR----QRDEYHQDllylghqpgikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 --TVKENVHF--------GEEYLENQLEKnielVNVkpiirdlsegietelhkSGVE------FSGGERKRLALLRAIVS 470
Cdd:PRK13538 88 elTALENLRFyqrlhgpgDDEALWEALAQ----VGL-----------------AGFEdvpvrqLSAGQQRRVALARLWLT 146
|
170
....*....|....*
gi 446589027 471 NPNLIILDEPTAGLD 485
Cdd:PRK13538 147 RAPLWILDEPFTAID 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
327-537 |
7.39e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSfqesdgEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkPSNGSIV--------YYGNE-ARMTT- 396
Cdd:PRK03695 1 MQLNDVA------VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQfagqpleaWSAAElARHRAy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 397 ------------VWQeprffrttvkenvhfgeeYLENQLEKNIELVNVKPIIRDLSE--GIETELHKSGVEFSGGE--RK 460
Cdd:PRK03695 74 lsqqqtppfampVFQ------------------YLTLHQPDKTRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEwqRV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 461 RLA--LL---RAIVSNPNLIILDEPTAGLDPSNQETVWNMIE---GLGREVtrIVVTHDVEKAIL-ADRVVIMKEGRIVA 531
Cdd:PRK03695 136 RLAavVLqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSelcQQGIAV--VMSSHDLNHTLRhADRVWLLKQGKLLA 213
|
....*.
gi 446589027 532 GGSPEK 537
Cdd:PRK03695 214 SGRRDE 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
347-539 |
9.76e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE----------ARMTTVWQEPRFFRTTVKENVHFGE 416
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigayglrelrRQFSMIPQDPVLFDGTVRQNVDPFL 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 417 EYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVEFSGGERKRLALLRAIVS-NPNLIILDEPTAGLDPSNQETVWNM 495
Cdd:PTZ00243 1409 EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQAT 1488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446589027 496 IEGLGREVTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:PTZ00243 1489 VMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
327-497 |
1.54e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDgeKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG-NEARMTTVWQEPRFF- 404
Cdd:PRK13540 2 LDVIELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqSIKKDLCTYQKQLCFv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 --RT------TVKENVHFGEEYLENQLEKNiELVNVKPI--IRDLSEGIetelhksgveFSGGERKRLALLRAIVSNPNL 474
Cdd:PRK13540 80 ghRSginpylTLRENCLYDIHFSPGAVGIT-ELCRLFSLehLIDYPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180
....*....|....*....|...
gi 446589027 475 IILDEPTAGLDPSNQETVWNMIE 497
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQ 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
329-531 |
3.82e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKcRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTvwqePRFFRT-- 406
Cdd:COG3845 260 VENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----PRERRRlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 -----------------TVKENV----HFGEEY----------LENQLEKNIELVNVKPiirdlsEGIETELHKsgveFS 455
Cdd:COG3845 335 vayipedrlgrglvpdmSVAENLilgrYRRPPFsrggfldrkaIRAFAEELIEEFDVRT------PGPDTPARS----LS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 456 GGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMI-----EGLGreVtrIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlelrdAGAA--V--LLISEDLDEILaLSDRIAVMYEGRI 480
|
..
gi 446589027 530 VA 531
Cdd:COG3845 481 VG 482
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
331-541 |
4.22e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 331 NVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKT-TLLKLM-----TG--------LYKPSNGSIVYYGNE----- 391
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGglvqcdkmLLRRRSRQVIELSEQsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 392 -----ARMTTVWQEPRffrTTVKENVHFGEEYLEN-----QLEKNIELVNVKPIIRDLS-EGIETELHKSGVEFSGGERK 460
Cdd:PRK10261 99 rhvrgADMAMIFQEPM---TSLNPVFTVGEQIAESirlhqGASREEAMVEAKRMLDQVRiPEAQTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 461 RLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTR--IVVTHDVE-KAILADRVVIMKEGRIVAGGSPEK 537
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGvVAEIADRVLVMYQGEAVETGSVEQ 255
|
....
gi 446589027 538 LINS 541
Cdd:PRK10261 256 IFHA 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
344-531 |
7.79e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkPS---NGSIVYYGNEARMTTV-----------WQEPRFFRT-TV 408
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrdteragiaiiHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFGEEYLEN-QLEKNIELVNVKPIIRDLSEGIETELHKSgvEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPS 487
Cdd:PRK13549 100 LENIFLGNEITPGgIMDYDAMYLRAQKLLAQLKLDINPATPVG--NLGLGQQQLVEIAKALNKQARLLILDEPTASLTES 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 488 NQETVWNMIEGLGRE-VTRIVVTHDVE--KAIlADRVVIMKEGRIVA 531
Cdd:PRK13549 178 ETAVLLDIIRDLKAHgIACIYISHKLNevKAI-SDTICVIRDGRHIG 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
340-533 |
7.85e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.28 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 340 EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGL--YKPSNGSIVYYGN-------EAR----MTTVWQEP----- 401
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllelspEDRagegIFMAFQYPveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 ---RFFRTTVKENV--HFGEEYL-----ENQLEKNIELVNVKPiirDLsegieteLHKS-GVEFSGGERKRLALLRAIVS 470
Cdd:PRK09580 93 vsnQFFLQTALNAVrsYRGQEPLdrfdfQDLMEEKIALLKMPE---DL-------LTRSvNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 471 NPNLIILDEPTAGLDPSNQETVWNMIEGLgREVTR--IVVTH--DVEKAILADRVVIMKEGRIVAGG 533
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSL-RDGKRsfIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
16-308 |
1.07e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 68.67 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 16 LLVIAAVCsgcFAAILNLSRPLFMGLIVDN-LIQRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYV 94
Cdd:cd18546 2 ALALLLVV---VDTAASLAGPLLVRYGIDSgVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 95 LRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKFILWVtpflfFSAMVPML 174
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVA-----LAALPPLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 175 MGKKV-RNIASIAQNNQ-SSVVEMVSQFVKGVQDLRSLQ---KEKWAIRLFKGVTAQSYKTEVKKtmmQHCIGVVGTVIE 249
Cdd:cd18546 154 LATRWfRRRSSRAYRRArERIAAVNADLQETLAGIRVVQafrRERRNAERFAELSDDYRDARLRA---QRLVAIYFPGVE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 250 ---TGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18546 231 llgNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
344-535 |
1.19e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPS--------NGSIVYYGNE---------ARMTTVW--QEPRFF 404
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaidaprlARLRAVLpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKENVHFGEeYLENQLEKNIELVNVKPIIRDLS-EGIETELHKSGVEFSGGERKRLALLRAI---------VSNPNL 474
Cdd:PRK13547 97 AFSAREIVLLGR-YPHARRAGALTHRDGEIAWQALAlAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 475 IILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAIL-ADRVVIMKEGRIVAGGSP 535
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAP 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
311-528 |
1.29e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 311 FLDKRGADSKVERAMGMTITNVSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSN--GSIVYY 388
Cdd:PLN03211 51 FENMKNKGSNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILAN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 389 GNE------ARMTTVWQEPRFF-RTTVKENVHFGEEY-LENQLEKNIELVNVKPIIRDL--SEGIETELHKSGVE-FSGG 457
Cdd:PLN03211 131 NRKptkqilKRTGFVTQDDILYpHLTVRETLVFCSLLrLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIRgISGG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 458 ERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVT-HDVEKAI--LADRVVIMKEGR 528
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVyqMFDSVLVLSEGR 284
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
346-485 |
1.31e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN--EARMTtvwQEP-RFFRTTVKENVHFG----EEY 418
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDliVARLQ---QDPpRNVEGTVYDFVAEGieeqAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 LE-----------NQLEKNI-ELVNVKPI------------IRDLSEGIETELHKSGVEFSGGERKRLALLRAIVSNPNL 474
Cdd:PRK11147 98 LKryhdishlvetDPSEKNLnELAKLQEQldhhnlwqlenrINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDV 177
|
170
....*....|.
gi 446589027 475 IILDEPTAGLD 485
Cdd:PRK11147 178 LLLDEPTNHLD 188
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
344-524 |
1.31e-12 |
|
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: 66.19 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKlmTGLYKpsngsivyygnEARMTTVWQEPRFFRTTVkenVHFGEeyLENQL 423
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA-----------SGKARLISFLPKFSRNKL---IFIDQ--LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 424 EKNIELVnvkPIIRDLSEgietelhksgveFSGGERKRLALLRAIVSNP--NLIILDEPTAGLDPSNQETVWNMIEGLGR 501
Cdd:cd03238 73 DVGLGYL---TLGQKLST------------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLID 137
|
170 180
....*....|....*....|....
gi 446589027 502 E-VTRIVVTHDVEKAILADRVVIM 524
Cdd:cd03238 138 LgNTVILIEHNLDVLSSADWIIDF 161
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
350-523 |
1.88e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 350 QIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIV----------YYGNEARMTTvwQEprFFRTTVKENvhFGEEYL 419
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqYISPDYDGTV--EE--FLRSANTDD--FGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 420 ENQleknielvnvkpIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGL 499
Cdd:COG1245 436 KTE------------IIKPL--GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*..
gi 446589027 500 --GREVTRIVVTHDVE-KAILADRVVI 523
Cdd:COG1245 502 aeNRGKTAMVVDHDIYlIDYISDRLMV 528
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
346-539 |
1.91e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-------EAR-----MT---TVWQEprffrTTVKE 410
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiATRrrvgyMSqafSLYGE-----LTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NV-------HFGEEYLENQLEKNIELVNVKPIIRDLSEGIetelhksgvefSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:NF033858 359 NLelharlfHLPAAEIAARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 484 LDPSNQETVWNMIEGLGRE--VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKLI 539
Cdd:NF033858 428 VDPVARDMFWRLLIELSREdgVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALV 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
344-529 |
2.06e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQ----------EPR-----FFRTTV 408
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyisEDRkrdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENV------HFGEEY--LENQLEKN-----IELVNVKPIIRDLSEGietelhksgvEFSGGERKRLALLRAIVSNPNLI 475
Cdd:PRK10762 348 KENMsltalrYFSRAGgsLKHADEQQavsdfIRLFNIKTPSMEQAIG----------LLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 476 ILDEPTAGLDPSNQETVWNMI-----EGLgrevTRIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLInqfkaEGL----SIILVSSEMPEVLgMSDRILVMHEGRI 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
339-485 |
4.83e-12 |
|
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: 68.42 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVY-------YGNEARMT-----TVWQEprffrt 406
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklaYVDQSRDAldpnkTVWEE------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 tvkenVHFGEEYLE-NQLEKN----IELVNVKpiirdlseGieTELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:TIGR03719 407 -----ISGGLDIIKlGKREIPsrayVGRFNFK--------G--SDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
....
gi 446589027 482 AGLD 485
Cdd:TIGR03719 472 NDLD 475
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
344-533 |
5.57e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNeaRMTTVwqePRFFRTTVKENVH--FGEEYLEN 421
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ--RIDTL---SPGKLQALRRDIQfiFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 422 QLEKNIELVNVKPI-IRDLSEGIETE------LHKSGV----------EFSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:PRK10261 415 DPRQTVGDSIMEPLrVHGLLPGKAAAarvawlLERVGLlpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 485 DPSNQETVWNMIEGLGRE--VTRIVVTHD---VEKaiLADRVVIMKEGRIVAGG 533
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfgIAYLFISHDmavVER--ISHRVAVMYLGQIVEIG 546
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
327-527 |
5.64e-12 |
|
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: 64.57 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 327 MTITNVSFQESDGEKCR--IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGlyKPSNGSIvyyGNEARMTTVWQEPRFF 404
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI---TGEILINGRPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTT---VKENVHFGEEYLENQLEKNIELvnvkpiiRDLSegietelhksgVEfsggERKRLALLRAIVSNPNLIILDEPT 481
Cdd:cd03232 79 RSTgyvEQQDVHSPNLTVREALRFSALL-------RGLS-----------VE----QRKRLTIGVELAAKPSILFLDEPT 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446589027 482 AGLDPSNQETVWNMIEGLGREVTRIVVT-HDVEKAILA--DRVVIMKEG 527
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
346-511 |
5.69e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGsivyygnEARMT---TVW---QEPRFFRT-TVKENVH----- 413
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPApgiKVGylpQEPQLDPEkTVRENVEegvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 --------------FGEEY------------------------LENQLEKNIELVNVKP---IIRDLSegietelhksgv 452
Cdd:PRK11819 98 vkaaldrfneiyaaYAEPDadfdalaaeqgelqeiidaadawdLDSQLEIAMDALRCPPwdaKVTKLS------------ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 453 efsGGERKRLALLRAIVSNPNLIILDEPTAGLDpsnQETV-WnmIEGLGREV--TRIVVTHD 511
Cdd:PRK11819 166 ---GGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVaW--LEQFLHDYpgTVVAVTHD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
350-512 |
6.72e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 350 QIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSI-----VYYgnearmttvwqEPRFFRTTVKENVhfgEEYLENQLE 424
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkISY-----------KPQYIKPDYDGTV---EDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 425 K------NIELvnVKPIirdlseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEG 498
Cdd:PRK13409 427 DlgssyyKSEI--IKPL------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170
....*....|....*.
gi 446589027 499 L--GREVTRIVVTHDV 512
Cdd:PRK13409 499 IaeEREATALVVDHDI 514
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
27-308 |
9.40e-12 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 65.97 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 27 FAAILNLSRPLFMGLIVDNLIQRELKAAYVYIAL-----FAGSRLLMWVNNLSFDYVSskasQRILRKKRIYVLRHFFLL 101
Cdd:cd18576 7 LSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALlllglFLLQAVFSFFRIYLFARVG----ERVVADLRKDLYRHLQRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 102 PFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPFLFFSAMVpmlMGKK 178
Cdd:cd18576 83 PLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKltlLMLATVPVVVLVAVL---FGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 179 VRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAYIVVLI 258
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446589027 259 IGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
344-542 |
9.99e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIV------YYGNEA----RMTTVWQEPrffRTTVKENVH 413
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSyrsqRIRMIFQDP---STSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGeEYLENQLEKNIELvnvKPIIRDlsEGIETELHKSGV----------EFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:PRK15112 106 IS-QILDFPLRLNTDL---EPEQRE--KQIIETLRQVGLlpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 484 LDPSNQETVWNMIEGL--GREVTRIVVTHDV--EKAIlADRVVIMKEGRIVAGGS------------PEKLINSH 542
Cdd:PRK15112 180 LDMSMRSQLINLMLELqeKQGISYIYVTQHLgmMKHI-SDQVLVMHQGEVVERGStadvlasplhelTKRLIAGH 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
359-540 |
1.17e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 359 IVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEAR--------------------------------------------- 393
Cdd:PTZ00265 1199 IVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsgk 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 394 -------------------MTTVWQEPRFFRTTVKENVHFG-EEYLENQLEKNIELVNVKPIIRDLSEGIETELHKSGVE 453
Cdd:PTZ00265 1279 illdgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 454 FSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVVT--HDVEKAILADRVVIM----KEG 527
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVVFnnpdRTG 1438
|
250
....*....|....
gi 446589027 528 RIV-AGGSPEKLIN 540
Cdd:PTZ00265 1439 SFVqAHGTHEELLS 1452
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
346-537 |
1.18e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE-------ARM------------------------ 394
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEinalstaQRLarglvylpedrqssglyldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 395 ---TTVWQEPRFFRTTVKENVHFgEEYlENQLekNIELVNVKPIIRDLSegietelhksgvefsGGERKRLALLRAIVSN 471
Cdd:PRK15439 361 nvcALTHNRRGFWIKPARENAVL-ERY-RRAL--NIKFNHAEQAARTLS---------------GGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIvaGGSPEK 537
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQnVAVLFISSDLEEIEqMADRVLVMHQGEI--SGALTG 487
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
449-538 |
1.83e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 449 KSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKA-ILADRVVIMKE 526
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAeQLAHELTVIDR 219
|
90
....*....|..
gi 446589027 527 GRIVAGGSPEKL 538
Cdd:NF000106 220 GRVIADGKVDEL 231
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
18-308 |
7.40e-11 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 63.19 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLSRPLFMGLIVDNLIQR-ELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVLR 96
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANgDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 97 HFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMKF---ILWVTPFLFFSAMVpm 173
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLaliLLVAIPILALVVFL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 174 lMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAY 253
Cdd:cd18548 159 -IMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 254 IVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18548 238 VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
344-530 |
8.89e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.14 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGsivyygnearmttvwqeprffrtTVK--ENVHFG------ 415
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG-----------------------TVKwsENANIGyyaqdh 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 EEYLENQL-----------EKNIELVnVKPIIRDLSEGiETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:PRK15064 392 AYDFENDLtlfdwmsqwrqEGDDEQA-VRGTLGRLLFS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 485 DPSNQETVWNMIEGLgrEVTRIVVTHDVE-KAILADRVVIMKEGRIV 530
Cdd:PRK15064 470 DMESIESLNMALEKY--EGTLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-531 |
1.09e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 349 LQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGN-----------EARMTTVWQE----PRFfrtTVKENVH 413
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkssqEAGIGIIHQElnliPQL---TIAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 414 FGEEY-----------LENQLEKNIELVNVKpiirdlsegietelHKSGV---EFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:PRK10762 102 LGREFvnrfgridwkkMYAEADKLLARLNLR--------------FSSDKlvgELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIV-VTHDVeKAI--LADRVVIMKEGRIVA 531
Cdd:PRK10762 168 PTDALTDTETESLFRVIRELKSQGRGIVyISHRL-KEIfeICDDVTVFRDGQFIA 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
339-485 |
1.19e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVyYGNEARMTTVWQeprfFRT------TVKENV 412
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVKLAYVDQ----SRDaldpnkTVWEEI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 413 HFGEEYLE-NQLEKN----IELVNVKpiirdlseGIETElHKSGVeFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:PRK11819 410 SGGLDIIKvGNREIPsrayVGRFNFK--------GGDQQ-KKVGV-LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
333-485 |
1.29e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 333 SFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEArMTTVWQEPRFFRTTVKENV 412
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ-LAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFGE-EY--LENQL----EKN--------------IELVNVKPIIRDLSEGI---ETELHKSGVEFSGGERKRLALLRAI 468
Cdd:PRK10636 85 IDGDrEYrqLEAQLhdanERNdghaiatihgkldaIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170
....*....|....*..
gi 446589027 469 VSNPNLIILDEPTAGLD 485
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD 181
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
347-496 |
1.33e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTtvwQEPRFFR-----------TTVKENVHFG 415
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAylghlpglkadLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 ---EEYLENQLEKN-IELVNVKpiirdlseGIETELHKsgvEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQET 491
Cdd:PRK13543 107 cglHGRRAKQMPGSaLAIVGLA--------GYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
....*
gi 446589027 492 VWNMI 496
Cdd:PRK13543 176 VNRMI 180
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
344-538 |
1.63e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKP----SNGSIVYYGNEA-------RMT-TVWQEPR--F-----F 404
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapcalrgRKIaTIMQNPRsaFnplhtM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKENVH-FGEEYLENQLEKNIELVNVKPIIRDLsegietELHKsgVEFSGGERKRLALLRAIVSNPNLIILDEPTAG 483
Cdd:PRK10418 99 HTHARETCLaLGKPADDATLTAALEAVGLENAARVL------KLYP--FEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 484 LDPSNQETVWNMIEGLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKraLGMLLVTHDMGvVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
339-515 |
1.91e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkP---SNGSIVYYGNEARMTTVWQEPRffrttvkenvHFG 415
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PqgySNDLTLFGRRRGSGETIWDIKK----------HIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 eeYLENQLEK----NIELVNVkpII-----------------RDLSE------GIETELHKSGVE-FSGGErKRLALL-R 466
Cdd:PRK10938 340 --YVSSSLHLdyrvSTSVRNV--ILsgffdsigiyqavsdrqQKLAQqwldilGIDKRTADAPFHsLSWGQ-QRLALIvR 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 467 AIVSNPNLIILDEPTAGLDPSNQETVWNMIEGL-GREVTRIV-VTHDVEKA 515
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLfVSHHAEDA 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
329-511 |
2.26e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDgeKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIvyygnearmttvwqeprffRTTV 408
Cdd:PRK11147 322 MENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------------HCGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVHFGEEYLEnqlekniELVNVKPIIRDLSEGiETELHKSGVE-----------------------FSGGERKRLALL 465
Cdd:PRK11147 381 KLEVAYFDQHRA-------ELDPEKTVMDNLAEG-KQEVMVNGRPrhvlgylqdflfhpkramtpvkaLSGGERNRLLLA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446589027 466 RAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLgrEVTRIVVTHD 511
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGTVLLVSHD 496
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-276 |
2.56e-10 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 61.35 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 21 AVCSGCFAAILNLSRPLFMGLIVDN--------LIQRELKAAY---VYIALFAGSRLlmwvnnlsfdYVSSKASQRILRK 89
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQgfaagntaLLNRAFLLLLavaLVLALASALRF----------YLVSWLGERVVAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 90 KRIYVLRHFFLLPFEESEKIKQGE-----------LETLVVSDIPNWVRlygsilieyihAIAQFIGAFIALQHIDMKFI 158
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFETTRTGEvlsrlttdttlIQTVVGSSLSIALR-----------NLLLLIGGLVMLFITSPKLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 159 LWVTpFLFFSAMVP-MLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMM 237
Cdd:cd18575 140 LLVL-LVIPLVVLPiILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRA 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 446589027 238 QHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVA 276
Cdd:cd18575 219 RALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQ 257
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
29-288 |
4.39e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 61.04 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 29 AILNLSRPLFMGLIVDN-LIQRELKAAYVYIA---LFAGSRLLMwvnNLSFDYVSSKASQRILRKKRIYVLRHFFLLP-- 102
Cdd:cd18568 15 QLLGLALPLFTQIILDRvLVHKNISLLNLILIgllIVGIFQILL---SAVRQYLLDYFANRIDLSLLSDFYKHLLSLPls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 103 -------------FEESEKIK----QGELETL--VVSdipnwVRLYGSILIEYIHAIAQFIGAFIALQHIdmkFILWVTP 163
Cdd:cd18568 92 ffasrkvgdiitrFQENQKIRrfltRSALTTIldLLM-----VFIYLGLMFYYNLQLTLIVLAFIPLYVL---LTLLSSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 164 FlffsamvpmlMGKKVRNIASIAQNNQSSVVEMVsqfvKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGV 243
Cdd:cd18568 164 K----------LKRNSREIFQANAEQQSFLVEAL----TGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446589027 244 VGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPV 288
Cdd:cd18568 230 ISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPL 274
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
339-538 |
4.43e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSI-VYYGNEARmttvwqepRFFRT----------- 406
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMAD--------ARHRRavcpriaympq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 ----------TVKENVHF-GEEYLENQLEKNIElvnvkpiIRDLSEGieTELHksgvEF--------SGGERKRLALLRA 467
Cdd:NF033858 84 glgknlyptlSVFENLDFfGRLFGQDAAERRRR-------IDELLRA--TGLA----PFadrpagklSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446589027 468 IVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE---VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPEKL 538
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAEL 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
329-531 |
8.07e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSfQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-----------V 397
Cdd:PRK10982 1 MSNIS-KSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSskealengismV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 398 WQEPRFFR-TTVKENVHFGEEYLENQLEKNIELVN-VKPIIRDLseGIETELHKSGVEFSGGERKRLALLRAIVSNPNLI 475
Cdd:PRK10982 79 HQELNLVLqRSVMDNMWLGRYPTKGMFVDQDKMYRdTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGLGREVTRIV-VTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFqLCDEITILRDGQWIA 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
339-511 |
1.27e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSI-----VYYGNEARmttvwQEPRFFR---TTVKE 410
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLGYFAQ-----HQLEFLRadeSPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 411 NVHFGEEYLENQLeknielvnvkpiiRDLSEGIETELHKSGVE---FSGGERKRLALLRAIVSNPNLIILDEPTAGLD-P 486
Cdd:PRK10636 398 LARLAPQELEQKL-------------RDYLGGFGFQGDKVTEEtrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDlD 464
|
170 180
....*....|....*....|....*
gi 446589027 487 SNQETVWNMIEGLGREVtriVVTHD 511
Cdd:PRK10636 465 MRQALTEALIDFEGALV---VVSHD 486
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
326-536 |
1.27e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 326 GMTITNVSFQESDGEKCrIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYG---NEA-RMTTVWQEP 401
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptRQAlQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 RF------FRTTVKENVHFGEE----YLENQLEKNIELVNVKPIIRDLSEgietELHKSGVEFSGGERKRLALLRAIVSN 471
Cdd:PRK15056 85 QSeevdwsFPVLVEDVVMMGRYghmgWLRRAKKRDRQIVTAALARVDMVE----FRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 472 PNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAILADRVVIMKEGRIVAGGSPE 536
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
15-289 |
1.44e-09 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 59.39 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 15 KLLVIAAVCSgCFAAILNLSRPLFMGLIVDNLI-QRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIY 93
Cdd:cd18549 2 KLFFLDLFCA-VLIAALDLVFPLIVRYIIDDLLpSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 94 VLRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPFLFFSAm 170
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPltlIVFALLPLMIIFT- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 171 vpMLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKgVTAQSYKTEVKKTM--MQHCIGVVGTVI 248
Cdd:cd18549 160 --IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFD-EGNDRFLESKKKAYkaMAYFFSGMNFFT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446589027 249 ETgAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVR 289
Cdd:cd18549 237 NL-LNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIR 276
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
343-531 |
2.04e-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: 59.84 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPS-NGSIVYYGNEARMTTVWQEPRFFRTTVKENVHFGEEYLEN 421
Cdd:TIGR02633 275 RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 422 QLEKNIELVNVKPI--IRDLSEGIETELHKSGVE---------------FSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:TIGR02633 355 GVGKNITLSVLKSFcfKMRIDAAAELQIIGSAIQrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446589027 485 DPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLgLSDRVLVIGEGKLKG 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
353-524 |
2.48e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 353 PGELVIIVGESGAGKTTLLKLMTGLYKPSNGSivyYGNEARMTTVWqepRFFRTTVKENvhfgeeYLENQLEKNIELVnV 432
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSWDEVL---KRFRGTELQN------YFKKLYNGEIKVV-H 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 433 KP-------------------------IIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:PRK13409 165 KPqyvdlipkvfkgkvrellkkvdergKLDEVVErlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446589027 486 PSNQETVWNMIEGLGREVTRIVVTHDVekAIL---ADRVVIM 524
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDL--AVLdylADNVHIA 284
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
18-308 |
2.49e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 58.64 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSGCFAAILNLsrplFMGLIVDNLIQREL-------------KAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQ 84
Cdd:cd18577 5 LLAAIAAGAALPLMTI----VFGDLFDAFTDFGSgesspdeflddvnKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 85 RIlRKKriyVLRHFFLLPFEESEKIKQGELETLVVSDIpNWVRL-YGSILIEYIHAIAQFIGAFI---------ALqhid 154
Cdd:cd18577 81 RI-RKR---YLKALLRQDIAWFDKNGAGELTSRLTSDT-NLIQDgIGEKLGLLIQSLSTFIAGFIiafiyswklTL---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 155 mkFILWVTPFLFFSAMVpmlMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKK 234
Cdd:cd18577 152 --VLLATLPLIAIVGGI---MGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKK 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 235 TMMQHC-IGVVGTVIeTGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18577 227 GLVSGLgLGLLFFII-FAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
346-530 |
4.62e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 346 NIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkPS---NGSIVYYGNEARmttvwqeprfFRT---------------- 406
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCR----------FKDirdsealgiviihqel 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 ------TVKENVHFGEEYLENQL----EKNIE----LVNVKpiirdLSEGIETELHKSGVefsgGERKRLALLRAIVSNP 472
Cdd:NF040905 88 alipylSIAENIFLGNERAKRGVidwnETNRRarelLAKVG-----LDESPDTLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 473 NLIILDEPTAGLDPSNQETVWNMIEGL-GREVTRIVVTHDV-EKAILADRVVIMKEGRIV 530
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELkAQGITSIIISHKLnEIRRVADSITVLRDGRTI 218
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
21-308 |
4.73e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 57.55 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 21 AVCSGCFAAILNLSRPLFMGLIVDNLIQRE-----LKAAYVYIALFAGSRLLMWVNNLSFDYvsskASQRILRKKRIYVL 95
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGsreafYRAVLLLLLLSVLSGLFSGLRGGCFSY----AGTRLVRRLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 96 RH-------FFllpfeesEKIKQGELETLVVSD---IPNWVRLYGSILIEYIhaiAQFIGAFIalqhidmkFILWVTPFL 165
Cdd:cd18572 77 RSllrqdiaFF-------DATKTGELTSRLTSDcqkVSDPLSTNLNVFLRNL---VQLVGGLA--------FMFSLSWRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 166 ---FFSAMVPMLM-----GKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMM 237
Cdd:cd18572 139 tllAFITVPVIALitkvyGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 238 QHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18572 219 YAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
356-522 |
4.75e-09 |
|
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: 56.46 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 356 LVIIVGESGAGKTTLLKLM----TGLYKPSNGSIVYYGNEARMTTVwqeprffRTTVKenVHF----GEEYLenqlekni 427
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyalTGELPPNSKGGAHDPKLIREGEV-------RAQVK--LAFenanGKKYT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 428 elvnvkpIIRDLS----------EGIETELHKSGVEFSGGERK------RLALLRAIVSNPNLIILDEPTAGLDPSNQET 491
Cdd:cd03240 87 -------ITRSLAilenvifchqGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180 190
....*....|....*....|....*....|....
gi 446589027 492 VW-NMIEGLGREVTR--IVVTHDVEKAILADRVV 522
Cdd:cd03240 160 SLaEIIEERKSQKNFqlIVITHDEELVDAADHIY 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
344-537 |
5.09e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMT----GLYKPSNGSIVYYG---NEARmttvwqepRFFRTTV---KEN-V 412
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEIK--------KHYRGDVvynAETdV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFGEEYLENQLEKNIEL--VNVKPI----------IRDLSEGI----ETELHKSGVEF----SGGERKRLALLRAIVSNP 472
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCktPQNRPDgvsreeyakhIADVYMATyglsHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 473 NLIILDEPTAGLDPSnqeTVWNMIEGLgREVTRIVVTHDV-------EKAI-LADRVVIMKEGRIVAGGSPEK 537
Cdd:TIGR00956 229 KIQCWDNATRGLDSA---TALEFIRAL-KTSANILDTTPLvaiyqcsQDAYeLFDKVIVLYEGYQIYFGPADK 297
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
353-530 |
6.55e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 353 PGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGnearmttvwqeprffrttvkenvhfGEEYLENQLEKNielvnv 432
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------GEDILEEVLDQL------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 433 kpiirdlsegIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREV------TRI 506
Cdd:smart00382 50 ----------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlkseknLTV 119
|
170 180
....*....|....*....|....
gi 446589027 507 VVTHDVEKAILADRVVIMKEGRIV 530
Cdd:smart00382 120 ILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
15-308 |
7.23e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 57.07 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 15 KLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLIQRELKAAYVYIAL-FAGSRLLMWVNNLSFDYVSSKASQRILRKKRIY 93
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIgLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 94 VLRHFFLLPFEESEKIKQGELeTLVVSDIPNWVRLYGSILIEyihAIAQFIGAFIALQhidmkFILWVTPFLFFSAMVPM 173
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEI-ISRFNDANKIREAISSTTIS---LFLDLLMVIISGI-----ILFFYNWKLFLITLLII 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 174 L------------MGKKVRNIASIAQNNQSSVVEMVsqfvKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCI 241
Cdd:cd18570 152 PlyiliillfnkpFKKKNREVMESNAELNSYLIESL----KGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQ 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446589027 242 GVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18570 228 SSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
353-517 |
7.30e-09 |
|
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: 56.61 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 353 PGELVIIVGESGAGKTTLLKLMTGLYKPSNGSivyYGNEARMTTVWqepRFFRTTVKENvhfgeeYLENQLEKNIELVnV 432
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEIL---DEFRGSELQN------YFTKLLEGDVKVI-V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 433 KPIIRDL----SEGIETEL----HKSGV-------------------EFSGGERKRLALLRAIVSNPNLIILDEPTAGLD 485
Cdd:cd03236 92 KPQYVDLipkaVKGKVGELlkkkDERGKldelvdqlelrhvldrnidQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|...
gi 446589027 486 PSNQETVWNMIEGLGREVTR-IVVTHDVekAIL 517
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYvLVVEHDL--AVL 202
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-288 |
1.07e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 56.72 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 16 LLVIAAVCsgcFAAILNLSRPLFMGLIVDN-LIQRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYV 94
Cdd:cd18550 2 ALVLLLIL---LSALLGLLPPLLLREIIDDaLPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 95 LRHFFLLPFEESEKIKQGELETLVVSDIPNWVRLYGSILIEYIHAIAQFIGAFIALQHIDMK---FILWVTPFLFFSAMv 171
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRlalLSLVLLPLFVLPTR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 172 pmLMGKKVRNIASIAQNNQSSVVEMVSQF--VKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIE 249
Cdd:cd18550 158 --RVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFT 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 446589027 250 TGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPV 288
Cdd:cd18550 236 AIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPL 274
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
339-525 |
1.21e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 54.29 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKlmtglykpsngSIVYYgnearmttvwqeprFFRTTVKENVHFGEEy 418
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGLA--------------LGGAQSATRRRSGVK- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 419 lenqleknielvnvkpiIRDLSEGIETELHKSGVEFSGGERKRLAL-----LRAIVSNPnLIILDEPTAGLDPSNQETVW 493
Cdd:cd03227 60 -----------------AGCIVAAVSAELIFTRLQLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|...
gi 446589027 494 NMIEG-LGREVTRIVVTHDVEKAILADRVVIMK 525
Cdd:cd03227 122 EAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
347-531 |
1.76e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 347 IDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTVWQ----------EPRFFR-----TTVKEN 411
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagimlcpEDRKAEgiipvHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 412 V------HF--GEEYLENQLEKNielvNVKPIIRDLSegIETELHKSGVEF-SGGERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:PRK11288 352 InisarrHHlrAGCLINNRWEAE----NADRFIRSLN--IKTPSREQLIMNlSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 483 GLDPSNQETVWNMIEGLG-REVTRIVVTHDVEKAI-LADRVVIMKEGRIVA 531
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAaQGVAVLFVSSDLPEVLgVADRIVVMREGRIAG 476
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
332-546 |
2.86e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 332 VSFQESDGEKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKpSNGSIVyyGNEARMTTV---WQEPRFFRTTV 408
Cdd:PRK15093 11 IEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVT--ADRMRFDDIdllRLSPRERRKLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 409 KENVH--FGE--------EYLENQLEKNIELVNVKPIIRD-----LSEGIETeLHKSGV------------EFSGGERKR 461
Cdd:PRK15093 88 GHNVSmiFQEpqscldpsERVGRQLMQNIPGWTYKGRWWQrfgwrKRRAIEL-LHRVGIkdhkdamrsfpyELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 462 LALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVEK-AILADRVVIMKEGRIVAGGSPEKL 538
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMlSQWADKINVLYCGQTVETAPSKEL 246
|
250
....*....|
gi 446589027 539 INS--HSFLQ 546
Cdd:PRK15093 247 VTTphHPYTQ 256
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
353-549 |
3.31e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 353 PGELVIIVGESGAGKTTLLKLMTGlyKPSNGsivYYGNEARMTTVWQEPRFF---------------RTTVKENVHFG-- 415
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAG--RKTGG---YIEGDIRISGFPKKQETFarisgyceqndihspQVTVRESLIYSaf 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 ---------EEYLE--NQLEKNIELVNVKPIIRDLS--EGIETElhksgvefsggERKRLALLRAIVSNPNLIILDEPTA 482
Cdd:PLN03140 980 lrlpkevskEEKMMfvDEVMELVELDNLKDAIVGLPgvTGLSTE-----------QRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 483 GLDPSN----QETVWNMIEgLGREVtrIVVTH----DVEKAIlaDRVVIMKEGRIVAGGSPEKLiNSHSFLQRYE 549
Cdd:PLN03140 1049 GLDARAaaivMRTVRNTVD-TGRTV--VCTIHqpsiDIFEAF--DELLLMKRGGQVIYSGPLGR-NSHKIIEYFE 1117
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
339-549 |
4.39e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 339 GEKCRI-HNIDLQIHPGELVIIVGESGAGKTTLL-----KLMTGLYKP----SNGSIVYYGNEARMTTVWQEPRFFRT-T 407
Cdd:TIGR00956 773 KEKRVIlNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGgdrlVNGRPLDSSFQRSIGYVQQQDLHLPTsT 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFgEEYLENQLEKNIELVN--VKPIIRDLsegiETELHKSGVEFSGGE------RKRLALLRAIVSNPNLII-LD 478
Cdd:TIGR00956 853 VRESLRF-SAYLRQPKSVSKSEKMeyVEEVIKLL----EMESYADAVVGVPGEglnveqRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 479 EPTAGLDPSNQETVWNMIEGLGREVTRIVVT-HDVEKAILA--DRVVIMKEG-RIVAGGSPEKliNSHSFLQRYE 549
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAILFEefDRLLLLQKGgQTVYFGDLGE--NSHTIINYFE 1000
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
344-546 |
5.18e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKT-TLLKLMtGLY----KPSNGSIVYYGNE--------------ARMTTVWQEPRF- 403
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLIdypgRVMAEKLEFNGQDlqrisekerrnlvgAEVAMIFQDPMTs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 404 --------FRTTVKENVHFGEEYLENQlEKNIELVNVKPIiRDLSEGIETELHksgvEFSGGERKRLALLRAIVSNPNLI 475
Cdd:PRK11022 102 lnpcytvgFQIMEAIKVHQGGNKKTRR-QRAIDLLNQVGI-PDPASRLDVYPH----QLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 476 ILDEPTAGLDPSNQETVWNMIEGLGRE--VTRIVVTHDVE-KAILADRVVIMKEGRIVAGGSPEKLINS--HSFLQ 546
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDIFRAprHPYTQ 251
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-308 |
5.22e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.41 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 15 KLLVIAAVCSGCFAAILNLSRPLFMGLIVDNLI-QRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRI---LRKK 90
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFItPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVsydLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 91 riyVLRHFFLLPFEESEKIKQGELETLVVSDIPnwvRLYGSI---LIEYIHAIAQFIGAFIALQHIDMKFILWVT---PF 164
Cdd:cd18540 81 ---AFEHLQTLSFSYFDKTPVGWIMARVTSDTQ---RLGEIIswgLVDLVWGITYMIGILIVMLILNWKLALIVLavvPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 165 LFFSAM---VPMLMG-KKVRNIASiaqnnqssvvEMVSQF---VKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMM 237
Cdd:cd18540 155 LAVVSIyfqKKILKAyRKVRKINS----------RITGAFnegITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 238 Q-------HCIGVVGTVIetgayivVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18540 225 SalflpivLFLGSIATAL-------VLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
455-548 |
6.88e-08 |
|
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: 55.40 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 455 SGGERKRLALLRAIVSNPN--LIILDEPTAGLDPSNQETVWNMIEGLgREV--TRIVVTHDVEKAILADRVVIMKE---- 526
Cdd:TIGR00630 490 SGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLgnTLIVVEHDEDTIRAADYVIDIGPgage 568
|
90 100
....*....|....*....|....*
gi 446589027 527 --GRIVAGGSPEKLI-NSHSFLQRY 548
Cdd:TIGR00630 569 hgGEVVASGTPEEILaNPDSLTGQY 593
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
351-523 |
7.26e-08 |
|
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: 52.57 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 351 IHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGsivyygnearmttvwqeprffrttvkenvhfgeeylenqlekNIELV 430
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD------------------------------------------NDEWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 431 NVKPIIRdlsegietelhKSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREV--TRIVV 508
Cdd:cd03222 60 GITPVYK-----------PQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVV 128
|
170
....*....|....*.
gi 446589027 509 THDVEKA-ILADRVVI 523
Cdd:cd03222 129 EHDLAVLdYLSDRIHV 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
353-524 |
1.14e-07 |
|
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: 54.41 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 353 PGELVIIVGESGAGKTTLLKLMTGLYKPsN------------------GSIVY------YGNEARMTT----VWQEPRFF 404
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKP-NlgdydeepswdevlkrfrGTELQdyfkklANGEIKVAHkpqyVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 405 RTTVKEnvhfgeeYLENQLEKN-----IELVNVKPII-RDLSEgietelhksgveFSGGERKRLALLRAIVSNPNLIILD 478
Cdd:COG1245 177 KGTVRE-------LLEKVDERGkldelAEKLGLENILdRDISE------------LSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446589027 479 EPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVekAIL---ADRVVIM 524
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEgKYVLVVEHDL--AILdylADYVHIL 285
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
343-529 |
3.80e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNE--------------ARMTTVWQEPRFFRT-T 407
Cdd:PRK09700 278 KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspldavkkgmAYITESRRDNGFFPNfS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 VKENVHFGEEYLENQLEKNIELVNVKPIIRDLSEGIE------TELHKSGVEFSGGERKRLALLRAIVSNPNLIILDEPT 481
Cdd:PRK09700 358 IAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQREllalkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446589027 482 AGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILA--DRVVIMKEGRI 529
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITvcDRIAVFCEGRL 487
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
343-529 |
6.16e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYK-PSNGSIVYYGNEARMTTVWQEPRFFRTTVKENVHFGEEYLEN 421
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 422 QLEKNIELVNVK-----PIIRDLSE--GIETELHKSGVE----------FSGGERKRLALLRAIVSNPNLIILDEPTAGL 484
Cdd:PRK13549 357 GVGKNITLAALDrftggSRIDDAAElkTILESIQRLKVKtaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446589027 485 DPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAI-LADRVVIMKEGRI 529
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQgVAIIVISSELPEVLgLSDRVLVMHEGKL 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
340-496 |
9.64e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 340 EKCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEarmTTVWQEPrfFRTTVKENVHFGeeyL 419
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN---INNIAKP--YCTYIGHNLGLK---L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 420 ENQLEKNIELVNVkpiIRDLSEGIETELH---------KSGVEFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQE 490
Cdd:PRK13541 84 EMTVFENLKFWSE---IYNSAETLYAAIHyfklhdlldEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
....*.
gi 446589027 491 TVWNMI 496
Cdd:PRK13541 161 LLNNLI 166
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
343-533 |
1.12e-06 |
|
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: 49.56 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHN---IDLQIHPGELVIIVGESGAGKTTL----------LKLMTGL-----------YKPSNGSIvyygnEARMTTVW 398
Cdd:cd03270 7 REHNlknVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLsayarqflgqmDKPDVDSI-----EGLSPAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 QEPRFFRTTVKENVHFGEE---YLEnQLEKNIELVNVKPIIRDLSEGIETeLHKSGVEFSGGERKRLALLRAIVSNPN-- 473
Cdd:cd03270 82 IDQKTTSRNPRSTVGTVTEiydYLR-LLFARVGIRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQIGSGLTgv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 474 LIILDEPTAGLDPSNQETVWNMIEGLgREV--TRIVVTHDVEKAILADRVVIM------KEGRIVAGG 533
Cdd:cd03270 160 LYVLDEPSIGLHPRDNDRLIETLKRL-RDLgnTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
343-510 |
1.53e-06 |
|
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: 50.39 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHNIDLQIHPGeLVIIVGESGAGKTTLLKLMTGLYKPSNGSIV----YYGN----------EARMTTVWQE--PRFFRT 406
Cdd:COG3593 13 SIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedFYLGddpdlpeieiELTFGSLLSRllRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 407 TVKENVHFGEEYLENQLEKNIELVN--VKPIIRDLSEGIETELHKSG-----------VEFSGGERKR------------ 461
Cdd:COG3593 92 EDKEELEEALEELNEELKEALKALNelLSEYLKELLDGLDLELELSLdeledllkslsLRIEDGKELPldrlgsgfqrli 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 462 -LALLRAIV-----SNPNLIILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTH 510
Cdd:COG3593 172 lLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpNQVIITTH 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
455-548 |
2.29e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 455 SGGERKRLALLRAIVSNPNLI--ILDEPTAGLDPSNQETVWNMIEGLGRE-VTRIVVTHDVEKAILADRVVIMKE----- 526
Cdd:PRK00635 478 SGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMISLADRIIDIGPgagif 557
|
90 100
....*....|....*....|....
gi 446589027 527 -GRIVAGGSPEK-LINSHSFLQRY 548
Cdd:PRK00635 558 gGEVLFNGSPREfLAKSDSLTAKY 581
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
342-535 |
3.24e-06 |
|
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: 48.76 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 342 CRIHN---IDLQIHPGELVIIVGESGAGKTTLLK--LMTGLYKPSNGSIVYYGNEA---------RMTTVWQEP------ 401
Cdd:cd03271 6 ARENNlknIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGNHDrieglehidKVIVIDQSPigrtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 -------RFFrTTVKE---NVHFGEEYLENQLE-----KNIELV-------------NVKPIIRDL----SEGIE-TELH 448
Cdd:cd03271 86 snpatytGVF-DEIRElfcEVCKGKRYNRETLEvrykgKSIADVldmtveealeffeNIPKIARKLqtlcDVGLGyIKLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 449 KSGVEFSGGERKRLAL---LRAIVSNPNLIILDEPTAGLDPsnqETVWNMIEGLGREV----TRIVVTHDVEKAILADRV 521
Cdd:cd03271 165 QPATTLSGGEAQRIKLakeLSKRSTGKTLYILDEPTTGLHF---HDVKKLLEVLQRLVdkgnTVVVIEHNLDVIKCADWI 241
|
250 260
....*....|....*....|
gi 446589027 522 VIM------KEGRIVAGGSP 535
Cdd:cd03271 242 IDLgpeggdGGGQVVASGTP 261
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
359-510 |
5.08e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 359 IVGESGAGKTTLLKLMT-----GLykPSNGSIVYYGNE------------------------------ARMTTVWQEPRF 403
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAmhaidGI--PKNCQILHVEQEvvgddttalqcvlntdiertqlleeeaqlvAQQRELEFETET 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 404 FRTTVKENVHFGEEYLENQLE---KNIELVNV-------KPIIRDLSEGIETElHKSGVEFSGGERKRLALLRAIVSNPN 473
Cdd:PLN03073 286 GKGKGANKDGVDKDAVSQRLEeiyKRLELIDAytaearaASILAGLSFTPEMQ-VKATKTFSGGWRMRIALARALFIEPD 364
|
170 180 190
....*....|....*....|....*....|....*..
gi 446589027 474 LIILDEPTAGLDPsnQETVWNMIEGLGREVTRIVVTH 510
Cdd:PLN03073 365 LLLLDEPTNHLDL--HAVLWLETYLLKWPKTFIVVSH 399
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
344-510 |
7.07e-06 |
|
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: 48.98 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYkPSNGSIVYYGNEARMTTVWQEPRFFRTTVKENV--------HFG 415
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIiypdssedMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 416 EEYLENQLEKNIELVnvkpiirDLSEGIETELHKSGV-----EFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSNQE 490
Cdd:TIGR00954 547 RGLSDKDLEQILDNV-------QLTHILEREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|
gi 446589027 491 TVWNMIEGLGreVTRIVVTH 510
Cdd:TIGR00954 620 YMYRLCREFG--ITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
343-539 |
7.90e-06 |
|
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: 48.86 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 343 RIHN---IDLQIHPGELVIIVGESGAGKTTLL----------KLMTGLYKPSNG-SIVYYGNEARMTTVWQEP------- 401
Cdd:TIGR00630 620 RENNlknITVSIPLGLFTCITGVSGSGKSTLIndtlypalanRLNGAKTVPGRYtSIEGLEHLDKVIHIDQSPigrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 402 ------------------------------RF-FRT------------TVKENVHF------------GEEYLENQLE-- 424
Cdd:TIGR00630 700 npatytgvfdeirelfaetpeakvrgytpgRFsFNVkggrceacqgdgVIKIEMHFlpdvyvpcevckGKRYNRETLEvk 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 425 ---KNIELV-------------NVKPIIRDL----SEGIE-TELHKSGVEFSGGERKRLAL---LRAIVSNPNLIILDEP 480
Cdd:TIGR00630 780 ykgKNIADVldmtveeayeffeAVPSISRKLqtlcDVGLGyIRLGQPATTLSGGEAQRIKLakeLSKRSTGRTLYILDEP 859
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446589027 481 TAGLdpsNQETVWNMIEGLGREV----TRIVVTH--DVEKAilADRVVIM------KEGRIVAGGSPEKLI 539
Cdd:TIGR00630 860 TTGL---HFDDIKKLLEVLQRLVdkgnTVVVIEHnlDVIKT--ADYIIDLgpeggdGGGTVVASGTPEEVA 925
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
329-485 |
9.92e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 329 ITNVSFQESDGEKCRIHniDLQIHPGELVIIVGESGAGKTTL-------LKLMTGLYKPSNGSIVYYGNEARMTTV---W 398
Cdd:PRK10938 6 ISQGTFRLSDTKTLQLP--SLTLNAGDSWAFVGANGSGKSALaralageLPLLSGERQSQFSHITRLSFEQLQKLVsdeW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 399 Q----------EPRFFRTTvkenvhfgEEYLENQLEKNielvnvkPIIRDLSE--GIETELHKSGVEFSGGERKRLALLR 466
Cdd:PRK10938 84 QrnntdmlspgEDDTGRTT--------AEIIQDEVKDP-------ARCEQLAQqfGITALLDRRFKYLSTGETRKTLLCQ 148
|
170
....*....|....*....
gi 446589027 467 AIVSNPNLIILDEPTAGLD 485
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLD 167
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
16-276 |
1.27e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 47.20 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 16 LLVIAAVCSgcfaAILNLSRPLFMGLIVDN-LIQRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYV 94
Cdd:cd18782 6 EVLALSFVV----QLLGLANPLLFQVIIDKvLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 95 LRHFFLLPFEESEKIKQGELETLVvSDIPNwVR--LYGSILIEYIHAIAQFIGAFIalqhidmkfILWVTPFLFFSAM-- 170
Cdd:cd18782 82 IDHLLRLPLGFFDKRPVGELSTRI-SELDT-IRgfLTGTALTTLLDVLFSVIYIAV---------LFSYSPLLTLVVLat 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 171 VPMLMG----------KKVRNIASIAQNNQSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHC 240
Cdd:cd18782 151 VPLQLLltflfgpilrRQIRRRAEASAKTQSYLVESLT----GIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTT 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 446589027 241 IGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVA 276
Cdd:cd18782 227 SGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIA 262
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
455-541 |
1.89e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 455 SGGE--RKRLAllRAIVSNpnLI----ILDEPTAGLDPSNQETVWNMIEGLgREV--TRIVVTHDvEKAIL-ADRVVIM- 524
Cdd:COG0178 487 SGGEaqRIRLA--TQIGSG--LVgvlyVLDEPSIGLHQRDNDRLIETLKRL-RDLgnTVIVVEHD-EDTIRaADYIIDIg 560
|
90 100
....*....|....*....|..
gi 446589027 525 -----KEGRIVAGGSPEKLINS 541
Cdd:COG0178 561 pgageHGGEVVAQGTPEEILKN 582
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
455-543 |
3.84e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 455 SGGERKRLAL---LRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGL---GREVtrIVVTHDVEKAILADRVVIM---- 524
Cdd:PRK00635 811 SGGEIQRLKLayeLLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLthqGHTV--VIIEHNMHVVKVADYVLELgpeg 888
|
90 100
....*....|....*....|.
gi 446589027 525 --KEGRIVAGGSPEKLINSHS 543
Cdd:PRK00635 889 gnLGGYLLASCSPEELIHLHT 909
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
344-532 |
4.58e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 344 IHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTT-----------VWQEPRFFRTTVKENV 412
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 HFgeeyleNQLEKNIE-------LVNVKPIIRDL-----SEGIETELHKSGV-EFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:PRK10982 344 GF------NSLISNIRnyknkvgLLDNSRMKSDTqwvidSMRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 480 PTAGLDPSNQETVWNMIEGLGREVTRIVVTHDVEKAILA--DRVVIMKEGRiVAG 532
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGitDRILVMSNGL-VAG 471
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
345-511 |
5.36e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 345 HNIDLqihPGELVIIVGESGAGKTTLLKLMT-GLY-------KPSNGSIVYYGNEARMTTVWQ-EPRFFRTT-------- 407
Cdd:COG0419 17 ETIDF---DDGLNLIVGPNGAGKSTILEAIRyALYgkarsrsKLRSDLINVGSEEASVELEFEhGGKRYRIErrqgefae 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 408 ------------------------VKENVHFGEEYLENQLEKNIELVNVK-PIIRDLSEGIETELhksgveFSGGERKRL 462
Cdd:COG0419 94 fleakpserkealkrllgleiyeeLKERLKELEEALESALEELAELQKLKqEILAQLSGLDPIET------LSGGERLRL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446589027 463 ALLRAIVsnpnlIILDepTAGLDPSNQETVWNMIEGLGrevtriVVTHD 511
Cdd:COG0419 168 ALADLLS-----LILD--FGSLDEERLERLLDALEELA------IITHV 203
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
189-276 |
1.27e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 44.03 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 189 NQSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGE 268
Cdd:cd18588 179 NQSFLVETVT----GIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGE 254
|
....*...
gi 446589027 269 MEVGALVA 276
Cdd:cd18588 255 LTIGQLIA 262
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
455-541 |
1.93e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 455 SGGE--RKRLAllRAIVSNPN--LIILDEPTAGLDPS-NQ---ETVWNMIEgLGRevTRIVVTHDvEKAIL-ADRVVIMK 525
Cdd:PRK00349 491 SGGEaqRIRLA--TQIGSGLTgvLYVLDEPSIGLHQRdNDrliETLKHLRD-LGN--TLIVVEHD-EDTIRaADYIVDIG 564
|
90 100
....*....|....*....|..
gi 446589027 526 E------GRIVAGGSPEKLINS 541
Cdd:PRK00349 565 PgagvhgGEVVASGTPEEIMKN 586
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
18-278 |
2.43e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 43.39 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 18 VIAAVCSgcfaAILNLSRPLFMGLIVDNLIQ----------RELKAAYVYI-------ALFAGSRllMWVNNLsfdyvss 80
Cdd:cd18780 2 TIALLVS----SGTNLALPYFFGQVIDAVTNhsgsggeealRALNQAVLILlgvvligSIATFLR--SWLFTL------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 81 kASQRILRKKRIYVLRH-------FFllpfeesEKIKQGELETLVVSD---IPNWVRLYGSILIEYIhaiAQFIGAFIAL 150
Cdd:cd18780 69 -AGERVVARLRKRLFSAiiaqeiaFF-------DVTRTGELLNRLSSDtqvLQNAVTVNLSMLLRYL---VQIIGGLVFM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 151 QHIDMKF---ILWVTPFLFFSAMvpmLMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQS 227
Cdd:cd18780 138 FTTSWKLtlvMLSVVPPLSIGAV---IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINES 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446589027 228 YKTEVKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVL 278
Cdd:cd18780 215 YLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFL 265
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
13-315 |
3.53e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 42.82 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 13 KEKLLVIAavcsGCFAAILN-LSRPLF----------MGLIVDNLIQRELK---AAYVYIALFAGsrLLMWVNNLSFDYV 78
Cdd:cd18578 6 PEWPLLLL----GLIGAIIAgAVFPVFailfsklisvFSLPDDDELRSEANfwaLMFLVLAIVAG--IAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 79 SSKASQRIlrKKRIY--VLRH---FFllpfeESEKIKQGELETLVVSDIPNwVR-LYGSILIEYIHAIAQFIGAFI---- 148
Cdd:cd18578 80 GERLTRRL--RKLAFraILRQdiaWF-----DDPENSTGALTSRLSTDASD-VRgLVGDRLGLILQAIVTLVAGLIiafv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 149 -----ALqhidmkFILWVTPFLFFSAMV--PMLMGKKVRNIASIAQNNQssvveMVSQFVKGVQDLRSLQKEKWAIRLFK 221
Cdd:cd18578 152 ygwklAL------VGLATVPLLLLAGYLrmRLLSGFEEKNKKAYEESSK-----IASEAVSNIRTVASLTLEDYFLEKYE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 222 GVTAQSYKTEVKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVgalVAVLATIEMLFFPVRYVGDLL-MMTQV 300
Cdd:cd18578 221 EALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTF---EQFFIVFMALIFGAQSAGQAFsFAPDI 297
|
330
....*....|....*..
gi 446589027 301 AAA--SANRVFSFLDKR 315
Cdd:cd18578 298 AKAkaAAARIFRLLDRK 314
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
455-522 |
5.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 5.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 455 SGGERK------RLALLRAIVSNPNLIILDEPTAGLDPSNQETVWNMIEGLGREVTR-IVVTHDVEKAILADRVV 522
Cdd:PRK03918 790 SGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQvIIVSHDEELKDAADYVI 864
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
334-479 |
6.58e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 334 FQESDGE-KCRIHNIDLQIHPGELVIIVGESGAGKTTLLKLMTGLYKPSNGSIVYYGNEARMTTvwqeprffrttvkenv 412
Cdd:PRK13545 29 FRSKDGEyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAI---------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 413 hfgEEYLENQLE--KNIELV---------NVKPIIRDLSE--GIETELHKSGVEFSGGERKRLALLRAIVSNPNLIILDE 479
Cdd:PRK13545 93 ---SSGLNGQLTgiENIELKglmmgltkeKIKEIIPEIIEfaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
28-306 |
8.46e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 41.50 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 28 AAILNLSRPLFMGLIVdnliqrelkaayVYIALFAGSRLLMWVNNLsfdyVSSKASQRILRKKRIYVLRHFFLLPFEESE 107
Cdd:cd18561 25 RIFAGGPWEDIMPPLA------------GIAGVIVLRAALLWLRER----VAHRAAQRVKQHLRRRLFAKLLKLGPGYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 108 KIKQGELETLVVSDIPNWVRLYGSILieyihaiAQFIGAFIALQHIdMKFILWVTP-----FLFFSAMVPMLMGKKVRNI 182
Cdd:cd18561 89 GERTGELQTTVVDGVEALEAYYGRYL-------PQLLVALLGPLLI-LIYLFFLDPlvaliLLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 183 ASIAQNNQSSVVEMVSQFVKGVQDLRSL-----------QKEKWAIRLFKGVTAQSYKTEVKktmmqhcIGVVGTVIETG 251
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLkafgaskrrgnELAARAEDLRQATMKVLAVSLLS-------SGIMGLATALG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 252 AyIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASAN 306
Cdd:cd18561 234 T-ALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAAD 287
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
30-297 |
8.81e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 41.44 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 30 ILNLSRPLFMGLIVDNL---IQRELKAAYVYIALFAGSRLLM----WVNNLSFDYVSSKASQRIlrkkRIYVLRHFFLLP 102
Cdd:cd18560 10 ACNVLAPLFLGRAVNALtlaKVKDLESAVTLILLYALLRFSSkllkELRSLLYRRVQQNAYREL----SLKTFAHLHSLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 103 FEESEKIKQGELETLV------VSDIPNWVRLY-GSILIEYIHAIAQFIgafialqhidMKFILWVTPFLFFSAMVPMLM 175
Cdd:cd18560 86 LDWHLSKKTGEVVRIMdrgtesANTLLSYLVFYlVPTLLELIVVSVVFA----------FHFGAWLALIVFLSVLLYGVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 176 GKKVRNI------ASIAQNNQSSVVEMVSQF----VKgvqdlrSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVG 245
Cdd:cd18560 156 TIKVTEWrtkfrrAANKKDNEAHDIAVDSLLnfetVK------YFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQ 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446589027 246 TVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMM 297
Cdd:cd18560 230 QLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRM 281
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
165-277 |
1.03e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 41.27 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 165 LFFSAMVPMLMGKKVRNIASIAQNNQSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVV 244
Cdd:cd18587 154 LLYGLLLQKPLRRLVEESMRESAQKNALLVESLS----GLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNF 229
|
90 100 110
....*....|....*....|....*....|...
gi 446589027 245 GTVIETGAYIVVLIIGAQKIMKGEMEVGALVAV 277
Cdd:cd18587 230 AQFVQQLVTVAIVIVGVYLISDGELTMGGLIAC 262
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
144-279 |
2.95e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 39.75 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 144 IGAFIALQHIDMKFILWVTPFLFFSAMVPMLMGKKVRN------IASIAQnnQSSVVEMVsqfvKGVQDLRSLQKEKWAI 217
Cdd:cd18567 130 ILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRateeqiVASAKE--QSHFLETI----RGIQTIKLFGREAERE 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446589027 218 RLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLA 279
Cdd:cd18567 204 ARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLA 265
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
16-278 |
4.31e-03 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 39.42 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 16 LLVIAAVCSGCFaailnlsrPLFMGLIVDNLIQRELKAA-------YVYIALF----AGSrllmwVNNLSFDYVSSKASQ 84
Cdd:cd18573 4 LLLVSSAVTMSV--------PFAIGKLIDVASKESGDIEifglslkTFALALLgvfvVGA-----AANFGRVYLLRIAGE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 85 RILRK--KRIY--VLRH---FFllpfeesEKIKQGEL------ETLVVSdipnwvRLYGSILIEYIHAIAQFIGAFIALQ 151
Cdd:cd18573 71 RIVARlrKRLFksILRQdaaFF-------DKNKTGELvsrlssDTSVVG------KSLTQNLSDGLRSLVSGVGGIGMML 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 152 HIDMK---FILWVTPFLFFSAMVpmlMGKKVRNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSY 228
Cdd:cd18573 138 YISPKltlVMLLVVPPIAVGAVF---YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVF 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446589027 229 ---KTEVK-KTMMQHCIGVVGTVietgAYIVVLIIGAQKIMKGEMEVGALVAVL 278
Cdd:cd18573 215 dlaKKEALaSGLFFGSTGFSGNL----SLLSVLYYGGSLVASGELTVGDLTSFL 264
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
453-513 |
5.03e-03 |
|
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: 39.30 E-value: 5.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446589027 453 EFSGGERKRLALLRAIVSNPN---LIILDEPTAGLDPSNQETVWNMIEGLGREVTRIVV-THDVE 513
Cdd:pfam13304 236 ELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILtTHSPL 300
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
28-304 |
5.38e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 38.86 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 28 AAILNLSRPLFMGLIVDNLIQRELKAAYVYI-----------ALFAGSR--LLMwvnnlsfdYVSSKASQRI---LRKKR 91
Cdd:cd18590 8 AVICETFIPYYTGRVIDILGGEYQHNAFTSAiglmclfslgsSLSAGLRggLFM--------CTLSRLNLRLrhqLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 92 IYVLRHFFllpfeesEKIKQGELETLVVSD---IPNWVRLYGSILIEyihAIAQFIGAFIALQHIDMKFILWVtpflFFS 168
Cdd:cd18590 80 VQQDIGFF-------EKTKTGDLTSRLSTDttlMSRSVALNANVLLR---SLVKTLGMLGFMLSLSWQLTLLT----LIE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 169 AMVPMLMGKKV----RNIASIAQNNQSSVVEMVSQFVKGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVV 244
Cdd:cd18590 146 MPLTAIAQKVYntyhQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLV 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 245 GTVIETGAYIVVLIIGAQKIMKGEMEVGALVA-VLATIEMlffpVRYVGDLL-----MMTQVAAAS 304
Cdd:cd18590 226 RRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSfILYQKNL----GSYVRTLVyiygdMLSNVGAAA 287
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
439-511 |
5.91e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 5.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446589027 439 LSEGIETELHkSGV--EFSGGERKRLALLRAIVSNPNLIILDEPTAGLDPSN---QETVWNmieglGREVTRIVVTHD 511
Cdd:PRK15064 140 LGVGIPEEQH-YGLmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTirwLEDVLN-----ERNSTMIIISHD 211
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
157-308 |
6.35e-03 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 38.96 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 157 FILWVTPFLffsamvpmlmgKKVRNIA----SIAQNNQSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEV 232
Cdd:cd18571 154 YILWILLFL-----------KKRKKLDykrfDLSSENQSKLIELIN----GMQEIKLNNSERQKRWEWERIQAKLFKINI 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446589027 233 KKTMMQHCIGVVGTVIETGAYIVVLIIGAQKIMKGEMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18571 219 KSLKLDQYQQIGALFINQLKNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
252-308 |
7.07e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 38.70 E-value: 7.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446589027 252 AYIVVLIIGAQKIMKG------EMEVGALVAVLATIEMLFFPVRYVGDLLMMTQVAAASANRV 308
Cdd:cd18565 251 GFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
30-277 |
7.31e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 38.72 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 30 ILNLSRPLFMGLIVDNLI-QRELKAAYVYIALFAGSRLLMWVNNLSFDYVSSKASQRILRKKRIYVLRHFFLLPFEESEK 108
Cdd:cd18566 16 ILALATPLFILQVYDRVIpNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 109 IKQG-------ELETL----------VVSDIPnWVRLYGSILIeyihaiaqFIGAFIALQHIDMKFIlwvtpFLFFSAMV 171
Cdd:cd18566 96 EPSGahlerlnSLEQIrefltgqallALLDLP-FVLIFLGLIW--------YLGGKLVLVPLVLLGL-----FVLVAILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446589027 172 PMLMGKKVRNIASIAQNNQSSVVEMVSqfvkGVQDLRSLQKEKWAIRLFKGVTAQSYKTEVKKTMMQHCIGVVGTVIETG 251
Cdd:cd18566 162 GPILRRALKERSRADERRQNFLIETLT----GIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQV 237
|
250 260
....*....|....*....|....*.
gi 446589027 252 AYIVVLIIGAQKIMKGEMEVGALVAV 277
Cdd:cd18566 238 SMVAVVAFGALLVINGDLTVGALIAC 263
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