|
Name |
Accession |
Description |
Interval |
E-value |
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
5-549 |
0e+00 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 932.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 5 KRGAIRELLALLR-PFRAIVAVSIALGMAGGLAITLLLASINNALHSENGLGQGVLLSFGGLCLLALVSSIVSDIGTSYV 83
Cdd:TIGR01194 1 KKAAIGEILALLRsPFPAITAFSIALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFGGLCLLALLFRIGADIFPAYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 84 GQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVV 163
Cdd:TIGR01194 81 GMHIIANLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 164 AIVIGTAAQYLARSRGFKGFYAARDLEDELQKHYTAIASGAKELRIHRPRRYRMHTGRISETANNIRDLHISSINIFILA 243
Cdd:TIGR01194 161 AIIIGTAAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIRRLSFAHGAIQESANNIADLHIIEILIFIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 244 KTFGSMLFFVVIGLALTLQAYWPSSNPAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAELSERFSSPEPHLLL 323
Cdd:TIGR01194 241 ENFGQLLFFLLIGCALFAAAMFASIDAAAISAFVLALLYIKGPLEMLVSALPILAQAQIACQRLADFGERFNEPEPELEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 324 SEQE-----APDKTVDSLELRDVRYSPPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEIL 398
Cdd:TIGR01194 321 SDADnvlllAHDKSVDSIELKDVHMNPKAPEGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 399 LNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQ---GKQASLQNATQYLQRLEIAHKVSVMDGNFS-TTDLSTGQRKRLA 474
Cdd:TIGR01194 401 LDGAAVSADSRDDYRDLFSAIFADFHLFDDLIGpdeGEHASLDNAQQYLQRLEIADKVKIEDGGFStTTALSTGQQKRLA 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 475 LINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKETETA 549
Cdd:TIGR01194 481 LICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCIVKDTECA 555
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-549 |
0e+00 |
|
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: 739.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 9 IRELLALLRPFRAIVAVSIALGMAGGLAITLLLASINNALHSENGLGQGVLLSFGGLCLLALVSSIVSDIGTSYVGQHII 88
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 89 AKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIG 168
Cdd:COG4615 81 ARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 169 TAAQYLARSRGFKGFYAARDLEDELQKHYTAIASGAKELRIHRPRRYRMHTGRISETANNIRDLHISSINIFILAKTFGS 248
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 249 MLFFVVIGLALTLQAYWPSSNPAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAELSERFSSPEPHLLLSEQEA 328
Cdd:COG4615 241 LLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 329 PDKTVDSLELRDVRYSPPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAET 408
Cdd:COG4615 321 APADFQTLELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 409 RDDYRQLFSTIFADYYLFDDLVQGKQASL-QNATQYLQRLEIAHKVSVMDGNFSTTDLSTGQRKRLALINAWLEERPVLV 487
Cdd:COG4615 401 REAYRQLFSAVFSDFHLFDRLLGLDGEADpARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPILV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 488 FDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKETETA 549
Cdd:COG4615 481 FDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-541 |
4.46e-135 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 403.20 E-value: 4.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 18 PFRAIVAVSIAlgmAGGLAItLLLASINNALHSENGLGQGVLLSFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGE 97
Cdd:PRK10522 14 PFISVMALSLA---SAALGI-GLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFVYRLRSEFIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 98 KVLSAPIEQIERYRTHRLIPVLTHDIDTISdFSFSFTP-LAIALTITFGCLGYLAYLSVPMFLLTVVAIVIGTAAQYLAR 176
Cdd:PRK10522 90 RILDTHVERIEQLGSASLLASLTSDVRNIT-IAFVRLPeLVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVTIWGGFVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 177 SRGFKGFYAARDLEDELQKHYTAIASGAKELRIHRPRRYRMHTGRISETANNIRDlHISSINIF-ILAKTFGSMLFFVVI 255
Cdd:PRK10522 169 ARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPDAQEYRH-HIIRADTFhLSAVNWSNIMMLGAI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 256 GLA--LTLQAYWPSSNPAAItgFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAEL-----SERFSSPEPHlllseqea 328
Cdd:PRK10522 248 GLVfyMANSLGWADTNVAAT--YSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKLalapyKAEFPRPQAF-------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 329 pdKTVDSLELRDVRYSPPAvegsEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAET 408
Cdd:PRK10522 318 --PDWQTLELRNVTFAYQD----NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 409 RDDYRQLFSTIFADYYLFDDLV--QGKQASLQNATQYLQRLEIAHKVSVMDGNFSTTDLSTGQRKRLALINAWLEERPVL 486
Cdd:PRK10522 392 PEDYRKLFSAVFTDFHLFDQLLgpEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDIL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 487 VFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGK 541
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-543 |
1.37e-67 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 228.90 E-value: 1.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 1 MTNPKRGAIRELLALLRPFRAIVAVSIALGMAG---GLAITLLLASINNALHSENGLGQ--GVLLSFGGLCLLALVSSIV 75
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSallELLLPLLLGRIIDALLAGGDLSAllLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 76 SDIGTSYVGQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITF-GCLGYLAYLS 154
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLiGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 155 VPMFLLTVVAIVIGTAAQYLARSRGFKGFYAARDLEDELQKHYTAIASGAKELRIHRPRRYRMHtgRISETANNIRDLHI 234
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELE--RFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 235 SSINIFILAKTFGSMLFFVVIGLALTLQAYWPSSN---PAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAELs 311
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGsltVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 312 erFSSPEPHLLLSEQEAPDKTVDSLELRDVRYS----PPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLL 387
Cdd:COG1132 318 --LDEPPEIPDPPGAVPLPPVRGEIEFENVSFSypgdRPVLKD--------ISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 388 GLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQ-----GK-QASLQ---------NATQYLQRLEiahk 452
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIReniryGRpDATDEeveeaakaaQAHEFIEALP---- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 453 vsvmDGnFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDP--------AFRRVfytellpdlkRQGKTI 518
Cdd:COG1132 464 ----DG-YDTvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTetealiqeALERL----------MKGRTT 528
|
570 580
....*....|....*....|....*..
gi 259663656 519 IVISHddRY--FEMADQLIRLSAGKVV 543
Cdd:COG1132 529 IVIAH--RLstIRNADRILVLDDGRIV 553
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-543 |
4.05e-50 |
|
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: 183.50 E-value: 4.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 3 NPKRGAIRELLALLRPFRAIVAVSIALGMAG---GLAITLLLASI------NNALHSENGLGQGVLLSFGGLCLLALVSS 73
Cdd:COG2274 138 GEKPFGLRWFLRLLRRYRRLLLQVLLASLLInllALATPLFTQVVidrvlpNQDLSTLWVLAIGLLLALLFEGLLRLLRS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 74 IVSDigtsYVGQHIIAKLRKELGEKVLSAPIEQIERYRT----HRLipvltHDIDTISDF---SFSFTPLAIALTITFgc 146
Cdd:COG2274 218 YLLL----RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVgdlaSRF-----RDVESIREFltgSLLTALLDLLFVLIF-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 147 LGYLAYLSVPMFLLTVVAIVIGTAAQYLARSRGFKGFYAARDLEDELQKHYTAIASGAKELRI-----HRPRRYRMHTGR 221
Cdd:COG2274 287 LIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKAlgaesRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 222 ISETANNIRDLHISSINIFILAKTFGSMLFFV-----VIGLALTLqaywpssnpAAITGFVMVLLYMKGPLEQVVTILPI 296
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATVALLWlgaylVIDGQLTL---------GQLIAFNILSGRFLAPVAQLIGLLQR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 297 VSRAQVAFQRVAELSErfSSPEPHLLLSEQEAPDKTvDSLELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENG 376
Cdd:COG2274 438 FQDAKIALERLDDILD--LPPEREEGRSKLSLPRLK-GDIELENVSFRYP---GDSPPVLDNISLTIKPGERVAIVGRSG 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 377 CGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDD------LVQGKQASLQNATQYLQRLEIA 450
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGtireniTLGDPDATDEEIIEAARLAGLH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 451 HKVSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFyTELLPDLkRQGKTIIVISHD 524
Cdd:COG2274 592 DFIEALPMGYDTvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII-LENLRRL-LKGRTVIIIAHR 669
|
570
....*....|....*....
gi 259663656 525 DRYFEMADQLIRLSAGKVV 543
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIV 688
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-545 |
1.61e-42 |
|
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: 159.92 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 5 KRGAIRELLALLRPFRAIVAVSIALGMAGGLAI---TLLLAS-INNALHSENGLGQgVLLSFGGLCLLALV---SSIVSD 77
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIiaqAWLLASlLAGLIIGGAPLSA-LLPLLGLLLAVLLLralLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 78 IGTSYVGQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTP-LAIALTITFGCLGYLAYLSVP 156
Cdd:COG4988 80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPqLFLAALVPLLILVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 157 ---MFLLTVVAIV-----IGTAAQYLARSRgFKGFYA-ARDLEDELQkhytaiasGAKELRIHRprRYRMHTGRISETAN 227
Cdd:COG4988 160 sglILLVTAPLIPlfmilVGKGAAKASRRQ-WRALARlSGHFLDRLR--------GLTTLKLFG--RAKAEAERIAEASE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 228 NIR-----------------DLhISSINIFILAKTFGsmlfFVVIGLALTLQaywpssnpaaiTGFVMVLL----YMkgP 286
Cdd:COG4988 229 DFRkrtmkvlrvaflssavlEF-FASLSIALVAVYIG----FRLLGGSLTLF-----------AALFVLLLapefFL--P 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 287 LEQVVTILPIVSRAQVAFQRVAELserFSSPEPHLLLSEQEAPDKTVDSLELRDVRYSPPAvegsEPFHLGPINLRIAQG 366
Cdd:COG4988 291 LRDLGSFYHARANGIAAAEKIFAL---LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPG----GRPALDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 367 DIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDD------LVQGKQASLQNA 440
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGtirenlRLGRPDASDEEL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 441 TQYLQRLEIAHKVSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPdlKRQ 514
Cdd:COG4988 444 EAALEAAGLDEFVAALPDGLDTplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR--LAK 521
|
570 580 590
....*....|....*....|....*....|.
gi 259663656 515 GKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
336-541 |
8.06e-40 |
|
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: 142.52 E-value: 8.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:cd03228 1 IEFKNVSFSYP---GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDlvqgkqaslqnatqylqrleiahkvSVMDgNFsttdLSTGQRKRLALINAWLEERPVLVFDEWAADQ 495
Cdd:cd03228 78 IAYVPQDPFLFSG-------------------------TIRE-NI----LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 259663656 496 DPAFRRVFYTELLPdlKRQGKTIIVISHDDRYFEMADQLIRLSAGK 541
Cdd:cd03228 128 DPETEALILEALRA--LAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-541 |
1.63e-38 |
|
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: 140.29 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 337 ELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLF 416
Cdd:cd03225 1 ELKNLSFSYP---DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 417 STIF--ADYYLF-----DDLVQG-------KQASLQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEE 482
Cdd:cd03225 78 GLVFqnPDDQFFgptveEEVAFGlenlglpEEEIEERVEEALELVGLEGLR-----DRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 483 RPVLVFDEWAADQDPAFRRVFyTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGK 541
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-549 |
2.31e-38 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 140.55 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYS----PPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD 411
Cdd:COG1122 1 IELENLSFSypggTPALDD--------VSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YRQLFSTIF--ADYYLF-----DDLVQG-------KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALIN 477
Cdd:COG1122 73 LRRKVGLVFqnPDDQLFaptveEDVAFGpenlglpREEIRERVEEALELVGLEHL-----ADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 478 AWLEERPVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKETETA 549
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELL-ELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
336-542 |
4.65e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 124.05 E-value: 4.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDV--RY-SPPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAEtRDDY 412
Cdd:cd03230 1 IEVRNLskRYgKKTALDD--------ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE-PEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFADYYLFDDLvqgkqaslqNATQYLqrleiahkvsvmdgnfsttDLSTGQRKRLALINAWLEERPVLVFDEWA 492
Cdd:cd03230 72 KRRIGYLPEEPSLYENL---------TVRENL-------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 259663656 493 ADQDPAFRRVFYtELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:cd03230 124 SGLDPESRREFW-ELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
356-541 |
5.93e-31 |
|
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: 117.73 E-value: 5.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFadyylfddlvqgkqa 435
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 slqnatqylqrleiahkvsvmdgnfsttDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRvFYTELLPDLKRQG 515
Cdd:cd00267 80 ----------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE-RLLELLRELAEEG 130
|
170 180
....*....|....*....|....*..
gi 259663656 516 KTIIVISHDDRYFEMA-DQLIRLSAGK 541
Cdd:cd00267 131 RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
359-543 |
9.98e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.90 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETR---------DDYRQLFS-TIFADYYLFDD 428
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigyvmqDVDYQLFTdSVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 LVQGKQaslQNATQYLQRLEIAHKvsvMDGNfsTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPA-FRRVfyTEL 507
Cdd:cd03226 99 ELDAGN---EQAETVLKDLDLYAL---KERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnMERV--GEL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 259663656 508 LPDLKRQGKTIIVISHDDRY-FEMADQLIRLSAGKVV 543
Cdd:cd03226 169 IRELAAQGKAVIVITHDYEFlAKVCDRVLLLANGAIV 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-537 |
4.04e-30 |
|
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: 123.94 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 20 RAIVAVSIALGMAGGLAI---TLLLASINNALHSENGLGQGVLLSFGGLCLLALVSSIVSdIGTSYVGQH----IIAKLR 92
Cdd:TIGR02857 2 RRALALLALLGVLGALLIiaqAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLG-WLQERAAARaaaaVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 93 KELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF---------SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVV 163
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYfarylpqlvLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 164 AIVIGTAAQYLARSRgFKGFyaardleDELQKHYTAIASGAKELRIHRprRYRMHTGRISETANNIRD-----LHISSIN 238
Cdd:TIGR02857 161 MILIGWAAQAAARKQ-WAAL-------SRLSGHFLDRLRGLPTLKLFG--RAKAQAAAIRRSSEEYRErtmrvLRIAFLS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 239 IFIL--AKTFGSMLFFVVIGLAL-----TLQaywpssnpaaiTGFVMVLL----YMkgPLEQVVTILPIVSRAQVAFQRV 307
Cdd:TIGR02857 231 SAVLelFATLSVALVAVYIGFRLlagdlDLA-----------TGLFVLLLapefYL--PLRQLGAQYHARADGVAAAEAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 308 AELSERFSSPEPhlllSEQEAPDKTVDSLELRDVRYSPPaveGSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLL 387
Cdd:TIGR02857 298 FAVLDAAPRPLA----GKAPVTAAPASSLEFSGVSVAYP---GRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 388 GLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLV---------QGKQASLQNAtqyLQRLEIAHKVSVMDG 458
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIaenirlarpDASDAEIREA---LERAGLDEFVAALPQ 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 459 NFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPdlKRQGKTIIVISHDDRYFEMAD 532
Cdd:TIGR02857 447 GLDTpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGRTVLLVTHRLALAALAD 524
|
....*
gi 259663656 533 QLIRL 537
Cdd:TIGR02857 525 RIVVL 529
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
336-547 |
6.62e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.07 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPavEGSEPFH-LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA---ETRDD 411
Cdd:COG1136 5 LELRNLTKSYG--TGEGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlseRELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YR-QLFSTIFADYYLFDDL-----V--------QGKQASLQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRL---- 473
Cdd:COG1136 83 LRrRHIGFVFQFFNLLPELtalenValplllagVSRKERRERARELLERVGLGDRL-----DHRPSQLSGGQQQRVaiar 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 474 ALINawleeRPVLVF-DE--WAADQDPAfRRVFytELLPDL-KRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKETE 547
Cdd:COG1136 158 ALVN-----RPKLILaDEptGNLDSKTG-EEVL--ELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-542 |
9.77e-30 |
|
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: 116.44 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPavEGSEPFH-LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDD 411
Cdd:cd03255 1 IELKNLSKTYG--GGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YR-QLFSTIFADYYLFDDL-----------VQGKQAS--LQNATQYLQRLEIAHKVSVMdgnfsTTDLSTGQRKRLALIN 477
Cdd:cd03255 79 FRrRHIGFVFQSFNLLPDLtalenvelpllLAGVPKKerRERAEELLERVGLGDRLNHY-----PSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 478 AWLEERPVLVFDEWAADQDPAFRRVFYtELLPDLKRQ-GKTIIVISHDDRYFEMADQLIRLSAGKV 542
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVM-ELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
336-545 |
3.97e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.16 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDV--RYSP-PAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAEtRDDY 412
Cdd:COG1131 1 IEVRGLtkRYGDkTALDG--------VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFADYYLFDDL--------------VQGKQASlQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINA 478
Cdd:COG1131 72 RRRIGYVPQEPALYPDLtvrenlrffarlygLPRKEAR-ERIDELLELFGLTDA-----ADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259663656 479 WLEERPVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHddrYFE----MADQLIRLSAGKVVKE 545
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELW-ELLRELAAEGKTVLLSTH---YLEeaerLCDRVAIIDKGRIVAD 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
336-545 |
8.77e-29 |
|
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: 114.14 E-value: 8.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppavEGSEPFHLGpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:cd03261 1 IELRGLTKS----FGGRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 ---FSTIFADYYLFDDLvqgkqASLQN-------------------ATQYLQRLEIAHKVSVMDGnfsttDLSTGQRKRL 473
Cdd:cd03261 76 rrrMGMLFQSGALFDSL-----TVFENvafplrehtrlseeeireiVLEKLEAVGLRGAEDLYPA-----ELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 474 ALINAWLEERPVLVFDEWAADQDPAFRRVFyTELLPDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVI-DDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAE 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
356-541 |
2.14e-28 |
|
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: 112.19 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVsAETRDDYRQLFSTIFADYYLFDDL------ 429
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPELtvrenl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 -----VQGKQASLQNATQYLQRLEIAHkvsVMDGNFSTtdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFY 504
Cdd:COG4133 97 rfwaaLYGLRADREAIDEALEAVGLAG---LADLPVRQ--LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 259663656 505 tELLPDLKRQGKTIIVISHDDRYFEmADQLIRLSAGK 541
Cdd:COG4133 172 -ELIAAHLARGGAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-493 |
3.24e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 110.04 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLF------DDL 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFprltvrENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 430 VQG-------KQASLQNATQYLQRLEIAHKV-SVMDGNFSTtdLSTGQRKRLALINAWLEERPVLVFDEWAA 493
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEKLGLGDLAdRPVGERPGT--LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
356-543 |
9.67e-28 |
|
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: 111.49 E-value: 9.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFStIFADYYLFDDL------ 429
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-LPDERGLYDRLtvreni 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 --------VQGKQASLQnATQYLQRLEIahkVSVMDGNFSTtdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRR 501
Cdd:COG4555 96 ryfaelygLFDEELKKR-IEELIELLGL---EEFLDRRVGE--LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 259663656 502 VFYTELLpDLKRQGKTIIVISHDdrYFEMA---DQLIRLSAGKVV 543
Cdd:COG4555 170 LLREILR-ALKKEGKTVLFSSHI--MQEVEalcDRVVILHKGKVV 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
87-524 |
2.31e-27 |
|
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: 115.92 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 87 IIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSF-SFTPLAIALTITFGCLGYLAYLSVP-------MF 158
Cdd:TIGR02868 84 SLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVrVIVPAGVALVVGAAAVAAIAVLSVPaalilaaGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 159 LLTVVAI------VIGTAAQYLARSRGfkgfYAARDLEDELQKHYTAIASGAKELRIHRPRRYRMHTGRISETANNIRDL 232
Cdd:TIGR02868 164 LLAGFVAplvslrAARAAEQALARLRG----ELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 233 HISSINIFILAKTFGSMLFFVVIGLALTLqaywpssNPAAITGFVMVLLymkgPLEQVVTILPIVS----RAQVAFQRVA 308
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAVADGRL-------APVTLAVLVLLPL----AAFEAFAALPAAAqqltRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 309 ELsERFSSPEPHLLLSEQEAPDKTVDSLELRDVRYSPPaveGSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLG 388
Cdd:TIGR02868 309 EV-LDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP---GAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 389 LYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQG------KQASLQNATQYLQRLEIAHKVSVMDGNFST 462
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVREnlrlarPDATDEELWAALERVGLADWLRALPDGLDT 463
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 463 ------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRvfytELLPDLKR--QGKTIIVISHD 524
Cdd:TIGR02868 464 vlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD----ELLEDLLAalSGRTVVLITHH 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-542 |
6.92e-27 |
|
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: 106.92 E-value: 6.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:cd03246 1 LEVENVSFRYP---GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDlvqgkqaslqnatqylqrleiahkvSVMDgNFsttdLSTGQRKRLALINAWLEERPVLVFDEWAADQ 495
Cdd:cd03246 78 VGYLPQDDELFSG-------------------------SIAE-NI----LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 259663656 496 DPAFRRVfYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKV 542
Cdd:cd03246 128 DVEGERA-LNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
356-545 |
1.14e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.37 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFStifadyYLfddlvqgkqa 435
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA------YV---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 slqnaTQYLQRLEIAHKVsvmDGNFSTtdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAfRRVFYTELLPDLKRQ- 514
Cdd:cd03214 79 -----PQALELLGLAHLA---DRPFNE--LSGGERQRVLLARALAQEPPILLLDEPTSHLDIA-HQIELLELLRRLAREr 147
|
170 180 190
....*....|....*....|....*....|..
gi 259663656 515 GKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03214 148 GKTVVMVLHDlNLAARYADRVILLKDGRIVAQ 179
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
359-545 |
3.23e-26 |
|
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: 106.93 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLF------------ 426
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFsgtimenirlgr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 ----DDLVQgKQASLQNATQYLQRLEIAHKVSVMDGNfstTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAfrrv 502
Cdd:cd03254 102 pnatDEEVI-EAAKEAGAHDFIMKLPNGYDTVLGENG---GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE---- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 259663656 503 fyTELL--PDLKR--QGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03254 174 --TEKLiqEALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
336-545 |
2.77e-25 |
|
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: 103.71 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPavEGSEPFH-LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDdyrq 414
Cdd:cd03293 1 LEVRNVSKTYG--GGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 415 lFSTIFADYYLFDDL-----------VQG--KQASLQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLE 481
Cdd:cd03293 75 -RGYVFQQDALLPWLtvldnvalgleLQGvpKAEARERAEELLELVGLSGFE-----NAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 482 ERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSA--GKVVKE 545
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDiDEAVFLADRVVVLSArpGRIVAE 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-543 |
1.11e-24 |
|
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: 102.75 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDDYRQLFSTIFADYYLFDDL-Vqgkq 434
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRIGMLFQGGALFDSLtV---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 435 asLQNATQYLQRL------EIAHKVSVM--------DGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFR 500
Cdd:COG1127 100 --FENVAFPLREHtdlseaEIRELVLEKlelvglpgAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 259663656 501 RVFYtELLPDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:COG1127 178 AVID-ELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
354-543 |
1.82e-24 |
|
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: 101.44 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 354 FHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS---AETRDdyrqlFSTIFADYYLFDDL- 429
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgvpPERRN-----IGMVFQDYALFPHLt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQ------------GKQASLQNATQYLQRLEIAHkvsvmDGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDP 497
Cdd:cd03259 89 VAeniafglklrgvPKAEIRARVRELLELVGLEG-----LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 259663656 498 AFRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:cd03259 164 KLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRIV 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
359-543 |
1.08e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.89 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY------RQLFStifaDYYLFDDLVQ- 431
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpeeRGLYP----KMKVIDQLVYl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 ------GKQASLQNATQYLQRLEIAHKVSVmdgnfSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYT 505
Cdd:cd03269 95 aqlkglKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 259663656 506 ELLpDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:cd03269 170 VIR-ELARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
359-541 |
1.40e-23 |
|
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: 97.64 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD--DYRQLFSTIFADYYLFddlvqgkqas 436
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALF---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 437 lqnatqylQRLEIAHKVsvmdgnfsTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFyTELLPDLKRQ-G 515
Cdd:cd03229 89 --------PHLTVLENI--------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV-RALLKSLQAQlG 151
|
170 180
....*....|....*....|....*..
gi 259663656 516 KTIIVISHD-DRYFEMADQLIRLSAGK 541
Cdd:cd03229 152 ITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
336-545 |
1.52e-23 |
|
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: 97.11 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:cd03216 1 LELRGITKRFGGVKA-----LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 -FSTIFadyylfddlvQgkqaslqnatqylqrleiahkvsvmdgnfsttdLSTGQRKRLALINAWLEERPVLVFDEWAAD 494
Cdd:cd03216 76 gIAMVY----------Q---------------------------------LSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 495 QDPA-FRRVFytELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03216 113 LTPAeVERLF--KVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
304-543 |
1.66e-23 |
|
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: 103.83 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 304 FQRVAELSERFSSPEPHLLLSEQEAPDKTVdsLELRDVRYS--------PPAVEGsepfhlgpINLRIAQGDIVFIVGEN 375
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPL--LEVRNLSKRypvrgkggVRAVDD--------VSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 376 GCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTI---FADYY--------LFDDLVQG--------KQAS 436
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVqmvFQDPYsslnprmtVGDIIAEPlrlhgllsRAER 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 437 LQNATQYLQRL----EIAHKvsvmdgnfSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFyTELLPDLK 512
Cdd:COG1123 381 RERVAELLERVglppDLADR--------YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI-LNLLRDLQ 451
|
250 260 270
....*....|....*....|....*....|...
gi 259663656 513 RQ-GKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:COG1123 452 RElGLTYLFISHDlAVVRYIADRVAVMYDGRIV 484
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-543 |
2.93e-23 |
|
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: 98.05 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 334 DSLELRDVRYSPPAVEGSEpfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYR 413
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPA---LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 QLFSTIFADYYLF-----DDLVQGKQ----------ASLQNATQYLQRLEIAHKVSVMDGNFSttdLSTGQRKRLALINA 478
Cdd:cd03245 78 RNIGYVPQDVTLFygtlrDNITLGAPladderilraAELAGVTDFVNKHPNGLDLQIGERGRG---LSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 479 WLEERPVLVFDEWAADQDPAFRRVFYTELlpDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-524 |
1.45e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 96.06 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 341 VRYS-PPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAET--------RDD 411
Cdd:cd03235 7 VSYGgHPVLED--------VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvpqRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YRQLF---------STIFADYYLFDDLvqgKQASLQNATQYLQRLEIAHKVsvmDGNFSTtdLSTGQRKRLALINAWLEE 482
Cdd:cd03235 79 IDRDFpisvrdvvlMGLYGHKGLFRRL---SKADKAKVDEALERVGLSELA---DRQIGE--LSGGQQQRVLLARALVQD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 483 RPVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHD 524
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIY-ELLRELRREGMTILVVTHD 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
336-543 |
8.82e-22 |
|
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: 93.71 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppavEGSEPFHLgpiNLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAEtrDDYRQL 415
Cdd:cd03298 1 VRLDKIRFS----YGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDLV------QGKQASLQNATQYLQRLEIAHKVSVMDGNFS--TTDLSTGQRKRLALINAWLEERPVLV 487
Cdd:cd03298 72 VSMLFQENNLFAHLTveqnvgLGLSPGLKLTAEDRQAIEVALARVGLAGLEKrlPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 488 FDEWAADQDPAfRRVFYTELLPDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:cd03298 152 LDEPFAALDPA-LRAEMLDLVLDLHAEtKMTVLMVTHQpEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
359-545 |
9.24e-22 |
|
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: 94.04 E-value: 9.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL-----F--STIFAD--------- 422
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrtFqiPRLFPEltvlenvmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 423 --------YYLFDDLVQGKQASLQNATQYLQRLEIAHKVSVMDGNfsttdLSTGQRKRLALINAwLEERP-VLVFDEWAA 493
Cdd:cd03219 99 aaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARA-LATDPkLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 494 DQDPAFRRVFyTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03219 173 GLNPEETEEL-AELIRELRERGITVLLVEHDmDVVMSLADRVTVLDQGRVIAE 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-549 |
1.11e-21 |
|
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: 98.44 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQ---SGEILLNGEPVSAETRDDY 412
Cdd:COG1123 5 LEVRDLSVRYP---GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFAD-------YYLFDDLVQGKQASLQNATQYLQR-LEIAHKVSVMD-GNFSTTDLSTGQRKRLALINAWLEER 483
Cdd:COG1123 82 GRRIGMVFQDpmtqlnpVTVGDQIAEALENLGLSRAEARARvLELLEAVGLERrLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 484 PVLVFDEWAADQDPAFRRVFYtELLPDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKVVKETETA 549
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEIL-DLLRELQRErGTTVLLITHDlGVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
337-544 |
1.37e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.67 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 337 ELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLF 416
Cdd:PRK13632 9 KVENVSFSYP---NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 417 STIFAD-------YYLFDDLVQGkqasLQNatQYLQRLEI-------AHKVSvMDG--NFSTTDLSTGQRKRLAlINAWL 480
Cdd:PRK13632 86 GIIFQNpdnqfigATVEDDIAFG----LEN--KKVPPKKMkdiiddlAKKVG-MEDylDKEPQNLSGGQKQRVA-IASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 481 EERP-VLVFDEWAADQDPAFRRVFYtELLPDLKRQG-KTIIVISHDDRYFEMADQLIRLSAGKVVK 544
Cdd:PRK13632 158 ALNPeIIIFDESTSMLDPKGKREIK-KIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIA 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-545 |
1.83e-21 |
|
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: 91.61 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSaETRDDYRQL 415
Cdd:cd03247 1 LSINNVSFSYP---EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-DLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDlvqgkqaSLQNatqylqrleiahkvsvmdgNFSTTdLSTGQRKRLALINAWLEERPVLVFDEWAADQ 495
Cdd:cd03247 77 ISVLNQRPYLFDT-------TLRN-------------------NLGRR-FSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 259663656 496 DPAFRRVFYTELLPDLKrqGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03247 130 DPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
359-542 |
4.45e-21 |
|
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: 91.82 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD--DYRQLFSTIFADYYLFDDL------- 429
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHLtvlenit 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 -----VQG--KQASLQNATQYLQRLEIAHKVSVMDGNfsttdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRR- 501
Cdd:cd03262 99 lapikVKGmsKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGe 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 502 VFytELLPDLKRQGKTIIVISHDDRY-FEMADQLIRLSAGKV 542
Cdd:cd03262 174 VL--DVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
336-543 |
9.58e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.35 E-value: 9.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppavEGSEPFHlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAetRDDYRQL 415
Cdd:COG3840 2 LRLDDLTYR----YGDFPLR---FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA--LPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDL-VQ-----GKQASLQ-NATQYLQRLEIAHKVSVMD-GNFSTTDLSTGQRKRLALINAWLEERPVLV 487
Cdd:COG3840 73 VSMLFQENNLFPHLtVAqniglGLRPGLKlTAEQRAQVEQALERVGLAGlLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 488 FDEWAADQDPAFRRVFYTeLLPDL-KRQGKTIIVISH---DDRYFemADQLIRLSAGKVV 543
Cdd:COG3840 153 LDEPFSALDPALRQEMLD-LVDELcRERGLTVLMVTHdpeDAARI--ADRVLLVADGRIA 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
336-543 |
1.55e-20 |
|
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: 90.64 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDDY 412
Cdd:cd03257 2 LEVKNLSVSFP-TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFADYY-----------LFDDLVQGKQASLQNATQYLQRLEIAHKVSvMDGNFST---TDLSTGQRKRLALINA 478
Cdd:cd03257 81 RKEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLLVGVG-LPEEVLNrypHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 479 WLEERPVLVFDEWAADQDPAFRRvFYTELLPDLKRQ-GKTIIVISHDdryF----EMADQLIRLSAGKVV 543
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQA-QILDLLKKLQEElGLTLLFITHD---LgvvaKIADRVAVMYAGKIV 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
336-545 |
2.60e-20 |
|
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: 89.98 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppaVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:cd03251 1 VEFKNVTFR---YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDLVQ-----GKQ----------ASLQNATQYLQRLEIAHKVSVMDgnfSTTDLSTGQRKRLALINAWL 480
Cdd:cd03251 78 IGLVSQDVFLFNDTVAeniayGRPgatreeveeaARAANAHEFIMELPEGYDTVIGE---RGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 481 EERPVLVFDEWAADQDPAFRRVFYTELlpDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAAL--ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
359-543 |
5.09e-20 |
|
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: 90.01 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL----FSTIFADYYLFDDL----- 429
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHRtvlen 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 ------VQG--KQASLQNATQYLQRLEIAHkvsvmDGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRR 501
Cdd:cd03294 123 vafgleVQGvpRAEREERAAEALELVGLEG-----WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 259663656 502 VFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLV 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
65-544 |
5.41e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.02 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 65 LCLLALVSSIVSDIGT---SYVGQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIAL 140
Cdd:TIGR00958 207 MCLLSIASSVSAGLRGgsfNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRsLSLNVNVLLRNL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 141 TITFGCLGYLAYLSVPMFLLTVVAIVIGTAAqylarSRGFKGFYaaRDLEDELQKhytAIA----------SGAKELRI- 209
Cdd:TIGR00958 287 VMLLGLLGFMLWLSPRLTMVTLINLPLVFLA-----EKVFGKRY--QLLSEELQE---AVAkanqvaeealSGMRTVRSf 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 210 ----HRPRRYRmhtGRISETANNIRDLHISSINIFILAKTFGSMLFFVV--IGLALTLQAYWPSSNpaaITGFVMVLLYM 283
Cdd:TIGR00958 357 aaeeGEASRFK---EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVlyYGGQLVLTGKVSSGN---LVSFLLYQEQL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 284 KGPLEQVVTILPIVSRAQVAFQRVAELSERfsspEPHLLLSEQEAPDKTVDSLELRDVRYSPPAvEGSEPFhLGPINLRI 363
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQAVGASEKVFEYLDR----KPNIPLTGTLAPLNLEGLIEFQDVSFSYPN-RPDVPV-LKGLTFTL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 364 AQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQ----------LFSTIFADYYLF------D 427
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRqvalvgqepvLFSGSVRENIAYgltdtpD 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 428 DLVQGkQASLQNATQYLQRLEIAHKVSVMD-GNFsttdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTe 506
Cdd:TIGR00958 585 EEIMA-AAKAANAHDFIMEFPNGYDTEVGEkGSQ----LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE- 658
|
490 500 510
....*....|....*....|....*....|....*...
gi 259663656 507 llpDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVK 544
Cdd:TIGR00958 659 ---SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
356-543 |
5.89e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD--DYRQLFSTIFAD---YYLFDDLV 430
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQDpeqQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 431 QGKQASLQNATqyLQRLEIAHKVsvmDGNFSTTD-----------LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAF 499
Cdd:PRK13638 97 SDIAFSLRNLG--VPEAEITRRV---DEALTLVDaqhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259663656 500 RrvfyTELLPDLKR---QGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:PRK13638 172 R----TQMIAIIRRivaQGNHVIISSHDiDLIYEISDAVYVLRQGQIL 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
356-542 |
6.35e-20 |
|
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: 88.23 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD---YRQLFSTIFADYYLFDDL--- 429
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLPDRnvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 -----------VQGKQASlQNATQYLQRLEIAHKVSVMdgnfsTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPA 498
Cdd:cd03292 97 envafalevtgVPPREIR-KRVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 259663656 499 F-RRVfyTELLPDLKRQGKTIIVISHDDRYFE-MADQLIRLSAGKV 542
Cdd:cd03292 171 TtWEI--MNLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
352-524 |
6.51e-20 |
|
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: 87.48 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 352 EPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD--DYRQLFSTIF--ADYYLF- 426
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGllERRQRVGLVFqdPDDQLFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 ----DDLVQGK----------QASLQNATQYLQRLEIAHKvsvmdgnfSTTDLSTGQRKRLALINAwLEERP-VLVFDEW 491
Cdd:TIGR01166 84 advdQDVAFGPlnlglseaevERRVREALTAVGASGLRER--------PTHCLSGGEKKRVAIAGA-VAMRPdVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 259663656 492 AADQDPAFRRVFyTELLPDLKRQGKTIIVISHD 524
Cdd:TIGR01166 155 TAGLDPAGREQM-LAILRRLRAEGMTVVISTHD 186
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
336-545 |
1.44e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 88.61 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGsePFH-LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDdyrq 414
Cdd:COG1116 8 LELRGVSKRFPTGGG--GVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 415 lFSTIFADYYLFDDL-----------VQG--KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAWLE 481
Cdd:COG1116 82 -RGVVFQEPALLPWLtvldnvalgleLRGvpKAERRERARELLELVGLAGF-----EDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 482 ERPVLVFDEwaadqdP-----AF-RRVFYTELLPDLKRQGKTIIVISHD-DryfE---MADQLIRLSA--GKVVKE 545
Cdd:COG1116 156 DPEVLLMDE------PfgaldALtRERLQDELLRLWQETGKTVLFVTHDvD---EavfLADRVVVLSArpGRIVEE 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
356-545 |
1.52e-19 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 88.18 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFS-----TIFADYYLFDDLV 430
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAyvpqePPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 431 ------------QGKQASLQNATQYLQRLEIAHKVsvmDGNFSTtdLSTGQRKRlalinAWL-----EERPVLVFDEWAA 493
Cdd:COG1120 97 algryphlglfgRPSAEDREAVEEALERTGLEHLA---DRPVDE--LSGGERQR-----VLIaralaQEPPLLLLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 494 DQDPAFR-RVFytELLPDLKR-QGKTIIVISHD----DRYfemADQLIRLSAGKVVKE 545
Cdd:COG1120 167 HLDLAHQlEVL--ELLRRLAReRGRTVVMVLHDlnlaARY---ADRLVLLKDGRIVAQ 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
359-545 |
2.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.25 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFAD-------YYLFDDLVQ 431
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpddqvfsSTVWDDVAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 GKQASLQNATQYLQRLEIAHKVSVMDG--NFSTTDLSTGQRKRLAlINAWLEERP-VLVFDEWAADQDPAFRRVFyTELL 508
Cdd:PRK13647 104 GPVNMGLDKDEVERRVEEALKAVRMWDfrDKPPYHLSYGQKKRVA-IAGVLAMDPdVIVLDEPMAYLDPRGQETL-MEIL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 259663656 509 PDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13647 182 DRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLAE 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-543 |
4.07e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.00 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDV--RY-SPPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS---AET 408
Cdd:COG3842 5 ALELENVskRYgDVTALDD--------VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 409 RDdyrqlFSTIFADYYLFDDL-----------VQG--KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLAL 475
Cdd:COG3842 77 RN-----VGMVFQDYALFPHLtvaenvafglrMRGvpKAEIRARVAELLELVGLEGL-----ADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 476 INAWLEERPVLVFDEwaadqdP-----AFRRV-FYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:COG3842 147 ARALAPEPRVLLLDE------PlsaldAKLREeMREELRRLQRELGITFIYVTHDqEEALALADRIAVMNDGRIE 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
359-543 |
4.22e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY-------------------RQLFSTI 419
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrlallpqhhltpegitvRELVAYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 420 FADYY-LFDDLVQGKQASLQNATQYLQRLEIAHKvsvmdgnfSTTDLSTGQRKR--LALINAwlEERPVLVFDEWAADQD 496
Cdd:PRK11231 101 RSPWLsLWGRLSAEDNARVNQAMEQTRINHLADR--------RLTDLSGGQRQRafLAMVLA--QDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 259663656 497 PAfRRVFYTELLPDLKRQGKTIIVISHD----DRYfemADQLIRLSAGKVV 543
Cdd:PRK11231 171 IN-HQVELMRLMRELNTQGKTVVTVLHDlnqaSRY---CDHLVVLANGHVM 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
340-545 |
5.73e-19 |
|
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: 86.39 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 340 DVRYSPpavegSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTI 419
Cdd:cd03252 7 RFRYKP-----DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 420 FADYYLF-----DDLVQGKQASLQNATQYLQRLEIAHK-VSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLV 487
Cdd:cd03252 82 LQENVLFnrsirDNIALADPGMSMERVIEAAKLAGAHDfISELPEGYDTivgeqgAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 488 FDEWAADQDPAFRRVFYTELLPDLKrqGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
336-545 |
1.20e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.28 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPavEGSEPfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD--DYR 413
Cdd:PRK13639 2 LETRDLKYSYP--DGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 QLFSTIF--ADYYLF-----DDLVQGKQASLQNATQYLQRLEIAHKVSVMDG--NFSTTDLSTGQRKRLAlINAWLEERP 484
Cdd:PRK13639 78 KTVGIVFqnPDDQLFaptveEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGfeNKPPHHLSGGQKKRVA-IAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 485 -VLVFDEWAADQDPAFRRVFyTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13639 157 eIIVLDEPTSGLDPMGASQI-MKLLYDLNKEGITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
356-543 |
1.53e-18 |
|
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: 84.98 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAetRDDYRQLFSTIFADYYLFDDLVQGKQA 435
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVFQNYALFPHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 SLQNATQYLQRLEIAHKVSVM--------DGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTEL 507
Cdd:cd03300 94 AFGLRLKKLPKAEIKERVAEAldlvqlegYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 259663656 508 LPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:cd03300 174 KRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKIQ 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-545 |
1.76e-18 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 89.03 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 17 RPFRAIVAVSIALgMAGGLAITLLLASINNALHSENGLGQGVLLSFGgLCLLALVSSIVSDIGTsYVGQHIIAKLRKELG 96
Cdd:TIGR01846 139 KQFREVLLISLAL-QLFALVTPLLFQVVIDKVLVHRGLSTLSVLALA-MLAVAIFEPALGGLRT-YLFAHLTSRIDVELG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 97 EKV----LSAPIEQIERYRTHRLIPVLtHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIgtaa 171
Cdd:TIGR01846 216 ARLyrhlLGLPLGYFESRRVGDTVARV-RELEQIRNFlTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVC---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 172 qYLARSRGFKGFYAARdLEDELQKHYTAIA------SG-----AKELRIHRPRRYR------MHTGRISETANNIRDLHI 234
Cdd:TIGR01846 291 -YALLSVFVGPILRKR-VEDKFERSAAATSflvesvTGietikATATEPQFQNRWDrqlaayVAASFRVTNLGNIAGQAI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 235 SSINifilAKTFGSMLFF---VVIGLALTlqaywpssnPAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAELS 311
Cdd:TIGR01846 369 ELIQ----KLTFAILLWFgahLVIGGALS---------PGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDIL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 312 ERFSSPEPHLLLSEQEAPDktvdSLELRDV--RYSPPAvegsePFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGL 389
Cdd:TIGR01846 436 NSPTEPRSAGLAALPELRG----AITFENIrfRYAPDS-----PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRL 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 390 YRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLF-----DDLVQGKQASLQNATQYLQRLEIAHK-VSVMDGNFST- 462
Cdd:TIGR01846 507 YTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFsrsirDNIALCNPGAPFEHVIHAAKLAGAHDfISELPQGYNTe 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 463 -----TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELlpDLKRQGKTIIVISHDDRYFEMADQLIRL 537
Cdd:TIGR01846 587 vgekgANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNM--REICRGRTVIIIAHRLSTVRACDRIIVL 664
|
....*...
gi 259663656 538 SAGKVVKE 545
Cdd:TIGR01846 665 EKGQIAES 672
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
359-543 |
1.89e-18 |
|
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: 84.23 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS---AETRDdyrqlFSTIFADYYL------FDDL 429
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlpPKDRD-----IAMVFQNYALyphmtvYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQG-------KQASLQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRV 502
Cdd:cd03301 94 AFGlklrkvpKDEIDERVREVAELLQIEHLL-----DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 259663656 503 FYTELLPDLKRQGKTIIVISHDdrYFE---MADQLIRLSAGKVV 543
Cdd:cd03301 169 MRAELKRLQQRLGTTTIYVTHD--QVEamtMADRIAVMNDGQIQ 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-543 |
2.06e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 10 RELLALLRPFRA--IVAVsIALgMAGGLAITLLLASINNALhsENGLGQG---VL----LSFGGLCLLALVSSIVSDIGT 80
Cdd:PRK11176 14 RRLWPTIAPFKAglIVAG-VAL-ILNAASDTFMLSLLKPLL--DDGFGKAdrsVLkwmpLVVIGLMILRGITSFISSYCI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 81 SYVGQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSftplAIALTITFGclGYLAYLSVPMFL- 159
Cdd:PRK11176 90 SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSG----ALITVVREG--ASIIGLFIMMFYy 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 160 ---LTVVAIVIGTAAQYLAR--SRGFkgfyaaRDLEDELQK---HYTAIAS----GAKELRI---------------HRP 212
Cdd:PRK11176 164 swqLSLILIVIAPIVSIAIRvvSKRF------RNISKNMQNtmgQVTTSAEqmlkGHKEVLIfggqevetkrfdkvsNRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 213 RRYRMHTGRISETANNIRDLhISSINI-FIL-AKTFGSmlffvvIGLALTlqaywpssnPAAITGFVMVLLYMKGPLEQV 290
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQL-IASLALaFVLyAASFPS------VMDTLT---------AGTITVVFSSMIALMRPLKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 291 VTIlpivsRAQvaFQR-VAELSERFSspephLLLSEQEAPDKTVD------SLELRDVRYSPPaveGSEPFHLGPINLRI 363
Cdd:PRK11176 302 TNV-----NAQ--FQRgMAACQTLFA-----ILDLEQEKDEGKRVierakgDIEFRNVTFTYP---GKEVPALRNINFKI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 364 AQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQGKQAslQNATQY 443
Cdd:PRK11176 367 PAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA--YARTEQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 444 LQRLEI------AHK---VSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELl 508
Cdd:PRK11176 445 YSREQIeeaarmAYAmdfINKMDNGLDTvigengVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL- 523
|
570 580 590
....*....|....*....|....*....|....*
gi 259663656 509 pDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:PRK11176 524 -DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-524 |
2.47e-18 |
|
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: 83.71 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDV--RYSP---PAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAEtRD 410
Cdd:cd03263 1 LQIRNLtkTYKKgtkPAVDD--------LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD-RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 411 DYRQLFSTIFADYYLFDDL-----------VQG---KQASlQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALI 476
Cdd:cd03263 72 AARQSLGYCPQFDALFDELtvrehlrfyarLKGlpkSEIK-EEVELLLRVLGLTDKA-----NKRARTLSGGMKRKLSLA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259663656 477 NAWLEERPVLVFDEWAADQDPAFRRVFYTELLpdLKRQGKTIIVISHD 524
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLIL--EVRKGRSIILTTHS 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
368-544 |
2.92e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 368 IVFIVGENGCGKTTLIKLLLGLYRPQSGEI----LLNGEPVSAETRDDY------------RQLFSTIFA--DYYLFDDL 429
Cdd:PRK13631 54 IYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQfpEYQLFKDT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 V------------QGKQASLQNATQYLQRLEIahKVSVMDgnFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDP 497
Cdd:PRK13631 134 IekdimfgpvalgVKKSEAKKLAKFYLNKMGL--DDSYLE--RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259663656 498 AFRRVFyTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:PRK13631 210 KGEHEM-MQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILK 256
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
21-307 |
3.98e-18 |
|
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: 84.91 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLAS-INNALHSEN-GLGQGVLLSFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGEK 98
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLlIDDVIPAGDlSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 99 VLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITF-GCLGYLAYLSVPMFLLTVVAIVIGTAAQYLARS 177
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLiGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 178 RGFKGFYAARDLEDELQKHYTAIASGAKELRIHrpRRYRMHTGRISETANNIRDLHISSINIFILAKTFGSMLFFVVIGL 257
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAF--AAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 258 ALTLQAYWPSSN---PAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd07346 240 VLLYGGYLVLQGsltIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
298-543 |
6.31e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 298 SRAQvAFQRVAELSERFSSPEPHLLLSEQEAPDKTVdsLELRDVRYSppavEGSEPFhLGPINLRIAQGDIVFIVGENGC 377
Cdd:COG0488 281 SRIK-ALEKLEREEPPRRDKTVEIRFPPPERLGKKV--LELEGLSKS----YGDKTL-LDDLSLRIDRGDRIGLIGPNGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 378 GKTTLIKLLLGLYRPQSGEILLnGEPVSAETrddYRQLFSTIFADYYLFDDLVQG-KQASLQNATQYLQRLeiahkvsvm 456
Cdd:COG0488 353 GKSTLLKLLAGELEPDSGTVKL-GETVKIGY---FDQHQEELDPDKTVLDELRDGaPGGTEQEVRGYLGRF--------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 457 dgNFSTTD-------LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFyTELLPDLKrqGkTIIVISHdDRYF- 528
Cdd:COG0488 420 --LFSGDDafkpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL-EEALDDFP--G-TVLLVSH-DRYFl 492
|
250
....*....|....*.
gi 259663656 529 -EMADQLIRLSAGKVV 543
Cdd:COG0488 493 dRVATRILEFEDGGVR 508
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
359-545 |
8.46e-18 |
|
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: 82.66 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQ-----GK 433
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGyniryGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 434 -QASLQNATQYLQRLEIAHKVSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRvfytE 506
Cdd:cd03253 100 pDATDEEVIEAAKAAQIHDKIMRFPDGYDTivgergLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER----E 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 259663656 507 LLPDLKR--QGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03253 176 IQAALRDvsKGRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
359-543 |
1.71e-17 |
|
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: 81.85 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFS---TIFADYYLFDDL------ 429
Cdd:cd03256 20 VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqigMIFQQFNLIERLsvlenv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 ----------VQG-----KQASLQNATQYLQRLEIAHKVSVMDGNfsttdLSTGQRKRLALINAwLEERPVLVF-DEWAA 493
Cdd:cd03256 100 lsgrlgrrstWRSlfglfPKEEKQRALAALERVGLLDKAYQRADQ-----LSGGQQQRVAIARA-LMQQPKLILaDEPVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 494 DQDPAF-RRVFytELLPDL-KRQGKTIIVISHDDRYF-EMADQLIRLSAGKVV 543
Cdd:cd03256 174 SLDPASsRQVM--DLLKRInREEGITVIVSLHQVDLArEYADRIVGLKDGRIV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-540 |
1.83e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDdyRql 415
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPA-LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 fSTIFADYYLF------DDLVQG-------KQASLQNATQYLQR--LEIAHKVSVMdgnfsttDLSTGQRKRLALINAWL 480
Cdd:COG4525 79 -GVVFQKDALLpwlnvlDNVAFGlrlrgvpKAERRARAEELLALvgLADFARRRIW-------QLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 481 EERPVLVFDEWAADQDpAFRRVFYTELLPDL-KRQGKTIIVISHD-DRYFEMADQLIRLSAG 540
Cdd:COG4525 151 ADPRFLLMDEPFGALD-ALTREQMQELLLDVwQRTGKGVFLITHSvEEALFLATRLVVMSPG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-543 |
2.21e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDV--RYSP-PAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD 411
Cdd:COG4152 1 MLELKGLtkRFGDkTAVDD--------VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 ----------YR------QLfstifadYYLfddlvqG------KQASLQNATQYLQRLEIAH----KVSvmdgnfsttDL 465
Cdd:COG4152 73 igylpeerglYPkmkvgeQL-------VYL------ArlkglsKAEAKRRADEWLERLGLGDrankKVE---------EL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 466 STGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLpDLKRQGKTIIVISHDDRYFE-MADQLIRLSAGKVV 543
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIR-ELAAKGTTVIFSSHQMELVEeLCDRIVIINKGRKV 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
359-490 |
2.22e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.62 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAEtRDDYRQ-LFstifadyYLfddlvqGKQASL 437
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQdLL-------YL------GHQPGI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 438 QNATQYLQRLEIAHKVSVMDGNFSTTD-----------------LSTGQRKRLALINAWLEERPVLVFDE 490
Cdd:PRK13538 86 KTELTALENLRFYQRLHGPGDDEALWEalaqvglagfedvpvrqLSAGQQRRVALARLWLTRAPLWILDE 155
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-545 |
2.95e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.99 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYR-- 413
Cdd:PRK13635 6 IRVEHISFRYP---DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 ----------QLFSTIFADYYLF---------DDLVQGKQASLQ--NATQYLQRlEIAHkvsvmdgnfsttdLSTGQRKR 472
Cdd:PRK13635 83 vgmvfqnpdnQFVGATVQDDVAFglenigvprEEMVERVDQALRqvGMEDFLNR-EPHR-------------LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 473 LAlINAWLEERP-VLVFDEWAADQDPAFRRvfytELLP---DLKRQGK-TIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13635 149 VA-IAGVLALQPdIIILDEATSMLDPRGRR----EVLEtvrQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
336-543 |
3.15e-17 |
|
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: 81.19 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDV--RY--SPPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD 411
Cdd:cd03295 1 IEFENVtkRYggGKKAVNN--------LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YRQ----------LFS--TIFADYYLFDDLVQGKQAslqnatQYLQR-LEIAHKVSVMDGNFS---TTDLSTGQRKRLAL 475
Cdd:cd03295 73 LRRkigyviqqigLFPhmTVEENIALVPKLLKWPKE------KIRERaDELLALVGLDPAEFAdryPHELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 476 INAWLEERPVLVFDEWAADQDPAFRRVFYTELLpDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFK-RLQQElGKTIVFVTHDiDEAFRLADRIAIMKNGEIV 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
336-545 |
3.57e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.72 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppaVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:PRK13648 8 IVFKNVSFQ---YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIF--ADYYLFDDLVQGKQA-SLQN---ATQYLQRL--EIAHKVSVMD-GNFSTTDLSTGQRKRLALINAWLEERPVL 486
Cdd:PRK13648 85 IGIVFqnPDNQFVGSIVKYDVAfGLENhavPYDEMHRRvsEALKQVDMLErADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 487 VFDEWAADQDPAFRRVFYtELLPDLKRQGK-TIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13648 165 ILDEATSMLDPDARQNLL-DLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
332-545 |
3.89e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 80.49 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 332 TVDSL--ELRDVRYSPPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETR 409
Cdd:cd03266 3 TADALtkRFRDVKKTVQAVDG--------VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 410 DDYRQL--FSTIFADY---------YLFDDLVQGKQASLQNATQYL-QRLEIAHKVSVmdgnfSTTDLSTGQRKRLALIN 477
Cdd:cd03266 75 EARRRLgfVSDSTGLYdrltarenlEYFAGLYGLKGDELTARLEELaDRLGMEELLDR-----RVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 478 AWLEERPVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-544 |
5.85e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.41 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDVRY--SPpavegSEPFH---LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETR 409
Cdd:PRK13641 2 SIKFENVDYiySP-----GTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 410 D----DYRQLFSTI--FADYYLFDDLV------------QGKQASLQNATQYLQRLEIAHKVSvmdgNFSTTDLSTGQRK 471
Cdd:PRK13641 77 NknlkKLRKKVSLVfqFPEAQLFENTVlkdvefgpknfgFSEDEAKEKALKWLKKVGLSEDLI----SKSPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 472 RLALINAWLEERPVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM-QLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIK 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
359-544 |
6.15e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETrdDYRQLFSTIFADYYLFDDLVQGKQASLQ 438
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 439 NATQYLQRLEIAHKVSVMDG-----NFSTT---DLSTGQRKRLALINAwLEERP-VLVFDEWAADQDPAFRRVFYTELLP 509
Cdd:PRK11607 116 LKQDKLPKAEIASRVNEMLGlvhmqEFAKRkphQLSGGQRQRVALARS-LAKRPkLLLLDEPMGALDKKLRDRMQLEVVD 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 259663656 510 DLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:PRK11607 195 ILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQ 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-543 |
6.26e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 305 QRVAELSERfsspEPHLLLSEQEAPDKTVDSLELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIK 384
Cdd:PRK11160 312 RRINEITEQ----KPEVTFPTTSTAAADQVSLTLNNVSFTYP---DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 385 LLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLF-----DDLVQGK-QASLQNATQYLQRLEIAHKVSVMDG 458
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFsatlrDNLLLAApNASDEALIEVLQQVGLEKLLEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 459 -NFSTTD----LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAF-RRVFytELLPDLKrQGKTIIVISHDDRYFEMAD 532
Cdd:PRK11160 465 lNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQIL--ELLAEHA-QNKTVLMITHRLTGLEQFD 541
|
250
....*....|.
gi 259663656 533 QLIRLSAGKVV 543
Cdd:PRK11160 542 RICVMDNGQII 552
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
328-542 |
8.33e-17 |
|
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: 79.82 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 328 APDKTVDSLELRDVRYSPPavegSEPFH--LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS 405
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYP----TRPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 406 AETRDDYRQLFSTIFADYYLF-----DDLVQG-KQASLQNATQYLQRLEIAHKVSVMDGNFST------TDLSTGQRKRL 473
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFarslqDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 474 ALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQgkTIIVISHDDRYFEMADQLIRLSAGKV 542
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
336-549 |
1.04e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDV--RYSP-PAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY 412
Cdd:COG1129 5 LEMRGIskSFGGvKALDG--------VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQL-FSTIFADYYLFDDL------------VQG----KQASLQNATQYLQRLEI----AHKVSvmdgnfsttDLSTGQRK 471
Cdd:COG1129 77 QAAgIAIIHQELNLVPNLsvaeniflgrepRRGglidWRAMRRRARELLARLGLdidpDTPVG---------DLSVAQQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 472 RLALINAWLEERPVLVFDE-WAADQDPAFRRVFytELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKETETA 549
Cdd:COG1129 148 LVEIARALSRDARVLILDEpTASLTEREVERLF--RIIRRLKAQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGTGPVA 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-545 |
1.33e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPavEGSEPfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV--SAETRDDYR 413
Cdd:PRK13636 6 LKVEELNYNYS--DGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 QLFSTIFA--DYYLF-----DDLVQG-------KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAW 479
Cdd:PRK13636 82 ESVGMVFQdpDNQLFsasvyQDVSFGavnlklpEDEVRKRVDNALKRTGIEHL-----KDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 480 LEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-543 |
1.36e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEV-LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 ----FSTIFADYYLFDDLVQ-------------GKQASLQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINA 478
Cdd:PRK10535 84 rrehFGFIFQRYHLLSHLTAaqnvevpavyaglERKQRLLRAQELLQRLGLEDRV-----EYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 479 WLEERPVLVFDEWAADQDpAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:PRK10535 159 LMNGGQVILADEPTGALD-SHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
23-307 |
1.58e-16 |
|
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: 80.17 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 23 VAVSIALGMAG---GLAITLLLASINNALHSENGLGQGVLLsfggLCLLALVSSIVSDIGT---SYVGQHIIAKLRKELG 96
Cdd:cd18551 1 LILALLLSLLGtaaSLAQPLLVKNLIDALSAGGSSGGLLAL----LVALFLLQAVLSALSSyllGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 97 EKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIGTAAQYLA 175
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELiTSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 176 RSRGFKGFYAARDLEDELQKHYTAIASGAKELRIHRPRRYrmHTGRISETANNIRDLHISSINIFILAKTFGSMLFFVVI 255
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEER--ETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 256 GLALTLQAYWPSSN---PAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd18551 235 LVVLGVGGARVASGaltVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
359-524 |
2.10e-16 |
|
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: 77.92 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVsAETRDDYRQlfstifADYYLfddlvqGKQASLQ 438
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIAR------GLLYL------GHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 439 NATQYLQRLEIAHKVSVMDGNFSTTD--------------LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFY 504
Cdd:cd03231 86 TTLSVLENLRFWHADHSDEQVEEALArvglngfedrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180
....*....|....*....|
gi 259663656 505 TELLPDLKRQGKTIIVISHD 524
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQD 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
359-544 |
4.35e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDdyrqlFSTIFADYYLFDDLVQGKQA 435
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrSIQQRD-----ICMVFQSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 SLQNATQYLQRLEIAHKVsvmDGNFSTTDL-----------STGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFy 504
Cdd:PRK11432 100 GYGLKMLGVPKEERKQRV---KEALELVDLagfedryvdqiSGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 505 TELLPDLKRQ-GKTIIVISHDD-RYFEMADQLIRLSAGKVVK 544
Cdd:PRK11432 176 REKIRELQQQfNITSLYVTHDQsEAFAVSDTVIVMNKGKIMQ 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
336-539 |
6.92e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPpaveGSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:PRK10247 8 LQLQNVGYLA----GDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADYYLFDDLV----------QGKQASLQNATQYLQRLEIAHKVSvmdgNFSTTDLSTGQRKRLALINAwLEERP- 484
Cdd:PRK10247 83 VSYCAQTPTLFGDTVydnlifpwqiRNQQPDPAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRN-LQFMPk 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 485 VLVFDEWAADQDPAFRRVFyTELLPDLKR-QGKTIIVISHDDRYFEMADQLIRLSA 539
Cdd:PRK10247 158 VLLLDEITSALDESNKHNV-NEIIHRYVReQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
336-547 |
1.06e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPavEGSEPfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETR-DDYRQ 414
Cdd:PRK13644 2 IRLENVSYSYP--DGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 415 LFSTIFAD-------YYLFDDLVQGKQASLQNATQYLQRLEIAHKVSVMDG--NFSTTDLSTGQRKRLALINAWLEERPV 485
Cdd:PRK13644 78 LVGIVFQNpetqfvgRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKyrHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 486 LVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKETE 547
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVL-ERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
359-549 |
1.12e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL--------FStifadyyLFDDL- 429
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgigmvhqhFM-------LVPNLt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 -----------VQGKQASLQNATQYLQR------LEI--AHKVSvmdgnfsttDLSTGQRKRLALINAWLEERPVLVFDE 490
Cdd:COG3845 97 vaenivlglepTKGGRLDRKAARARIRElserygLDVdpDAKVE---------DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 491 waadqdP-AF------RRVFytELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKETETA 549
Cdd:COG3845 168 ------PtAVltpqeaDELF--EILRRLAAEGKSIIFITHKlREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
359-548 |
1.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTI------------------- 419
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKlviqktrfkkikkikeirr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 420 -------FADYYLFD-----DLVQG-------KQASLQNATQYLqrleiahKVSVMDGNF---STTDLSTGQRKRLALIN 477
Cdd:PRK13651 106 rvgvvfqFAEYQLFEqtiekDIIFGpvsmgvsKEEAKKRAAKYI-------ELVGLDESYlqrSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 478 AWLEERPVLVFDEWAADQDPAfRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKETET 548
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQ-GVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
359-546 |
1.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY-RQLFSTI-----FADYYLFDDLVQG 432
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKRIgmvfqFPESQLFEDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 K--------QASLQNATQYLQRL--EIAHKVSVMdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRV 502
Cdd:PRK13646 106 EiifgpknfKMNLDEVKNYAHRLlmDLGFSRDVM--SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 259663656 503 FyTELLPDLK-RQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKET 546
Cdd:PRK13646 184 V-MRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
354-543 |
2.00e-15 |
|
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: 75.84 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 354 FHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGE---PVSAETRDdyrqlFSTIFADYYLFDDLV 430
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRD-----ISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 431 QGKQASLQNATQYLQRLEIAHKVSVMDG--------NFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRV 502
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEmlgidhllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 259663656 503 FYTELLPDLKRQGKTIIVISHDdryFE----MADQLIRLSAGKVV 543
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHD---FEeawaLADKVAIMLNGKLI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
359-542 |
2.18e-15 |
|
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: 75.84 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDyRQLfSTIFADYYLF------DDLVQG 432
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNV-GFVFQHYALFrhmtvfDNVAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 ----KQASLQNATQYLQRLEIAHKVSVMDG--NFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRvfytE 506
Cdd:cd03296 99 lrvkPRSERPPEAEIRAKVHELLKLVQLDWlaDRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK----E 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 259663656 507 LLPDLKR----QGKTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:cd03296 175 LRRWLRRlhdeLHVTTVFVTHDqEEALEVADRVVVMNKGRI 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
359-543 |
2.31e-15 |
|
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: 75.26 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSaetrddyrqlfstIFADYYLFDDLVQGKQASLQ 438
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-------------LLGLGGGFNPELTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 439 NATQY-LQRLEIAhkvSVMD--------GNFSTT---DLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYtE 506
Cdd:cd03220 108 NGRLLgLSRKEID---EKIDeiiefselGDFIDLpvkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ-R 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 259663656 507 LLPDLKRQGKTIIVISHDDRYF-EMADQLIRLSAGKVV 543
Cdd:cd03220 184 RLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIR 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-543 |
2.74e-15 |
|
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: 74.51 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDVRYS-PPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQ--SGEILLNGEPVSAETrdd 411
Cdd:cd03213 3 TLSFRNLTVTvKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YRQLFSTIFADYYLFDDL-VQgkqaslqnatqylQRLEIAHKVSVmdgnfsttdLSTGQRKRLALINAWLEERPVLVFDE 490
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLtVR-------------ETLMFAAKLRG---------LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 491 WAADQDpAFRRVFYTELLPDLKRQGKTIIVISHDDRY--FEMADQLIRLSAGKVV 543
Cdd:cd03213 138 PTSGLD-SSSALQVMSLLRRLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
359-542 |
3.32e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD--YRQLFSTIFADYYLFDDL------- 429
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFPHLtalenvm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 ---VQGKQASLQNATQylQRLEIAHKVSVMD-GNFSTTDLSTGQRKRLALINAwLEERPVL-VFDEWAADQDPAFRRVFY 504
Cdd:PRK09493 100 fgpLRVRGASKEEAEK--QARELLAKVGLAErAHHYPSELSGGQQQRVAIARA-LAVKPKLmLFDEPTSALDPELRHEVL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 259663656 505 TeLLPDLKRQGKTIIVISHDDRYFE-MADQLIRLSAGKV 542
Cdd:PRK09493 177 K-VMQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRI 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
359-545 |
4.53e-15 |
|
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: 74.33 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRdDYRQLFSTIFADYYLFDDL-------VQ 431
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDELtgwenlyIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 GKQASLQNAT---------QYLQRLEIAHKVSvmdGNFsttdlSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRV 502
Cdd:cd03265 98 ARLYGVPGAErreridellDFVGLLEAADRLV---KTY-----SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 259663656 503 FYTELLPDLKRQGKTIIVISHddrYFEMADQLIR----LSAGKVVKE 545
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTH---YMEEAEQLCDrvaiIDHGRIIAE 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-523 |
5.16e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 360 NLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDdyRQLFSTIFADYYLFDDLVQGKQASLQ- 438
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 439 ------NATQYLQRLEIAHKVSVMDG-NFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTeLLPDL 511
Cdd:PRK10771 97 npglklNAAQREKLHAIARQMGIEDLlARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT-LVSQV 175
|
170
....*....|...
gi 259663656 512 KRQGK-TIIVISH 523
Cdd:PRK10771 176 CQERQlTLLMVSH 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
337-543 |
5.82e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.50 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 337 ELRDVRYSPPavegSEPFH--LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYR- 413
Cdd:cd03249 2 EFKNVSFRYP----SRPDVpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 ---------QLFSTIFAD---YYLFD-DLVQGKQASLQ-NATQYLQRLEiaHKVSVMDGNfSTTDLSTGQRKRLALINAW 479
Cdd:cd03249 78 qiglvsqepVLFDGTIAEnirYGKPDaTDEEVEEAAKKaNIHDFIMSLP--DGYDTLVGE-RGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 480 LEERPVLVFDEWAADQDPAFRRVFYTELlpDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEAL--DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
322-542 |
1.05e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.75 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 322 LLSEQEAPDKTVdsLELRDVRYSppaVEGSEPfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNG 401
Cdd:PRK09452 3 KLNKQPSSLSPL--VELRGISKS---FDGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 402 EPVS---AETRDdyrqlFSTIFADYYLFDDLVQGKQASLQNATQYLQRLEIAHKvsVMD----------GNFSTTDLSTG 468
Cdd:PRK09452 76 QDIThvpAENRH-----VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR--VMEalrmvqleefAQRKPHQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 469 QRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTElLPDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNE-LKALQRKlGITFVFVTHDqEEALTMSDRIVVMRDGRI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
359-543 |
1.12e-14 |
|
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: 73.52 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEpVSAETRDDYRQLFSTIFAD-------------YYL 425
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFGQktqlwwdlpvidsFYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 426 FDDLVQGKQASLQNATQYL-QRLEIAHKVSVmdgnfSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQD-PAFRRVF 503
Cdd:cd03267 119 LAAIYDLPPARFKKRLDELsELLDLEELLDT-----PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 504 ytELLPDLKRQ-GKTIIVISHDDRYFE-MADQLIRLSAGKVV 543
Cdd:cd03267 194 --NFLKEYNRErGTTVLLTSHYMKDIEaLARRVLVIDKGRLL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
336-548 |
1.18e-14 |
|
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: 73.37 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLY-----RPQSGEILLNGEPVSAETRD 410
Cdd:cd03260 1 IELRDLNVYYGDKHA-----LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 411 DY--RQLFSTIFADYYLFDdlvqgkqASLQNATQYLQRL----------EIAHKV--------SVMDgNFSTTDLSTGQR 470
Cdd:cd03260 76 VLelRRRVGMVFQKPNPFP-------GSIYDNVAYGLRLhgiklkeeldERVEEAlrkaalwdEVKD-RLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 471 KRLALINAWLEERPVLVFDEWAADQDPAFRRVFyTELLPDLKRQgKTIIVISHD----DRyfeMADQLIRLSAGKVVKET 546
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNmqqaAR---VADRTAFLLNGRLVEFG 222
|
..
gi 259663656 547 ET 548
Cdd:cd03260 223 PT 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
336-543 |
1.47e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVrysppavegSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYrPQSGEILLNGEPVS-------AET 408
Cdd:PRK03695 1 MQLNDV---------AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaaelARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 409 RDDYRQLFSTIFA-DYYLFDDLVQGKQASLQNATQYLQrlEIAHKVSVMDG-NFSTTDLSTG--QRKRLA--LINAWLEE 482
Cdd:PRK03695 71 RAYLSQQQTPPFAmPVFQYLTLHQPDKTRTEAVASALN--EVAEALGLDDKlGRSVNQLSGGewQRVRLAavVLQVWPDI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 483 RP---VLVFDEWAADQDPAFRRVFYTeLLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:PRK03695 149 NPagqLLLLDEPMNSLDVAQQAALDR-LLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
359-545 |
2.42e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLY--RPQSGEILLNGEPVSAEtrddyrqlfSTIFADYYLFDDLVQGKQ-- 434
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE---------ASLIDAIGRKGDFKDAVEll 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 435 --ASLQNATQYLQRleiahkvsvmdgnFSTtdLSTGQRKR--LALInawLEERP-VLVFDEWAADQDPAFRRVFYTELLP 509
Cdd:COG2401 120 naVGLSDAVLWLRR-------------FKE--LSTGQKFRfrLALL---LAERPkLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 259663656 510 DLKRQGKTIIVISHDDRYFE--MADQLIRLSAGKVVKE 545
Cdd:COG2401 182 LARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEE 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
356-545 |
2.87e-14 |
|
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: 71.84 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGdIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSaETRDDYRQLFS------TIFADYYLFDDL 429
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGylpqefGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 vqGKQASLQNATQYLQRLEIAH---KVSVMD-GNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFyT 505
Cdd:cd03264 94 --DYIAWLKGIPSKEVKARVDEvleLVNLGDrAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF-R 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 259663656 506 ELLPDLKrQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03264 171 NLLSELG-EDRIVILSTHIvEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
336-535 |
3.35e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppavEGSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD---DY 412
Cdd:PRK11831 8 VDMRGVSFT----RGNRCI-FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFADYYLFDDLVQGKQAS--LQNATQYLQrlEIAHKVSVMD---------GNFSTTDLSTGQRKRLALINAWLE 481
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAypLREHTQLPA--PLLHSTVMMKleavglrgaAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 482 ERPVLVFDEWAADQDPAFRRVFyTELLPDLKRQ-GKTIIVISHD--------DRYFEMADQLI 535
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVL-VKLISELNSAlGVTCVVVSHDvpevlsiaDHAYIVADKKI 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-544 |
3.49e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.85 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDVRYSPPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD-DYR 413
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 QLFSTI-----FADYYLFDDLV--------QGKQASLQNATQyLQRlEIAHKVSVMDGNFSTT--DLSTGQRKRLALINA 478
Cdd:PRK13649 82 QIRKKVglvfqFPESQLFEETVlkdvafgpQNFGVSQEEAEA-LAR-EKLALVGISESLFEKNpfELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 479 WLEERPVLVFDEWAADQDPAFRRVFYTeLLPDLKRQGKTIIVISH--DDrYFEMADQLIRLSAGKVVK 544
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHlmDD-VANYADFVYVLEKGKLVL 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
286-545 |
3.80e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 286 PLEQVVTILPIVSRAQVAFQRVAELSERfsspePHLLLSEQEAPdKTVDSLELRDVRYSppavEGSEPFHLGPINLRIAQ 365
Cdd:PRK10790 297 PLIELTTQQSMLQQAVVAGERVFELMDG-----PRQQYGNDDRP-LQSGRIDIDNVSFA----YRDDNLVLQNINLSVPS 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFS------TIFADyYLFDDLVQGKQASLQN 439
Cdd:PRK10790 367 RGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAmvqqdpVVLAD-TFLANVTLGRDISEEQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 440 ATQYLQRLEIAHKVSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELlpDLKR 513
Cdd:PRK10790 446 VWQALETVQLAELARSLPDGLYTplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL--AAVR 523
|
250 260 270
....*....|....*....|....*....|..
gi 259663656 514 QGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK10790 524 EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
349-548 |
5.43e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.39 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 349 EGSePFH---LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAE--TRDDYRQLFSTIFA-- 421
Cdd:PRK13637 14 EGT-PFEkkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvKLSDIRKKVGLVFQyp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 422 DYYLFDDLVQgKQASLQNATQYLQRLEIAHKV-SVMD---------GNFSTTDLSTGQRKRLALINAWLEERPVLVFDEW 491
Cdd:PRK13637 93 EYQLFEETIE-KDIAFGPINLGLSEEEIENRVkRAMNivgldyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 492 AADQDPAFRRVFYtELLPDLKRQGK-TIIVISHD-DRYFEMADQLIRLSAGKVV---------KETET 548
Cdd:PRK13637 172 TAGLDPKGRDEIL-NKIKELHKEYNmTIILVSHSmEDVAKLADRIIVMNKGKCElqgtprevfKEVET 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
359-542 |
6.72e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYL-FDdlVQGKQASL 437
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE--FDVRQVVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 438 QNATQYLQRLEIAHKV------SVMD-------GNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDpAFRRVFY 504
Cdd:PRK09536 100 MGRTPHRSRFDTWTETdraaveRAMErtgvaqfADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-INHQVRT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 505 TELLPDLKRQGKTIIVISHDdryFEMA----DQLIRLSAGKV 542
Cdd:PRK09536 179 LELVRRLVDDGKTAVAAIHD---LDLAarycDELVLLADGRV 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
356-542 |
7.79e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVsAETRDDYRQLFStifaDYYLF------DDL 429
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-AEAREDTRLMFQ----DARLLpwkkviDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQGKQASLQNATqyLQRLEiahKVSVMD-GNFSTTDLSTGQRKRLALINAwLEERP-VLVFDEWAADQDpAFRRVFYTEL 507
Cdd:PRK11247 103 GLGLKGQWRDAA--LQALA---AVGLADrANEWPAALSGGQKQRVALARA-LIHRPgLLLLDEPLGALD-ALTRIEMQDL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 259663656 508 LPDLKRQ-GKTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:PRK11247 176 IESLWQQhGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
337-543 |
9.83e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 337 ELRDVRYS----PPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY 412
Cdd:PRK13657 336 EFDDVSFSydnsRQGVED--------VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFADYYLF-----DDLVQGK----QASLQNATQYLQRLE-IAHKvsvmDGNFST------TDLSTGQRKRLALI 476
Cdd:PRK13657 408 RRNIAVVFQDAGLFnrsieDNIRVGRpdatDEEMRAAAERAQAHDfIERK----PDGYDTvvgergRQLSGGERQRLAIA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 477 NAWLEERPVLVFDEWAADQDPAF-RRVfyTELLPDLkRQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETeAKV--KAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
356-497 |
1.01e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFAdyyLFDDLvqgkqA 435
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG---LKADL-----S 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 436 SLQNaTQYLQRLEiAHKVSVMDGNFSTT------------DLSTGQRKRLALINAWLEERPVLVFDEWAADQDP 497
Cdd:PRK13543 99 TLEN-LHFLCGLH-GRRAKQMPGSALAIvglagyedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
359-549 |
1.03e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEpVSA--EtrddyrqlFSTIFadyylfddlvqgkQAS 436
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAllE--------LGAGF-------------HPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 437 L---QNAtqYLQ-------RLEIAHKV-SVMDgnFSttDL-----------STGQRKRLAL-INAWLEerP-VLVFDEWA 492
Cdd:COG1134 103 LtgrENI--YLNgrllglsRKEIDEKFdEIVE--FA--ELgdfidqpvktySSGMRARLAFaVATAVD--PdILLVDEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 493 ADQDPAFRRVFYTELLpDLKRQGKTIIVISHDDRYF-EMADQLIRLSAGKVVKETETA 549
Cdd:COG1134 175 AVGDAAFQKKCLARIR-ELRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
359-548 |
1.33e-13 |
|
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: 70.30 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS----AETRdDYRQLFSTIFADYYLFDDL-VQG- 432
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELR-KARRRIGMIFQHFNLLSSRtVFEn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 -----------KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAfrr 501
Cdd:cd03258 103 valpleiagvpKAEIEERVLELLELVGLEDK-----ADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE--- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 502 vfyT-----ELLPDLKRQ-GKTIIVISHddryfEM------ADQLIRLSAGKVVKETET 548
Cdd:cd03258 175 ---TtqsilALLRDINRElGLTIVLITH-----EMevvkriCDRVAVMEKGEVVEEGTV 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
359-544 |
1.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD----DYRQLFSTI--FADYYLFDDLVQ- 431
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKVGIVfqFPEHQLFEETVEk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 -----------GKQASLQNATQYLQRLEIAHKVSvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFR 500
Cdd:PRK13634 106 dicfgpmnfgvSEEDAKQKAREMIELVGLPEELL----ARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 501 R----VFYTellpdL-KRQGKTIIVISH--DD--RYfemADQLIRLSAGKVVK 544
Cdd:PRK13634 182 KemmeMFYK-----LhKEKGLTTVLVTHsmEDaaRY---ADQIVVMHKGTVFL 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-534 |
2.22e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL-----FSTIFADYYLFDDL-VQG 432
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvpqFDNLDPDFTVRENLlVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 KQASLqNATQYLQR----LEIAHKVSVMDGNFSttDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYtELL 508
Cdd:PRK13537 106 RYFGL-SAAAARALvpplLEFAKLENKADAKVG--ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW-ERL 181
|
170 180
....*....|....*....|....*.
gi 259663656 509 PDLKRQGKTIIVISHddrYFEMADQL 534
Cdd:PRK13537 182 RSLLARGKTILLTTH---FMEEAERL 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
356-523 |
2.35e-13 |
|
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: 70.11 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSG-EILLNGEPVSAETRDDYRQ---LFSTIFADYYLFDDLVQ 431
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKrigLVSPALQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 -----GKQASL-----------QNATQYLQRLEIAHKvsvMDGNFSTtdLSTGQRKRLALINAWLEERPVLVFDEWAADQ 495
Cdd:COG1119 99 dvvlsGFFDSIglyreptdeqrERARELLELLGLAHL---ADRPFGT--LSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180
....*....|....*....|....*....
gi 259663656 496 DPAFRRVFyTELLPDLKRQG-KTIIVISH 523
Cdd:COG1119 174 DLGARELL-LALLDKLAAEGaPTLVLVTH 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-542 |
2.47e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNG---------EPVSaetrDDYRQLFSTIFADYYLFDDL 429
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqEPPL----DDDLTVLDTVLDGDAELRAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQGKQ---ASLQNATQYLQRL-EIAHKVSVMDG--------------NFSTTD-------LSTGQRKRLALINAWLEERP 484
Cdd:COG0488 93 EAELEeleAKLAEPDEDLERLaELQEEFEALGGweaearaeeilsglGFPEEDldrpvseLSGGWRRRVALARALLSEPD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259663656 485 VLVFDE-----------WAADQdpafrrvfytellpdLKRQGKTIIVISHdDRYF--EMADQLIRLSAGKV 542
Cdd:COG0488 173 LLLLDEptnhldlesieWLEEF---------------LKNYPGTVLVVSH-DRYFldRVATRILELDRGKL 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
335-543 |
7.35e-13 |
|
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: 67.82 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRD--VRYSP--PAVegsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD 410
Cdd:cd03369 6 EIEVENlsVRYAPdlPPV-------LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 411 DYRQLFSTIFADYYLFDDLVqgkQASLQNATQYLQRlEIAHKVSVMDGNfstTDLSTGQRKRLALINAWLEERPVLVFDE 490
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTI---RSNLDPFDEYSDE-EIYGALRVSEGG---LNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 491 WAA----DQDPAFRRVFYTELlpdlkrQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:cd03369 152 ATAsidyATDALIQKTIREEF------TNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
336-541 |
7.65e-13 |
|
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: 67.49 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNG-------EP--VSA 406
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvsqEPwiQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 407 ETRDDYrqLFSTIFaDYYLFDDLVQgkqaslqnATQYLQRLEIahkvsVMDGNFST-----TDLSTGQRKRLALINAWLE 481
Cdd:cd03250 81 TIRENI--LFGKPF-DEERYEKVIK--------ACALEPDLEI-----LPDGDLTEigekgINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 482 ERPVLVFDE--WAADQDPAfRRVFYTELLPDLKRqGKTIIVISHDDRYFEMADQLIRLSAGK 541
Cdd:cd03250 145 DADIYLLDDplSAVDAHVG-RHIFENCILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
356-543 |
8.63e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.79 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA--ETRDdyRQL-FstIFADYYLF------ 426
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlPPRE--RRVgF--VFQHYALFphmtva 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 -------DDLVQGKQASLQNATQYLQRLEIAHkvsvMDGNFSTTdLSTGQRKRLALINAwLEERP-VLVFDEwaadqdP- 497
Cdd:COG1118 94 eniafglRVRPPSKAEIRARVEELLELVQLEG----LADRYPSQ-LSGGQRQRVALARA-LAVEPeVLLLDE------Pf 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 498 ----AFRRvfyTEL---LPDL-KRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:COG1118 162 galdAKVR---KELrrwLRRLhDELGGTTVFVTHDqEEALELADRVVVMNQGRIE 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
363-534 |
9.25e-13 |
|
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: 68.20 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 363 IAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSaetrddYRQlfSTIFADYYL-FDDLVQGKQASLQNAT 441
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKP--QYIKADYEGtVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 442 QYlqRLEIAHKV---SVMDGNfsTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAfRRVFYTELlpdLKR----Q 514
Cdd:cd03237 94 YF--KTEIAKPLqieQILDRE--VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKV---IRRfaenN 165
|
170 180
....*....|....*....|
gi 259663656 515 GKTIIVISHDdryFEMADQL 534
Cdd:cd03237 166 EKTAFVVEHD---IIMIDYL 182
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
353-543 |
1.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.88 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 353 PFHLGPIN---LRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA------ETRDDYRQLFSTI-FAD 422
Cdd:PRK13645 21 PFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVFqFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 423 YYLFDDLVQ------------GKQASLQNATQYLQRLEIAHKVSvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDE 490
Cdd:PRK13645 101 YQLFQETIEkdiafgpvnlgeNKQEAYKKVPELLKLVQLPEDYV----KRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 259663656 491 WAADQDPAFRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVI 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
336-543 |
1.38e-12 |
|
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: 68.93 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRD--VRYSPP-----AVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQ---SGEILLNGEPVS 405
Cdd:COG0444 2 LEVRNlkVYFPTRrgvvkAVDG--------VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 406 AETRDDYRQL----FSTIFAD------------------YYLFDDLvqGKQASLQNATQYLQRLEIAHKVSVMDgnfstt 463
Cdd:COG0444 74 KLSEKELRKIrgreIQMIFQDpmtslnpvmtvgdqiaepLRIHGGL--SKAEARERAIELLERVGLPDPERRLD------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 464 D----LSTGQRKR----LALINawleeRP-VLVFDEwaadqdPafrrvfyT------------ELLPDLKRQ-GKTIIVI 521
Cdd:COG0444 146 RypheLSGGMRQRvmiaRALAL-----EPkLLIADE------P-------TtaldvtiqaqilNLLKDLQRElGLAILFI 207
|
250 260
....*....|....*....|...
gi 259663656 522 SHDdr-yfEMADQLIRLSAGKVV 543
Cdd:COG0444 208 THDlgvvaEIADRVAVMYAGRIV 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
356-541 |
3.09e-12 |
|
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: 64.39 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEIllngepvsaetrddyrqlfstifadyylfddlvqgkqa 435
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 slqnatQYLQRLEIAHkvsvmdgnFSTtdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRrvfytELLPD-LKRQ 514
Cdd:cd03221 58 ------TWGSTVKIGY--------FEQ--LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI-----EALEEaLKEY 116
|
170 180
....*....|....*....|....*....
gi 259663656 515 GKTIIVISHdDRYF--EMADQLIRLSAGK 541
Cdd:cd03221 117 PGTVILVSH-DRYFldQVATKIIELEDGK 144
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
360-544 |
3.34e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.52 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 360 NLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS----AETRDDYRQLFSTIFADYYL------FDDL 429
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRRKKIAMVFQSFALmphmtvLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQGKQ-ASLQNATQYLQRLEIAHKVSVMDGNFSTTD-LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTEL 507
Cdd:PRK10070 128 AFGMElAGINAEERREKALDALRQVGLENYAHSYPDeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 259663656 508 LPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQ 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
335-543 |
3.66e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.79 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDVRYSPPAVEgsepfHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS---AETRDd 411
Cdd:COG3839 3 SLELENVSKSYGGVE-----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlpPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 yrqlFSTIFADYYLFDDL-----------VQGKQASLQNA--TQYLQRLEIAH----KVSvmdgnfsttDLSTGQRKRLA 474
Cdd:COG3839 77 ----IAMVFQSYALYPHMtvyeniafplkLRKVPKAEIDRrvREAAELLGLEDlldrKPK---------QLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 475 LINAWLEERPVLVFDEWAADQDPAFRRVFYTElLPDL-KRQGKTIIVISHDdrYFE---MADQLIRLSAGKVV 543
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAE-IKRLhRRLGTTTIYVTHD--QVEamtLADRIAVMNDGRIQ 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
298-542 |
3.80e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 298 SRAQVAFQRVAELSERFSSPE-P---HLLLSEQE----APDKTVDSLELRDVRYSPPAVEgsepfhlgPINLRIAQGDIV 369
Cdd:TIGR01257 888 TREERALEKTEPLTEEMEDPEhPegiNDSFFERElpglVPGVCVKNLVKIFEPSGRPAVD--------RLNITFYENQIT 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 370 FIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETrDDYRQ----------LFSTI-FADYYLFDDLVQGK---QA 435
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL-DAVRQslgmcpqhniLFHHLtVAEHILFYAQLKGRsweEA 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 SLQNATQyLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPdlKRQG 515
Cdd:TIGR01257 1039 QLEMEAM-LEDTGLHHK-----RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK--YRSG 1110
|
250 260
....*....|....*....|....*...
gi 259663656 516 KTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:TIGR01257 1111 RTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
356-545 |
3.98e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.75 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAqgdivfIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIF--ADYYLFDDLVQgK 433
Cdd:PRK13652 26 IAPRNSRIA------VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFqnPDDQIFSPTVE-Q 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 434 QASLQNATQYLQRLEIAHKVSVMDGNFSTTD--------LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYT 505
Cdd:PRK13652 99 DIAFGPINLGLDEETVAHRVSSALHMLGLEElrdrvphhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 259663656 506 ELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13652 179 FLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
349-542 |
4.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 66.68 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 349 EGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFAD------ 422
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNpdnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 423 -YYLFDDLVQGkqasLQNatQYLQRLEIAHKVS-----VMDGNFSTTD---LSTGQRKRLALINAwLEERP-VLVFDEWA 492
Cdd:PRK13650 96 gATVEDDVAFG----LEN--KGIPHEEMKERVNealelVGMQDFKEREparLSGGQKQRVAIAGA-VAMRPkIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 259663656 493 ADQDPAFRRvfytELLPDLK----RQGKTIIVISHDDRYFEMADQLIRLSAGKV 542
Cdd:PRK13650 169 SMLDPEGRL----ELIKTIKgirdDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-545 |
5.87e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETR------------DDYRQLFsTIFADYYLF 426
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARlararigvvpqfDNLDLEF-TVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 DDLVQGKQASLQNATQYLqrLEIAHKVSVMDGNFSttDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYtE 506
Cdd:PRK13536 139 GRYFGMSTREIEAVIPSL--LEFARLESKADARVS--DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW-E 213
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 259663656 507 LLPDLKRQGKTIIVISHddrYFEMA----DQLIRLSAGKVVKE 545
Cdd:PRK13536 214 RLRSLLARGKTILLTTH---FMEEAerlcDRLCVLEAGRKIAE 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
359-532 |
5.94e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDDYR-QLFSTIFADYYLFDD------ 428
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklSSAAKAELRnQKLGFIYQFHHLLPDftalen 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 -----LVQGK--QASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAwLEERPVLVF-DEWAA--DQDPA 498
Cdd:PRK11629 108 vamplLIGKKkpAEINSRALEMLAAVGLEHR-----ANHRPSELSGGERQRVAIARA-LVNNPRLVLaDEPTGnlDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 499 fRRVFytELLPDL-KRQGKTIIVISHD-------DRYFEMAD 532
Cdd:PRK11629 182 -DSIF--QLLGELnRLQGTAFLVVTHDlqlakrmSRQLEMRD 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
356-532 |
6.90e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLF-----STIFADYYLFDDLV 430
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCfvghrSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 431 QGKQASLQNA--TQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTElL 508
Cdd:PRK13540 97 YDIHFSPGAVgiTELCRLFSLEHLI-----DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK-I 170
|
170 180
....*....|....*....|....
gi 259663656 509 PDLKRQGKTIIVISHDDRYFEMAD 532
Cdd:PRK13540 171 QEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
359-524 |
7.40e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.78 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAET-------------------RD--------- 410
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiarmgvvrtfqhvrlfREmtvienllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 411 -DYRQLFSTIFADYYLFDDLVQGKQASLQNATQYLQR---LEIAhkvsvmdgNFSTTDLSTGQRKRLALINAWLEERPVL 486
Cdd:PRK11300 104 aQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERvglLEHA--------NRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 259663656 487 VFDEWAADQDPAFRRVFyTELLPDLKRQ-GKTIIVISHD 524
Cdd:PRK11300 176 MLDEPAAGLNPKETKEL-DELIAELRNEhNVTVLLIEHD 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
341-543 |
7.85e-12 |
|
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: 64.82 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 341 VRY---SPPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFS 417
Cdd:cd03244 10 LRYrpnLPPVLKN--------ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 418 TIFADYYLFDDLVQGKQASLQNAT-----QYLQRLEIAHKVSVMDGNFSTT------DLSTGQRKRLALINAWLEERPVL 486
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGEYSdeelwQALERVGLKEFVESLPGGLDTVveeggeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 487 VFDEWAADQDPA----FRRVFYTELlpdlkrQGKTIIVISH------DdryfemADQLIRLSAGKVV 543
Cdd:cd03244 162 VLDEATASVDPEtdalIQKTIREAF------KDCTVLTIAHrldtiiD------SDRILVLDKGRVV 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
359-545 |
9.67e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 64.76 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD-------Y----RQLFST-------IF 420
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragigYvpegRRIFPEltveenlLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 421 ADYYLFDDlvqGKQASLQNATQYLQRL-EIAHKvsvMDGNfsttdLSTGQRKRLALINAwLEERP-VLVFDEWAADQDPA 498
Cdd:cd03224 99 GAYARRRA---KRKARLERVYELFPRLkERRKQ---LAGT-----LSGGEQQMLAIARA-LMSRPkLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 259663656 499 F-RRVFytELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:cd03224 167 IvEEIF--EAIRELRDEGVTILLVEQNaRFALEIADRAYVLERGRVVLE 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-542 |
1.51e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSaETRDDYRQLfSTIFADYYLF------DDLVQG 432
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGV-GMVFQSYALYphlsvaENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 KQASLQNATQYLQR-------LEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYT 505
Cdd:PRK11000 100 LKLAGAKKEEINQRvnqvaevLQLAHLL-----DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 259663656 506 ELLPDLKRQGKTIIVISHDD-RYFEMADQLIRLSAGKV 542
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQvEAMTLADKIVVLDAGRV 212
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
21-168 |
1.64e-11 |
|
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: 65.12 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLASINNALHSENGLGQGV--------LLSFGGLCLLALVSSIVSDIGTSYVGQHIIAKLR 92
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVdfsgllriLLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 93 KELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIG 168
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQAlSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-544 |
1.72e-11 |
|
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: 63.85 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 355 HLGPINLRIA---QGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVsaetrDDYRQLFST---------IFAD 422
Cdd:cd03297 9 RLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL-----FDSRKKINLppqqrkiglVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 423 YYLFDDL-----------VQGKQASLQNATQYLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEW 491
Cdd:cd03297 84 YALFPHLnvrenlafglkRKRNREDRISVDELLDLLGLDHLL-----NRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 492 AADQDPAFRrvfyTELLPDLKRQGK----TIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:cd03297 159 FSALDRALR----LQLLPELKQIKKnlniPVIFVTHDlSEAEYLADRIVVMEDGRLQY 212
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
109-544 |
2.12e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.27 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 109 RYRTHRLIPVLTHDIDTISdFSFSFTPLAIALTITFGC-------------LGYLAYLSVPmflltVVAIVIGTAAQYLA 175
Cdd:PRK10789 89 RHRTGDLMARATNDVDRVV-FAAGEGVLTLVDSLVMGCavlivmstqiswqLTLLALLPMP-----VMAIMIKRYGDQLH 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 176 RSrgFKGFYAA-RDLEDELQKHYTAI----ASGAKELRIHRPRRYRMHTGRisetanniRDLHISSIN------IFI--- 241
Cdd:PRK10789 163 ER--FKLAQAAfSSLNDRTQESLTSIrmikAFGLEDRQSALFAADAEDTGK--------KNMRVARIDarfdptIYIaig 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 242 ----LAKTFGSmlFFVVIGlALTLqaywpssnpAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV-AELSERFSS 316
Cdd:PRK10789 233 manlLAIGGGS--WMVVNG-SLTL---------GQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIrAMLAEAPVV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 317 PEPHLLLSEQeapdKTVDSLELRDVRY---SPPAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQ 393
Cdd:PRK10789 301 KDGSEPVPEG----RGELDVNIRQFTYpqtDHPALEN--------VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 394 SGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQGKQA-SLQNATQyLQRLEIAHKVSVMDG------NFST---- 462
Cdd:PRK10789 369 EGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIAlGRPDATQ-QEIEHVARLASVHDDilrlpqGYDTevge 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 463 --TDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRvfytELLPDLK--RQGKTIIVISHDDRYFEMADQLIRLS 538
Cdd:PRK10789 448 rgVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH----QILHNLRqwGEGRTVIISAHRLSALTEASEILVMQ 523
|
....*.
gi 259663656 539 AGKVVK 544
Cdd:PRK10789 524 HGHIAQ 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
206-545 |
2.43e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 206 ELRIHRPRRYRMHTGRISETANNIRDLHISSINIFILAKTFGSmlfFVVIGLALTlqaywpssnPAAITGFVMVLLYMKG 285
Cdd:PLN03232 502 ESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGV---FVLLGGDLT---------PARAFTSLSLFAVLRS 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 286 PLEQVVTILPIVSRAQVAFQRVAEL---SERFSSPEPHLllsEQEAPDKTVDSLELR-DVRYSPPAvegsepfhLGPINL 361
Cdd:PLN03232 570 PLNMLPNLLSQVVNANVSLQRIEELllsEERILAQNPPL---QPGAPAISIKNGYFSwDSKTSKPT--------LSDINL 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 362 RIAQGDIVFIVGENGCGKTTLIKLLLG-LYRPQSGEILLNGEPVsaetrddYRQLFSTIFaDYYLFDDLVQGKQASLQNA 440
Cdd:PLN03232 639 EIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVA-------YVPQVSWIF-NATVRENILFGSDFESERY 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 441 TQYLQRLEIAHKVSVMDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDE--WAADQDPAfRRVFYTELLPDLk 512
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDplSALDAHVA-HQVFDSCMKDEL- 788
|
330 340 350
....*....|....*....|....*....|...
gi 259663656 513 rQGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:PLN03232 789 -KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-496 |
2.78e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.02 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 309 ELSERFSSPEPHLLLSEQEAPDKTVDSLELRD-VRYSPpavEGSEPfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLL 387
Cdd:PRK11174 323 SLVTFLETPLAHPQQGEKELASNDPVTIEAEDlEILSP---DGKTL--AGPLNFTLPAGQRIALVGPSGAGKTSLLNALL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 388 GlYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLF-----DDLVQGK-QASLQNATQYLQRLEIAHKVSVMDGNFS 461
Cdd:PRK11174 398 G-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPhgtlrDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 259663656 462 TT------DLSTGQRKRLALINAWLEERPVLVFDEWAADQD 496
Cdd:PRK11174 477 TPigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
351-545 |
2.83e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 351 SEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFAD-------Y 423
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpdnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 424 YLFDDLVQGKQASLQNATQYLQRLEIA-HKVSVMDgnFSTTD---LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAF 499
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEAlLAVNMLD--FKTREparLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 259663656 500 RRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-545 |
3.68e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAeTRD--------DYRQL------FSTIFA 421
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL-VRDkdgqlkvaDKNQLrllrtrLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 422 DYYLFDDL----------VQ----GKQASLQNATQYLQRLEIAHKVSvmdGNFStTDLSTGQRKRLALINAWLEERPVLV 487
Cdd:PRK10619 100 HFNLWSHMtvlenvmeapIQvlglSKQEARERAVKYLAKVGIDERAQ---GKYP-VHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 488 FDEWAADQDPAF-RRVFytELLPDLKRQGKTIIVISHDDRYFE-MADQLIRLSAGKVVKE 545
Cdd:PRK10619 176 FDEPTSALDPELvGEVL--RIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEE 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
356-549 |
4.96e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.44 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL---FSTIFADYYL------F 426
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqIGMIFQHFNLlssrtvF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 DDL-----VQG--KQASLQNATQYLQRLEIAHKVSVMDGNfsttdLSTGQRKRLALINAwLEERP-VLVFDEWAADQDPA 498
Cdd:PRK11153 101 DNValpleLAGtpKAEIKARVTELLELVGLSDKADRYPAQ-----LSGGQKQRVAIARA-LASNPkVLLCDEATSALDPA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 499 FRRVFYtELLPDLKRQ-GKTIIVISHddryfEM------ADQLIRLSAGKVVKETETA 549
Cdd:PRK11153 175 TTRSIL-ELLKDINRElGLTIVLITH-----EMdvvkriCDRVAVIDAGRLVEQGTVS 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-549 |
5.00e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 342 RYSPPAVEGSEPFH--LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTI 419
Cdd:PRK10419 12 HYAHGGLSGKHQHQtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 420 FAdyyLFDD---LVQGKQA-------------SLQNATQYLQRLEIAHKVSVMDGNFST--TDLSTGQRKRLALINAWLE 481
Cdd:PRK10419 92 QM---VFQDsisAVNPRKTvreiireplrhllSLDKAERLARASEMLRAVDLDDSVLDKrpPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 482 ERPVLVFDEWAADQDpafrRVFYTE---LLPDLKRQGKTIIV-ISHDDRYFE-MADQLIRLSAGKVVKETETA 549
Cdd:PRK10419 169 EPKLLILDEAVSNLD----LVLQAGvirLLKKLQQQFGTACLfITHDLRLVErFCQRVMVMDNGQIVETQPVG 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
356-540 |
5.03e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETrddyrqlfSTIFADYYLF------ 426
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpGAER--------GVVFQNEGLLpwrnvq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 DDLVQG-------KQASLQNATQYLQR--LEIAHKVSVMdgnfsttDLSTGQRKRLALINAWLEERPVLVFDEWAADQDp 497
Cdd:PRK11248 89 DNVAFGlqlagveKMQRLEIAHQMLKKvgLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALD- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 259663656 498 AFRRVFYTELLPDL-KRQGKTIIVISHD-DRYFEMADQLIRLSAG 540
Cdd:PRK11248 161 AFTREQMQTLLLKLwQETGKQVLLITHDiEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
336-543 |
5.62e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPaveGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGE---ILLNGEPVSAETRDDY 412
Cdd:PRK13640 6 VEFKHVSFTYP---DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFAD-------YYLFDDLVQGkqasLQN-ATQYLQRLEIAHKVSVMDGNFSTTD-----LSTGQRKRLALINAW 479
Cdd:PRK13640 83 REKVGIVFQNpdnqfvgATVGDDVAFG----LENrAVPRPEMIKIVRDVLADVGMLDYIDsepanLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 480 LEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-532 |
5.68e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.95 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEpVSAETRDDYRQLFSTIF------------------ 420
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFKRRKEFARRIGVVFgqrsqlwwdlpaidsfrl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 421 -ADYYLFDDlvqgkqaslqnaTQYLQRLEiaHKVSVMD-GNFSTT---DLSTGQRKRLALINAWLEERPVLVFDEwaadq 495
Cdd:COG4586 120 lKAIYRIPD------------AEYKKRLD--ELVELLDlGELLDTpvrQLSLGQRMRCELAAALLHRPKILFLDE----- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259663656 496 dP----------AFRrvfytELLPDL-KRQGKTIIVISHDdryfeMAD 532
Cdd:COG4586 181 -PtigldvvskeAIR-----EFLKEYnRERGTTILLTSHD-----MDD 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
359-544 |
5.82e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.82 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGE--ILLNGEPVS-AETRDDYR----QLFSTIFADYYLFDdlvq 431
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmTKPGPDGRgrakRYIGILHQEYDLYP---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 gKQASLQNATQYLQrLEIAHKVSVMDG-------NFS-----------TTDLSTGQRKRLALINAWLEERPVLVFDEWAA 493
Cdd:TIGR03269 379 -HRTVLDNLTEAIG-LELPDELARMKAvitlkmvGFDeekaeeildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 259663656 494 DQDPAFRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIVK 508
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
349-545 |
6.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.18 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 349 EGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD-DYR------------QL 415
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRnkagmvfqnpdnQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 FSTIFADyylfdDLVQGKQASLQNATQYLQRLEIAHKVSVMD--GNFSTTDLSTGQRKRLAlINAWLEERP-VLVFDEWA 492
Cdd:PRK13633 99 VATIVEE-----DVAFGPENLGIPPEEIRERVDESLKKVGMYeyRRHAPHLLSGGQKQRVA-IAGILAMRPeCIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 259663656 493 ADQDPAFRR-VFYTelLPDL-KRQGKTIIVISHddrYFE---MADQLIRLSAGKVVKE 545
Cdd:PRK13633 173 AMLDPSGRReVVNT--IKELnKKYGITIILITH---YMEeavEADRIIVMDSGKVVME 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
363-528 |
7.82e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 363 IAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLnGEPVSAETRDDYRQLFStifADYYLFDDLVQGKQASLQNATQ 442
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAELD---PEKTVMDNLAEGKQEVMVNGRP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 443 -----YLQrleiahkvsvmDGNFS-------TTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDpafrrVFYTELLPD 510
Cdd:PRK11147 418 rhvlgYLQ-----------DFLFHpkramtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD-----VETLELLEE 481
|
170 180
....*....|....*....|
gi 259663656 511 L--KRQGkTIIVISHdDRYF 528
Cdd:PRK11147 482 LldSYQG-TVLLVSH-DRQF 499
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
347-415 |
7.85e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.60 E-value: 7.85e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 347 AVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:COG4608 33 AVDG--------VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPL 93
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
359-543 |
1.42e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 61.71 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS-------AETRDDYRQLFSTIFAdyYLFDDLV- 430
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspaelARRRAVLPQHSSLSFP--FTVEEVVa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 431 -------QGKQASLQNATQYLQRLEIAHkvsvmdgnFSTTD---LSTG--QRKRLA--LINAWL--EERPVLVFDEWAAD 494
Cdd:PRK13548 99 mgraphgLSRAEDDALVAAALAQVDLAH--------LAGRDypqLSGGeqQRVQLArvLAQLWEpdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 495 QDPAFR-RVFytELLPDL-KRQGKTIIVISHD----DRYfemADQLIRLSAGKVV 543
Cdd:PRK13548 171 LDLAHQhHVL--RLARQLaHERGLAVIVVLHDlnlaARY---ADRIVLLHQGRLV 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
359-543 |
1.45e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 61.13 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQ---SGEILLNGEPVSaetrddyRQLFSTIFAdyYL--FDDLVQGK 433
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK-------PDQFQKCVA--YVrqDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 434 QA------SLQNATQYLQRLEIAHKVSV----------MDGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDP 497
Cdd:cd03234 97 TVretltyTAILRLPRKSSDAIRKKRVEdvllrdlaltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 259663656 498 --AFRRVfytELLPDLKRQGKTIIVISHDDR--YFEMADQLIRLSAGKVV 543
Cdd:cd03234 177 ftALNLV---STLSQLARRNRIVILTIHQPRsdLFRLFDRILLLSSGEIV 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
359-497 |
1.83e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNG------EPVSAETRDDYRQLFSTIFADYYLFDDL--- 429
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHLtvq 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 430 ---------VQG--KQASLQNATQYLQRLEIAHKVsvmdGNFStTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDP 497
Cdd:PRK11124 101 qnlieapcrVLGlsKDQALARAEKLLERLRLKPYA----DRFP-LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
356-542 |
2.34e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFstIFADYYLF------DDL 429
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFrhmtvfDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQG-----------KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPA 498
Cdd:PRK10851 96 AFGltvlprrerpnAAAIKAKVTQLLEMVQLAHL-----ADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259663656 499 FR---RVFYTELLPDLKRqgkTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:PRK10851 171 VRkelRRWLRQLHEELKF---TSVFVTHDqEEAMEVADRVVVMSQGNI 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
359-543 |
2.97e-10 |
|
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: 62.04 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEP-VSAETRDD---YRQLFSTIFADYYLFDDL-VQG- 432
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGIFlppHRRRIGYVFQEARLFPHLsVRGn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 -----KQASLQNATQYLQR----LEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRvf 503
Cdd:COG4148 98 llygrKRAPRAERRISFDEvvelLGIGHLL-----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 259663656 504 ytELLPDLKR-QGKT---IIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:COG4148 171 --EILPYLERlRDELdipILYVSHSlDEVARLADHVVLLEQGRVV 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
354-524 |
3.25e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.27 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 354 FHLGPinlriaqGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD---YRQLFSTIFADYYL----- 425
Cdd:PRK10908 23 FHMRP-------GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLlmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 426 -FDDLVQGKQASLQNATQYLQRLEIA-HKVSVMDG--NFStTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRR 501
Cdd:PRK10908 96 vYDNVAIPLIIAGASGDDIRRRVSAAlDKVGLLDKakNFP-IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180
....*....|....*....|...
gi 259663656 502 VFYtELLPDLKRQGKTIIVISHD 524
Cdd:PRK10908 175 GIL-RLFEEFNRVGVTVLMATHD 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
359-523 |
3.30e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA---ETRddYR-----QLFStifadyyLFDDL- 429
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdiATR--RRvgymsQAFS-------LYGELt 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQgkqaslQNatqyLQ---RL------EIAHKVSVMDGNFSTTD--------LSTGQRKRLALINAWLEERPVLVFDEWA 492
Cdd:NF033858 356 VR------QN----LElhaRLfhlpaaEIAARVAEMLERFDLADvadalpdsLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190
....*....|....*....|....*....|..
gi 259663656 493 ADQDPAFRRVFYtELLPDLKRQ-GKTIIVISH 523
Cdd:NF033858 426 SGVDPVARDMFW-RLLIELSREdGVTIFISTH 456
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
359-545 |
3.37e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGL--YRPQSGEILLN----------------GEPVS--------------- 405
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvGEPCPvcggtlepeevdfwn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 406 ---AETRDDYRQ---LFSTIFADYYlfDDLV-------------QGKQAsLQNATQYLQRLEIAHKVSVMdgnfsTTDLS 466
Cdd:TIGR03269 99 lsdKLRRRIRKRiaiMLQRTFALYG--DDTVldnvlealeeigyEGKEA-VGRAVDLIEMVQLSHRITHI-----ARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 467 TGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFE-MADQLIRLSAGKVVKE 545
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENGEIKEE 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
359-544 |
4.09e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS-AETRDDYRQLFSTIFADYYLFDDL-------- 429
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMtvaenlyl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 --------VQGKQASLQNATQYLQRLEIAhkvsvMDGNFSTTDLSTGQRKRLALINAWLEERPVLVFDE-----WAADQD 496
Cdd:PRK11288 103 gqlphkggIVNRRLLNYEAREQLEHLGVD-----IDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEptsslSAREIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 259663656 497 PAFRrvfyteLLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVK 544
Cdd:PRK11288 178 QLFR------VIRELRAEGRVILYVSHRmEEIFALCDAITVFKDGRYVA 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-543 |
4.82e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL---FSTIFADYYLFDDL------ 429
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAArrkIGMIFQHFNLLSSRtvaenv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 -----VQG--KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRL----ALINawleeRP-VLVFDEwaADQ-- 495
Cdd:COG1135 104 alpleIAGvpKAEIRKRVAELLELVGLSDK-----ADAYPSQLSGGQKQRVgiarALAN-----NPkVLLCDE--ATSal 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 496 DPAfrrvfyT-----ELLPDLKRQ-GKTIIVISHddryfEM------ADQLIRLSAGKVV 543
Cdd:COG1135 172 DPE------TtrsilDLLKDINRElGLTIVLITH-----EMdvvrriCDRVAVLENGRIV 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
272-542 |
5.28e-10 |
|
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: 62.66 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 272 AITGFVMVLLY--MKGPLEQVVTILPIVSRAQVAFQRVaelserfsspepHLLLSEQEAPDKTVDSLELRD-------VR 342
Cdd:TIGR00957 573 AEKAFVSLALFniLRFPLNILPMVISSIVQASVSLKRL------------RIFLSHEELEPDSIERRTIKPgegnsitVH 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 343 YSPPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGE----PVSAETRDDYRQlfst 418
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvPQQAWIQNDSLR---- 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 419 ifaDYYLFDDLVQGK--QASLQnATQYLQRLEIAHKVSVMDGNFSTTDLSTGQRKRLALINAWLEERPVLVFDE--WAAD 494
Cdd:TIGR00957 717 ---ENILFGKALNEKyyQQVLE-ACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDplSAVD 792
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 259663656 495 QDPAfRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKV 542
Cdd:TIGR00957 793 AHVG-KHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
86-544 |
6.38e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 86 HIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTI----SDFSFSFTPLAIALTITFGCLGYLAYLSV----PM 157
Cdd:PLN03232 980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIdrnvANLMNMFMNQLWQLLSTFALIGTVSTISLwaimPL 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 158 FLLTVVAIVIgtaaqYLARSRGFKGFYAARdlEDELQKHYTAIASGAKELRIHRPRRyRMHTGRISETANNIR-DLHISS 236
Cdd:PLN03232 1060 LILFYAAYLY-----YQSTSREVRRLDSVT--RSPIYAQFGEALNGLSSIRAYKAYD-RMAKINGKSMDNNIRfTLANTS 1131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 237 IN--IFILAKTFGSMLFFVVIGLALTlqAYWPSSNPAAITGFVMVLL-YMKGPLEQVVTILPIVSRAQVAFQRVAELSER 313
Cdd:PLN03232 1132 SNrwLTIRLETLGGVMIWLTATFAVL--RNGNAENQAGFASTMGLLLsYTLNITTLLSGVLRQASKAENSLNSVERVGNY 1209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 314 FSSPEPHLLLSEQEAPDK---TVDSLELRDV--RYSP--PAVEGSEPFHLGPinlriaqGDIVFIVGENGCGKTTLIKLL 386
Cdd:PLN03232 1210 IDLPSEATAIIENNRPVSgwpSRGSIKFEDVhlRYRPglPPVLHGLSFFVSP-------SEKVGVVGRTGAGKSSMLNAL 1282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 387 LGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQGK--QASLQNATQYLQRLEIAHKVSVMDGNFSTTD 464
Cdd:PLN03232 1283 FRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNidPFSEHNDADLWEALERAHIKDVIDRNPFGLD 1362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 465 ---------LSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKrqGKTIIVISHDDRYFEMADQLI 535
Cdd:PLN03232 1363 aevseggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKIL 1440
|
....*....
gi 259663656 536 RLSAGKVVK 544
Cdd:PLN03232 1441 VLSSGQVLE 1449
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
21-307 |
1.21e-09 |
|
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: 59.43 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLAS-INNALHSENGlgqGVL----LSFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKEL 95
Cdd:cd18546 2 ALALLLVVVDTAASLAGPLLVRYgIDSGVRAGDL---GVLllaaAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 96 GEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIGTAAQYL 174
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELlQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 175 ARSRGFKGFYAARDLEDELQKHYTAIASGAKELRIHrpRRYRMHTGRISETANNIRDLHISSINIFILAKTFGSMLFFVV 254
Cdd:cd18546 159 FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAF--RRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 255 IGLALTLQAYWPSSN---PAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd18546 237 TAAVLLVGAWRVAAGtltVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
336-541 |
1.23e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYrPQ---SGEILLNGEPVSAET-RDD 411
Cdd:PRK13549 6 LEMKNITKTFGGVKA-----LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNiRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 412 YRQLFSTIFADYYLFDDLVQGKQASLQN----------------ATQYLQRLEIAhkvsvMDGNFSTTDLSTGQRKRLAL 475
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNeitpggimdydamylrAQKLLAQLKLD-----INPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 476 INAWLEERPVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGK 541
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLL-DIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
358-549 |
1.25e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 358 PINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVsaeTRDDYR---QLFSTIFAD------------ 422
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL---HFGDYSyrsQRIRMIFQDpstslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 423 ------YYLFDDLVQGKQASLQNATQYLQRLEIAHkvsvmdGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQD 496
Cdd:PRK15112 108 qildfpLRLNTDLEPEQREKQIIETLRQVGLLPDH------ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 259663656 497 PAFRRVFYTELLPDLKRQGKTII-VISHDDRYFEMADQLIRLSAGKVVKETETA 549
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIyVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
359-545 |
1.30e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA-ETRDDYRQL-----FSTIFADYYLFDDLVQG 432
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIgllaqNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 KQASLQNATQYLQRLEIA-----HKVSVMD-GNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAfRRVFYTE 506
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAvtkamQATGITHlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS-HQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 259663656 507 LLPDLKR-QGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK10253 185 LLSELNReKGYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
359-523 |
2.11e-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: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYrPQ---SGEILLNGEPVSAET-RDDYRQLFSTIFADYYLFDDLVQGKQ 434
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 435 ASLQN-----------ATQYLQRLEIAHKVSVMDGNFS--TTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRR 501
Cdd:TIGR02633 99 IFLGNeitlpggrmayNAMYLRAKNLLRELQLDADNVTrpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETE 178
|
170 180
....*....|....*....|..
gi 259663656 502 VFYtELLPDLKRQGKTIIVISH 523
Cdd:TIGR02633 179 ILL-DIIRDLKAHGVACVYISH 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
318-549 |
2.32e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 59.70 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 318 EPHLLLSEQEAPDKTVdsLELRDVRYSPP--------------AVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLI 383
Cdd:COG4172 260 EPRGDPRPVPPDAPPL--LEARDLKVWFPikrglfrrtvghvkAVDG--------VSLTLRRGETLGLVGESGSGKSTLG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 384 KLLLGLYrPQSGEILLNGEPVSAETRDDYRQL---FSTIFADYYlfddlvqgkqASL--------------------QNA 440
Cdd:COG4172 330 LALLRLI-PSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDPF----------GSLsprmtvgqiiaeglrvhgpgLSA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 441 TQYLQR-LEIAHKVSvMDGNFST---TDLSTGQRKRL----ALInawLEERpVLVFDEwaadqdPafrrvfyT------- 505
Cdd:COG4172 399 AERRARvAEALEEVG-LDPAARHrypHEFSGGQRQRIaiarALI---LEPK-LLVLDE------P-------Tsaldvsv 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 506 -----ELLPDL-KRQGKTIIVISHD---DRYfeMADQLIRLSAGKVVKETETA 549
Cdd:COG4172 461 qaqilDLLRDLqREHGLAYLFISHDlavVRA--LAHRVMVMKDGKVVEQGPTE 511
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
359-547 |
2.66e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.84 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLN------GEPVSAETR--DDYRQLFSTIFADYYLF---- 426
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGliRQLRQHVGFVFQNFNLFphrt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 427 --DDLVQG--------KQASLQNATQYLQRLEIAHKvsvmdGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQD 496
Cdd:PRK11264 102 vlENIIEGpvivkgepKEEATARARELLAKVGLAGK-----ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 497 PAF-RRVFYTelLPDLKRQGKTIIVISHDDRYF-EMADQLIRLSAGKVVKETE 547
Cdd:PRK11264 177 PELvGEVLNT--IRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGP 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
366-543 |
2.71e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRP---QSGEILLNGEPVSAE---TRDDYRQLFSTIFADYYLFDDLVQGKQASLQN 439
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKemrAISAYVQQDDLFIPTLTVREHLMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 440 ATQYLQRLEIAHKVSVMDGNFSTTD-----------LSTGQRKRLALINAWLEERPVLVFDEWAADQDpAFRRVFYTELL 508
Cdd:TIGR00955 131 RVTKKEKRERVDEVLQALGLRKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD-SFMAYSVVQVL 209
|
170 180 190
....*....|....*....|....*....|....*..
gi 259663656 509 PDLKRQGKTIIVISHDDRY--FEMADQLIRLSAGKVV 543
Cdd:TIGR00955 210 KGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVA 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
356-532 |
2.75e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL-FSTIFADYYLFDDLvqgkq 434
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEL----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 435 ASLQNAtqYLQRL--------------EIAHKVSVM--------DGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWA 492
Cdd:PRK09700 96 TVLENL--YIGRHltkkvcgvniidwrEMRVRAAMMllrvglkvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 259663656 493 AD-QDPAFRRVFYteLLPDLKRQGKTIIVISHD--------DRYFEMAD 532
Cdd:PRK09700 174 SSlTNKEVDYLFL--IMNQLRKEGTAIVYISHKlaeirricDRYTVMKD 220
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
21-189 |
3.23e-09 |
|
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: 58.17 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAG----GLAITLLLASINNALhseNGLGQGVLLsFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELG 96
Cdd:cd18544 6 LLLLLATALELLGplliKRAIDDYIVPGQGDL---QGLLLLALL-YLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 97 EKVLSAPIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIGTAAQYLA 175
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNElFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161
|
170
....*....|....
gi 259663656 176 RSRGFKGFYAARDL 189
Cdd:cd18544 162 RKKSRKAYREVREK 175
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
21-307 |
3.50e-09 |
|
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: 58.20 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLASINNALHSENGLGQGVLLSFGGLCLLAL--VSSIVSDIGTSYVGQHIIAKLRKELGEK 98
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLrgLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 99 VLSAPIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAI-VIGTAAQYLAR 176
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLpLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 177 SrgFKGfyAARDLEDELQKHYTAI---ASGAKELRIHrpRRYRMHTGRISETANNIRDLHISSINIFILAKTFgsMLFFV 253
Cdd:cd18552 162 R--LRK--ISRRSQESMGDLTSVLqetLSGIRVVKAF--GAEDYEIKRFRKANERLRRLSMKIARARALSSPL--MELLG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 254 VIGLALTL-QAYWPSSN----PAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd18552 234 AIAIALVLwYGGYQVISgeltPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
91-496 |
3.97e-09 |
|
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: 59.57 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 91 LRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISdfsfSFTPLAIALTIT--FGCLGYLA--YLSVPMFLLTVVAI- 165
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVD----SMIPPVIKMFMGslFNVIGALIviLLATPIAAVIIPPLg 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 166 VIGTAAQ--YLARSRGFKGFYAARdlEDELQKHYTAIASGAKELRIHRPRRYRMHTGRISETANNiRDLHISSINIFILA 243
Cdd:TIGR00957 1116 LLYFFVQrfYVASSRQLKRLESVS--RSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQ-KAYYPSIVANRWLA 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 244 KTFGSMLFFVVIGLALTLQAYWPSSNPAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAELSErfSSPEPHLLL 323
Cdd:TIGR00957 1193 VRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSE--TEKEAPWQI 1270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 324 SEQEAPDK--TVDSLELRD--VRYSPpavegSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIkllLGLYR---PQSGE 396
Cdd:TIGR00957 1271 QETAPPSGwpPRGRVEFRNycLRYRE-----DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGE 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 397 ILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVqgkQASLQNATQYLQR-----LEIAHK---VSVM-DG-NFSTTD-- 464
Cdd:TIGR00957 1343 IIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL---RMNLDPFSQYSDEevwwaLELAHLktfVSALpDKlDHECAEgg 1419
|
410 420 430
....*....|....*....|....*....|....
gi 259663656 465 --LSTGQRKRLALINAWLEERPVLVFDEWAADQD 496
Cdd:TIGR00957 1420 enLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
359-543 |
8.72e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDD----YRQLFSTIFA--DYYLFDDLVQ- 431
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEETVLk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 -----------GKQASLQNATQYLQRLEIAHKVsvmdGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAfR 500
Cdd:PRK13643 105 dvafgpqnfgiPKEKAEKIAAEKLEMVGLADEF----WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK-A 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 259663656 501 RVFYTELLPDLKRQGKTIIVISH-DDRYFEMADQLIRLSAGKVV 543
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHII 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-528 |
1.62e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLnGEPV-------SAETRDDYRQLFSTIFADYylfDDLVQ 431
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVklayvdqSRDALDPNKTVWEEISGGL---DIIKL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 GKQASlqNATQYLQRLeiahkvsvmdgNFSTTD-------LSTGQRKRLALINAWLEERPVLVFDEWAADQDpafrrvfy 504
Cdd:TIGR03719 417 GKREI--PSRAYVGRF-----------NFKGSDqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-------- 475
|
170 180
....*....|....*....|....*...
gi 259663656 505 TELLPDLKRQ----GKTIIVISHdDRYF 528
Cdd:TIGR03719 476 VETLRALEEAllnfAGCAVVISH-DRWF 502
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
351-542 |
1.81e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 351 SEPFH----LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLY---RPQSGEILLNGEPVSAETR--DDYRQLFST--- 418
Cdd:PRK09984 11 AKTFNqhqaLHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRlaRDIRKSRANtgy 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 419 IFADYYLFDDLVQGK---------------------QASLQNATQYLQRLEIAH----KVSVMDGnfsttdlstGQRKRL 473
Cdd:PRK09984 91 IFQQFNLVNRLSVLEnvligalgstpfwrtcfswftREQKQRALQALTRVGMVHfahqRVSTLSG---------GQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 474 ALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
226-472 |
1.97e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 226 ANNIRDLHISSINIFILAK-TFGSMLFFVVIGLALTLQAYWPSSNPAAITGF---VMVLLYMkgpleqVVTILPIVSRAQ 301
Cdd:PTZ00265 276 ANFMESLHIGMINGFILASyAFGFWYGTRIIISDLSNQQPNNDFHGGSVISIllgVLISMFM------LTIILPNITEYM 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 302 VAFQRVAELSERFSSpEPHLLLSEQEAPDKTVDSLELRDVRYSPPAVEGSEPFHlgPINLRIAQGDIVFIVGENGCGKTT 381
Cdd:PTZ00265 350 KSLEATNSLYEIINR-KPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYK--DLNFTLTEGKTYAFVGESGCGKST 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 382 LIKLLLGLYRPQSGEILLNGepvSAETRDD----YRQLFSTIFADYYLFDDlvqgkqaSLQNATQY----LQRLEIAHKV 453
Cdd:PTZ00265 427 ILKLIERLYDPTEGDIIIND---SHNLKDInlkwWRSKIGVVSQDPLLFSN-------SIKNNIKYslysLKDLEALSNY 496
|
250
....*....|....*....
gi 259663656 454 SVMDGNFSTTDLSTGQRKR 472
Cdd:PTZ00265 497 YNEDGNDSQENKNKRNSCR 515
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
336-545 |
2.70e-08 |
|
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: 54.07 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSppaVEGSEPfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGL--YRPQSGEILLNGEPVSAETRDDYR 413
Cdd:cd03217 1 LEIKDLHVS---VGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 414 QLfsTIFAdyylfddlvqgkqaslqnATQYLQRLEiahKVSVMD-------GnfsttdLSTGQRKRLALINAWLEERPVL 486
Cdd:cd03217 76 RL--GIFL------------------AFQYPPEIP---GVKNADflryvneG------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 487 VFDEWAA--DQDpAFRRVfyTELLPDLKRQGKTIIVISHDDRYFEM--ADQLIRLSAGKVVKE 545
Cdd:cd03217 127 ILDEPDSglDID-ALRLV--AEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKS 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
335-542 |
4.49e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDV--RYSppavEGSePFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY 412
Cdd:PTZ00243 1308 SLVFEGVqmRYR----EGL-PLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 413 RQLFSTIFADYYLFDDLVQGK-----QASLQNATQYLQRLEIAHKVS---------VMDGNfstTDLSTGQRKRLALINA 478
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNvdpflEASSAEVWAALELVGLRERVAsesegidsrVLEGG---SNYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259663656 479 WLEE-RPVLVFDEWAADQDPAFRRVFYTELLPDLkrQGKTIIVISHDDRYFEMADQLIRLSAGKV 542
Cdd:PTZ00243 1460 LLKKgSGFILMDEATANIDPALDRQIQATVMSAF--SAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
356-545 |
5.17e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA-ETRDDYRQLFST------IFADYYLFDD 428
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIvpegrrVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 LVQGkqASLQNATQYLQRLE--------IAHKVSVMDGNfsttdLSTGQRKRLALINAWLEERPVLVFDEWAADQDP-AF 499
Cdd:PRK11614 101 LAMG--GFFAERDQFQERIKwvyelfprLHERRIQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPiII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 259663656 500 RRVFYTelLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:PRK11614 174 QQIFDT--IEQLREQGMTIFLVEQNaNQALKLADRGYVLENGHVVLE 218
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-265 |
7.76e-08 |
|
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: 53.80 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 22 IVAVSIALGMAGGLAITLLLASINNAL--HSENGLGQGVLLS--FGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGE 97
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVLlpDGDPETQALNVYSlaLLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 98 KVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITFGCLGYLA-YLSVPMFLLTVVAIVIGTAAQYLaR 176
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMfYYGWKLTLVLLAVLPLYILVSAV-F 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 177 SRGFKGFYAARDLE-DELQKHYTAIASGAKELRIhrprrYRMHTGRISETANNIRDLHISSINIFILAKTFGSMLFFvvI 255
Cdd:pfam00664 162 AKILRKLSRKEQKAvAKASSVAEESLSGIRTVKA-----FGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQF--I 234
|
250
....*....|
gi 259663656 256 GLALTLQAYW 265
Cdd:pfam00664 235 GYLSYALALW 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
359-543 |
8.01e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRI-AQGdIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGepvsaetrddyRQLFST---------------IFAD 422
Cdd:PRK11144 17 VNLTLpAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-----------RVLFDAekgiclppekrrigyVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 423 YYLFDDL-VQG------KQASLQNATQYLQRLEIAHKVSvmdgNFSTTdLSTGQRKRLALINAWLEERPVLVFDEWAADQ 495
Cdd:PRK11144 85 ARLFPHYkVRGnlrygmAKSMVAQFDKIVALLGIEPLLD----RYPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 496 DPAFRRvfytELLPDLKRQGKT----IIVISHD-DRYFEMADQLIRLSAGKVV 543
Cdd:PRK11144 160 DLPRKR----ELLPYLERLAREinipILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
359-546 |
8.82e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSA---ETRDDYR-QLFSTIFADYYLFDDL----- 429
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeEARAKLRaKHVGFVFQSFMLIPTLnalen 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 VQ--------GKQASLQNATQYLQRLEIAHKVSVMdgnfsTTDLSTGQRKRLALINAWlEERPVLVF-DEWAADQD-PAF 499
Cdd:PRK10584 109 VElpallrgeSSRQSRNGAKALLEQLGLGKRLDHL-----PAQLSGGEQQRVALARAF-NGRPDVLFaDEPTGNLDrQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259663656 500 RRVfyTELLPDLKR-QGKTIIVISHDDRYFEMADQLIRLSAGKVVKET 546
Cdd:PRK10584 183 DKI--ADLLFSLNReHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
336-404 |
9.18e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 9.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 336 LELRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYrPQ---SGEILLNGEPV 404
Cdd:NF040905 2 LEMRGITKTFPGVKA-----LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVC 67
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
336-549 |
9.69e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS-AETRDDYRQ 414
Cdd:PRK10762 5 LQLKGIDKAFPGVKA-----LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 415 LFSTIFADYYLFDDLVQGKQASL-----------------QNATQYLQRLEIAHKVSVMDGnfsttDLSTGQRKRLALIN 477
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLgrefvnrfgridwkkmyAEADKLLARLNLRFSSDKLVG-----ELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 478 AWLEERPVLVFDEWA-ADQDPAFRRVFytELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKETETA 549
Cdd:PRK10762 155 VLSFESKVIIMDEPTdALTDTETESLF--RVIRELKSQGRGIVYISHRlKEIFEICDDVTVFRDGQFIAEREVA 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
363-524 |
1.18e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 363 IAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNgEPVS---AETRDDY----RQLFSTIFADY---YLFDDLVQG 432
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpQYIKPDYdgtvEDLLRSITDDLgssYYKSEIIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 kqasLQnatqyLQRLeiahkvsvMDGNFstTDLSTGQRKRLALINAWLEERPVLVFDEWAADQD--------PAFRRvfY 504
Cdd:PRK13409 441 ----LQ-----LERL--------LDKNV--KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRR--I 499
|
170 180
....*....|....*....|
gi 259663656 505 TEllpdlkRQGKTIIVISHD 524
Cdd:PRK13409 500 AE------EREATALVVDHD 513
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
25-170 |
1.21e-07 |
|
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: 53.33 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 25 VSIALGMAGGLAITLLLASINNALhSENGLGQGVLLSFGGLCLLALVSSIVSDIGT---SYVGQHIIAKLRKELGEKVLS 101
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTI-IKGGDLDVLNELALILLAIYLLQSVFTFVRYylfNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 102 APIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIALTITFGCLGYLAYLSV---PMFLLTVVAIVIGTA 170
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSaVTDNLSQLLRNILQVIGGLIILFILSWkltLVLLLVIPLLLIASK 154
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
309-545 |
1.63e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 309 ELSERFSSPEPhlllseqeAPDKTVdsLELRDVRySPPAVEgsepfhlgPINLRIAQGDIVFIVGENGCGKTTLIKLLLG 388
Cdd:COG1129 240 ELEDLFPKRAA--------APGEVV--LEVEGLS-VGGVVR--------DVSFSVRAGEILGIAGLVGAGRTELARALFG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 389 LYRPQSGEILLNGEPVSAET-RD-------------------------------DYRQLFSTIFADyylfddlvQGKQAS 436
Cdd:COG1129 301 ADPADSGEIRLDGKPVRIRSpRDairagiayvpedrkgeglvldlsirenitlaSLDRLSRGGLLD--------RRRERA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 437 LqnATQYLQRLEIahKVSVMDGNFSTtdLSTG-QRKrlALINAWLEERP-VLVFDEwaadqdP-------AfRRVFYtEL 507
Cdd:COG1129 373 L--AEEYIKRLRI--KTPSPEQPVGN--LSGGnQQK--VVLAKWLATDPkVLILDE------PtrgidvgA-KAEIY-RL 436
|
250 260 270
....*....|....*....|....*....|....*....
gi 259663656 508 LPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKVVKE 545
Cdd:COG1129 437 IRELAAEGKAVIVISSElPELLGLSDRILVMREGRIVGE 475
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
359-525 |
2.02e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.80 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPvsaetrDDYRQLFSTIfadYYL------------- 425
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEAC---HYLghrnamkpaltva 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 426 -----FDDLVQGKQASLQNAtqyLQRLEIAHkvsVMDGNFSttDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFR 500
Cdd:PRK13539 92 enlefWAAFLGGEELDIAAA---LEAVGLAP---LAHLPFG--YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*
gi 259663656 501 RVFyTELLPDLKRQGKTIIVISHDD 525
Cdd:PRK13539 164 ALF-AELIRAHLAQGGIVIAATHIP 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-404 |
2.37e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 2.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDVRYSPPAveGSEPFHlgPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV 404
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIK--GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV 68
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-524 |
2.64e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 337 ELRDVRYSPPAVEGsePFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS-AETRDDYRQ- 414
Cdd:PRK11288 252 PLGEVRLRLDGLKG--PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAg 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 415 --------LFSTIFA--------------DYYLFDDLVQGKQASlQNATQYLQRLEI---AHKVSVMdgnfsttDLSTG- 468
Cdd:PRK11288 330 imlcpedrKAEGIIPvhsvadninisarrHHLRAGCLINNRWEA-ENADRFIRSLNIktpSREQLIM-------NLSGGn 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 469 QRKrlALINAWLEER-PVLVFDEWAADQDPAFRRVFYtELLPDLKRQGKTIIVISHD 524
Cdd:PRK11288 402 QQK--AILGRWLSEDmKVILLDEPTRGIDVGAKHEIY-NVIYELAAQGVAVLFVSSD 455
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
328-415 |
2.78e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 328 APDKTVdsLELRDVRYSP----PAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEP 403
Cdd:COG3845 252 EPGEVV--LEVENLSVRDdrgvPALKD--------VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
90
....*....|..
gi 259663656 404 VSAETRDDYRQL 415
Cdd:COG3845 322 ITGLSPRERRRL 333
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
338-404 |
2.94e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 2.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 338 LRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV 404
Cdd:PRK10982 1 MSNISKSFPGVKA-----LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI 62
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
24-167 |
4.11e-07 |
|
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: 51.72 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 24 AVSIALGMAGGLAITLLLAS-INNALHSENGLG-QGVLLSFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGEKVLS 101
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQlIDAALGGGDTASlNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 102 APIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIALTITFGCLGYLAYLSVP---MFLLTVVAIVI 167
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDtLTTTLAEFLRQILTLIGGVVLLFFISWKltlLMLATVPVVVL 151
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-540 |
4.41e-07 |
|
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: 50.79 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 350 GSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY--RQLFSTIFADY--YL 425
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsRNRYSVAYAAQkpWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 426 FDDLVQ---------GKQ--------ASLQNATQYL---QRLEIAHKvsvmdgnfsTTDLSTGQRKRLALINAWLEERPV 485
Cdd:cd03290 91 LNATVEenitfgspfNKQrykavtdaCSLQPDIDLLpfgDQTEIGER---------GINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 486 LVFDEWAADQDPAFRRVFYTE-LLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAG 540
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
366-524 |
5.16e-07 |
|
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: 51.21 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRPQSGEilLNGEPVSAETRDDYRqlfSTIFADYY---LFDDL------------- 429
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFR---GSELQNYFtklLEGDVkvivkpqyvdlip 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 --VQGKQASLQNAT-------QYLQRLEIAHkvsVMDGNFSttDLSTGQRKRLALINAWLEERPVLVFDEWAADQDpAFR 500
Cdd:cd03236 101 kaVKGKVGELLKKKdergkldELVDQLELRH---VLDRNID--QLSGGELQRVAIAAALARDADFYFFDEPSSYLD-IKQ 174
|
170 180
....*....|....*....|....
gi 259663656 501 RVFYTELLPDLKRQGKTIIVISHD 524
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
234-545 |
5.97e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 234 ISSINIFILAK-----TFGSMLFFVVIGLALTlqaywpssnPAaiTGFVMVLLY--MKGPLEQVVTILPIVSRAQVAFQR 306
Cdd:PLN03130 522 LSAFNSFILNSipvlvTVVSFGVFTLLGGDLT---------PA--RAFTSLSLFavLRFPLFMLPNLITQAVNANVSLKR 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 307 VAEL---SERFSSPEPHLllsEQEAPdktvdSLELRDVRYSPPAvEGSEPfHLGPINLRIAQGDIVFIVGENGCGKTTLI 383
Cdd:PLN03130 591 LEELllaEERVLLPNPPL---EPGLP-----AISIKNGYFSWDS-KAERP-TLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 384 KLLLGLYRPQS-GEILLNGepvsaetRDDYRQLFSTIF----ADYYLFddlvqgkqASLQNATQYLQRLEIA---HKVSV 455
Cdd:PLN03130 661 SAMLGELPPRSdASVVIRG-------TVAYVPQVSWIFnatvRDNILF--------GSPFDPERYERAIDVTalqHDLDL 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 456 MDGNFST------TDLSTGQRKRLALINAWLEERPVLVFDE--WAADQDPAfRRVFYTELLPDLkrQGKTIIVISHDDRY 527
Cdd:PLN03130 726 LPGGDLTeigergVNISGGQKQRVSMARAVYSNSDVYIFDDplSALDAHVG-RQVFDKCIKDEL--RGKTRVLVTNQLHF 802
|
330
....*....|....*...
gi 259663656 528 FEMADQLIRLSAGKVVKE 545
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEE 820
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
21-167 |
7.38e-07 |
|
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: 50.93 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLA-SINNALHSEN--GLGQGVLLsFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGE 97
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKiAIDEYIPNGDlsGLLIIALL-FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259663656 98 KVLSAPIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVI 167
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDlLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
363-524 |
7.98e-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: 51.71 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 363 IAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGE----P--VSAETRDDYRQLFSTIFADYYlfddlvqgkQAS 436
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykPqyISPDYDGTVEEFLRSANTDDF---------GSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 437 LQNaTQYLQRLEIAHkvsVMDGNFSttDLSTGQRKRLALINAWLEERPVLVFDEWAADQD--------PAFRRvfYTEll 508
Cdd:COG1245 434 YYK-TEIIKPLGLEK---LLDKNVK--DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRR--FAE-- 503
|
170
....*....|....*.
gi 259663656 509 pdlkRQGKTIIVISHD 524
Cdd:COG1245 504 ----NRGKTAMVVDHD 515
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
356-543 |
9.35e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDDYRQLFSTIFADYYlfddlvqg 432
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 kqASLQ---------------NATqyLQRLEIAHKVSVMdgnFSTTDL------------STGQRKRLALINAWLEERPV 485
Cdd:PRK11308 103 --GSLNprkkvgqileeplliNTS--LSAAERREKALAM---MAKVGLrpehydryphmfSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259663656 486 LVFDEWAADQDPAFR-RVFytELLPDLKRQGKTIIV-ISHDDRYFE-MADQLIRLSAGKVV 543
Cdd:PRK11308 176 VVADEPVSALDVSVQaQVL--NLMMDLQQELGLSYVfISHDLSVVEhIADEVMVMYLGRCV 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-548 |
9.37e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEgsepfHLGPINLRIAQGDIVFIVGENGCGKTTLIKL---LLGLYrPQ---SGEILLNGEPV----S 405
Cdd:PRK14247 4 IEIRDLKVSFGQVE-----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELY-PEarvSGEVYLDGQDIfkmdV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 406 AETRDDYRQLFS--------TIFADYYL---FDDLVQGKQASLQNATQYLQRLEIAHKVSvMDGNFSTTDLSTGQRKRLA 474
Cdd:PRK14247 78 IELRRRVQMVFQipnpipnlSIFENVALglkLNRLVKSKKELQERVRWALEKAQLWDEVK-DRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 475 LINAWLEERPVLVFDEWAADQDPAfRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKETET 548
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPE-NTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
343-422 |
1.27e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 343 YSPP----AVEGsepfhlgpINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDDYRQL 415
Cdd:PRK15079 28 WQPPktlkAVDG--------VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSD 99
|
....*..
gi 259663656 416 FSTIFAD 422
Cdd:PRK15079 100 IQMIFQD 106
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
21-167 |
1.70e-06 |
|
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: 49.70 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLAS-INNALHSENglgQGVLLSFGGL----CLLALVSSIVSDIGTSYVGQHIIAKLRKEL 95
Cdd:cd18548 2 ILAPLFKLLEVLLELLLPTLMADiIDEGIANGD---LSYILRTGLLmlllALLGLIAGILAGYFAAKASQGFGRDLRKDL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 96 GEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVI 167
Cdd:cd18548 79 FEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFvMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPI 151
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
326-545 |
1.83e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.40 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 326 QEAPDKTVDSLELRDVRYSPPaveGSEPFHlgPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS 405
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVP---GRTLLH--PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 406 aetrddyrQLFSTIFAD--YYLFDDLVQGKQASLQNAT---QY-----LQRLEIAHKVSVMD----------GNFSTTDL 465
Cdd:PRK10575 77 --------SWSSKAFARkvAYLPQQLPAAEGMTVRELVaigRYpwhgaLGRFGAADREKVEEaislvglkplAHRLVDSL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 466 STGQRKRlalinAWL-----EERPVLVFDEWAADQDPAfRRVFYTELLPDLKRQ-GKTIIVISHDdryFEMA----DQLI 535
Cdd:PRK10575 149 SGGERQR-----AWIamlvaQDSRCLLLDEPTSALDIA-HQVDVLALVHRLSQErGLTVIAVLHD---INMAarycDYLV 219
|
250
....*....|
gi 259663656 536 RLSAGKVVKE 545
Cdd:PRK10575 220 ALRGGEMIAQ 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-528 |
2.66e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEIL---------LNGEPVSAETRD----------DYRQL---F 416
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgikvgyLPQEPQLDPTKTvrenveegvaEIKDAldrF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 417 STIFADYYL----FDDLVQgKQASLQNATQYL------QRLEIAhkvsvMD------GNFSTTDLSTGQRKRLALINAWL 480
Cdd:TIGR03719 104 NEISAKYAEpdadFDKLAA-EQAELQEIIDAAdawdldSQLEIA-----MDalrcppWDADVTKLSGGERRRVALCRLLL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 481 EERPVLVFDE-----------WaadqdpafrrvfyteLLPDLKRQGKTIIVISHdDRYF 528
Cdd:TIGR03719 178 SKPDMLLLDEptnhldaesvaW---------------LERHLQEYPGTVVAVTH-DRYF 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
336-523 |
2.89e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 336 LELRDVRYSPPAVEGsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:PRK15439 12 LCARSISKQYSGVEV-----LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 416 -FSTIFADYYLFDDL---------VQGKQASLQNATQYLQRLEIAHKVSVMDGNFSTTDlstgqRKRLALINAWLEERPV 485
Cdd:PRK15439 87 gIYLVPQEPLLFPNLsvkenilfgLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVAD-----RQIVEILRGLMRDSRI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 259663656 486 LVFDEWAADQDPAFRRVFYTElLPDLKRQGKTIIVISH 523
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSR-IRELLAQGVGIVFISH 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
366-524 |
3.15e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.11 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDY----RQLFSTIFADYYLFDDLV----------- 430
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLvayvPQSEEVDWSFPVLVEDVVmmgryghmgwl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 431 -QGKQASLQNATQYLQR---LEIAHKvsvmdgnfSTTDLSTGQRKRLALINAWLEERPVLVFDE--WAADQDPAFRRVfy 504
Cdd:PRK15056 113 rRAKKRDRQIVTAALARvdmVEFRHR--------QIGELSGGQKKRVFLARAIAQQGQVILLDEpfTGVDVKTEARII-- 182
|
170 180
....*....|....*....|
gi 259663656 505 tELLPDLKRQGKTIIVISHD 524
Cdd:PRK15056 183 -SLLRELRDEGKTMLVSTHN 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
335-543 |
3.19e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 335 SLELRDV--RYSP--PAVegsepfhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRD 410
Cdd:PLN03130 1237 SIKFEDVvlRYRPelPPV-------LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 411 DYRQLFSTIFADYYLF--------DDLVQGKQASLQNAtqylqrLEIAHKVSVMDGNFSTTD---------LSTGQRKRL 473
Cdd:PLN03130 1310 DLRKVLGIIPQAPVLFsgtvrfnlDPFNEHNDADLWES------LERAHLKDVIRRNSLGLDaevseagenFSVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259663656 474 ALINAWLEERPVLVFDEWAADQDpafrrVFYTELLPDLKRQ---GKTIIVISHDDRYFEMADQLIRLSAGKVV 543
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD-----VRTDALIQKTIREefkSCTMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
394-535 |
4.72e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 394 SGEILLNGEPVSAETRDDYRQLFSTIFADYYLF-----DDLVQGKQ-ASLQNATQYLQRLEIAHKVSVMDGNFSTT---- 463
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFnmsiyENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNvgpy 1355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 464 --DLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLI 535
Cdd:PTZ00265 1356 gkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
21-307 |
5.06e-06 |
|
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: 48.58 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLAS-INNALhsENGLGQGVLLSFGGLCLLALVSSI---VSDIGTSYVGQHIIAKLRKELG 96
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRiIDSVI--GGGLRELLWLLALLILGVALLRGVfryLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 97 EKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFL--LTVVAIVIGTAAQY 173
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFlAFGLVELVRAVLLFIGALIIMFSINWKLTLisLAIIPFIALFSYVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 174 LARSRgfKGFYAARDLEDELqkhyTAIA----SG-------AKElrihrprRYRMhtGRISETANNIRDLHISSINIFil 242
Cdd:cd18542 160 FKKVR--PAFEEIREQEGEL----NTVLqenlTGvrvvkafARE-------DYEI--EKFDKENEEYRDLNIKLAKLL-- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 243 AKTFGSM--LFFVVIGLALTLQAYWpssnpaAITG---------FVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd18542 223 AKYWPLMdfLSGLQIVLVLWVGGYL------VINGeitlgelvaFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
365-419 |
1.13e-05 |
|
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: 45.44 E-value: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 365 QGDIVFIVGENGCGKTTLIKLLLGLYRPQSGE-ILLNGEPVSAETRDDYRQLFSTI 419
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGG 56
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
366-524 |
2.13e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPV---SAETRDDYRQLFSTIFADYYLFDD-------------- 428
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYASLDprqtvgdsimeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 ---LVQGKQASlQNATQYLQR--LEIAHKVSVmdgnfsTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVF 503
Cdd:PRK10261 430 vhgLLPGKAAA-ARVAWLLERvgLLPEHAWRY------PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180
....*....|....*....|..
gi 259663656 504 yTELLPDLKRQ-GKTIIVISHD 524
Cdd:PRK10261 503 -INLLLDLQRDfGIAYLFISHD 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
359-397 |
2.38e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 2.38e-05
10 20 30
....*....|....*....|....*....|....*....
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEI 397
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
336-397 |
2.77e-05 |
|
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: 44.45 E-value: 2.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259663656 336 LELRDVRYSPPAvegSEPFhLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEI 397
Cdd:cd03223 1 IELENLSLATPD---GRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI 58
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
359-544 |
3.08e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLG--LYRPQSGEILLNGEPVSAETRDDYRQLfsTIF-ADYYLFD-------D 428
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL--GIFlAFQYPIEipgvsnaD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 LVQ----GKQASLQ----NATQYLQRLEIAHKVSVMDGNFSTTDL----STGQRKR-----LALINAWLEerpvlVFDEW 491
Cdd:CHL00131 104 FLRlaynSKRKFQGlpelDPLEFLEIINEKLKLVGMDPSFLSRNVnegfSGGEKKRneilqMALLDSELA-----ILDET 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 259663656 492 AADQD-PAFRRVfyTELLPDLKRQGKTIIVISHDDRYFE--MADQLIRLSAGKVVK 544
Cdd:CHL00131 179 DSGLDiDALKII--AEGINKLMTSENSIILITHYQRLLDyiKPDYVHVMQNGKIIK 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
360-404 |
3.26e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 259663656 360 NLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLnGEPV 404
Cdd:PRK11819 344 SFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV 387
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
359-526 |
3.47e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.27 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGE-----PVSAETRDD----------YRQL--FSTIFA 421
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRGigylpqeasiFRRLsvYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 422 DYYLFDDLVQGKQAslQNATQYLQRLEIAHkvsvMDGNFSTTdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPaFRR 501
Cdd:PRK10895 102 VLQIRDDLSAEQRE--DRANELMEEFHIEH----LRDSMGQS-LSGGERRRVEIARALAANPKFILLDEPFAGVDP-ISV 173
|
170 180
....*....|....*....|....*
gi 259663656 502 VFYTELLPDLKRQGKTIIVISHDDR 526
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNVR 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
366-523 |
4.35e-05 |
|
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: 46.55 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL-----FSTIfadyylfDDLVQGKQ-----A 435
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycpqFDAI-------DDLLTGREhlylyA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 SLQN---------ATQYLQRLEIAHKVSVMDGNFsttdlSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTE 506
Cdd:TIGR01257 2038 RLRGvpaeeiekvANWSIQSLGLSLYADRLAGTY-----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170
....*....|....*..
gi 259663656 507 LLpDLKRQGKTIIVISH 523
Cdd:TIGR01257 2113 IV-SIIREGRAVVLTSH 2128
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-524 |
4.74e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLngepvSAETRDDYrqlfstiFADYYLfdDLVQGKQA 435
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----AKGIKLGY-------FAQHQL--EFLRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 SLQNATQYLQRlEIAHKVSVMDGNFS---------TTDLSTGQRKR--LALInAWleERP-VLVFDEWAADQDPAFRRVF 503
Cdd:PRK10636 394 PLQHLARLAPQ-ELEQKLRDYLGGFGfqgdkvteeTRRFSGGEKARlvLALI-VW--QRPnLLLLDEPTNHLDLDMRQAL 469
|
170 180
....*....|....*....|.
gi 259663656 504 yTELLPDLKrqgKTIIVISHD 524
Cdd:PRK10636 470 -TEALIDFE---GALVVVSHD 486
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-167 |
6.74e-05 |
|
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: 44.78 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAggLAITLLLAS-INNALHSENG--LGQGVLLSFGGLCLLALVSSIVSDIgTSYVGQHIIAKLRKELGE 97
Cdd:cd18575 1 ALIALLIAAAAT--LALGQGLRLlIDQGFAAGNTalLNRAFLLLLAVALVLALASALRFYL-VSWLGERVVADLRKAVFA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259663656 98 KVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITF-GCLGYLAYLSVPMFLLTVVAIVI 167
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLiGGLVMLFITSPKLTLLVLLVIPL 148
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
303-399 |
6.76e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.57 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 303 AFQRVAELSERFSSPEPHLLLSEQeapdktvDSLELRDVRYSPPAvegSEPFhLGPINLRIAQGDIVFIVGENGCGKTTL 382
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSED-------GALALEDLTLRTPD---GRPL-LEDLSLSLKPGERLLITGPSGSGKSTL 405
|
90
....*....|....*..
gi 259663656 383 IKLLLGLYRPQSGEILL 399
Cdd:COG4178 406 LRAIAGLWPYGSGRIAR 422
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
25-281 |
7.24e-05 |
|
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: 44.96 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 25 VSIALGMAGGLAITLLLASINNALHSENglgqgVLLSFGGLCLLALVSSIV---SDIGTSYVGQHIIAKLRKELGEKVLS 101
Cdd:cd18561 7 LITALYIAQAWLLARALARIFAGGPWED-----IMPPLAGIAGVIVLRAALlwlRERVAHRAAQRVKQHLRRRLFAKLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 102 APIEQIERYRTHRLIPVLTHDIDTISDFSFSFTP-LAIALTITFGCLGYLAYLSVPMFLL---TVVAIVIGTAAQY-LAR 176
Cdd:cd18561 82 LGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPqLLVALLGPLLILIYLFFLDPLVALIllvFALLIPLSPALWDrLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 177 SRGFKGFYAARDLEDelqkHYTAIASGAKELRIhrprrYRMHTGRISETANNIRDLHISSINIFILAK-TFGSMLFFVVI 255
Cdd:cd18561 162 DTGRRHWAAYGRLSA----QFLDSLQGMTTLKA-----FGASKRRGNELAARAEDLRQATMKVLAVSLlSSGIMGLATAL 232
|
250 260
....*....|....*....|....*...
gi 259663656 256 GLALTL--QAYWPSSNPAAITGFVMVLL 281
Cdd:cd18561 233 GTALALgvGALRVLGGQLTLSSLLLILF 260
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
356-406 |
7.39e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 7.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLY----RPQ----SGEILLNGEPVSA 406
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRgarvTGDVTLNGEPLAA 75
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-542 |
1.20e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAE-TRDDYRQLFSTIFAD---YYLFDD------ 428
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLPEDrqsSGLYLDaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 ---LVQGKQASLQNATQYLQRLEIAHK---VSVMDGNFSTTDLSTGQRKRLaLINAWLEERP-VLVFDEWAADQDPAFRR 501
Cdd:PRK15439 362 vcaLTHNRRGFWIKPARENAVLERYRRalnIKFNHAEQAARTLSGGNQQKV-LIAKCLEASPqLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 259663656 502 VFYtELLPDLKRQGKTIIVISHD-DRYFEMADQLIRLSAGKV 542
Cdd:PRK15439 441 DIY-QLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
356-524 |
2.64e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.79 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLngepvSAETRDDY----RQLFSTIFADYYLFDDLVQ 431
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR-----NGKLRIGYvpqkLYLDTTLPLTVNRFLRLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 432 G-KQASLQNAtqyLQRLEIAHKVsvmdgNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYtELLPD 510
Cdd:PRK09544 95 GtKKEDILPA---LKRVQAGHLI-----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY-DLIDQ 165
|
170
....*....|....*
gi 259663656 511 LKRQ-GKTIIVISHD 524
Cdd:PRK09544 166 LRRElDCAVLMVSHD 180
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
363-405 |
3.60e-04 |
|
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: 41.79 E-value: 3.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 259663656 363 IAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVS 405
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV 64
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-184 |
4.38e-04 |
|
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: 42.50 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 27 IALGMAGGLAITLL-LAS-------INNALH--SENGLGQGVLLSFGGLCLLALVSSIVSDIGT---SYVGQHIIAKLRK 93
Cdd:cd18563 1 LILGFLLMLLGTALgLVPpyltkilIDDVLIqlGPGGNTSLLLLLVLGLAGAYVLSALLGILRGrllARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 94 ELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDF-SFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIGTAAQ 172
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFlSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170
....*....|..
gi 259663656 173 YLARSRGFKGFY 184
Cdd:cd18563 161 YFFWKKIRRLFH 172
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
81-173 |
7.59e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, 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. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 41.76 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 81 SYVGQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDidtISDFSFSFTpLAI-----ALTITFGCLGYLAYLSV 155
Cdd:cd18574 67 SVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSSFK-QCVsqglrSVTQTVGCVVSLYLISP 142
|
90 100
....*....|....*....|
gi 259663656 156 PM--FLLTVVAIVIGTAAQY 173
Cdd:cd18574 143 KLtlLLLVIVPVVVLVGTLY 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-540 |
9.67e-04 |
|
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: 42.20 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGepvsaetRDDYRQLFSTIFADyYLFDDLVQG--- 432
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQTSWIMPG-TIKDNIIFGlsy 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 433 ---KQASLQNATQY---LQRLEIAHKVSVMDGNFSttdLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTE 506
Cdd:TIGR01271 514 deyRYTSVIKACQLeedIALFPEKDKTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
170 180 190
....*....|....*....|....*....|....
gi 259663656 507 LLPDLkRQGKTIIVISHDDRYFEMADQLIRLSAG 540
Cdd:TIGR01271 591 CLCKL-MSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
346-402 |
9.80e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 9.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 346 PAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGE 402
Cdd:PRK13546 30 PKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
12-167 |
1.26e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 40.96 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 12 LLALLRP--FRAIV-AVSIALGMAGGLAITLLLASINNALhsenglgqgVLLSFGGLCLLALVSSIVS---DIGTSYVGQ 85
Cdd:cd18564 13 ALRLLEPwpLKVVIdDVLGDKPLPGLLGLAPLLGPDPLAL---------LLLAAAALVGIALLRGLASyagTYLTALVGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 86 HIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFS-FTPLAIALTITFGCLGYLAYLSVPmflLTVVA 164
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSgVLPLLTNLLTLVGMLGVMFWLDWQ---LALIA 160
|
...
gi 259663656 165 IVI 167
Cdd:cd18564 161 LAV 163
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
366-398 |
1.66e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|...
gi 259663656 366 GDIVFIVGENGCGKTTLIKLLLGLYRPQSGEIL 398
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
368-540 |
1.67e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 368 IVFIVGENGCGKTTLIKLL-LGLYRPQSGEILLNGEPVSAETRDDYRQlfSTIFAdYY-----LFDDLVQGKQASLQNAT 441
Cdd:COG3950 27 LTVLVGENGSGKTTLLEAIaLALSGLLSRLDDVKFRKLLIRNGEFGDS--AKLIL-YYgtsrlLLDGPLKKLERLKEEYF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 442 QYLQRLeiahkvsvmDGNFSttdlstgQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFY--TELLPDLK-----RQ 514
Cdd:COG3950 104 SRLDGY---------DSLLD-------EDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREalNKLLPDFKdiridRD 167
|
170 180
....*....|....*....|....*.
gi 259663656 515 GKTIIVISHDDRYFEMADqlirLSAG 540
Cdd:COG3950 168 PGRLVILDKNGEELPLNQ----LSDG 189
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
21-307 |
1.74e-03 |
|
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: 40.54 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLAS-INNAL--HSENGLGQGVLLsFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGE 97
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTRRaIDGPIahGDRSALWPLVLL-LLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 98 KVLSAPIEQIERYRTHRLIPVLTHDIDTISDFsFSFTPLAIALTITF-GCLGYLAYLSVPMFLLTVVAIVIGTAAQYLAR 176
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF-LAFGPFLLGNLLTLvVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 177 SRGFKGFYAARDLEDELQKHYTAIASGakeLRIHRP--RRYRMhTGRISETANNIRDLHISSIniFILAKTFGSMLFFVV 254
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTG---IRVVKAfgRERRE-LDRFEAAARRLRATRLRAA--RLRARFWPLLEALPE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 255 IGLALTLqAY--WpssnpAAITG---------FVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd18543 234 LGLAAVL-ALggW-----LVANGsltlgtlvaFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
371-525 |
1.96e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 371 IVGENGCGKTTLIKLLLGLYrPQ--SGEILL------NGEP----------VSAETRDDYR---QLFSTIFADYylFDDL 429
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGDH-PQgySNDLTLfgrrrgSGETiwdikkhigyVSSSLHLDYRvstSVRNVILSGF--FDSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 430 -----VQGKQASLqnATQYLQRLEIAHKVSvmDGNFSttDLSTGQrKRLALI-NAWLEERPVLVFDEWAADQDPAFR--- 500
Cdd:PRK10938 368 giyqaVSDRQQKL--AQQWLDILGIDKRTA--DAPFH--SLSWGQ-QRLALIvRALVKHPTLLILDEPLQGLDPLNRqlv 440
|
170 180
....*....|....*....|....*.
gi 259663656 501 RVFYTELLpdlkRQGKT-IIVISHDD 525
Cdd:PRK10938 441 RRFVDVLI----SEGETqLLFVSHHA 462
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
349-523 |
2.17e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 349 EGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGepvSAetrddyrqlfSTIFADYYLFDD 428
Cdd:PRK13545 33 DGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SA----------ALIAISSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 429 LVQGKQASLQNATQYLQRLEIAHKV-SVMD----GNF---STTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFR 500
Cdd:PRK13545 100 LTGIENIELKGLMMGLTKEKIKEIIpEIIEfadiGKFiyqPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180
....*....|....*....|...
gi 259663656 501 RVFYtELLPDLKRQGKTIIVISH 523
Cdd:PRK13545 180 KKCL-DKMNEFKEQGKTIFFISH 201
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
356-544 |
2.30e-03 |
|
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: 39.89 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 356 LGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQGKQA 435
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 436 SLQNAT--QYLQRLEIAH---KVSVMDGNFSTT------DLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFY 504
Cdd:cd03288 117 PECKCTddRLWEALEIAQlknMVKSLPGGLDAVvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 259663656 505 TELLPDLKrqGKTIIVISHDDRYFEMADQLIRLSAGKVVK 544
Cdd:cd03288 197 KVVMTAFA--DRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
465-538 |
3.21e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 465 LSTGQRK--RLALINAWLEERPV--LVFDEWAADQDPAfrrvfYTELLPD-LKRQGKT--IIVISHDDRYFEMADQLIRL 537
Cdd:pfam02463 1078 LSGGEKTlvALALIFAIQKYKPApfYLLDEIDAALDDQ-----NVSRVANlLKELSKNaqFIVISLREEMLEKADKLVGV 1152
|
.
gi 259663656 538 S 538
Cdd:pfam02463 1153 T 1153
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
346-415 |
3.26e-03 |
|
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: 40.05 E-value: 3.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259663656 346 PAVEGsepfhlgpINLRIAQGDIVFIVGENGCGKT----TLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQL 415
Cdd:COG4172 24 EAVKG--------VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRI 89
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
359-410 |
3.27e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.63 E-value: 3.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 259663656 359 INLRIAQGDIVFIVGENGCGKTTLIKLL---LGLYRPQ--SGEILLNGEPVSAETRD 410
Cdd:COG1117 30 INLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEDIYDPDVD 86
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
353-401 |
4.54e-03 |
|
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: 39.07 E-value: 4.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 259663656 353 PFHLGP----INLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNG 401
Cdd:cd03291 46 CLVGAPvlknINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
368-397 |
4.74e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 4.74e-03
10 20 30
....*....|....*....|....*....|
gi 259663656 368 IVFIVGENGCGKTTLIKLLLGLYRPQSGEI 397
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-307 |
5.65e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 39.00 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 21 AIVAVSIALGMAGGLAITLLLAS-INNALhSENGLGQGVLLSfGGLCLLALVSSIVSdIGTSY----VGQHIIAKLRKEL 95
Cdd:cd18550 2 ALVLLLILLSALLGLLPPLLLREiIDDAL-PQGDLGLLVLLA-LGMVAVAVASALLG-VVQTYlsarIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 96 GEKVLSAPIEQIERYRTHRLIPVLTHDIDTISD-FSFSFTPLAIALTITFGCLGYLAYLSVPmflLTVVAIVIGTAAQYL 174
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSvVTGTLTSVVSNVVTLVATLVAMLALDWR---LALLSLVLLPLFVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 175 ARSRGFKgfyaARDLEDELQKHYTAI---------ASGAKELRIHRPRRYRMHtgRISETANNIRDLHISSiniFILAKT 245
Cdd:cd18550 156 TRRVGRR----RRKLTREQQEKLAELnsimqetlsVSGALLVKLFGREDDEAA--RFARRSRELRDLGVRQ---ALAGRW 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259663656 246 FGSMLFFVV-IGLALTlqaYWPSSNPAA--------ITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRV 307
Cdd:cd18550 227 FFAALGLFTaIGPALV---YWVGGLLVIgggltigtLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
368-390 |
8.74e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 8.74e-03
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
363-531 |
8.91e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 37.97 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 363 IAQGDIVFIVGENGCGKTTLikLLLGLYrpqsgEILLNGEPVSaetrddyrqlfstifadYYLFDdlvQGKQASLQNATQ 442
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTTL--ALQFLA-----EGLRRGEKGL-----------------YVSFE---ESPEQLLRRAES 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259663656 443 Y---LQRLEIAHKVSVMDgnFSTTDLSTGQRKRLALINAWLEERP--VLVFDEW----AADQDPAFRRVFYTELLPDLKR 513
Cdd:COG0467 70 LgldLEEYIESGLLRIID--LSPEELGLDLEELLARLREAVEEFGakRVVIDSLsgllLALPDPERLREFLHRLLRYLKK 147
|
170
....*....|....*...
gi 259663656 514 QGKTIIVISHDDRYFEMA 531
Cdd:COG0467 148 RGVTTLLTSETGGLEDEA 165
|
|
| |
