|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-524 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 736.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 30 PAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLG 109
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAS-THEDELVRLMVGRD 268
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAeLTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 269 ITEQYPRRTHTPGdEVLLDVRGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPR 348
Cdd:COG1129 241 LEDLFPKRAAAPG-EVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 349 SVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGN 428
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 429 QQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAA 508
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDRE 479
|
490
....*....|....*.
gi 502628485 509 TATQDQVMALAVKHAD 524
Cdd:COG1129 480 EATEEAIMAAATGGAA 495
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-519 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 531.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGI 110
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARV 190
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 191 LILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP--ASTHEDELVRLMVGRD 268
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdmAQVDRDQLVQAMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 269 ITEQYPRRTHTPGDeVLLDVRGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPR 348
Cdd:PRK11288 242 IGDIYGYRPRPLGE-VRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 349 SVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSRAG-FADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGG 427
Cdd:PRK11288 321 SPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPA 507
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAR 480
|
490
....*....|..
gi 502628485 508 ATATQDQVMALA 519
Cdd:PRK11288 481 EQATERQALSLA 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-524 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 528.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYqPDG---GRVVVDGKPVHLGSVRDAERL 108
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIATIHQELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 189 RVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST-HEDELVRLMVGR 267
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGmTEDDIITMMVGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 268 DITEQYPRRTHTPGDEVlLDVRGLS-------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADP-YDAGTVH 339
Cdd:PRK13549 243 ELTALYPREPHTIGEVI-LEVRNLTawdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 340 VDGQRLPPRSVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQ 419
Cdd:PRK13549 322 IDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 420 AARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGG 499
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
490 500
....*....|....*....|....*
gi 502628485 500 RLTGELPAATATQDQVMALAVKHAD 524
Cdd:PRK13549 482 KLKGDLINHNLTQEQVMEAALRSEH 506
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-517 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 522.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 29 APAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERL 108
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIATIHQELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 189 RVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEV-PASTHEDELVRLMVGR 267
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVdTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 268 DITEQYPRRTHTPGdEVLLDVRGLSRTG-----VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDG 342
Cdd:COG3845 241 EVLLRVEKAPAEPG-EVVLEVENLSVRDdrgvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 343 QRLPPRSVGSAVAAGIGHVPEDRKGQGLVLDASVAEN--LGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQA 420
Cdd:COG3845 320 EDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENliLGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 421 ARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490 500
....*....|....*....|
gi 502628485 501 LTGELPAATATQDQV---MA 517
Cdd:COG3845 480 IVGEVPAAEATREEIgllMA 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-520 |
1.80e-172 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 496.83 E-value: 1.80e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIA 111
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENVLMGRLP-SRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARV 190
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFvNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 191 LILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP-ASTHEDELVRLMVGRDI 269
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREvADLTEDSLIEMMVGRKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 270 TEQYPRRTHTPGdEVLLDVRGLSRTGVlHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRS 349
Cdd:PRK10762 243 EDQYPRLDKAPG-EVRLKVDNLSGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 350 VGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRL-RIRMRDVDQAARDLSGGN 428
Cdd:PRK10762 321 PQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLfNIKTPSMEQAIGLLSGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 429 QQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAA 508
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
490
....*....|..
gi 502628485 509 TATQDQVMALAV 520
Cdd:PRK10762 481 QATQEKLMAAAV 492
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
33-518 |
2.99e-169 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 488.53 E-value: 2.99e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYqPDG---GRVVVDGKPVHLGSVRDAERLG 109
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST---HEDELVRLMVG 266
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRAdevTEDRIIRGMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 267 RDITEQYPRRTHTPGdEVLLDVRGLS--------RTgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAD--PYDAG 336
Cdd:NF040905 240 RDLEDRYPERTPKIG-EVVFEVKNWTvyhplhpeRK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 337 TVHVDGQRLPPRSVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRD 416
Cdd:NF040905 318 TVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 417 VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVM 496
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVM 477
|
490 500
....*....|....*....|..
gi 502628485 497 SGGRLTGELPAATATQDQVMAL 518
Cdd:NF040905 478 NEGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-523 |
3.90e-146 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 429.97 E-value: 3.90e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIA 111
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENVLMGRLPSRGGF----VSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLN 187
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 188 ARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE-VPASTHEDELVRLMVG 266
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSgMVSDVSNDDIVRLMVG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 267 RDITEQYPRRTHTPGD---EVLLDVRGLSR--TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVD 341
Cdd:PRK09700 244 RELQNRFNAMKENVSNlahETVFEVRNVTSrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 342 GQRLPPRSVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSR----AGFADRRGQRSRAQEVASRLRIRMRDV 417
Cdd:PRK09700 324 GKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGykgaMGLFHEVDEQRTAENQRELLALKCHSV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 418 DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMS 497
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC 483
|
490 500
....*....|....*....|....*..
gi 502628485 498 GGRLTGELPA-ATATQDQVMALAVKHA 523
Cdd:PRK09700 484 EGRLTQILTNrDDMSEEEIMAWALPQE 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-520 |
5.73e-143 |
|
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: 421.54 E-value: 5.73e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYqPDG---GRVVVDGKPVHLGSVRDAERLG 109
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLMG-RLPSRGGFVSRRTMRRLAREALDRVRLDVSLDT-PVGELGIARQQLVEIAKALSLN 187
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 188 ARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST-HEDELVRLMVG 266
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTmSEDDIITMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 267 RDITEQYPRRTHTPGDEVLlDVRGLS-------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYD-AGTV 338
Cdd:TIGR02633 240 REITSLYPHEPHEIGDVIL-EARNLTcwdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 339 HVDGQRLPPRSVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVD 418
Cdd:TIGR02633 319 FINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 419 QAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSG 498
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
490 500
....*....|....*....|..
gi 502628485 499 GRLTGELPAATATQDQVMALAV 520
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAAL 500
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-522 |
3.72e-136 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 403.73 E-value: 3.72e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 39 VSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATIHQELN 118
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 119 LVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 199 ALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAS-THEDELVRLMVGRDITEQYPRRT 277
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAgLTMDKIIAMMVGRSLTQRFPDKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 278 HTPGdEVLLDVRGLS--RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVA 355
Cdd:PRK10982 244 NKPG-EVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 356 AGIGHVPEDRKGQGLVLDASVAENLGYATLAA-TSRAGFADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVF 434
Cdd:PRK10982 323 HGFALVTEERRSTGIYAYLDIGFNSLISNIRNyKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVII 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 435 GRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAATATQDQ 514
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNE 482
|
....*...
gi 502628485 515 VMALAVKH 522
Cdd:PRK10982 483 ILRLASLH 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-519 |
2.74e-127 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 381.71 E-value: 2.74e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 25 TSVPAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD 104
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 105 AERLGIATIHQELNLVPSMTVAENVLMGrLPSRggfvsRRTMRRLArEALDRVRLDVSLDTPVGELGIARQQLVEIAKAL 184
Cdd:PRK15439 83 AHQLGIYLVPQEPLLFPNLSVKENILFG-LPKR-----QASMQKMK-QLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 185 SLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV-AEVPASTHEDELVRL 263
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAlSGKTADLSTDDIIQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 264 MV----GRDITEQYP--------RRTHTPGDEVLlDVRGLSRTGvLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAD 331
Cdd:PRK15439 236 ITpaarEKSLSASQKlwlelpgnRRQQAAGAPVL-TVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 332 PYDAGTVHVDGQRLPPRSVGSAVAAGIGHVPEDRKGQGLVLDASVAENLGYATLaatSRAGFADRRGQRSRAQEVASR-L 410
Cdd:PRK15439 314 PARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTH---NRRGFWIKPARENAVLERYRRaL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 411 RIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVS 490
Cdd:PRK15439 391 NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMA 470
|
490 500
....*....|....*....|....*....
gi 502628485 491 DRVLVMSGGRLTGELPAATATQDQVMALA 519
Cdd:PRK15439 471 DRVLVMHQGEISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
283-501 |
8.52e-74 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 232.32 E-value: 8.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHVP 362
Cdd:cd03215 2 EPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 363 EDRKGQGLVLDASVAENLgyatlaatsragfadrrgqrsraqeVASRLrirmrdvdqaardLSGGNQQKIVFGRWVLAGS 442
Cdd:cd03215 82 EDRKREGLVLDLSVAENI-------------------------ALSSL-------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 443 RVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-250 |
1.21e-71 |
|
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: 225.77 E-value: 1.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATI 113
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQelnlvpsmtvaenvlmgrlpsrggfvsrrtmrrlarealdrvrldvsldtpvgeLGIARQQLVEIAKALSLNARVLIL 193
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-508 |
1.65e-58 |
|
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: 202.83 E-value: 1.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSF--GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG---GRVVVDGKPVHLGSVRDA 105
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 106 ERLgIATIHQE--LNLVPSmTVAENVlmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKA 183
Cdd:COG1123 82 GRR-IGMVFQDpmTQLNPV-TVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 184 LSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPASTHEDELVR 262
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 263 L-MVGRDITEQYPRRTHTPGDEVLLDVRGLSRT---------GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADP 332
Cdd:COG1123 237 LaAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRypvrgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 333 YDAGTVHVDGQRLPPRSVGSavaagighVPEDRKGQGLV-------LDA--SVAENLGYATLAatsrAGFADRRGQRSRA 403
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRS--------LRELRRRVQMVfqdpyssLNPrmTVGDIIAEPLRL----HGLLSRAERRERV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 404 QEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSS-D 482
Cdd:COG1123 385 AELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFIShD 464
|
490 500
....*....|....*....|....*.
gi 502628485 483 LPEVLGVSDRVLVMSGGRLTGELPAA 508
Cdd:COG1123 465 LAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
34-250 |
9.07e-56 |
|
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: 187.26 E-value: 9.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATI 113
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGRLPSRGGFV-------SRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSL 186
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
30-250 |
2.07e-54 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 184.09 E-value: 2.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 30 PAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLG 109
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLMGRLPSRGGFV------------SRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQL 177
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 178 VEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
34-250 |
5.10e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.79 E-value: 5.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATi 113
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 hQELNLVPSMTVAENV-LMGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGEL--GIarQQLVEIAKALSLNARV 190
Cdd:COG1131 80 -QEPALYPDLTVRENLrFFARL--YG--LPRKEARERIDELLELFGLTDAADRKVGTLsgGM--KQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 191 LILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
33-262 |
2.68e-44 |
|
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: 156.94 E-value: 2.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIat 112
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENVLM-GRLpsRGGFVSRRTMRrlAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfAEL--YGLFDEELKKR--IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 192 ILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPASTHEDELVR 262
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
34-249 |
1.81e-43 |
|
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: 153.44 E-value: 1.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgSVRDAERLGIATI 113
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVlmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:cd03259 78 FQDYALFPHLTVAENI---AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
34-262 |
9.53e-43 |
|
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: 152.72 E-value: 9.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFG-PVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD--AERLGI 110
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMGRLPSRG------GFVSRRTmRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKAL 184
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRStwrslfGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 185 SLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFIS-HHLEEIAAIGDEVSVLRDGALVAEVPASTHEDELVR 262
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSlHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
33-250 |
2.71e-42 |
|
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: 151.73 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgIAT 112
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENVLMGRLPSRGGFVS-RRTMRRLAREALDRVRLDVSLDTPVGEL--GiaRQQLVEIAKALSLNAR 189
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGLFGRpSAEDREAVEEALERTGLEHLADRPVDELsgG--ERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 190 VLILDEPTAAL-TGSETEVLfGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:COG1120 158 LLLLDEPTSHLdLAHQLEVL-ELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
34-245 |
4.44e-42 |
|
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: 148.31 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIatI 113
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMgrlpSRGgfvsrrtMRrlarealdrvrldvsldtpvgelgiarqQLVEIAKALSLNARVLIL 193
Cdd:cd03230 79 PEEPSLYENLTVRENLKL----SGG-------MK----------------------------QRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
29-245 |
3.87e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 3.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 29 APAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRdaerl 108
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 gIATIHQELNLVPS--MTVAENVLMGRLPSRGGFVS-RRTMRRLAREALDRVRLDVSLDTPVGEL--GiaRQQLVEIAKA 183
Cdd:COG1121 77 -IGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRpSRADREAVDEALERVGLEDLADRPIGELsgG--QQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 184 LSLNARVLILDEPTAAL-TGSEtEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVdAATE-EALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-254 |
5.81e-40 |
|
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: 151.98 E-value: 5.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 9 ASEPSGGRASGPARSRTsvPAPAPVLTLDSVSKSF-----GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIY 83
Cdd:COG1123 238 AAVPRLGAARGRAAPAA--AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 84 QPDGGRVVVDGKPVHLGSVRDAERLG--IATIHQ--ELNLVPSMTVAENVLMGrlPSRGGFVSRRTMRRLAREALDRVRL 159
Cdd:COG1123 316 RPTSGSILFDGKDLTKLSRRSLRELRrrVQMVFQdpYSSLNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 160 DVS-LDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGD 237
Cdd:COG1123 394 PPDlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIAD 473
|
250
....*....|....*..
gi 502628485 238 EVSVLRDGALVAEVPAS 254
Cdd:COG1123 474 RVAVMYDGRIVEDGPTE 490
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
34-247 |
7.82e-40 |
|
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: 144.17 E-value: 7.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFG----PVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD----- 104
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 105 AERLGIatIHQELNLVPSMTVAENVLMGRLPSRggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKAL 184
Cdd:cd03255 81 RRHIGF--VFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 185 SLNARVLILDEPTAALTGSETEVLFGVVEELRRDD-VAMVFISHHlEEIAAIGDEVSVLRDGAL 247
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
34-250 |
5.42e-39 |
|
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: 142.09 E-value: 5.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD-AERLGIa 111
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 tIHQ--ELNLVpSMTVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:COG1122 80 -VFQnpDDQLF-APTVEEDVAFG--PENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
49-198 |
5.92e-39 |
|
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: 139.32 E-value: 5.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvRDAERLGIATIHQELNLVPSMTVAEN 128
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE-RKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 129 VlmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIA----RQQLVEIAKALSLNARVLILDEPTA 198
Cdd:pfam00005 80 L---RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTlsggQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
34-254 |
3.49e-38 |
|
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: 139.49 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATI 113
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGRLPSRggfvsrrtmRRLAREALDRV-----RLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR---------RAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 189 RVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAS 254
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
34-249 |
1.63e-37 |
|
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: 137.41 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPvhlgsVRDAERLGIATI 113
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP-----LDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVL-MGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03269 76 PEERGLYPKMKVIDQLVyLAQL--KG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 193 LDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
29-262 |
1.27e-36 |
|
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: 135.88 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 29 APAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSV--RDAE 106
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkeLYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 RLGIATIHQELNLVPSMTVAENVLM-----GRLPsrggfvsRRTMRRLAREALDRVRLDVSLDTPVGEL--GIARQqlVE 179
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFplrehTDLS-------EAEIRELVLEKLELVGLPGAADKMPSELsgGMRKR--VA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 180 IAKALSLNARVLILDEPTAAL---TgseTEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAS- 254
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLdpiT---SAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEe 228
|
250
....*....|
gi 502628485 255 --THEDELVR 262
Cdd:COG1127 229 llASDDPWVR 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
36-245 |
3.53e-36 |
|
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: 133.75 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 36 LDSVSKSF--GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAeRLGIATI 113
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQ--ELNLVpSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:cd03225 81 FQnpDDQFF-GPTVEEEVAFG-LENLG--LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 192 ILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-266 |
7.78e-35 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 130.87 E-value: 7.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGI 110
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMGRLPSRGgfvsrrtmRRLAREALDRV-----RLDVSLDTPVGELGIARQQLVEIAKALS 185
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRD--------RAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 186 LNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST--HEDELVRL 263
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEllADPEVREA 232
|
...
gi 502628485 264 MVG 266
Cdd:COG0410 233 YLG 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
36-262 |
8.42e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 130.70 E-value: 8.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 36 LDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD--AERLGIATI 113
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLM-----GRLPsrggfvsRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:cd03261 83 FQSGALFDSLTVFENVAFplrehTRLS-------EEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 189 RVLILDEPTAALtgseTEVLFGVVEELRRD-----DVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAS---THEDEL 260
Cdd:cd03261 156 ELLLYDEPTAGL----DPIASGVIDDLIRSlkkelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEelrASDDPL 231
|
..
gi 502628485 261 VR 262
Cdd:cd03261 232 VR 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
30-248 |
9.92e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.07 E-value: 9.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 30 PAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRdAERLG 109
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLP-PEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGEL--GiaRQQLVEIAKALSLN 187
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFG-LRMRG--VPKAEIRARVAELLELVGLEGLADRYPHQLsgG--QQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 188 ARVLILDEPTAALTGSetevlfgVVEELRRD--------DVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:COG3842 154 PRVLLLDEPLSALDAK-------LREEMREElrrlqrelGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-248 |
4.87e-34 |
|
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: 129.69 E-value: 4.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 22 RSRTSVPAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGS 101
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 102 ---VRDAERLGIATIHQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLV 178
Cdd:cd03294 93 rkeLRELRRKKISMVFQSFALLPHRTVLENVAFG-LEVQG--VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 179 EIAKALSLNARVLILDEPTAALT----GSETEVLFGVVEELRRddvAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
34-247 |
5.61e-34 |
|
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: 128.03 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVR-DAERLGIAT 112
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 193 LDEPTAALTgSET--EVLfGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGAL 247
Cdd:cd03262 159 FDEPTSALD-PELvgEVL-DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
36-242 |
1.87e-33 |
|
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: 126.49 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 36 LDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRdaerlgIATIHQ 115
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 116 ELNLVPSM--TVAENVLMGRLPSRGGFVS-RRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03235 76 RRSIDRDFpiSVRDVVLMGLYGHKGLFRRlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 193 LDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVL 242
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
34-252 |
2.26e-33 |
|
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: 126.43 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFG----PVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlGSVRDaerlg 109
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-GPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLmgrLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVA---LGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 190 VLILDEPTAAL-----TGSETEVLfgvvEELRRDDVAMVFISHHLEEIAAIGDEVSVL--RDGALVAEVP 252
Cdd:cd03293 152 VLLLDEPFSALdaltrEQLQEELL----DIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-250 |
2.52e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.69 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD-----AER 107
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 lGiatihqelnLVPSMTVAENVL-MGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSL 186
Cdd:COG4152 81 -G---------LYPKMKVGEQLVyLARL--KG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
33-253 |
4.21e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.55 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPvhLGSVRDAE----- 106
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD--LSRLKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 -RLGIatIHQELNLVPSMTVAENVLmgrLPSR--GgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKA 183
Cdd:COG2884 79 rRIGV--VFQDFRLLPDRTVYENVA---LPLRvtG--KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 184 LSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPA 253
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
34-252 |
8.59e-33 |
|
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: 124.99 E-value: 8.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIY-----QPDGGRVVVDGKPV-HLGSVRDAER 107
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 LGIATIHQELNLVPsMTVAENVLMGrlPSRGGFVSRRTMRRLAREALDRVRLD--VSLDTPVGELGIARQQLVEIAKALS 185
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALWdeVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 186 LNARVLILDEPTAALTGSETEVLFGVVEELRRdDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP 252
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
38-230 |
1.45e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.82 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 38 SVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAE-RLGIATIHQE 116
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 117 LNLVPSMTVAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEP 196
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVRG--ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190
....*....|....*....|....*....|....*
gi 502628485 197 TAALTGS-ETEVLfGVVEELRRDDVAMVFISHHLE 230
Cdd:PRK09493 164 TSALDPElRHEVL-KVMQDLAEEGMTMVIVTHEIG 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
32-252 |
3.60e-32 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 124.04 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPG-RVqVLLGENGAGKSTLIKMMSG-IYQPDGGRVVVDGKPVHLGSVRD-AERL 108
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGeHW-AILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWElRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIATIHQELNLVPSMTVAENVLMGRLPSRGgfVSRR---TMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALS 185
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDVVLSGFFDSIG--LYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 186 LNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP 252
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
34-245 |
4.44e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 123.12 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERlGIATI 113
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKR-PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:cd03300 78 FQNYALFPHLTVFENIAFG-LRLKK--LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 194 DEPTAALTGSETEVLfgvVEELRR--DDVAM--VFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03300 155 DEPLGALDLKLRKDM---QLELKRlqKELGItfVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-266 |
7.41e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 128.61 E-value: 7.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 15 GRASGPARSRTSVPAPAPVLTLDSVS-KSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVD 93
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 94 GKPVHLGSVRDAERLGIATIHQELN---LVPSMTVAENVLMGRLP----SRGGFVSRRTMRRLAREALDR--VRLDvSLD 164
Cdd:COG3845 319 GEDITGLSPRERRRLGVAYIPEDRLgrgLVPDMSVAENLILGRYRrppfSRGGFLDRKAIRAFAEELIEEfdVRTP-GPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 165 TPVGEL--GiaRQQLVEIAKALSLNARVLILDEPTAAL-TGSeTEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSV 241
Cdd:COG3845 398 TPARSLsgG--NQQKVILARELSRDPKLLIAAQPTRGLdVGA-IEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAV 474
|
250 260
....*....|....*....|....*.
gi 502628485 242 LRDGALVAEVPAS-THEDELVRLMVG 266
Cdd:COG3845 475 MYEGRIVGEVPAAeATREEIGLLMAG 500
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
36-451 |
4.16e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 126.72 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 36 LDSVSKSFGPVDVLKDITVHVRPG-RVqVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpvhlgsvrdaeRLGIATIH 114
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 115 QELNLVPSMTVAENVLMG------------RLPSRGGFVSRRTMR--RL---------------AREALDRVRLDVS-LD 164
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGdaelraleaeleELEAKLAEPDEDLERlaELqeefealggweaearAEEILSGLGFPEEdLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 165 TPVGEL--GIARQqlVEIAKALSLNARVLILDEPT--------AALtgsetevlfgvvEE-LRRDDVAMVFISH--HL-- 229
Cdd:COG0488 148 RPVSELsgGWRRR--VALARALLSEPDLLLLDEPTnhldlesiEWL------------EEfLKNYPGTVLVVSHdrYFld 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 230 ---EEIAAIGDEVSVLRDG---------ALVAEVPASTHE---DELVRLMV----------------GRD------ITEQ 272
Cdd:COG0488 214 rvaTRILELDRGKLTLYPGnysayleqrAERLEQEAAAYAkqqKKIAKEEEfirrfrakarkakqaqSRIkaleklEREE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 273 YPRRTHTP----------GDEVlLDVRGLS-----RTgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGT 337
Cdd:COG0488 294 PPRRDKTVeirfppperlGKKV-LELEGLSksygdKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 338 VHvdgqrlpprsVGSAVAagIGHVPEDRkgQGLVLDASVAENLgyatlaatsRAGFADRRGQRSRAqeVASRLRIRMRDV 417
Cdd:COG0488 372 VK----------LGETVK--IGYFDQHQ--EELDPDKTVLDEL---------RDGAPGGTEQEVRG--YLGRFLFSGDDA 426
|
490 500 510
....*....|....*....|....*....|....
gi 502628485 418 DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPT 451
Cdd:COG0488 427 FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
35-245 |
9.33e-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: 116.96 E-value: 9.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 35 TLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAeRLGIATIH 114
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 115 QelnlvpsmtvaenvLMGrlpsrggfvsrrtmrrlarealdrvrldvsldtpvGElgiarQQLVEIAKALSLNARVLILD 194
Cdd:cd00267 80 Q--------------LSG-----------------------------------GQ-----RQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 195 EPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-258 |
1.18e-30 |
|
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: 126.49 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 20 PARSRTSVPAPAPVLTLDSVSKSFGP--VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKP- 96
Cdd:COG2274 460 EGRSKLSLPRLKGDIELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDl 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 97 --VHLGSVRDAerlgIATIHQELNLVpSMTVAENVLMGRlPSrggfVSRRTMRRLAREA-LDRV--RLDVSLDTPVGELG 171
Cdd:COG2274 540 rqIDPASLRRQ----IGVVLQDVFLF-SGTIRENITLGD-PD----ATDEEIIEAARLAgLHDFieALPMGYDTVVGEGG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 172 IA-----RQQLvEIAKALSLNARVLILDEPTAAL-TGSETEVLfgvvEELRR--DDVAMVFISHHLeEIAAIGDEVSVLR 243
Cdd:COG2274 610 SNlsggqRQRL-AIARALLRNPRILILDEATSALdAETEAIIL----ENLRRllKGRTVIIIAHRL-STIRLADRIIVLD 683
|
250
....*....|....*
gi 502628485 244 DGALVAEvpaSTHED 258
Cdd:COG2274 684 KGRIVED---GTHEE 695
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-250 |
1.28e-30 |
|
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: 119.15 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSF----GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERL 108
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 G--IATIHQE----LNlvPSMTVAEnVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVS-LDTPVGELGIARQQLVEIA 181
Cdd:cd03257 81 RkeIQMVFQDpmssLN--PRMTIGE-QIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 182 KALSLNARVLILDEPTAAL-TGSETEVLfGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03257 158 RALALNPKLLIADEPTSALdVSVQAQIL-DLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
33-250 |
1.52e-30 |
|
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: 118.84 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGP----VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD--AE 106
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 RLGIATIHQELNLVPSMTVAENVlmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSL 186
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
34-249 |
2.64e-30 |
|
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: 117.99 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVD--VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERLGIA 111
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENV-LMGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARV 190
Cdd:cd03263 79 YCPQFDALFDELTVREHLrFYARL--KG--LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 191 LILDEPTAALTGSETEVLFGVVEELRRDDvAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
32-234 |
2.76e-30 |
|
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: 117.58 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIA 111
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TihQELNLVPSMTVAENVLM-GRLpsRGGFVSRRTmrrlAREALDRVRLDVSLDTPVGEL--GIarQQLVEIAKALSLNA 188
Cdd:COG4133 81 G--HADGLKPELTVRENLRFwAAL--YGLRADREA----IDEALEAVGLAGLADLPVRQLsaGQ--KRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502628485 189 RVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAA 234
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
34-248 |
4.07e-30 |
|
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: 117.36 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERlGIATI 113
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDR-DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFG-LKLRK--VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 194 DEPTAALtgsETEVLFGVVEEL----RRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:cd03301 155 DEPLSNL---DAKLRVQMRAELkrlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
34-245 |
4.30e-30 |
|
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: 115.56 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFG--PVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVH---LGSVRDAerl 108
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdldLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 gIATIHQELNLVpSMTVAENVLMGrlpsrggfvsrrtmrrlarealdrvrldvsldtpvGElgiarQQLVEIAKALSLNA 188
Cdd:cd03228 78 -IAYVPQDPFLF-SGTIRENILSG-----------------------------------GQ-----RQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 189 RVLILDEPTAALTgSETEVLfgVVEELRR--DDVAMVFISHHLEEIaAIGDEVSVLRDG 245
Cdd:cd03228 116 PILILDEATSALD-PETEAL--ILEALRAlaKGKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
286-513 |
5.40e-30 |
|
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: 117.15 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHV 361
Cdd:cd03224 1 LEVENLNagygKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDRkgqGLVLDASVAENLgyaTLAATSRAGfADRRGQRSRAQEVASRLRIRMrdvDQAARDLSGGNQQKIVFGRWVLAG 441
Cdd:cd03224 81 PEGR---RIFPELTVEENL---LLGAYARRR-AKRKARLERVYELFPRLKERR---KQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 442 SRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAATATQD 513
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
34-250 |
6.06e-30 |
|
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: 116.70 E-value: 6.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSF----GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLG 109
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IatIHQELNLVPSMTVAENVL-MGRLPSrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:cd03266 82 F--VSDSTGLYDRLTARENLEyFAGLYG----LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 189 RVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
283-513 |
9.83e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 116.62 E-value: 9.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGI 358
Cdd:COG0410 1 MPMLEVENLHagygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 359 GHVPEDRkgqGLVLDASVAENLgyaTLAATSRAGFADRRGQRSRAQEVASRLRIRMRdvdQAARDLSGGNQQKIVFGRWV 438
Cdd:COG0410 81 GYVPEGR---RIFPSLTVEENL---LLGAYARRDRAEVRADLERVYELFPRLKERRR---QRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 439 LAGSRVLLLDEPTRG-----VDvgarvEIYELI---------------NavaaaggavllvssdLPEVLGVSDRVLVMSG 498
Cdd:COG0410 152 MSRPKLLLLDEPSLGlapliVE-----EIFEIIrrlnregvtillveqN---------------ARFALEIADRAYVLER 211
|
250
....*....|....*
gi 502628485 499 GRLTGELPAATATQD 513
Cdd:COG0410 212 GRIVLEGTAAELLAD 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
34-245 |
1.25e-29 |
|
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: 114.59 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVH-LGSVRDAERLGIAT 112
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENVlmgRLPSRGGfvsrrtmrrlarealdrvrldvsldtpvgelgiaRQQLVEIAKALSLNARVLI 192
Cdd:cd03229 81 VFQDFALFPHLTVLENI---ALGLSGG----------------------------------QQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 193 LDEPTAALTGSETEVLFGVVEELR-RDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
58-249 |
1.58e-29 |
|
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: 115.47 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 58 PGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG-------KPVHLGSvrdaERLGIATIHQELNLVPSMTVAENVL 130
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPP----QQRKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 131 MGrLPsrggFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFG 210
Cdd:cd03297 98 FG-LK----RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502628485 211 VVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
286-501 |
3.11e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.55 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT-G---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAVAAGIGHV 361
Cdd:COG1131 1 IEVRGLTKRyGdktALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE--DVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDrkgQGLVLDASVAENLGYAtlaatsrAGF--ADRRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVL 439
Cdd:COG1131 79 PQE---PALYPDLTVRENLRFF-------ARLygLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 440 AGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-250 |
5.01e-29 |
|
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: 121.02 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 20 PARSRTSVPAPAPVLTLDSVSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVH 98
Cdd:COG4988 323 PAGTAPLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 99 lgsvrdaeRLGIATIHQELNLVP------SMTVAENVLMGRlPSrggfVSRRTMRRLAREA-LDRV--RLDVSLDTPVGE 169
Cdd:COG4988 403 --------DLDPASWRRQIAWVPqnpylfAGTIRENLRLGR-PD----ASDEELEAALEAAgLDEFvaALPDGLDTPLGE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 170 LGIA-----RQQLVeIAKALSLNARVLILDEPTAAL-TGSETEVLfGVVEELRRdDVAMVFISHHLEEIAAIgDEVSVLR 243
Cdd:COG4988 470 GGRGlsggqAQRLA-LARALLRDAPLLLLDEPTAHLdAETEAEIL-QALRRLAK-GRTVILITHRLALLAQA-DRILVLD 545
|
....*..
gi 502628485 244 DGALVAE 250
Cdd:COG4988 546 DGRIVEQ 552
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
34-250 |
7.82e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 113.47 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgsVRDAERLG-IAT 112
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY----QKNIEALRrIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENV-LMGRLPsrgGFVSRRTMrrlarEALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:cd03268 77 LIEAPGFYPNLTARENLrLLARLL---GIRKKRID-----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 192 ILDEPTAALTGsetevlFGvVEELR------RDDVAMVFISHH-LEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03268 149 ILDEPTNGLDP------DG-IKELRelilslRDQGITVLISSHlLSEIQKVADRIGIINKGKLIEE 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-262 |
2.75e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.73 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 4 AAPVPASEPSGGRASGPARSRtsvpapapvLTLDSVSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI 82
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPVRGE---------IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 83 YQPDGGRVVVDGKPVH---LGSVRDAerlgIATIHQELNLVpSMTVAENVLMGRLPsrggfVSRRTMRRLAREA-LDRV- 157
Cdd:COG1132 390 YDPTSGRILIDGVDIRdltLESLRRQ----IGVVPQDTFLF-SGTIRENIRYGRPD-----ATDEEVEEAAKAAqAHEFi 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 158 -RLDVSLDTPVGELGIA-----RQQLVeIAKALSLNARVLILDEPTAALtGSETEVL-FGVVEELRRdDVAMVFISHHLE 230
Cdd:COG1132 460 eALPDGYDTVVGERGVNlsggqRQRIA-IARALLKDPPILILDEATSAL-DTETEALiQEALERLMK-GRTTIVIAHRLS 536
|
250 260 270
....*....|....*....|....*....|...
gi 502628485 231 EIA-AigDEVSVLRDGALVAEvpaSTHEdELVR 262
Cdd:COG1132 537 TIRnA--DRILVLDDGRIVEQ---GTHE-ELLA 563
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
34-262 |
3.76e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 112.25 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-HLGSVRDAeRLGIAT 112
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENvLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03218 80 LPQEASIFRKLTVEEN-ILAVLEIRG--LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 193 LDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE-VPASTHEDELVR 262
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEgTPEEIAANELVR 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
41-250 |
4.46e-28 |
|
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: 111.69 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 41 KSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgsVRDAE--RLGIATIHQELN 118
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPRevRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 119 LVPSMTVAENVLM-GRLPSrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPT 197
Cdd:cd03265 84 VDDELTGWENLYIhARLYG----VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 198 AALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
39-245 |
5.98e-28 |
|
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: 112.05 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 39 VSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgSVRDAERLGIATIHQELN 118
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 119 LVPSMTVAENVLMG-RLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPT 197
Cdd:cd03296 85 LFRHMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 198 AALTGSetevlfgVVEELRR------DD--VAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03296 165 GALDAK-------VRKELRRwlrrlhDElhVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
35-250 |
6.87e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 35 TLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgIATIH 114
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 115 QelnlvpsmtvaenvlmgrlpsrggfvsrrtmrrlareALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILD 194
Cdd:cd03214 80 Q-------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 195 EPTAAL-TGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03214 123 EPTSHLdIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-249 |
7.46e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.32 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgI 110
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMGRLPSRGGFVSR-RTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
34-250 |
4.29e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.82 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD-AERLGIAT 112
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLvpSMTVAENVLMGRLPsrgGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKAL-------S 185
Cdd:COG4559 82 QHSSLAF--PFTVEEVVALGRAP---HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 186 LNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
34-314 |
1.07e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSF----GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD--AER 107
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 LGIATIHQELNLVPSMTVAENV-----LMGrlpsrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAK 182
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENValpleIAG--------VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 183 ALSLNARVLILDEPTAAL----TGSETEVLFGVVEELrrdDVAMVFISHHLEEIAAIGDEVSVLRDGAL-----VAEV-- 251
Cdd:COG1135 154 ALANNPKVLLCDEATSALdpetTRSILDLLKDINREL---GLTIVLITHEMDVVRRICDRVAVLENGRIveqgpVLDVfa 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 252 -PASTHEDELVRLMVGRDITEQYPRR-THTPGDEVLLDV--RG-------LSRTGVLHDIDVQVRAGEVVGVAG 314
Cdd:COG1135 231 nPQSELTRRFLPTVLNDELPEELLARlREAAGGGRLVRLtfVGesadeplLSELARRFGVDVNILSGGIEEIQG 304
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
34-501 |
1.20e-26 |
|
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: 113.36 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI--YQPDGGRVVVD----------GKPVHLG- 100
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 101 ---------------------SVRDAERLGIATIHQE-LNLVPSMTVAENVLmgRLPSRGGFVSRRTMRRlAREALDRVR 158
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRtFALYGDDTVLDNVL--EALEEIGYEGKEAVGR-AVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 159 LDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGD 237
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 238 EVSVLRDGALVAEvpaSTHEDELVRLMVGRDITEQYprRTHTPGDEVLlDVRGLSR------TGVLHDID---VQVRAGE 308
Cdd:TIGR03269 238 KAIWLENGEIKEE---GTPDEVVAVFMEGVSEVEKE--CEVEVGEPII-KVRNVSKryisvdRGVVKAVDnvsLEVKEGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 309 VVGVAGLVGAGRTELLRAIAGADPYDAGTVH-------VDGQRLPPRSVGSAVA-AGIGHvpedrKGQGLVLDASVAENL 380
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRyIGILH-----QEYDLYPHRTVLDNL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 381 GYA----------------TLAAtsrAGFADRrgqrsRAQEVasrlrirmrdVDQAARDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:TIGR03269 387 TEAiglelpdelarmkaviTLKM---VGFDEE-----KAEEI----------LDKYPDELSEGERHRVALAQVLIKEPRI 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 445 LLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-250 |
1.29e-26 |
|
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: 107.28 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGrVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlGSVRDAERLGIATI 113
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENV-LMGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03264 78 PQEFGVYPNFTVREFLdYIAWL--KG--IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 193 LDEPTAALTGSETEVLFGVVEELRRDDVamVFISHHL-EEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRI--VILSTHIvEDVESLCNQVAVLNKGKLVFE 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-246 |
2.00e-26 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 107.13 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSF-----GPV--DVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVV--DGKPVHLGSV 102
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 103 RDAERLGI--ATI---HQELNLVPSMTvAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSL-DTPV-----GElg 171
Cdd:COG4778 83 SPREILALrrRTIgyvSQFLRVIPRVS-ALDVVAEPLLERG--VDREEARARARELLARLNLPERLwDLPPatfsgGE-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 172 iarQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGA 246
Cdd:COG4778 158 ---QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-247 |
2.29e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 105.59 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSfgpvDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGI 110
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATI----HQELnLVPSMTVAENVLMGRLPSrGGfvsrrtmrrlarealdrvrldvsldtpvgelgiaRQQLVEIAKALSL 186
Cdd:cd03215 78 AYVpedrKREG-LVLDLSVAENIALSSLLS-GG----------------------------------NQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGAL 247
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
285-501 |
3.30e-26 |
|
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: 107.25 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAVAAGIGH 360
Cdd:COG4555 1 MIEVENLSKKygkvPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE--DVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 VPEDRkgqGLVLDASVAENLGY-ATLAATSRagfadrRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVL 439
Cdd:COG4555 79 LPDER---GLYDRLTVRENIRYfAELYGLFD------EELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 440 AGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-249 |
4.97e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGI 110
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMG---RLPSR--GGFVSRRTMRRLAREA-------LDRVRLDVSLDTPVGELGIARQQLV 178
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAqhqQLKTGlfSGLLKTPAFRRAESEAldraatwLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 179 EIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
35-281 |
8.29e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 8.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 35 TLDSVSKSF----GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD--AERL 108
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIATIHQELNLVPSMTVAENVlmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNV---ALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 189 RVLILDEPTAAL----TGSETEVLFGVVEELrrdDVAMVFISHHLEEIAAIGDEVSVLRDGAL-----VAEVPASTHED- 258
Cdd:PRK11153 160 KVLLCDEATSALdpatTRSILELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLveqgtVSEVFSHPKHPl 236
|
250 260
....*....|....*....|....*
gi 502628485 259 --ELVRLMVGRDITEQYPRRTHTPG 281
Cdd:PRK11153 237 trEFIQSTLHLDLPEDYLARLQAEP 261
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-250 |
2.19e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.78 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSF----------------------GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGG 88
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 89 RVVVDGKPVHLgsvrdaerLGIATIhqelnLVPSMTVAENV-LMGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPV 167
Cdd:COG1134 82 RVEVNGRVSAL--------LELGAG-----FHPELTGRENIyLNGRL--LG--LSRKEIDEKFDEIVEFAELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 168 G--------ELGIArqqlVeiakALSLNARVLILDEPTAalTGSET--EVLFGVVEELRRDDVAMVFISHHLEEIAAIGD 237
Cdd:COG1134 145 KtyssgmraRLAFA----V----ATAVDPDILLVDEVLA--VGDAAfqKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|...
gi 502628485 238 EVSVLRDGALVAE 250
Cdd:COG1134 215 RAIWLEKGRLVMD 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
34-268 |
2.82e-25 |
|
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: 104.30 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVD-VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgSVRDAERL--GI 110
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI---REQDPVELrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVlmGRLPSRGGFvSRRTMRRLAREALDRVRLDVS--LDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENI--ALVPKLLKW-PKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 189 RVLILDEPTAALT----GSETEVLFGVVEELRRddvAMVFISHHLEEIAAIGDEVSVLRDGALV-----AEVPASTHeDE 259
Cdd:cd03295 155 PLLLMDEPFGALDpitrDQLQEEFKRLQQELGK---TIVFVTHDIDEAFRLADRIAIMKNGEIVqvgtpDEILRSPA-ND 230
|
....*....
gi 502628485 260 LVRLMVGRD 268
Cdd:cd03295 231 FVAEFVGAD 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
286-501 |
6.13e-25 |
|
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: 101.32 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT-G---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAVAAGIGHV 361
Cdd:cd03230 1 IEVRNLSKRyGkktALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDRkgqGLVLDASVAENLgyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaarDLSGGNQQKIVFGRWVLAG 441
Cdd:cd03230 79 PEEP---SLYENLTVRENL------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 442 SRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
32-245 |
8.51e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-HLgsvrDAERLGI 110
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDItHV----PAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMG-RLPSrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGlRMQK----TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 190 VLILDEPTAAL-------TGSETEVLfgvveeLRRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:PRK09452 165 VLLLDESLSALdyklrkqMQNELKAL------QRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-273 |
1.17e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.12 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 28 PAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAER 107
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 LGIatIHQELNLVPSMTVAENVLMGrlpSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLN 187
Cdd:PRK13537 82 VGV--VPQFDNLDPDFTVRENLLVF---GRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 188 ARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPASthedELVRLMVGR 267
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH----ALIESEIGC 232
|
....*.
gi 502628485 268 DITEQY 273
Cdd:PRK13537 233 DVIEIY 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-255 |
1.27e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.14 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGpvDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlGSVRDAERlGIATI 113
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAER-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGRLPSRggfvsR--RTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALsLNAR-V 190
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGL-----KltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VRKRpI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 191 LILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST 255
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-252 |
1.37e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQ--PDG---GRVVVDGKPVHLGSVRDAER 107
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 LgIATIHQELNLVPSMTVAENVLMG----RLPSrggfvSRRTMRRLAREALDRVRL--DVS--LDTPVGELGIARQQLVE 179
Cdd:PRK14247 83 R-VQMVFQIPNPIPNLSIFENVALGlklnRLVK-----SKKELQERVRWALEKAQLwdEVKdrLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 180 IAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRdDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP 252
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
48-262 |
1.62e-24 |
|
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: 101.92 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvRDAERLGIATIHQELNLVPSmTVAE 127
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGRLPSRggfvsRRTMRRLAREA-LDRV--RLDVSLDTPVGE----LGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:cd03254 96 NIRLGRPNAT-----DEEVIEAAKEAgAHDFimKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 201 TgSETEVLF-GVVEELRRDDVAMVfISHHLEEIAAiGDEVSVLRDGALVAEvpaSTHEDELVR 262
Cdd:cd03254 171 D-TETEKLIqEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEE---GTHDELLAK 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-250 |
2.94e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD-AERLgi 110
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLMGRLPSRGgfvSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKAL------ 184
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMGRAPHGL---SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 185 SLNARVLILDEPTAALTGSETEVLFGVVEEL-RRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
35-248 |
8.37e-24 |
|
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: 99.25 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 35 TLDSVSKSFGPV-DVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLgsvrdAERLG-IAT 112
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-----KERRKsIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELN-LVPSMTVAENVLMG-RLPSRGGFVSRRTMRRLAREAL-DRVRLDVSLdtpvGElgiarQQLVEIAKALSLNAR 189
Cdd:cd03226 76 VMQDVDyQLFTDSVREELLLGlKELDAGNEQAETVLKDLDLYALkERHPLSLSG----GQ-----KQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-200 |
1.69e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGP-----VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-HLGSVRDAER 107
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 lgIATIHQE--LNLVPSMTVAENVLM--GRLPSRG-GFVSRRTMRRLAREALDRVRLDVS--LDTPVGEL-GIARQqlve 179
Cdd:COG1101 82 --IGRVFQDpmMGTAPSMTIEENLALayRRGKRRGlRRGLTKKRRELFRELLATLGLGLEnrLDTKVGLLsGGQRQ---- 155
|
170 180
....*....|....*....|....*..
gi 502628485 180 iakALSL------NARVLILDEPTAAL 200
Cdd:COG1101 156 ---ALSLlmatltKPKLLLLDEHTAAL 179
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
48-258 |
3.86e-23 |
|
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: 98.07 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG---KPVHLGSVRDAerlgIATIHQELNLVpSMT 124
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRQ----IGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 125 VAENVLMGRLPsrggfVSRRTMRRLAR--EALDRV-RLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVLILDEPT 197
Cdd:cd03251 92 VAENIAYGRPG-----ATREEVEEAARaaNAHEFImELPEGYDTVIGERGVklsgGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 198 AALTgSETEVLF-GVVEELRRDDVAMVfISHHLEEIAAIgDEVSVLRDGALVAEvpaSTHED 258
Cdd:cd03251 167 SALD-TESERLVqAALERLMKNRTTFV-IAHRLSTIENA-DRIVVLEDGKIVER---GTHEE 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
34-249 |
4.28e-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: 97.66 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSF--GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERlGIA 111
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVpSMTVAENVLMGRLPSRggfvSRRTMRRLAREALDRV--RLDVSLDTPVGE----LGIARQQLVEIAKALS 185
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLAD----DERILRAAELAGVTDFvnKHPNGLDLQIGErgrgLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 186 LNARVLILDEPTAAL-TGSETEvlfgVVEELRR--DDVAMVFISHHLeEIAAIGDEVSVLRDGALVA 249
Cdd:cd03245 157 NDPPILLLDEPTSAMdMNSEER----LKERLRQllGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
297-451 |
5.12e-23 |
|
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: 95.02 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgSAVAAGIGHVPEDRkgqGLVLDASV 376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQDP---QLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 377 AENLGYAtlaatSRAGFADRRGQRSRAQEVASRLRI---RMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPT 451
Cdd:pfam00005 77 RENLRLG-----LLLKGLSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
286-501 |
7.99e-23 |
|
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: 96.43 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsavaagIGHV 361
Cdd:cd03259 1 LELKGLSKTygsvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD-------------VTGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDRKGQGLVLDA-------SVAENLGYATlaatsRAGFADRRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVF 434
Cdd:cd03259 68 PPERRNIGMVFQDyalfphlTVAENIAFGL-----KLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 435 GRWVLAGSRVLLLDEPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELReELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-262 |
1.72e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.25 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGK-----PVHlgsvRDAe 106
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMH----KRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 RLGIATIHQElnlvPS----MTVAENVLMgrlpsrggFVSRRTMRRLAREAldrvRLDVSLDtpvgELGIA--RQQL--- 177
Cdd:COG1137 77 RLGIGYLPQE----ASifrkLTVEDNILA--------VLELRKLSKKEREE----RLEELLE----EFGIThlRKSKays 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 178 --------VEIAKALSLNARVLILDEPTAaltgsetevlfGV-----------VEELRRDDVAmVFIS-HHLEEIAAIGD 237
Cdd:COG1137 137 lsggerrrVEIARALATNPKFILLDEPFA-----------GVdpiavadiqkiIRHLKERGIG-VLITdHNVRETLGICD 204
|
250 260
....*....|....*....|....*.
gi 502628485 238 EVSVLRDGALVAE-VPASTHEDELVR 262
Cdd:COG1137 205 RAYIISEGKVLAEgTPEEILNNPLVR 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-255 |
2.35e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.64 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSV--RDaerlgIA 111
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIqqRD-----IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYG-LKMLG--VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 192 ILDEPTAALTGSETEVLFGVVEEL-RRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST 255
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
48-248 |
2.93e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGS---VRDAERL--GIATIHQELNLVPS 122
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifQIDAIKLrkEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 123 MTVAENVLMgrlPSRG-GFVSRRTMRRLAREALDRVRL--DV--SLDTPVGELGIARQQLVEIAKALSLNARVLILDEPT 197
Cdd:PRK14246 105 LSIYDNIAY---PLKShGIKEKREIKKIVEECLRKVGLwkEVydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 198 AALTGSETEVLFGVVEELRRdDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
286-501 |
3.03e-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: 95.58 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT--GV--LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVgsaVAAGI 358
Cdd:cd03219 1 LEVRGLTKRfgGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditGLPPHEI---ARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 359 GhvpedRKGQGLVL--DASVAENLGYATLAATSRAGFADR-RGQRSRAQEVASRL--RIRMRDV-DQAARDLSGGNQQKI 432
Cdd:cd03219 78 G-----RTFQIPRLfpELTVLENVMVAAQARTGSGLLLARaRREEREARERAEELleRVGLADLaDRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 433 VFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-273 |
3.13e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.98 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 21 ARSRTSVPAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlG 100
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 101 SVRDAeRLGIATIHQELNLVPSMTVAENVLMGrlpSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEI 180
Cdd:PRK13536 108 RARLA-RARIGVVPQFDNLDLEFTVRENLLVF---GRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 181 AKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEvpasTHEDEL 260
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE----GRPHAL 259
|
250
....*....|...
gi 502628485 261 VRLMVGRDITEQY 273
Cdd:PRK13536 260 IDEHIGCQVIEIY 272
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
44-230 |
4.59e-22 |
|
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: 93.64 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 44 GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgsvrDAERLGIATIHQELNLV--- 120
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL------DYSRKGLLERRQRVGLVfqd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 121 P-----SMTVAENVLMGrlPSRGGFVSRRTMRRLaREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDE 195
Cdd:TIGR01166 77 PddqlfAADVDQDVAFG--PLNLGLSEAEVERRV-REALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 502628485 196 PTAALTGSETEVLFGVVEELRRDDVAMVFISHHLE 230
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-500 |
5.16e-22 |
|
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: 99.37 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 29 APAPVLTLDSVSKSFG----PVDVLKDITVHVRPGRVQVLLGENGAGKS----TLIKMMSGIYQPDGGRVVVDGKPV--- 97
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 98 ---HLGSVRDAErlgIATIHQE----LNlvPSMTVAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDvSLDTPVG-- 168
Cdd:COG4172 82 serELRRIRGNR---IAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRG--LSGAAARARALELLERVGIP-DPERRLDay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 169 --ELGIARQQLVEIAKALSLNARVLILDEPTAAL--TgSETEVLfGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLR 243
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANEPDLLIADEPTTALdvT-VQAQIL-DLLKDLQRElGMALLLITHDLGVVRRFADRVAVMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 244 DGALV-----AEVPASTHEDELVRLMvgrDITEQYPRRTHTPGDEVLLDVRGLS-----RTGVL----------HDIDVQ 303
Cdd:COG4172 232 QGEIVeqgptAELFAAPQHPYTRKLL---AAEPRGDPRPVPPDAPPLLEARDLKvwfpiKRGLFrrtvghvkavDGVSLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 304 VRAGEVVGVAGLVGAGRTELLRAIAGADPYDaGTVHVDGQRL---------------------P-----PR-SVGSAVAA 356
Cdd:COG4172 309 LRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLdglsrralrplrrrmqvvfqdPfgslsPRmTVGQIIAE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 357 GIG-HVPEdrkgqglvldasvaenlgyatlaatsragfADRRGQRSRAQEVasrlrirMRDV--DQAARD-----LSGGN 428
Cdd:COG4172 388 GLRvHGPG------------------------------LSAAERRARVAEA-------LEEVglDPAARHrypheFSGGQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 429 QQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYEL--------------InavaaaggavllvSSDLPEVLGVSDRVL 494
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLlrdlqrehglaylfI-------------SHDLAVVRALAHRVM 497
|
....*.
gi 502628485 495 VMSGGR 500
Cdd:COG4172 498 VMKDGK 503
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
39-247 |
5.27e-22 |
|
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: 94.40 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 39 VSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-HL-GSVRDAERLGIATIHQ 115
Cdd:cd03292 6 VTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLrGRAIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 116 ELNLVPSMTVAENVLmgrLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDE 195
Cdd:cd03292 86 DFRLLPDRNVYENVA---FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502628485 196 PTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGAL 247
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-230 |
7.34e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.70 E-value: 7.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 36 LDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAE-----RLGI 110
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKairelRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQELNLVPSMTVAENVLmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARV 190
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLI--EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502628485 191 LILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLE 230
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
286-501 |
1.03e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 93.34 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRTG----VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRL---PPRSVGSAVAagi 358
Cdd:COG4619 1 LELEGLSFRVggkpILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsamPPPEWRRQVA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 359 gHVPedrkgQGLVL-DASVAENLGYAtlaatsrAGFADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRW 437
Cdd:COG4619 78 -YVP-----QEPALwGGTVRDNLPFP-------FQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 438 VLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVL-LVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVlWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
283-539 |
1.81e-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: 97.67 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLS------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDA---GTVHVDGQRLPPRSVgSA 353
Cdd:COG1123 2 TPLLEVRDLSvrypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 354 VAAGIGHVPEDRKGQ--GLVLDASVAENLgyatlaatsRAGFADRRGQRSRAQEVASRLRIRMRdVDQAARDLSGGNQQK 431
Cdd:COG1123 81 RGRRIGMVFQDPMTQlnPVTVGDQIAEAL---------ENLGLSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 432 IVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVMSGGRLTGELPAATA 510
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLIThDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260
....*....|....*....|....*....
gi 502628485 511 TQDQVMALAVKHADDDDHVAPSHGPEGSP 539
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-250 |
3.37e-21 |
|
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: 91.79 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVhvRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpVHLGSVRDAERlGIATI 113
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADR-PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGRLPsrgGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSP---GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
49-263 |
3.57e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgIATIHQEL-NLVPSMTVAE 127
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ-VGMVFQNPdNQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL--TGSEt 205
Cdd:PRK13635 102 DVAFG-LENIG--VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLdpRGRR- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 206 EVLfGVVEELRRD-DVAMVFISHHLEEiAAIGDEVSVLRDGALVAE-VPAS--THEDELVRL 263
Cdd:PRK13635 178 EVL-ETVRQLKEQkGITVLSITHDLDE-AAQADRVIVMNKGEILEEgTPEEifKSGHMLQEI 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
293-500 |
4.08e-21 |
|
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: 91.57 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 293 RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGqrlppRSVGSAVAAGIGHVPEDRkgqGLVL 372
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYLPEER---GLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLGYatlaatsragFADRRG-----QRSRAQEVASRLRIRMRDvDQAARDLSGGNQQKIVFGRWVLAGSRVLLL 447
Cdd:cd03269 84 KMKVIDQLVY----------LAQLKGlkkeeARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 448 DEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-269 |
4.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.33 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSF--GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG---GRVVVDGKPVHLGSVRDA-E 106
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIrE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 RLGIATIHQELNLVPSmTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSL 186
Cdd:PRK13640 85 KVGIVFQNPDNQFVGA-TVGDDVAFG-LENRA--VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVF-ISHHLEEiAAIGDEVSVLRDGALVAE-VPASTHEDELVRLM 264
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITHDIDE-ANMADQVLVLDDGKLLAQgSPVEIFSKVEMLKE 239
|
....*
gi 502628485 265 VGRDI 269
Cdd:PRK13640 240 IGLDI 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-250 |
4.56e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIA 111
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENVLMgrlpsrGGFVSRRT--MRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAM------GGFFAERDqfQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
49-250 |
5.15e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgsvrDAERLGIATIHQELNLV---P---- 121
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI------DYSRKGLMKLRESVGMVfqdPdnql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 122 -SMTVAENVLMG----RLPSRGgfVSRRTMRRLAREALDRVRldvslDTPVGELGIARQQLVEIAKALSLNARVLILDEP 196
Cdd:PRK13636 96 fSASVYQDVSFGavnlKLPEDE--VRKRVDNALKRTGIEHLK-----DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 197 TAALTGSET-EVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK13636 169 TAGLDPMGVsEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
32-242 |
5.92e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.10 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGgrvvvdgkpvhlGSVRDAERLGIA 111
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE------------GVIKRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENVLMgRLpsRGGFVSRRTMrrlarEALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFL-RL--RPGTKKEDIL-----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502628485 192 ILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVL 242
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
296-499 |
6.27e-21 |
|
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: 91.06 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAvaagIGHVPedrkgQGLVLD-- 373
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK--PLEKERKR----IGYVP-----QRRSIDrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 --ASVAENLGyatLAATSRAGFAdRRGQRSRAQEVASRL-RIRMRDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:cd03235 83 fpISVRDVVL---MGLYGHKGLF-RRLSKADKAKVDEALeRVGLSELaDRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 450 PTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGG 499
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
285-501 |
8.86e-21 |
|
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: 91.64 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRsvgsAVAAG 357
Cdd:COG1120 1 MLEAENLSvgygGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaSLSRR----ELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 358 IGHVPEDRkgqGLVLDASVAEN--LG-YATLAATSRAGFADRRgqrsRAQEVASRLRI---RMRDVDQaardLSGGNQQK 431
Cdd:COG1120 77 IAYVPQEP---PAPFGLTVRELvaLGrYPHLGLFGRPSAEDRE----AVEEALERTGLehlADRPVDE----LSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 432 IVFGRwVLA-GSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVMSGGRL 501
Cdd:COG1120 146 VLIAR-ALAqEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLhDLNLAARYADRLVLLKDGRI 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
46-248 |
1.31e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgsvrdaERLGIATIHQELNLVP---- 121
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--------VQYDHHYLHRQVALVGqepv 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 122 --SMTVAENVLMGRlpsrgGFVSRRTMRRLAREALDR---VRLDVSLDTPVGELGIAR----QQLVEIAKALSLNARVLI 192
Cdd:TIGR00958 566 lfSGSVRENIAYGL-----TDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVGEKGSQLsggqKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 193 LDEPTAALtgsETEVLFGVVEELRRDDVAMVFISHHLeEIAAIGDEVSVLRDGALV 248
Cdd:TIGR00958 641 LDEATSAL---DAECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVV 692
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
44-250 |
1.33e-20 |
|
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: 90.67 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 44 GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLgsvrdaerLGIATihqelNLVPSM 123
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGG-----GFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 TVAENV-LMGRLpsRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELG---IARqqlVEIAKALSLNARVLILDEPTAA 199
Cdd:cd03220 100 TGRENIyLNGRL--LG--LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSsgmKAR---LAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 200 ltGSETEVL--FGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03220 173 --GDAAFQEkcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-245 |
1.55e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDaERLGIatI 113
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKVGF--V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMG--RLPSRGGfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltVLPRRER-PNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 192 ILDEPTAALTGSetevlfgVVEELRR--------DDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:PRK10851 159 LLDEPFGALDAQ-------VRKELRRwlrqlheeLKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
34-252 |
1.66e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.18 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLgsVRDAE------- 106
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL--VRDKDgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 -------RLGIATIHQELNLVPSMTVAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSLDT--PVgELGIARQQL 177
Cdd:PRK10619 84 knqlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKVGIDERAQGkyPV-HLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 178 VEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP 252
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
32-251 |
2.02e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSF--GPV--DVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVH-LGSVRDAE 106
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 ----RLGIatIHQELNLVPSMTVAENVLMgrlPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAK 182
Cdd:PRK11629 84 lrnqKLGF--IYQFHHLLPDFTALENVAM---PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 183 ALSLNARVLILDEPTAALTGSETEVLFGVVEEL-RRDDVAMVFISHHLEEIAAIGDEVSvLRDGALVAEV 251
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAEL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
282-501 |
2.04e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 282 DEVLLDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAvaag 357
Cdd:COG1121 3 MMPAIELENLTvsygGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK--PPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 358 IGHVPedrkgQGLVLD----ASVAEnlgYATLAATSRAGFADRRGQRSRAQeVASRL-RIRMRDV-DQAARDLSGGNQQK 431
Cdd:COG1121 77 IGYVP-----QRAEVDwdfpITVRD---VVLMGRYGRRGLFRRPSRADREA-VDEALeRVGLEDLaDRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 432 IVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
282-501 |
3.20e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.10 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 282 DEVLLDVRGLSRT--GV--LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVgsaV 354
Cdd:COG0411 1 SDPLLEVRGLTKRfgGLvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditGLPPHRI---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 355 AAGIGhvpedRKGQ--GLVLDASVAENL--------GYATLAATSR--AGFADRRGQRSRAQEVASRLRIRmRDVDQAAR 422
Cdd:COG0411 78 RLGIA-----RTFQnpRLFPELTVLENVlvaaharlGRGLLAALLRlpRARREEREARERAEELLERVGLA-DRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 423 DLSGGNQQKIVFGRwVLAGS-RVLLLDEPTRGVDVGARVEIYELINAVAAAGGAvllvsS------DLPEVLGVSDRVLV 495
Cdd:COG0411 152 NLSYGQQRRLEIAR-ALATEpKLLLLDEPAAGLNPEETEELAELIRRLRDERGI-----TilliehDMDLVMGLADRIVV 225
|
....*.
gi 502628485 496 MSGGRL 501
Cdd:COG0411 226 LDFGRV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-248 |
4.00e-20 |
|
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: 93.60 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 9 ASEPSGgrasgpaRSRTSVPAPAPVLTLDSVSKSF-----------GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIK 77
Cdd:COG4172 258 AAEPRG-------DPRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 78 MMSGIyQPDGGRVVVDGKPVHLGSVRD--AERLGIATIHQE----LNlvPSMTVAENVLMGrLPSRGGFVSRRTMRRLAR 151
Cdd:COG4172 331 ALLRL-IPSEGEIRFDGQDLDGLSRRAlrPLRRRMQVVFQDpfgsLS--PRMTVGQIIAEG-LRVHGPGLSAAERRARVA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 152 EALDRVRLD-VSLDTPVGEL-GIARQQlVEIAKALSLNARVLILDEPTAALTGSeteVLFGVVEELR----RDDVAMVFI 225
Cdd:COG4172 407 EALEEVGLDpAARHRYPHEFsGGQRQR-IAIARALILEPKLLVLDEPTSALDVS---VQAQILDLLRdlqrEHGLAYLFI 482
|
250 260
....*....|....*....|...
gi 502628485 226 SHHLEEIAAIGDEVSVLRDGALV 248
Cdd:COG4172 483 SHDLAVVRALAHRVMVMKDGKVV 505
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
34-231 |
5.39e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvrdAERlgiATI 113
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---AER---GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFG-LQLAG--VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRDDVAMVF-ISHHLEE 231
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLlITHDIEE 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-248 |
6.25e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.78 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAE--RLG 109
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSMTVAENVLMgrlPSRGGFVSRRTMRRLAREALDRV-RLDVSLDTPVgELGIARQQLVEIAKALSLNA 188
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDIRRRVSAALDKVgLLDKAKNFPI-QLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 189 RVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
49-272 |
6.30e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAeRLGIATIHQELN-LVPSMTVAE 127
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-RSKVGLVFQDPDdQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrlPSRGGFVSRRTMRRlAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:PRK13647 100 DVAFG--PVNMGLDKDEVERR-VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 208 LFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPasthedelVRLMVGRDITEQ 272
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD--------KSLLTDEDIVEQ 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
49-248 |
6.33e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG-----KPVHLGSVRdaERLGIATIHQELNLVPSm 123
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIR--KKVGLVFQYPEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 TVAENVLMGrlPSRGGFVSRRTMRRLaREALDRVRLDVS--LDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALT 201
Cdd:PRK13637 100 TIEKDIAFG--PINLGLSEEEIENRV-KRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 202 GSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK13637 177 PKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-234 |
7.06e-20 |
|
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: 92.73 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 1 MTAAAPVPASEPSGGRASGParSRTSVPAPAPVLTLDSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMM 79
Cdd:TIGR02857 291 VAAAEALFAVLDAAPRPLAG--KAPVTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 80 SGIYQPDGGRVVVDGKPVHLGSvRDAERLGIATIHQELNLVPSmTVAENVLMGRLPSRGGFVSRRTMRRLAREALDrvRL 159
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGVPLADAD-ADSWRDQIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVA--AL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 160 DVSLDTPVGE----LGIARQQLVEIAKALSLNARVLILDEPTAALTGsETEVLfgVVEELRR--DDVAMVFISHHLEEIA 233
Cdd:TIGR02857 445 PQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA-ETEAE--VLEALRAlaQGRTVLLVTHRLALAA 521
|
.
gi 502628485 234 A 234
Cdd:TIGR02857 522 L 522
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
283-520 |
8.48e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLSRT--GV--LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGI 358
Cdd:COG3845 3 PPALELRGITKRfgGVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 359 GHVPEDRKgqgLVLDASVAEN--LGyatlAATSRAGFADRRGQRSRAQEVASRLRIRMrDVDQAARDLSGGNQQK--IVf 434
Cdd:COG3845 83 GMVHQHFM---LVPNLTVAENivLG----LEPTKGGRLDRKAARARIRELSERYGLDV-DPDAKVEDLSVGEQQRveIL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 435 gRWVLAGSRVLLLDEPTrgvdvgArV----EIYEL----------------InavaaaggavllvSSDLPEVLGVSDRVL 494
Cdd:COG3845 154 -KALYRGARILILDEPT------A-VltpqEADELfeilrrlaaegksiifI-------------THKLREVMAIADRVT 212
|
250 260
....*....|....*....|....*.
gi 502628485 495 VMSGGRLTGELPAATATQDQVMALAV 520
Cdd:COG3845 213 VLRRGKVVGTVDTAETSEEELAELMV 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
33-262 |
9.81e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIAT 112
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENvLMGRLPSRGGFVSRRTMRRlAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:PRK10895 83 LPQEASIFRRLSVYDN-LMAVLQIRDDLSAEQREDR-ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 193 LDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE-VPASTHEDELVR 262
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHgTPTEILQDEHVK 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
285-467 |
1.03e-19 |
|
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: 87.53 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLS-----RTgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRL--PPRSVGSAVAAg 357
Cdd:COG4133 2 MLEAENLScrrgeRL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 358 IGHVPedrkgqGLVLDASVAENLGYAtlaatsrAGFADRRGQRSRAQEVASRLRIRMRDvDQAARDLSGGNQQKIVFGRW 437
Cdd:COG4133 80 LGHAD------GLKPELTVRENLRFW-------AALYGLRADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARL 145
|
170 180 190
....*....|....*....|....*....|
gi 502628485 438 VLAGSRVLLLDEPTRGVDVGARVEIYELIN 467
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-250 |
1.11e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-HLGSVRDAERLgiAT 112
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRQLARRL--AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELnLVPS-MTVAENVLMGRLP--SRGGFVSRRTmRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNAR 189
Cdd:PRK11231 81 LPQHH-LTPEgITVRELVAYGRSPwlSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
46-250 |
1.47e-19 |
|
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: 87.77 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIaTIHQELNLVPSMTV 125
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMGRL-----PSRggfvSRRTMRRLArEALDRVRLdvsLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:cd03267 113 IDSFYLLAAiydlpPAR----FKKRLDELS-ELLDLEEL---LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 201 TGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:cd03267 185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
49-262 |
1.50e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.00 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVH---LGSVRDAerlgIATIHQELNLVPSmTV 125
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytLASLRNQ----VALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMgrlpSRGGFVSRRTMRRLAR--EALDRV-RLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:PRK11176 434 ANNIAY----ARTEQYSREQIEEAARmaYAMDFInKMDNGLDTVIGENGVllsgGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 199 AL-TGSETEVLfGVVEELRRDDVAMVfISHHLEEIAAiGDEVSVLRDGALVAEvpaSTHEDELVR 262
Cdd:PRK11176 510 ALdTESERAIQ-AALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIVER---GTHAELLAQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-262 |
1.76e-19 |
|
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: 87.67 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG---KPVHLGSVRDAerlg 109
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 IATIHQELNLVPSmTVAENVLMGRLPsrggfVSRRTMRRLAREAL--DRV-RLDVSLDTPVGELGI----ARQQLVEIAK 182
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYGRPD-----ATDEEVIEAAKAAQihDKImRFPDGYDTIVGERGLklsgGEKQRVAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 183 ALSLNARVLILDEPTAAL-TGSETEVLfgvvEELRR--DDVAMVFISHHLEEIAAiGDEVSVLRDGALVAEvpaSTHEDE 259
Cdd:cd03253 151 AILKNPPILLLDEATSALdTHTEREIQ----AALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVER---GTHEEL 222
|
...
gi 502628485 260 LVR 262
Cdd:cd03253 223 LAK 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
296-500 |
2.28e-19 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 86.75 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGsAVAAGIGHVPEDRKGQ--GLVLD 373
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK-ELRRKVGLVFQNPDDQffGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVA---ENLGYatlaatsragfaDRRGQRSRAQEVASRLRIRmrdvDQAARD---LSGGNQQKIVFGRwVLA-GSRVLL 446
Cdd:cd03225 95 EEVAfglENLGL------------PEEEIEERVEEALELVGLE----GLRDRSpftLSGGQKQRVAIAG-VLAmDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 447 LDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
35-196 |
2.46e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 35 TLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD-AERLgiATI 113
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElAKRL--AIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVLMGRLP-SRGgfvsRRTM--RRLAREALDRVRL----DVSLDtpvgELGIARQQLVEIAKALSL 186
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPySKG----RLTAedREIIDEAIAYLDLedlaDRYLD----ELSGGQRQRAFIAMVLAQ 152
|
170
....*....|
gi 502628485 187 NARVLILDEP 196
Cdd:COG4604 153 DTDYVLLDEP 162
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
34-255 |
4.16e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVV------DGKPV--HLGSVRdA 105
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLsqQKGLIR-Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 106 ERLGIATIHQELNLVPSMTVAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALS 185
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 186 LNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST 255
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
34-250 |
4.75e-19 |
|
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: 84.67 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVD--VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERLGIA 111
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVpSMTVAENVlmGRLPSRGgfvsrrTMRRLArealdrvrldvsldtpvgelgiarqqlveIAKALSLNARVL 191
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNL--GRRFSGG------ERQRLA-----------------------------LARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 192 ILDEPTAALTG-SETEVLFGVVEELRrdDVAMVFISHHLEEIAAIgDEVSVLRDGALVAE 250
Cdd:cd03247 121 LLDEPTVGLDPiTERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
31-253 |
5.10e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 31 APVLTLDSVSKSF----GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV------HLG 100
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 101 SVRdAERLGIatIHQELNLVPSMTVAENVlmgRLPSRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEI 180
Cdd:PRK10535 82 QLR-REHFGF--IFQRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 181 AKALSLNARVLILDEPTAALTGSETEVLFGVVEELrRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPA 253
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
48-247 |
5.43e-19 |
|
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: 85.99 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgIATIHQELNLVpSMTVAE 127
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLF-ARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrLPSrggfVSRRTMRRLAREALDR---VRLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:cd03248 107 NIAYG-LQS----CSFECVKEAAQKAHAHsfiSELASGYDTEVGEKGSqlsgGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 201 -TGSETEVLFGVVEELRRDDVAMvfISHHLEEIAAiGDEVSVLRDGAL 247
Cdd:cd03248 182 dAESEQQVQQALYDWPERRTVLV--IAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
286-501 |
5.84e-19 |
|
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: 85.63 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRTG------VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLppRSVGSAVAAGIG 359
Cdd:cd03263 1 LQIRNLTKTYkkgtkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 360 HVPEDRkgqGLVLDASVAENLGYatlaatsragFADRRGQRSR-AQEVASRLRIRMRDVDQA---ARDLSGGNQQKIVFG 435
Cdd:cd03263 79 YCPQFD---ALFDELTVREHLRF----------YARLKGLPKSeIKEEVELLLRVLGLTDKAnkrARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 436 RWVLAGSRVLLLDEPTRGVDVGARVEIYELINavaaaggAVLLVSS------DLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLIL-------EVRKGRSiiltthSMDEAEALCDRIAIMSDGKL 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
49-269 |
8.12e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDA-ERLGIATIHQELNLVPSmTVAE 127
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrKHIGIVFQNPDNQFVGS-IVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGRlpsRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:PRK13648 104 DVAFGL---ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 208 LFGVVEELRRD-DVAMVFISHHLEEiAAIGDEVSVLRDGALVAE-VPASTHEDELVRLMVGRDI 269
Cdd:PRK13648 181 LLDLVRKVKSEhNITIISITHDLSE-AMEADHVIVMNKGTVYKEgTPTEIFDHAEELTRIGLDL 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
48-250 |
9.09e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.28 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVH-----LGSVRdaERLGIATIHQELNLVpS 122
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksLLEVR--KTVGIVFQNPDDQLF-A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 123 MTVAENVLMGrlPSRGGFVSRRTMRRLaREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTG 202
Cdd:PRK13639 94 PTVEEDVAFG--PLNLGLSKEEVEKRV-KEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 203 SETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
296-502 |
9.59e-19 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 84.02 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRsvgsAVAAGIGHVPEdrkgqglvl 372
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaSLSPK----ELARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 dasvaenlgyaTLAATSRAGFADRRgqrsraqevasrlrirmrdvdqaARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTR 452
Cdd:cd03214 81 -----------ALELLGLAHLADRP-----------------------FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 453 GVDVGARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVMSGGRLT 502
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLhDLNLAARYADRVILLKDGRIV 177
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-248 |
1.02e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 20 PARSRT---SVPAPA----PVLTLDSVSKSFGPVDVLKDITVHVRPG-RVqVLLGENGAGKSTLIKMMSGIYQPDGGRVV 91
Cdd:COG0488 295 PRRDKTveiRFPPPErlgkKVLELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 92 VdGKPVHLGSVrdaerlgiaTIHQElNLVPSMTVAENVlmgrlpSRGgfvSRRTMRRLAREAL-------DRVRldvsld 164
Cdd:COG0488 374 L-GETVKIGYF---------DQHQE-ELDPDKTVLDEL------RDG---APGGTEQEVRGYLgrflfsgDDAF------ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 165 TPVGEL--G-IARQQLveiAKALSLNARVLILDEPT-----AALTgsetevlfgVVEELRRD-DVAMVFISH--HLeeIA 233
Cdd:COG0488 428 KPVGVLsgGeKARLAL---AKLLLSPPNVLLLDEPTnhldiETLE---------ALEEALDDfPGTVLLVSHdrYF--LD 493
|
250
....*....|....*
gi 502628485 234 AIGDEVSVLRDGALV 248
Cdd:COG0488 494 RVATRILEFEDGGVR 508
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-248 |
1.03e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.17 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGpvdvLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpVHLGSVRDAE-----RL 108
Cdd:PRK10070 33 QILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAElrevrRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIATIHQELNLVPSMTVAENVLMGRlpsRGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNA 188
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGM---ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 189 RVLILDEPTAALTG-SETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK10070 184 DILLMDEAFSALDPlIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
47-250 |
1.07e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.50 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 47 DVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI--YQPDGGRVVVDGK-----PVHlgsvrdaER--LGIATIHQ-- 115
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEdilelSPD-------ERarAGIFLAFQyp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 116 -ElnlVPSMTVAeNVLMGRLPS-RGGFVSRRTMRRLAREALDRVRLDVS-LDTPV------GElgiarQQLVEIAKALSL 186
Cdd:COG0396 87 vE---IPGVSVS-NFLRTALNArRGEELSAREFLKLLKEKMKELGLDEDfLDRYVnegfsgGE-----KKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 187 NARVLILDEPTA-----ALtgsetEVLFGVVEELRRDDVAMVFISHH---LEEIAAigDEVSVLRDGALVAE 250
Cdd:COG0396 158 EPKLAILDETDSgldidAL-----RIVAEGVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGRIVKS 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
286-465 |
1.27e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT-G---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPrsvgsAVAAGIGHV 361
Cdd:COG4152 2 LELKGLTKRfGdktAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDRkgqGLVLDASVAENLGYatlaatsragFADRRGQ-----RSRAQEVASRLRIRMRDvDQAARDLSGGNQQKIVFGR 436
Cdd:COG4152 77 PEER---GLYPKMKVGEQLVY----------LARLKGLskaeaKRRADEWLERLGLGDRA-NKKVEELSKGNQQKVQLIA 142
|
170 180 190
....*....|....*....|....*....|...
gi 502628485 437 WVLAGSRVLLLDEPTRGVD-VGARV---EIYEL 465
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDpVNVELlkdVIREL 175
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
49-248 |
3.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.80 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAerlgIATIHQELNLVPSM----- 123
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD----IKQIRKKVGLVFQFpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 ---TVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVSL-DTPVGELGIARQQLVEIAKALSLNARVLILDEPTAA 199
Cdd:PRK13649 99 feeTVLKDVAFG--PQNFG-VSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 200 LTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
46-261 |
3.38e-18 |
|
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: 83.74 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgIATIHQELNLVpSMTV 125
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLF-DGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMGRLPsrggfVSRRTMRRLAREALDR---VRLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:cd03249 94 AENIRYGKPD-----ATDEEVEEAAKKANIHdfiMSLPDGYDTLVGERGSqlsgGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 199 AL-TGSETEVLfGVVEELRRDDVAMVfISHHLEEIAAiGDEVSVLRDGALVAEvpaSTHeDELV 261
Cdd:cd03249 169 ALdAESEKLVQ-EALDRAMKGRTTIV-IAHRLSTIRN-ADLIAVLQNGQVVEQ---GTH-DELM 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
48-247 |
3.59e-18 |
|
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: 82.26 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvRDAERLGIATIHQELNLVPSmTVAE 127
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-PNELGDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLmgrlpSRGgfvsrrtmrrlarealdrvrldvsldtpvgelgiaRQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:cd03246 95 NIL-----SGG-----------------------------------QRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502628485 208 LFGVVEELRRDDVAMVFISHHLEEIAAIgDEVSVLRDGAL 247
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
296-501 |
4.06e-18 |
|
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: 83.19 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRL--PPRsvgsAVAAGIGHVPEdrkGQGLVLD 373
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvkEPA----EARRRLGFVSD---STGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAENLGYatlaatsragFAD-----RRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:cd03266 93 LTARENLEY----------FAGlyglkGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 449 EPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
285-508 |
4.08e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 84.08 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLS--------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGsAVAA 356
Cdd:COG1124 1 MLEVRNLSvsygqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK-AFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 357 GIGHVPED-------RKGqglvLDASVAEnlgyaTLAATSRAGFADRRGQRSRAQEVASRLRirmrdvDQAARDLSGGNQ 429
Cdd:COG1124 80 RVQMVFQDpyaslhpRHT----VDRILAE-----PLRIHGLPDREERIAELLEQVGLPPSFL------DRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 430 QKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVL-LVSSDLPEVLGVSDRVLVMSGGRLTGELPAA 508
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYlFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
49-245 |
4.78e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLgIATIHQEL-NLVPSMTVAE 127
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:PRK13650 102 DVAFG-LENKG--IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 502628485 208 LFGVVEELRRD-DVAMVFISHHLEEIaAIGDEVSVLRDG 245
Cdd:PRK13650 179 LIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
48-249 |
5.21e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLgSVRD--AERLGIATIHQELNLVPSMTV 125
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-SKRGllALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSET 205
Cdd:PRK13638 95 IDSDIAFSLRNLG--VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502628485 206 EVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-245 |
6.81e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 20 PARSRTSVPapapvLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPvhL 99
Cdd:PRK11247 4 TARLNQGTP-----LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 100 GSVRDAERLgiatIHQELNLVPSMTVAENVLMGRlpsRGGFvsrrtmRRLAREALDRVRL-DVSLDTPVGeLGIARQQLV 178
Cdd:PRK11247 77 AEAREDTRL----MFQDARLLPWKKVIDNVGLGL---KGQW------RDAALQALAAVGLaDRANEWPAA-LSGGQKQRV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 179 EIAKALSLNARVLILDEPTAALTGSETEVLFGVVEEL-RRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
29-248 |
7.20e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 85.27 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 29 APAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpVHLGSVRDAERl 108
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIATIHQELNLVPSMTVAENVLMG----RLPsRGGFVSRrtmrrlAREALDRVRLDVSLDTPVGELGIARQQLVEIAKAL 184
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGlkqdKLP-KAEIASR------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 185 SLNARVLILDEPTAALTGSETEVL-FGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
33-245 |
9.25e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPD---GGRVVVDGKPVH-----LGSVRD 104
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 105 AeRLGIATIHQELNLVPSMTVAENVLMGRLPSRGGFVS-----RRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVE 179
Cdd:PRK09984 84 S-RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 180 IAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDD-VAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
34-262 |
1.13e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 82.53 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGP--VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpVHLGSVRDAE-RLGI 110
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG--HDLALADPAWlRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 ATIHQElNLVPSMTVAENVLMGRlPSrggfVSRRTMRRLAR--EALDRVR-LDVSLDTPVGELGIA----RQQLVEIAKA 183
Cdd:cd03252 79 GVVLQE-NVLFNRSIRDNIALAD-PG----MSMERVIEAAKlaGAHDFISeLPEGYDTIVGEQGAGlsggQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 184 LSLNARVLILDEPTAALtgsETEVLFGVVEELRR--DDVAMVFISHHLEEIAAiGDEVSVLRDGALVAevpASTHeDELV 261
Cdd:cd03252 153 LIHNPRILIFDEATSAL---DYESEHAIMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE---QGSH-DELL 224
|
.
gi 502628485 262 R 262
Cdd:cd03252 225 A 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-249 |
1.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.12 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVD--VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDA-ERL 108
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 GIatIHQEL-NLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLN 187
Cdd:PRK13632 86 GI--IFQNPdNQFIGATVEDDIAFG-LENKK--VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 188 ARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEiAAIGDEVSVLRDGALVA 249
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDE-AILADKVIVFSEGKLIA 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
48-250 |
1.70e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.83 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG----KPVHLGSVRdaERLGIATIHQELNLVPSM 123
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLWDIR--NKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 tVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGS 203
Cdd:PRK13633 103 -VEEDVAFG--PENLG-IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 204 -ETEVLFGVVEELRRDDVAMVFISHHLEEiAAIGDEVSVLRDGALVAE 250
Cdd:PRK13633 179 gRREVVNTIKELNKKYGITIILITHYMEE-AVEADRIIVMDSGKVVME 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-254 |
2.02e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 28 PAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAER 107
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 lGIATIHQELNLVPSMTVAENVLMGRLPSRGGFVS-RRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSL 186
Cdd:PRK10575 86 -KVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 187 NARVLILDEPTAAL-TGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAS 254
Cdd:PRK10575 165 DSRCLLLDEPTSALdIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-266 |
2.89e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 9 ASEPSGGRaSGPArsrtSVPAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI------ 82
Cdd:PRK14271 2 ACERLGGQ-SGAA----DVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 83 --YQPD---GGRVVVDGKPVhlgsVRDAERLGIatIHQELNLVPsMTVAENVLMGRLPSRggFVSRRTMRRLAREALDRV 157
Cdd:PRK14271 77 yrYSGDvllGGRSIFNYRDV----LEFRRRVGM--LFQRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 158 RL-----DVSLDTPVgELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELrRDDVAMVFISHHLEEI 232
Cdd:PRK14271 148 GLwdavkDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQA 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 502628485 233 AAIGDEVSVLRDGALVAEVP-----ASTHEDELVRLMVG 266
Cdd:PRK14271 226 ARISDRAALFFDGRLVEEGPteqlfSSPKHAETARYVAG 264
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
296-500 |
2.95e-17 |
|
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: 78.83 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgSAVAAGIGHVPEdrkgqglvldas 375
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-EELRRRIGYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 vaenlgyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaardLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502628485 456 VGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
37-248 |
2.96e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.01 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 37 DSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG---KPVHLGSVRDAerlgIAT 112
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRN----IAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVpSMTVAENVLMGRlPSrggfVSRRTMRRLAR--EALDRV-RLDVSLDTPVGELGIA-----RQQLvEIAKAL 184
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGR-PD----ATDEEMRAAAEraQAHDFIeRKPDGYDTVVGERGRQlsggeRQRL-AIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 185 SLNARVLILDEPTAALTgSETEV-LFGVVEELRRDDVAMVfISHHLEEIAAiGDEVSVLRDGALV 248
Cdd:PRK13657 487 LKDPPILILDEATSALD-VETEAkVKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
286-501 |
4.37e-17 |
|
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: 80.46 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRTG---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSvgsavaAGIG 359
Cdd:cd03299 1 LKVENLSKDWkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK------RDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 360 HVPEDrkgQGLVLDASVAENLGYATlaatsRAGFADRRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVL 439
Cdd:cd03299 75 YVPQN---YALFPHMTVYKNIAYGL-----KKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 440 AGSRVLLLDEPTRGVDVGARVE-IYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKlREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
296-506 |
6.73e-17 |
|
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: 79.92 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAG---ADPY--DAGTVHVDGQrlpprsvgsAVAAGIGHVPEDRKGQGL 370
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGapDEGEVLLDGK---------DIYDLDVDVLELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 371 V------LDASVAENLGYA-TLAATSRAGFADRRGQRS--RA---QEVASRLrirmrdvdqAARDLSGGNQQKIVFGRWV 438
Cdd:cd03260 86 VfqkpnpFPGSIYDNVAYGlRLHGIKLKEELDERVEEAlrKAalwDEVKDRL---------HALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 439 LAGSRVLLLDEPTRGVDVGARVEIYELInAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELP 506
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELI-AELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
296-501 |
8.85e-17 |
|
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: 79.59 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsavaagIGHVPEDRKGQGLVLDA- 374
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-------------ITNLPPHKRPVNTVFQNy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ------SVAENLGYA-TLAATSRAgfadrrgqrSRAQEVASRLR-IRM-----RDVDQaardLSGGNQQKIVFGRWVLAG 441
Cdd:cd03300 82 alfphlTVFENIAFGlRLKKLPKA---------EIKERVAEALDlVQLegyanRKPSQ----LSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 442 SRVLLLDEPTRGVDVGARVEI-YELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
296-506 |
9.91e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 79.05 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgsavaAGIGHVPEDrkgqglvlDA- 374
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------PDRGYVFQQ--------DAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ----SVAENLGYatlaatsraGFADRRGQRSRAQEVASRLrIRMRDVDQAA----RDLSGGNQQKIVFGRWVLAGSRVLL 446
Cdd:cd03293 85 lpwlTVLDNVAL---------GLELQGVPKAEARERAEEL-LELVGLSGFEnaypHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 447 LDEPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSG--GRLTGELP 506
Cdd:cd03293 155 LDEPFSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
296-499 |
1.09e-16 |
|
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: 78.84 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAvaagIGHVPEDRKGQglVLDAS 375
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQDVDYQ--LFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYatlaatsRAGFADRRGQRsrAQEVASRLRIrMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:cd03226 89 VREELLL-------GLKELDAGNEQ--AETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502628485 456 VGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGG 499
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
48-252 |
1.12e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.26 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIY----QPDG----GRVVVDGKPVHlgsVRDAERLGI--ATIHQEL 117
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGarvtGDVTLNGEPLA---AIDAPRLARlrAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 118 NLVPSMTVAENVLMGRLP--SRGGFVSRRTmRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALS---------L 186
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPhaRRAGALTHRD-GEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP 252
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
53-248 |
1.58e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.86 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 53 TVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvrDAERlGIATIHQELNLVPSMTVAENVLMG 132
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--PSRR-PVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 133 RLPS-RGGFVSRRTMRRLARealdRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGV 211
Cdd:PRK10771 96 LNPGlKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 502628485 212 VEEL-RRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
48-228 |
1.95e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAER-LGiatiHQElNLVPSMTVA 126
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG----HRN-AMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 127 ENVLMGRlpsrgGFvsRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETE 206
Cdd:PRK13539 92 ENLEFWA-----AF--LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 502628485 207 VLFGVVEElRRDDVAMVFISHH 228
Cdd:PRK13539 165 LFAELIRA-HLAQGGIVIAATH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
48-254 |
2.00e-16 |
|
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: 77.95 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI--YQPDGGRVVVDGKPVHLGSVRDAERLGIATIHQELNLVPSMTV 125
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AE---NVLMGrlpSRGGFVSRrtmrrlarealdrvrldvsldtpvgelgiarqqlVEIAKALSLNARVLILDEPTAALTG 202
Cdd:cd03217 95 ADflrYVNEG---FSGGEKKR----------------------------------NEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 203 SETEVLFGVVEELRRDDVAMVFISHHLEEIAAI-GDEVSVLRDGALVAEVPAS 254
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
286-504 |
2.45e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 76.70 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT--GV--LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHV 361
Cdd:cd03216 1 LELRGITKRfgGVkaLDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEdrkgqglvldasvaenlgyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaardLSGGNQQKIVFGRWVLAG 441
Cdd:cd03216 81 YQ------------------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 442 SRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
286-500 |
2.54e-16 |
|
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: 76.84 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsaVAAGIGHV 361
Cdd:cd03229 1 LELKNVSKRygqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED---------LTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDRKGQGLVLDA-------SVAENLGYAtlaatsragfadrrgqrsraqevasrlrirmrdvdqaardLSGGNQQKIVF 434
Cdd:cd03229 72 PPLRRRIGMVFQDfalfphlTVLENIALG----------------------------------------LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 435 GRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVMSGGR 500
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVThDLDEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
49-276 |
4.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGG------RVVVDGK-PVHLGSVRdaERLGIATIHQELNLVP 121
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKkNKKLKPLR--KKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 122 SmTVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVS-LDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:PRK13634 101 E-TVEKDICFG--PMNFG-VSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 201 TGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVA-----EVPAstHEDELVRLMVGRDITEQYP 274
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLqgtprEIFA--DPDELEAIGLDLPETVKFK 254
|
..
gi 502628485 275 RR 276
Cdd:PRK13634 255 RA 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-501 |
5.72e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSF----GPVDVLKDITVHVRPGRVQVLLGENGAGKS-TLIKMMSGIYQPDG------------GRVVVDGK 95
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGlvqcdkmllrrrSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 96 PVHLGSVRDAERLGIATIHQE--LNLVPSMTVAENVLMGRLPSRGgfVSRRTMRRLAREALDRVRLDVS---LDTPVGEL 170
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 171 GIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 250 --------EVPASTHEDELV----RL--MVGRDITEQYP---------------RRTHTPGdEVLLDVRGLS-----RTG 295
Cdd:PRK10261 250 tgsveqifHAPQHPYTRALLaavpQLgaMKGLDYPRRFPlislehpakqeppieQDTVVDG-EPILQVRNLVtrfplRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRA----------GEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGS--AVAAGIGHVPE 363
Cdd:PRK10261 329 LLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 364 DRKGQglvLDASvaENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSR 443
Cdd:PRK10261 409 DPYAS---LDPR--QTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPK 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 444 VLLLDEPTRGVDVGARVEIYEL-INAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLlLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
286-501 |
7.06e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 77.20 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHV 361
Cdd:cd03218 1 LRAENLSkrygKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDrkgQGLVLDASVAENLgyatLAATSRAGFaDRRGQRSRAQEVASRLRI-RMRDvdQAARDLSGGNQQKIVFGRWVLA 440
Cdd:cd03218 81 PQE---ASIFRKLTVEENI----LAVLEIRGL-SKKEREEKLEELLEEFHItHLRK--SKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 441 GSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
299-519 |
7.83e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.00 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 299 DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpprsvgSAVAAGIGHVPEDRKGQGLVLDA---- 374
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL------FDSRKGIFLPPEKRRIGYVFQEArlfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 --SVAENLGYATlaatSRAGFADRRGQRSRAQEVasrLRIRMRdVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTR 452
Cdd:TIGR02142 89 hlSVRGNLRYGM----KRARPSERRISFERVIEL---LGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 453 GVDVGARVEIYE-LINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAATATQDQVMALA 519
Cdd:TIGR02142 161 ALDDPRKYEILPyLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-247 |
8.33e-16 |
|
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: 81.21 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 8 PASEPSGGRASGPARSRTSVPA---PAPVLTLDSVSKSFGPVD--VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI 82
Cdd:TIGR01257 1909 PAKEPIFDEDDDVAEERQRIISggnKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD 1988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 83 YQPDGGRVVVDGKPVhLGSVRDaerlgiatIHQELNLVPSMTVAENVLMGR----LPSRGGFVSRRTMRRLAREALDRVR 158
Cdd:TIGR01257 1989 TTVTSGDATVAGKSI-LTNISD--------VHQNMGYCPQFDAIDDLLTGRehlyLYARLRGVPAEEIEKVANWSIQSLG 2059
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 159 LDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDE 238
Cdd:TIGR01257 2060 LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTR 2139
|
....*....
gi 502628485 239 VSVLRDGAL 247
Cdd:TIGR01257 2140 LAIMVKGAF 2148
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
44-250 |
9.75e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.54 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 44 GPVDVLKDIT-VHVRPGRVQVLlGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATIHQELNLVPS 122
Cdd:PRK13652 15 GSKEALNNINfIAPRNSRIAVI-GPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 123 MTVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTG 202
Cdd:PRK13652 94 PTVEQDIAFG--PINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 203 SETEVLFGVVEEL-RRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK13652 171 QGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
32-248 |
1.84e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMS--GIYQPD---GGRVVVDGKPVHLGSVRDAE 106
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 -RLGIATIHQELNLVPsMTVAENVLMG-RLpsrGGFVSRRTMRRLAREAL------DRVRlDVSLDTPVGELGiARQQLV 178
Cdd:PRK14239 84 lRKEIGMVFQQPNPFP-MSIYENVVYGlRL---KGIKDKQVLDEAVEKSLkgasiwDEVK-DRLHDSALGLSG-GQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 179 EIAKALSLNARVLILDEPTAAL----TGSETEVLFGVveelrRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALdpisAGKIEETLLGL-----KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
286-502 |
1.94e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlpPRSVGSAVAAG--IG 359
Cdd:PRK09536 4 IDVSDLSvefgDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD---DVEALSARAASrrVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 360 HVPEdrkgqglvlDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQ-AARD---LSGGNQQKIVFG 435
Cdd:PRK09536 81 SVPQ---------DTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQfADRPvtsLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 436 RWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLT 502
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
298-501 |
2.00e-15 |
|
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: 75.41 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 298 HDIDVQVRA-GEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSavaagigHVPEDRKGQGLVLDA-- 374
Cdd:cd03297 13 FTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKI-------NLPPQQRKIGLVFQQya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 -----SVAENLGYATlaatsraGFADRRGQRSRAQEVASRLRIR---MRDVDQaardLSGGNQQKIVFGRWVLAGSRVLL 446
Cdd:cd03297 86 lfphlNVRENLAFGL-------KRKRNREDRISVDELLDLLGLDhllNRYPAQ----LSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 447 LDEPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03297 155 LDEPFSALDRALRLQLLpELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
289-501 |
2.35e-15 |
|
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: 75.22 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 289 RGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAVAAGIGHVPEDR 365
Cdd:cd03255 12 GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisKLSEKELAAFRRRHIGFVFQSF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 366 KgqgLVLDASVAENLGYATLAATSRagfadRRGQRSRAQEVASRLRIRMRdVDQAARDLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:cd03255 92 N---LLPDLTALENVELPLLLAGVP-----KKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 446 LLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
285-500 |
2.70e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.68 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLSR----TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsavaagIGH 360
Cdd:PRK09452 14 LVELRGISKsfdgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-------------ITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 VPEDRKGQGLVLDA-------SVAENLGYATlaatsragfadrRGQRSRAQEVASRLR--IRMRDVDQAA----RDLSGG 427
Cdd:PRK09452 81 VPAENRHVNTVFQSyalfphmTVFENVAFGL------------RMQKTPAAEITPRVMeaLRMVQLEEFAqrkpHQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEI-YELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
296-455 |
3.05e-15 |
|
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: 74.87 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgsavaagigHVPEDRKGQGLVLDA- 374
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK---------NINELRQKVGMVFQQf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ------SVAENLgyaTLAATSRagfadRRGQRSRAQEVASRLRIRMRDVDQA---ARDLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:cd03262 86 nlfphlTVLENI---TLAPIKV-----KGMSKAEAEERALELLEKVGLADKAdayPAQLSGGQQQRVAIARALAMNPKVM 157
|
170
....*....|
gi 502628485 446 LLDEPTRGVD 455
Cdd:cd03262 158 LFDEPTSALD 167
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
37-266 |
4.60e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 37 DSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-HLGSVRDAERLGIatIHQ 115
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGL--LAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 116 ELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSL-DTPVGELGIARQQLVEIAKALSLNARVLILD 194
Cdd:PRK10253 89 NATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 195 EPTAALTGSETEVLFGVVEELRRDD-VAMVFISHHLEEIAAIGDEVSVLRDGALVAE-VPASTHEDELVRLMVG 266
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQgAPKEIVTAELIERIYG 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
49-249 |
4.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVdGKPVHLGSVRDAE------RLGIATIHQELNLVPS 122
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEikpvrkKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 123 mTVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVSL--DTPVgELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:PRK13643 101 -TVLKDVAFG--PQNFG-IPKEKAEKIAAEKLEMVGLADEFweKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 201 TGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-251 |
4.81e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGP----VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERL 108
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 109 ---GIATIHQELNLVPSMTVAENVlmgRLPS--RGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKA 183
Cdd:PRK10584 86 rakHVGFVFQSFMLIPTLNALENV---ELPAllRG--ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 184 LSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEV 251
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
48-248 |
7.29e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 77.55 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKP---VHLGSVRDAerLGIatihqelnlVPSMT 124
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLRAA--IGI---------VPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 125 V------AENVLMGRlPSrggfVSRRTMRRLAREA-LDR--VRLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVL 191
Cdd:COG5265 442 VlfndtiAYNIAYGR-PD----ASEEEVEAAARAAqIHDfiESLPDGYDTRVGERGLklsgGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 192 ILDEPTAAL-TGSETEVLfgvvEELRRddVA----MVFISHHLEEIA-AigDEVSVLRDGALV 248
Cdd:COG5265 517 IFDEATSALdSRTERAIQ----AALRE--VArgrtTLVIAHRLSTIVdA--DEILVLEAGRIV 571
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
34-214 |
8.66e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERLGIATI 113
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQELNLVPSMTVAENVlmgrlpsrgGFVSR--RTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVL 191
Cdd:TIGR01189 79 GHLPGLKPELSALENL---------HFWAAihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180
....*....|....*....|...
gi 502628485 192 ILDEPTAALTGSETEVLFGVVEE 214
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRA 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
296-517 |
8.98e-15 |
|
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: 73.69 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgsavAAGIGHVpedRKGQGLVL--- 372
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-----EAELYRL---RRRMGMLFqsg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 ----DASVAENLGYATLAATsragfadrRGQRSRAQEVAsRLRIRMRDVDQAAR----DLSGGNQQKIVFGRWVLAGSRV 444
Cdd:cd03261 87 alfdSLTVFENVAFPLREHT--------RLSEEEIREIV-LEKLEAVGLRGAEDlypaELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 445 LLLDEPTRGVD-VGARVeIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLtgelpAATATQDQVMA 517
Cdd:cd03261 158 LLYDEPTAGLDpIASGV-IDDLIrSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI-----VAEGTPEELRA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
285-501 |
1.10e-14 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 73.31 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLSRTG--------VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAA 356
Cdd:cd03257 1 LLEVKNLSVSFptgggsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 357 G--IGHVPEDrkgQGLVLDA--SVAEnlgyaTLAATSRAGFADRRgqRSRAQEVASRLRIRMRDVDQAAR----DLSGGN 428
Cdd:cd03257 81 RkeIQMVFQD---PMSSLNPrmTIGE-----QIAEPLRIHGKLSK--KEARKEAVLLLLVGVGLPEEVLNryphELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 429 QQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLL-VSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLfITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
48-248 |
1.15e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVrPGRVQV-LLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRdAERLGIATIHQElNLVPSMTVA 126
Cdd:PRK10790 356 VLQNINLSV-PSRGFVaLVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQQD-PVVLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 127 ENVLMGRLPSRGGFVSRRTMRRLArealDRVR-LDVSLDTPVGE----LGIARQQLVEIAKALSLNARVLILDEPTAAL- 200
Cdd:PRK10790 433 ANVTLGRDISEEQVWQALETVQLA----ELARsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANId 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 201 TGSETevlfGVVEELR--RDDVAMVFISHHLEEIAAiGDEVSVLRDGALV 248
Cdd:PRK10790 509 SGTEQ----AIQQALAavREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-229 |
1.21e-14 |
|
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: 76.63 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 2 TAAAPVPASEPSGGRASGparsrtsVPAPAPVLTLDSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMS 80
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGA-------VGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 81 GIYQPDGGRVVVDGKPVHLGSVRDAERLgIATIHQELNLVPSmTVAENVLMGRlpsrgGFVSRRTMRRlareALDRVRL- 159
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLFDT-TVRENLRLAR-----PDATDEELWA----ALERVGLa 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 160 ------DVSLDTPVGELGIA-----RQQLVeIAKALSLNARVLILDEPTA---ALTGSE-TEVLFGVVEELrrddvAMVF 224
Cdd:TIGR02868 452 dwlralPDGLDTVLGEGGARlsggeRQRLA-LARALLADAPILLLDEPTEhldAETADElLEDLLAALSGR-----TVVL 525
|
....*
gi 502628485 225 ISHHL 229
Cdd:TIGR02868 526 ITHHL 530
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
46-266 |
1.22e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVR-DAERlgIATIHQElnlvPSMT 124
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSyRSQR--IRMIFQD----PSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 125 VAENVLMGRL---PSR-GGFVSRRTMRRLAREALDRVRL--DVSLDTPvGELGIARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:PRK15112 100 LNPRQRISQIldfPLRlNTDLEPEQREKQIIETLRQVGLlpDHASYYP-HMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 199 ALTGSETEVLFGVVEELR-RDDVAMVFISHHLEEIAAIGDEVSVLRDGALV-----AEVPASTHEDELVRLMVG 266
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVergstADVLASPLHELTKRLIAG 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-456 |
1.86e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.13 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPdggrvvvdgkpvHLGSVRDAERLGIA 111
Cdd:TIGR03719 4 IYTMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------------FNGEARPQPGIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQELNLVPSMTVAENVLMG-----RLPSRGGFVSRR------TMRRLAREA--------------LDRvRLDVSL--- 163
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGvaeikDALDRFNEISAKyaepdaDFDKLAAEQaelqeiidaadawdLDS-QLEIAMdal 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 164 -----DTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLfgvvEE-LRRDDVAMVFISHH---LEEIA- 233
Cdd:TIGR03719 151 rcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL----ERhLQEYPGTVVAVTHDryfLDNVAg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 234 ----------------------------AIGDEVSVLRDGALVAEV------PASTHEDELVRLMVGRDI-TEQYPRRTH 278
Cdd:TIGR03719 227 wileldrgrgipwegnysswleqkqkrlEQEEKEESARQKTLKRELewvrqsPKGRQAKSKARLARYEELlSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 279 T------PGD---EVLLDVRGLSRT-G---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVhvdgqrl 345
Cdd:TIGR03719 307 TaeiyipPGPrlgDKVIEAENLTKAfGdklLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 346 pprSVGSAVAagIGHVPEDRKGqglvLDAS------VAENLGYATLaatsragfadrrGQRsraqEVASRL---RIRMRD 416
Cdd:TIGR03719 380 ---EIGETVK--LAYVDQSRDA----LDPNktvweeISGGLDIIKL------------GKR----EIPSRAyvgRFNFKG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 502628485 417 VDQAAR--DLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDV 456
Cdd:TIGR03719 435 SDQQKKvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-250 |
2.83e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.10 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG----KPVHLGSVRdaER 107
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIR--KL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 108 LGIATIHQELNLVpSMTVAENVLMGR----LPSRGgfVSRRTMRRLAREALDRVRLDvSLDTPVGELGiarqQLVEIAKA 183
Cdd:PRK13644 79 VGIVFQNPETQFV-GRTVEEDLAFGPenlcLPPIE--IRKRVDRALAEIGLEKYRHR-SPKTLSGGQG----QCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 184 LSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAiGDEVSVLRDGALVAE 250
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLE 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
296-504 |
3.85e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHVPEDRKgqgLVLDAS 375
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYATLaatsragFADRRGQRSRAQEVASRL-RIRMRDVdQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:PRK11614 97 VEENLAMGGF-------FAERDQFQERIKWVYELFpRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 455 DVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
46-200 |
4.33e-14 |
|
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: 71.53 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG---GRVVVDGKPVHLGSVRDAerlgIATIHQELNLVPS 122
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC----VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 123 MTVAENVLmgrlpsrggFVSRRTMRRLAREALDRVRLDVSL-----DTPVGE-----LGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03234 96 LTVRETLT---------YTAILRLPRKSSDAIRKKRVEDVLlrdlaLTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLI 166
|
....*...
gi 502628485 193 LDEPTAAL 200
Cdd:cd03234 167 LDEPTSGL 174
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
49-251 |
5.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlGSVRDAErlgIATIHQELNLV---PSM-- 123
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKY---IRPVRKRIGMVfqfPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 ---TVAENVLMGrlPSRGGF----VSRRTMRRLAREALDRvrlDVSLDTPVGELGiARQQLVEIAKALSLNARVLILDEP 196
Cdd:PRK13646 99 fedTVEREIIFG--PKNFKMnldeVKNYAHRLLMDLGFSR---DVMSQSPFQMSG-GQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 197 TAALTGSETEVLFGVVEELRRDD-VAMVFISHHLEEIAAIGDEVSVLRDGALVAEV 251
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
296-501 |
6.67e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.18 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQR---LPPRsvgsavAAGIGHVPedrkgQGLVL 372
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdLPPK------DRNIAMVF-----QSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 --DASVAENLGYA-TLAATSRAgfadrrGQRSRAQEVASRLRIRMRdVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:COG3839 87 ypHMTVYENIAFPlKLRKVPKA------EIDRRVREAAELLGLEDL-LDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 450 PTRGVD----VGARVEIYELINavaaaggaVLLVSS-----DLPEVLGVSDRVLVMSGGRL 501
Cdd:COG3839 160 PLSNLDaklrVEMRAEIKRLHR--------RLGTTTiyvthDQVEAMTLADRIAVMNDGRI 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
296-501 |
6.88e-14 |
|
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: 71.08 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDG---QRLPPrsvgSAVAAGIGHVPEDrkgqGLVL 372
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDP----ADLRRNIGYVPQD----VTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENL----GYAT----LAATSRAGFAD--RRGQRSRAQEVASRlrirmrdvdqaARDLSGGNQQKIVFGRWVLAGS 442
Cdd:cd03245 91 YGTLRDNItlgaPLADderiLRAAELAGVTDfvNKHPNGLDLQIGER-----------GRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 443 RVLLLDEPTRGVDVGARVEIYEliNAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKE--RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
296-515 |
7.21e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHVPEDrkgQGLVLDAS 375
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLgyatLAATSRAGFADRRGQRSRAQEVASRLRI-RMRDvdQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:PRK10895 95 VYDNL----MAVLQIRDDLSAEQREDRANELMEEFHIeHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 455 DVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGE-LPAATATQDQV 515
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHgTPTEILQDEHV 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
297-501 |
7.27e-14 |
|
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: 71.22 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsavaagIGHVPEDRKGQGLVLD--- 373
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED-------------ATDVPVQERNVGFVFQhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ----ASVAENLGYATLaatsragfADRRGQRSRAQEVASRLRIRMRDV------DQAARDLSGGNQQKIVFGRWVLAGSR 443
Cdd:cd03296 85 lfrhMTVFDNVAFGLR--------VKPRSERPPEAEIRAKVHELLKLVqldwlaDRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 444 VLLLDEPTRGVDVGARVEIYE-LINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRwLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
296-501 |
7.86e-14 |
|
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: 70.75 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgsavaagighvPEDRkGQGLVLDA- 374
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP------------PKDR-DIAMVFQNy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ------SVAENLGYATlaaTSRAgfADRRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:cd03301 82 alyphmTVYDNIAFGL---KLRK--VPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 449 EPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03301 156 EPLSNLDAKLRVQMRaELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-466 |
9.40e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 9.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVD----VLKDITVHVRPGRVQVLLGENGAGKS-TLIKMMSGIYQPD----GGRVVVDGKPVHLGSV 102
Cdd:PRK15134 4 PLLAIENLSVAFRQQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 103 RDAERL---GIATIHQE--LNLVPSMTVAEN---VL-----MGRLPSRGGFVSrrtmrrlareALDRV-------RLDvs 162
Cdd:PRK15134 84 QTLRGVrgnKIAMIFQEpmVSLNPLHTLEKQlyeVLslhrgMRREAARGEILN----------CLDRVgirqaakRLT-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 163 lDTPVGELGIARQQlVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSV 241
Cdd:PRK15134 152 -DYPHQLSGGERQR-VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 242 LRDGALV------AEVPASTHeDELVRLMVGRDITEQYPRRTHTPgdeVLLDVRGLS-----RTG----------VLHDI 300
Cdd:PRK15134 230 MQNGRCVeqnraaTLFSAPTH-PYTQKLLNSEPSGDPVPLPEPAS---PLLDVEQLQvafpiRKGilkrtvdhnvVVKNI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 301 DVQVRAGEVVGVAGLVGAGRT----ELLRAIAGadpydAGTVHVDGQ---RLPPRSVgsavaagighVPEDRKGQGLVLD 373
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSttglALLRLINS-----QGEIWFDGQplhNLNRRQL----------LPVRHRIQVVFQD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAEN--LGYATLAAtsrAGFADRRGQRSRAQEVAsRLRIRMRDV--DQAAR-----DLSGGNQQKIVFGRWVLAGSRV 444
Cdd:PRK15134 371 PNSSLNprLNVLQIIE---EGLRVHQPTLSAAQREQ-QVIAVMEEVglDPETRhrypaEFSGGQRQRIAIARALILKPSL 446
|
490 500
....*....|....*....|..
gi 502628485 445 LLLDEPTRGVDVGARVEIYELI 466
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALL 468
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
49-249 |
1.03e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYqPDGGRVVVDGKPVHLGSVRDAERLGiATIHQELNLVPSMTVAEN 128
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR-AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 129 VLMGRLPSRGGFVSRRTMRRLARealdRVRLDVSLDTPVGELGIARQQLVEIAKAL-----SLN--ARVLILDEPTAALT 201
Cdd:COG4138 90 LALHQPAGASSEAVEQLLAQLAE----ALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINpeGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 202 GSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-248 |
1.42e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 28 PAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVV---DGKPVHLGSVRD 104
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 105 AERLGIAT-----IHQELNLVPSMTVaenvlmgrlpSRGGFVSRRTM----------RRLAREALDRVRLDVSL--DTPV 167
Cdd:PRK11701 81 AERRRLLRtewgfVHQHPRDGLRMQV----------SAGGNIGERLMavgarhygdiRATAGDWLERVEIDAARidDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 168 GELGIARQQLvEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGA 246
Cdd:PRK11701 151 TFSGGMQQRL-QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
..
gi 502628485 247 LV 248
Cdd:PRK11701 230 VV 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
282-501 |
1.47e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.05 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 282 DEVLLDVRGLSR----TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsavaag 357
Cdd:COG3842 2 AMPALELENVSKrygdVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 358 IGHVPEDRKGQGLV---------LdaSVAENLGYAtLaatsRAGFADRRGQRSRAQEVASRLRIRmrdvDQAAR---DLS 425
Cdd:COG3842 69 VTGLPPEKRNVGMVfqdyalfphL--TVAENVAFG-L----RMRGVPKAEIRARVAELLELVGLE----GLADRyphQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 426 GGNQQKIVFGRwVLA-GSRVLLLDEPTRGVDVGARVEIYELInavaaaggavllvSS--------------DLPEVLGVS 490
Cdd:COG3842 138 GGQQQRVALAR-ALApEPRVLLLDEPLSALDAKLREEMREEL-------------RRlqrelgitfiyvthDQEEALALA 203
|
250
....*....|.
gi 502628485 491 DRVLVMSGGRL 501
Cdd:COG3842 204 DRIAVMNDGRI 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-248 |
1.65e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVD--VLK---DITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVD--------GKPVH 98
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 99 LGSVRDAERLGIatIHQELNLVPSMTVAENVLMG---RLPSRggFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQ 175
Cdd:TIGR03269 358 DGRGRAKRYIGI--LHQEYDLYPHRTVLDNLTEAiglELPDE--LARMKAVITLKMVGFDEEKAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 176 QLVEIAKALSLNARVLILDEPTAAL----TGSETEVLFGVVEELRRddvAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMdpitKVDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
48-283 |
1.66e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.87 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHL--GSVRDAERLGIATIHQE-LNLV-PSM 123
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQDsISAVnPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 TVAENVlmgRLPSRGGF-VSRRTMRRLAREALDRVRLDVS-LDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALT 201
Cdd:PRK10419 107 TVREII---REPLRHLLsLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 202 GSETEVLFGVVEELR-RDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP--ASTHEDELVRLMVGRDITEQYPRRTH 278
Cdd:PRK10419 184 LVLQAGVIRLLKKLQqQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTFSSPAGRVLQNAVLPAFPVRRR 263
|
....*
gi 502628485 279 TPGDE 283
Cdd:PRK10419 264 TTEKV 268
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
286-467 |
1.75e-13 |
|
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: 72.70 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgSAVAAGIGHVPEdr 365
Cdd:TIGR02857 327 VSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQIAWVPQ-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 366 kgQGLVLDASVAENLGYATLAATSRAgfADRRGQRSRAQEVASRLRIRM-RDVDQAARDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:TIGR02857 404 --HPFLFAGTIAENIRLARPDASDAE--IREALERAGLDEFVAALPQGLdTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180
....*....|....*....|...
gi 502628485 445 LLLDEPTRGVDVGARVEIYELIN 467
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALR 502
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
52-248 |
2.05e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 52 ITVHVRPGRVQVLLGENGAGKSTLIKMMSGI--YQpdgGRVVVDGKPVhlgsvRDAE----RLGIATIHQELNLvPSMTV 125
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIEL-----RELDpeswRKHLSWVGQNPQL-PHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMGRlpsrggfvSRRTMRRLaREALDRV-------RLDVSLDTPVGE----LGIARQQLVEIAKALSLNARVLILD 194
Cdd:PRK11174 440 RDNVLLGN--------PDASDEQL-QQALENAwvseflpLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 195 EPTAAL-TGSETEVLFGVVEELRRDDVAMVfiSHHLEEIAAIgDEVSVLRDGALV 248
Cdd:PRK11174 511 EPTASLdAHSEQLVMQALNAASRRQTTLMV--THQLEDLAQW-DQIWVMQDGQIV 562
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
34-245 |
2.30e-13 |
|
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: 67.47 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKpvhlgsvrdaerLGIATI 113
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQelnlvpsmtvaenvLMGrlpsrggfvsrrtmrrlarealdrvrldvsldtpvGELgiARqqlVEIAKALSLNARVLIL 193
Cdd:cd03221 69 EQ--------------LSG-----------------------------------GEK--MR---LALAKLLLENPNLLLL 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 194 DEPT--------AALtgsetevlfgvVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03221 95 DEPTnhldlesiEAL-----------EEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
296-466 |
2.72e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 69.31 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRsvgsAVAA---GIGHVPEDRKgqg 369
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRR----EIPYlrrRIGVVFQDFR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 370 LVLDASVAENLGYATLAATsragfADRRGQRSRAQEVASRLRIRMRDvDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:COG2884 90 LLPDRTVYENVALPLRVTG-----KSRKEIRRRVREVLDLVGLSDKA-KALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170
....*....|....*..
gi 502628485 450 PTRGVDVGARVEIYELI 466
Cdd:COG2884 164 PTGNLDPETSWEIMELL 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
272-466 |
2.78e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 72.49 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 272 QYPRRTHTPGDEVLLDVRGLS------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRL 345
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSfrypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 346 PPRSvGSAVAAGIGHVPEDrkgqGLVLDASVAENLGYATLAATsragfadrrgqRSRAQEVASRLRI-----RMRD---- 416
Cdd:COG4987 400 RDLD-EDDLRRRIAVVPQR----PHLFDTTLRENLRLARPDAT-----------DEELWAALERVGLgdwlaALPDgldt 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 417 -VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI 466
Cdd:COG4987 464 wLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
57-462 |
2.98e-13 |
|
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: 72.12 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 57 RPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVvvDGKPV---------------HLGSVRDAErlgIATIH--QELNL 119
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPSwdevlkrfrgtelqdYFKKLANGE---IKVAHkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 120 VPSM---TVAEnvLMGRLPSRGgfvsrrtmrrLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEP 196
Cdd:COG1245 172 IPKVfkgTVRE--LLEKVDERG----------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 197 TAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVL---------------------------------- 242
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygepgvygvvskpksvrvginqyldgylpeenvr 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 243 -RDGALVAEVPASTHEDELVRLMVGRDITEQYprrthtpgDEVLLDVRGlsrtGvlhdidvQVRAGEVVGVAGLVGAGRT 321
Cdd:COG1245 320 iRDEPIEFEVHAPRREKEEETLVEYPDLTKSY--------GGFSLEVEG----G-------EIREGEVLGIVGPNGIGKT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 322 ELLRAIAGADPYDAGTVHVD------GQRLPPRSvgsavaagighvpedrkgqglvlDASVAENLgyatlaatsRAGFAD 395
Cdd:COG1245 381 TFAKILAGVLKPDEGEVDEDlkisykPQYISPDY-----------------------DGTVEEFL---------RSANTD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 396 RRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFgrwVLAGSR---VLLLDEPTRGVDVGARVEI 462
Cdd:COG1245 429 DFGSSYYKTEIIKPLGLE-KLLDKNVKDLSGGELQRVAI---AACLSRdadLYLLDEPSAHLDVEQRLAV 494
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
46-248 |
3.02e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGiatihqelnlvpsmtv 125
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIG---------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 aenVLMGR-------LPSRGGFVSRRTM----RRLAREALDRV--RLDVS--LDTPVGELGIARQQLVEIAKALSLNARV 190
Cdd:COG4586 99 ---VVFGQrsqlwwdLPAIDSFRLLKAIyripDAEYKKRLDELveLLDLGelLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 191 LILDEPTAALTgsetevlfgVV--EELR--------RDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:COG4586 176 LFLDEPTIGLD---------VVskEAIReflkeynrERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
48-228 |
3.35e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlgsvrDAERlgiATIHQELNLV------- 120
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDL---CTYQKQLCFVghrsgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 121 PSMTVAENVLMGRLPSRGGFVSRRTMRRLAREALdrvrldvsLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:PRK13540 87 PYLTLRENCLYDIHFSPGAVGITELCRLFSLEHL--------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 502628485 201 TGSETEVLFGVVEELRRDDVAMVFISHH 228
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
284-534 |
4.42e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 284 VLLDVRGLS-RTG---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPR-------- 348
Cdd:PRK13548 1 AMLEARNLSvRLGgrtLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRplaDWSPAelarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 349 -----------SVGSAVAAG-IGHVPEDRKGQGLVLDAsvaenlgyatLAATSRAGFADRRGQRsraqevasrlrirmrd 416
Cdd:PRK13548 81 lpqhsslsfpfTVEEVVAMGrAPHGLSRAEDDALVAAA----------LAQVDLAHLAGRDYPQ---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 417 vdqaardLSGGNQQKIVFGRwVLA-------GSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVllvssdlpeVLGV 489
Cdd:PRK13548 135 -------LSGGEQQRVQLAR-VLAqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLA---------VIVV 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 490 ----------SDRVLVMSGGRLTGELPAATATQDQVMAlAVKHADDDDHVAPSHG 534
Cdd:PRK13548 198 lhdlnlaaryADRIVLLHQGRLVADGTPAEVLTPETLR-RVYGADVLVQPHPETG 251
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
297-501 |
5.27e-13 |
|
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: 68.20 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVgSAVAAGIGHVPEDRKgqgLVLD 373
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAI-PYLRRKIGVVFQDFR---LLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAENLGYATlaatsRAGFADRRGQRSRAQEVASRLRIRMRDVDQAArDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRG 453
Cdd:cd03292 93 RNVYENVAFAL-----EVTGVPPREIRKRVPAALELVGLSHKHRALPA-ELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 454 VDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
32-233 |
5.73e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvRDAERLGIA 111
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 112 TIHQelnlVPSM---TVAENVLmgrLPS--RGGFVSRRTMRR-LAREALDrvrlDVSLDTPVGELGIARQQLVEIAKALS 185
Cdd:PRK10247 85 YCAQ----TPTLfgdTVYDNLI---FPWqiRNQQPDPAIFLDdLERFALP----DTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 186 LNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIA 233
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEIN 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
299-517 |
5.97e-13 |
|
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: 70.13 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 299 DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpprsVGSAvaAGIgHVPEDRKGQGLVL-DA--- 374
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL----QDSA--RGI-FLPPHRRRIGYVFqEArlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ---SVAENLGYAtlaatsrAGFADRRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPT 451
Cdd:COG4148 90 phlSVRGNLLYG-------RKRAPRAERRISFDEVVELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 452 RGVDVGARVEIYELInavaaaggAVLLVSSDLP---------EVLGVSDRVLVMSGGRLTGELPAATATQDQVMA 517
Cdd:COG4148 162 AALDLARKAEILPYL--------ERLRDELDIPilyvshsldEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
299-504 |
6.47e-13 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 68.17 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 299 DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGsaVAAGIGHVPEDRkgqglvldaSVAE 378
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE--VRRRIGIVFQDL---------SVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 379 NL-GYATLAATSRAGFADRRGQRSRAQEVASRLRIrMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVG 457
Cdd:cd03265 87 ELtGWENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502628485 458 ARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTThYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-247 |
7.26e-13 |
|
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: 71.58 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 28 PAPAPVLTLDSVSKSFGP-----VDVLkDITVHvrPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSV 102
Cdd:TIGR01257 923 PGLVPGVCVKNLVKIFEPsgrpaVDRL-NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TN 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 103 RDAERLGIATIHQELNLVPSMTVAENVLM-GRLPSRGGFVSRRTMRRLareaLDRVRLDVSLDTPVGELGIARQQLVEIA 181
Cdd:TIGR01257 998 LDAVRQSLGMCPQHNILFHHLTVAEHILFyAQLKGRSWEEAQLEMEAM----LEDTGLHHKRNEEAQDLSGGMQRKLSVA 1073
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 182 KALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDvAMVFISHHLEEIAAIGDEVSVLRDGAL 247
Cdd:TIGR01257 1074 IAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR-TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
286-504 |
7.45e-13 |
|
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: 70.94 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgSAVAAGIGHVPEdr 365
Cdd:COG4988 342 VSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-ASWRRQIAWVPQ-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 366 kgQGLVLDASVAENLGYATLAATSRAgfADRRGQRSRAQEVASRLR--IRMRdVDQAARDLSGGNQQKIVFGRWVLAGSR 443
Cdd:COG4988 419 --NPYLFAGTIRENLRLGRPDASDEE--LEAALEAAGLDEFVAALPdgLDTP-LGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 444 VLLLDEPTRGVDVGARVEIYELINavaaaggavllvssDL------------PEVLGVSDRVLVMSGGRLTGE 504
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALR--------------RLakgrtvilithrLALLAQADRILVLDDGRIVEQ 552
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
296-467 |
8.57e-13 |
|
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: 66.64 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAvaagIGHVPEDrkgqGLVL 372
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrDLDLESLRKN----IAYVPQD----PFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLgyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaardLSGGNQQKIVFGRWVLAGSRVLLLDEPTR 452
Cdd:cd03228 89 SGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170
....*....|....*
gi 502628485 453 GVDVGARVEIYELIN 467
Cdd:cd03228 126 ALDPETEALILEALR 140
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-248 |
1.20e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFG---PVD--VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVV-DGK-PVHLGSVRDAE 106
Cdd:PRK13645 7 IILDNVSYTYAkktPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAiPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 RL----GIATIHQELNLVPSmTVAENVLMGrlPSRGGFVSRRTMRRLArEALDRVRL--DVSLDTPVgELGIARQQLVEI 180
Cdd:PRK13645 87 RLrkeiGLVFQFPEYQLFQE-TIEKDIAFG--PVNLGENKQEAYKKVP-ELLKLVQLpeDYVKRSPF-ELSGGQKRRVAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 181 AKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
59-200 |
1.21e-12 |
|
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: 66.75 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 59 GRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERLGIATIHQELNLVPSMTVAENVlmgrlpsrg 138
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYLGHAPGIKTTLSVLENL--------- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 139 GFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-237 |
1.54e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.75 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG-----GRVVVDGKPVHLGSVR-DA 105
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 106 ERLGIATIHQELNLVPsMTVAENVLMGrlPSRGGFVSRRTMRRLAREALDRVRL----DVSLDTPVGELGIARQQLVEIA 181
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYG--VKIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 182 KALSLNARVLILDEPTAALTGSETEVLFGVVEELR-RDDVAMVFISHHLEEIAAIGD 237
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
294-462 |
1.73e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.43 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 294 TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGsavaagighVPEDRKGQGLVLD 373
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD---------ERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASvaeNLgYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQAAR------DLSGGNQQKIVFGRWVLAGSRVLLL 447
Cdd:PRK09493 85 QF---YL-FPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERahhypsELSGGQQQRVAIARALAVKPKLMLF 160
|
170
....*....|....*
gi 502628485 448 DEPTRGVDVGARVEI 462
Cdd:PRK09493 161 DEPTSALDPELRHEV 175
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-248 |
1.75e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 9 ASEPSGgrasgparsrTSVPAP---APVLTLDSVSKSF-----------GPVDVLKDITVHVRPGRVQVLLGENGAGKST 74
Cdd:PRK15134 258 NSEPSG----------DPVPLPepaSPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKST 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 75 ----LIKMMsgiyqPDGGRVVVDGKPVHLGSVRD--AERLGIATIHQELN--LVPSMTVAENVlmgrlpSRGGFVSRRTM 146
Cdd:PRK15134 328 tglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDPNssLNPRLNVLQII------EEGLRVHQPTL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 147 RRLAREA-LDRVRLDVSLDTPV-----GELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELR-RDD 219
Cdd:PRK15134 397 SAAQREQqVIAVMEEVGLDPETrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQ 476
|
250 260
....*....|....*....|....*....
gi 502628485 220 VAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK15134 477 LAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-251 |
1.84e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 35 TLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAERlGIATIH 114
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAER-GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 115 QELNLVPSMTVAENVLMG-RLPSrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGlKLAG----AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 194 DEP----TAALTGSETEVLFGVVEELRRddvAMVFISHHLEEIAAIGDEVSVLrDGALVAEV 251
Cdd:PRK11000 158 DEPlsnlDAALRVQMRIEISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVL-DAGRVAQV 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
40-248 |
1.87e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 40 SKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVdgKPVHLGSVRDAERLGIATIH----- 114
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSkkikn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 115 -QELNLVPSM------------TVAENVLMGrlPSRGGfVSRRTMRRLAREALDRVRLDVS-LDTPVGELGIARQQLVEI 180
Cdd:PRK13631 111 fKELRRRVSMvfqfpeyqlfkdTIEKDIMFG--PVALG-VKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 181 AKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
296-494 |
1.95e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPprsvgsAVAAGIGHVPEdrkgqglVLDAS 375
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV------AYVPQRSEVPD-------SLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAEnlgYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:NF040873 74 VRD---LVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502628485 455 DVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVL 494
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
258-524 |
2.16e-12 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 69.86 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 258 DELVRLMVGRDITEQYPRRTHTPGDevlLDVRGLS------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAD 331
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGD---IELENVSfrypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 332 PYDAGTVHVDGQ---RLPPRSVGSAvaagIGHVPEDrkgqGLVLDASVAENLGYATLAATsragfadrrgqRSRAQEVAS 408
Cdd:COG2274 526 EPTSGRILIDGIdlrQIDPASLRRQ----IGVVLQD----VFLFSGTIRENITLGDPDAT-----------DEEIIEAAR 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 409 RLRI-----RMRD-----VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINavaaaggavll 478
Cdd:COG2274 587 LAGLhdfieALPMgydtvVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR----------- 655
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 479 vssDL------------PEVLGVSDRVLVMSGGRLtgelpAATATQDQVMALAVKHAD 524
Cdd:COG2274 656 ---RLlkgrtviiiahrLSTIRLADRIIVLDKGRI-----VEDGTHEELLARKGLYAE 705
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
282-500 |
2.59e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 282 DEVLLDVRGLS-----RTGvLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAA 356
Cdd:PRK11701 3 DQPLLSVRGLTklygpRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 357 GI--------GHVPEDRKgQGLVLDASVAENLGYATLAATSRagfadRRGQ-RSRAQEVASRLRIRMRDVDQAARDLSGG 427
Cdd:PRK11701 82 ERrrllrtewGFVHQHPR-DGLRMQVSAGGNIGERLMAVGAR-----HYGDiRATAGDWLERVEIDAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
296-467 |
2.70e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.93 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGqrLPPRSV-GSAVAAGIGHVPEDRKgqglVLDA 374
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLdQDEVRRRVSVCAQDAH----LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAENLGYA--------TLAATSRAGFADrrgqrsraqEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLL 446
Cdd:TIGR02868 424 TVRENLRLArpdatdeeLWAALERVGLAD---------WLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL 494
|
170 180
....*....|....*....|.
gi 502628485 447 LDEPTRGVDVGARVEIYELIN 467
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLL 515
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-253 |
2.75e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 43 FGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQ--PDG---GRVVVDGKPVHLGSVRDAE-RLGIATIHQE 116
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPIEvRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 117 LNLVPSMTVAENVLMGrLPSRGGFVSRRTMRRLAREALDRVRL-----DVSLDTPVGELGIARQQLVeIAKALSLNARVL 191
Cdd:PRK14267 94 PNPFPHLTIYDNVAIG-VKLNGLVKSKKELDERVEWALKKAALwdevkDRLNDYPSNLSGGQRQRLV-IARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 192 ILDEPTAALTGSETEVLFGVVEELrRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPA 253
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-249 |
2.76e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 28 PAPAPVLTLDSVSKSF--GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSvRDA 105
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 106 ERLGIATIHQELNLVpSMTVAENVLMGRlpsrggfvSRRTMRRLArEALDRVRL------DVSLDTPVGELGiarQQL-- 177
Cdd:PRK11160 412 LRQAISVVSQRVHLF-SATLRDNLLLAA--------PNASDEALI-EVLQQVGLeklledDKGLNAWLGEGG---RQLsg 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 178 -----VEIAKALSLNARVLILDEPTAALTgSETE--VLFGVVEELRrdDVAMVFISHHLEEIAAIgDEVSVLRDGALVA 249
Cdd:PRK11160 479 geqrrLGIARALLHDAPLLLLDEPTEGLD-AETErqILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
56-249 |
2.92e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 56 VRPGRVQVLLGENGAGKSTLIKMMSGIYqPDGGRVVVDGKPVHLGSVRDAERLGiATIHQELNLVPSMTVAENVLMGRLP 135
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 136 SRGGFVSRRTMRRLARealdRVRLDVSLDTPVGELGIARQQLVEIA-------KALSLNARVLILDEPTAALTGSETEVL 208
Cdd:PRK03695 97 KTRTEAVASALNEVAE----ALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502628485 209 FGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-231 |
4.22e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 22 RSRTSVPAPAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYqPDG--------GRVVVD 93
Cdd:PRK10938 249 SARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGysndltlfGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 94 GKPV-----HLGSVRdaerlgiATIHQELNLvpSMTVAENVLMGRLPSRGGF--VSRRtMRRLAREALDRVRLDVSL-DT 165
Cdd:PRK10938 328 GETIwdikkHIGYVS-------SSLHLDYRV--STSVRNVILSGFFDSIGIYqaVSDR-QQKLAQQWLDILGIDKRTaDA 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 166 PVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEE 231
Cdd:PRK10938 398 PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLFVSHHAED 464
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
285-515 |
5.36e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLS-RTGVL---HDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvGSAVAagigh 360
Cdd:PRK11300 5 LLSVSGLMmRFGGLlavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 vpedRKG-----QGLVL--DASVAENLgyatLAATSR---AGF--------ADRRGQRSRAQEVASRL-RIRMRDV-DQA 420
Cdd:PRK11300 79 ----RMGvvrtfQHVRLfrEMTVIENL----LVAQHQqlkTGLfsgllktpAFRRAESEALDRAATWLeRVGLLEHaNRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 421 ARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAA-GGAVLLVSSDLPEVLGVSDRVLVMSGG 499
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250
....*....|....*.
gi 502628485 500 RltgelPAATATQDQV 515
Cdd:PRK11300 231 T-----PLANGTPEEI 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
280-506 |
5.84e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 65.88 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 280 PGDEVLLDVRGLSRT-----G---VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvg 351
Cdd:COG1116 2 SAAAPALELRGVSKRfptggGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 352 savaAGIGHVPEDrkgqglvlDA-----SVAENLGYATlaatsRAGFADRRGQRSRAQEVasrlrIRMRDVDQAA----R 422
Cdd:COG1116 80 ----PDRGVVFQE--------PAllpwlTVLDNVALGL-----ELRGVPKAERRERAREL-----LELVGLAGFEdaypH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 423 DLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELInavaaAGGAVLLVSS------DLPEVLGVSDRVLVM 496
Cdd:COG1116 138 QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDEL-----LRLWQETGKTvlfvthDVDEAVFLADRVVVL 212
|
250
....*....|..
gi 502628485 497 SG--GRLTGELP 506
Cdd:COG1116 213 SArpGRIVEEID 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
46-254 |
6.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATIHQELNLVPSMTV 125
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMGrLPSRGgfVSRRTMRRLAREALDRVR-LDVSLDTPvGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSE 204
Cdd:PRK13642 100 EDDVAFG-MENQG--IPREEMIKRVDEALLAVNmLDFKTREP-ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 205 TEVLFGVVEELR-RDDVAMVFISHHLEEiAAIGDEVSVLRDGALVAEVPAS 254
Cdd:PRK13642 176 RQEIMRVIHEIKeKYQLTVLSITHDLDE-AASSDRILVMKAGEIIKEAAPS 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
283-500 |
6.16e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.53 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLSRTGVLH-----------DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ-------R 344
Cdd:COG4778 2 TTLLEVENLSKTFTLHlqggkrlpvldGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 345 LPPRSVGSAVAAGIGHVpedrkGQGLV-------LDAsVAENLgyatlaatsRAGFADRRGQRSRAQEVASRLRIRMRDV 417
Cdd:COG4778 82 ASPREILALRRRTIGYV-----SQFLRviprvsaLDV-VAEPL---------LERGVDREEARARARELLARLNLPERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 418 DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMS 497
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 502628485 498 GGR 500
Cdd:COG4778 227 PFS 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
296-451 |
7.28e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPP--RsvgsavAAGIGHVPEDRKgQGL 370
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtKLPEykR------AKYIGRVFQDPM-MGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 371 VLDASVAENLGYATLAATSRA-GFADRRGQRSRAQEVASRLRI----RMrdvDQAARDLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:COG1101 94 APSMTIEENLALAYRRGKRRGlRRGLTKKRRELFRELLATLGLglenRL---DTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
....*.
gi 502628485 446 LLDEPT 451
Cdd:COG1101 171 LLDEHT 176
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
299-465 |
7.69e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 299 DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpprsvgsavaagiGHVPEDRKGQGLVLDA---- 374
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-------------NDVPPAERGVGMVFQSyaly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ---SVAENLGYA-TLAATSRAGFADRRGQRSRAQEVASRLrirmrdvDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK11000 88 phlSVAENMSFGlKLAGAKKEEINQRVNQVAEVLQLAHLL-------DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170
....*....|....*....
gi 502628485 451 TRGVD----VGARVEIYEL 465
Cdd:PRK11000 161 LSNLDaalrVQMRIEISRL 179
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
56-241 |
7.70e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.51 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 56 VRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVvvdgkpvhlgsvrDAERLGIATIHQELNLVPSMTVaENVLMGRLP 135
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------------EIELDTVSYKPQYIKADYEGTV-RDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 136 SRGGFVSRRTmrrlarEALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTgSETEVLfgVVEEL 215
Cdd:cd03237 88 DFYTHPYFKT------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-VEQRLM--ASKVI 158
|
170 180 190
....*....|....*....|....*....|.
gi 502628485 216 RR-----DDVAMVfISHHLEEIAAIGDEVSV 241
Cdd:cd03237 159 RRfaennEKTAFV-VEHDIIMIDYLADRLIV 188
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
296-451 |
8.37e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.02 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgsavaagigHVPEDRKGQGLVL--- 372
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK---------DINKLRRKVGMVFqqf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 ----DASVAENLgyaTLAATSRagfadRRGQRSRAQEVASRL--RIRMRD-VDQAARDLSGGNQQKIVFGRwVLAGS-RV 444
Cdd:COG1126 87 nlfpHLTVLENV---TLAPIKV-----KKMSKAEAEERAMELleRVGLADkADAYPAQLSGGQQQRVAIAR-ALAMEpKV 157
|
....*..
gi 502628485 445 LLLDEPT 451
Cdd:COG1126 158 MLFDEPT 164
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
49-248 |
9.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV-------HLGSVRdaERLGIATIHQELNLVP 121
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnkNLKKLR--KKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 122 SmTVAENVLMGrlPSRGGFvSRRTMRRLAREALDRVRLDVSL--DTPVgELGIARQQLVEIAKALSLNARVLILDEPTAA 199
Cdd:PRK13641 101 N-TVLKDVEFG--PKNFGF-SEDEAKEKALKWLKKVGLSEDLisKSPF-ELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 200 LTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
285-508 |
9.08e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 65.60 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLS---RTG----------VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPP--RS 349
Cdd:TIGR02769 2 LLEVRDVThtyRTGglfgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 350 VGSAVAAGIGHVPEDRKGQ---GLVLDASVAENLGYATLAATSRagfadrrgQRSRAQEVASRLRIRMRDVDQAARDLSG 426
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAvnpRMTVRQIIGEPLRHLTSLDESE--------QKARIAELLDMVGLRSEDADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 427 GNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAV-LLVSSDLPEVLGVSDRVLVMSGGRLTGEL 505
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
...
gi 502628485 506 PAA 508
Cdd:TIGR02769 234 DVA 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
286-515 |
1.10e-11 |
|
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: 64.90 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT-----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLP--PRSVGSAVAAGI 358
Cdd:cd03256 1 IEVENLSKTypngkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 359 GHVPEDrkgQGLVLDASVAENLGYATLAATS--RAGF-----ADRRGQRSRAQEV--ASRLRIRmrdVDQaardLSGGNQ 429
Cdd:cd03256 81 GMIFQQ---FNLIERLSVLENVLSGRLGRRStwRSLFglfpkEEKQRALAALERVglLDKAYQR---ADQ----LSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 430 QKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEV-LGVSDRVLVMSGGRLTGELPAA 508
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPA 230
|
....*..
gi 502628485 509 TATQDQV 515
Cdd:cd03256 231 ELTDEVL 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
267-502 |
1.16e-11 |
|
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: 64.66 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 267 RDITEQYPRRTHTPGdeVLLDVRGLSRTG-----VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVD 341
Cdd:cd03267 4 SNLSKSYRVYSKEPG--LIGSLKSLFKRKyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 342 GQRlpPRSVGSAVAAGIGHVPEDRkgQGLVLDASVAEnlGYATLAATSRagfADRRGQRSRAQEVASRLRIRmRDVDQAA 421
Cdd:cd03267 82 GLV--PWKRRKKFLRRIGVVFGQK--TQLWWDLPVID--SFYLLAAIYD---LPPARFKKRLDELSELLDLE-ELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 422 RDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVMSGGR 500
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTShYMKDIEALARRVLVIDKGR 231
|
..
gi 502628485 501 LT 502
Cdd:cd03267 232 LL 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
296-501 |
1.65e-11 |
|
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: 63.00 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLppRSVG-SAVAAGIGHVPEDRKgqglVLDA 374
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI--SQWDpNELGDHVGYLPQDDE----LFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAENLgyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaardLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:cd03246 91 SIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502628485 455 DVGARVEIYELINAVAAAGGAVLLVSSDlPEVLGVSDRVLVMSGGRL 501
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
47-248 |
1.91e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.66 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 47 DVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVR-DAERLGIATIHQELNLVpSMTV 125
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT--KLQlDSWRSRLAVVSQTPFLF-SDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMGRlPSrggfVSRRTMRRLAREAL---DRVRLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:PRK10789 406 ANNIALGR-PD----ATQQEIEHVARLASvhdDILRLPQGYDTEVGERGVmlsgGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502628485 199 ALTG-SETEVLfgvvEELRR-DDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK10789 481 AVDGrTEHQIL----HNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
284-504 |
1.92e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 284 VLLDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgSAVAAGIG 359
Cdd:PRK13536 40 VAIDLAGVSKSygdkAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 360 HVPE-DRkgqgLVLDASVAENLgyatlaatsrAGFADRRGQRSRAQEVA-------SRLRirmRDVDQAARDLSGGNQQK 431
Cdd:PRK13536 118 VVPQfDN----LDLEFTVRENL----------LVFGRYFGMSTREIEAVipsllefARLE---SKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 432 IVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
48-248 |
2.05e-11 |
|
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: 63.67 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPG-RVQVlLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKP---VHLGSVRDAerlgIATIHQELNLVpSM 123
Cdd:cd03244 19 VLKNISFSIKPGeKVGI-VGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskIGLHDLRSR----ISIIPQDPVLF-SG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 124 TVAENVlmgrlpsrgGFVSRRTMRRLaREALDRVRLD-------VSLDTPVGE----LGIARQQLVEIAKALSLNARVLI 192
Cdd:cd03244 93 TIRSNL---------DPFGEYSDEEL-WQALERVGLKefveslpGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 193 LDEPTAALTgSETEVLfgVVEELRR--DDVAMVFISHHLEEIAAIgDEVSVLRDGALV 248
Cdd:cd03244 163 LDEATASVD-PETDAL--IQKTIREafKDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
286-466 |
2.43e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGL-----SRTgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPP--RSvgsavA 355
Cdd:COG1137 4 LEAENLvksygKRT-VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEditHLPMhkRA-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 356 AGIGHVPED----RKgqgLvldaSVAENLgYATLAATSRagfaDRRGQRSRAQEVASRLRI-RMRdvDQAARDLSGGNQQ 430
Cdd:COG1137 78 LGIGYLPQEasifRK---L----TVEDNI-LAVLELRKL----SKKEREERLEELLEEFGItHLR--KSKAYSLSGGERR 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 502628485 431 KIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI 466
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAVADIQKII 179
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
300-500 |
2.71e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.62 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 300 IDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgsavaagighvPEDRKGQGLVLDA----- 374
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------------PAERPVSMLFQENnlfph 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 -SVAENLGYATlaatsRAGFADRRGQRSRAQEVASRLRIrmrdVDQAAR---DLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:COG3840 86 lTVAQNIGLGL-----RPGLKLTAEQRAQVEQALERVGL----AGLLDRlpgQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 451 TRGVDVGARVEIYELINAVAAAGGAVL-LVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVlMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-504 |
3.11e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 280 PGDEVLLDVRGLSR----TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVA 355
Cdd:PRK13537 2 PMSVAPIDFRNVEKrygdKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 356 AGIghVPEdrkGQGLVLDASVAENL----GYATLAATSragfadrrgQRSRAQEVASRLRIRMRdVDQAARDLSGGNQQK 431
Cdd:PRK13537 82 VGV--VPQ---FDNLDPDFTVRENLlvfgRYFGLSAAA---------ARALVPPLLEFAKLENK-ADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 432 IVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
47-200 |
4.72e-11 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 62.18 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 47 DVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSG--IYQPDGGRVVVDGKPVHLGSVRDAerlgIATIHQELNLVPSMT 124
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 125 VAENVLM-GRLpsRGgfVSRRTMRRLArealdrvrldvsldtpvgelgiarqqlveIAKALSLNARVLILDEPTAAL 200
Cdd:cd03213 99 VRETLMFaAKL--RG--LSGGERKRVS-----------------------------IALELVSNPSLLFLDEPTSGL 142
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
296-467 |
4.75e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAagighVPEDRKGQGLVLDA- 374
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA-----IRLLRQKVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ------SVAENLgyatLAATSRAGFADRRGQRSRAQEVASRLRIRmrdvDQAAR---DLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:COG4161 92 nlwphlTVMENL----IEAPCKVLGLSKEQAREKAMKLLARLRLT----DKADRfplHLSGGQQQRVAIARALMMEPQVL 163
|
170 180
....*....|....*....|..
gi 502628485 446 LLDEPTRGVDVGARVEIYELIN 467
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIR 185
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
282-501 |
6.26e-11 |
|
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: 62.69 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 282 DEVLLDVRGLS-----RTgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRlpprsvgsavaa 356
Cdd:COG1127 2 SEPMIEVRNLTksfgdRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 357 gIGHVPED-----RKGQGLV------LDA-SVAENLGYATLAATsragfadrRGQRSRAQEVAsRLRIRMRDVDQAAR-- 422
Cdd:COG1127 69 -ITGLSEKelyelRRRIGMLfqggalFDSlTVFENVAFPLREHT--------DLSEAEIRELV-LEKLELVGLPGAADkm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 423 --DLSGGnQQKivfgRWVLAgsR-------VLLLDEPTRGVD-VGARVeIYELINavaaAGGAVLLVSS-----DLPEVL 487
Cdd:COG1127 139 psELSGG-MRK----RVALA--RalaldpeILLYDEPTAGLDpITSAV-IDELIR----ELRDELGLTSvvvthDLDSAF 206
|
250
....*....|....
gi 502628485 488 GVSDRVLVMSGGRL 501
Cdd:COG1127 207 AIADRVAVLADGKI 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
296-501 |
6.86e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgsavaagighvpEDR------KGQG 369
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI------------QQRdicmvfQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 370 LVLDASVAENLGYAtLAATSRAgfADRRGQRSR-AQEVASRLRIRMRDVDQaardLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:PRK11432 89 LFPHMSLGENVGYG-LKMLGVP--KEERKQRVKeALELVDLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 449 EPTRGVDVGARVEIYELINAVAAAGGAVLL-VSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLyVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
296-455 |
9.27e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.42 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAvaagIGHVPEDrkgqGLVL 372
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirDLTLESLRRQ----IGVVPQD----TFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLGYATLAATsragfadrrgqRSRAQEVASRLRI-----RMRD-----VDQAARDLSGGNQQKIVFGRWVLAGS 442
Cdd:COG1132 427 SGTIRENIRYGRPDAT-----------DEEVEEAAKAAQAhefieALPDgydtvVGERGVNLSGGQRQRIAIARALLKDP 495
|
170
....*....|...
gi 502628485 443 RVLLLDEPTRGVD 455
Cdd:COG1132 496 PILILDEATSALD 508
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
49-255 |
9.41e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgsvRDAERLGIATIHQ--ELNLVPSMTVA 126
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQseEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 127 ENVLMGRLpSRGGFVSRRTM--RRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSE 204
Cdd:PRK15056 99 DVVMMGRY-GHMGWLRRAKKrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 205 TEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDeVSVLRDGALVAEVPAST 255
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTET 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
286-456 |
9.91e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.22 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGL--SRTG--VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPP-RSVGSAVAAGIGH 360
Cdd:TIGR01189 1 LAARNLacSRGErmLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 VPedrkgqGLVLDASVAENLGY--ATLAATSRAGFA--DRRGQRSRAqevasrlrirmrdvDQAARDLSGGNQQKIVFGR 436
Cdd:TIGR01189 81 LP------GLKPELSALENLHFwaAIHGGAQRTIEDalAAVGLTGFE--------------DLPAAQLSAGQQRRLALAR 140
|
170 180
....*....|....*....|
gi 502628485 437 WVLAGSRVLLLDEPTRGVDV 456
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDK 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
286-528 |
1.00e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYdAGTVHVDGQrlpprSVGSAVAAGIGHvpedR 365
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQ-----PLEAWSAAELAR----H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 366 KGQgLVLDASVAENLG---YATLaatSRAGFADRRGQRSRAQEVASRLRIRM---RDVDQaardLSGGNQQkivfgRWVL 439
Cdd:PRK03695 71 RAY-LSQQQTPPFAMPvfqYLTL---HQPDKTRTEAVASALNEVAEALGLDDklgRSVNQ----LSGGEWQ-----RVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 440 AG------------SRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTgelpa 507
Cdd:PRK03695 138 AAvvlqvwpdinpaGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL----- 212
|
250 260 270
....*....|....*....|....*....|
gi 502628485 508 ATATQDQVM---------ALAVKHADDDDH 528
Cdd:PRK03695 213 ASGRRDEVLtpenlaqvfGVNFRRLDVEGH 242
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
296-498 |
1.05e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlpprsvgsavaAGIGHVPedrkgQGLVLDAs 375
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRIGYVP-----QKLYLDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 vaenlgyaTLAAT-SRagFADRRGQRSRAQEVASRLRIRMRD-VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRG 453
Cdd:PRK09544 81 --------TLPLTvNR--FLRLRPGTKKEDILPALKRVQAGHlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502628485 454 VDVGARVEIYELINAVAAAGG-AVLLVSSDLPEVLGVSDRVLVMSG 498
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
64-249 |
1.07e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 64 LLGENGAGKSTLIKMMSGIYQPDGGRVVVDGK---PVHLGSVRDAERLGIATIHQELNLVPSMTVAENVLMGrlpsrggf 140
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 141 vsrrtMRRLAREALDRVrldVSLdtpvgeLGI-------------ARQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:PRK11144 101 -----MAKSMVAQFDKI---VAL------LGIeplldrypgslsgGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502628485 208 LFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK11144 167 LLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
56-460 |
1.12e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 56 VRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRvvVDGKPV---------------HLGSVRDAErlgIATIH--QELN 118
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSwdevlkrfrgtelqnYFKKLYNGE---IKVVHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 119 LVPSM---TVAEnvLMGRLPSRGGFvsrrtmrrlaREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDE 195
Cdd:PRK13409 171 LIPKVfkgKVRE--LLKKVDERGKL----------DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 196 PTAALTGSETEVLFGVVEELRRDDVAMVfISHHLEEIAAIGDEVSVL--------------------------------- 242
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEGKYVLV-VEHDLAVLDYLADNVHIAygepgaygvvskpkgvrvgineylkgylpeenm 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 243 --RDGALVAEVPASTHEDELVRLMVGRDITEQYprrthtpgDEVLLDVRGlsrtGvlhdidvQVRAGEVVGVAGLVGAGR 320
Cdd:PRK13409 318 riRPEPIEFEERPPRDESERETLVEYPDLTKKL--------GDFSLEVEG----G-------EIYEGEVIGIVGPNGIGK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 321 TELLRAIAGADPYDAGTVHVD------GQRLPPRSVGSaVAAGIGHVPEDrkgqglvLDASVAENlgyatlaatsragfa 394
Cdd:PRK13409 379 TTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGT-VEDLLRSITDD-------LGSSYYKS--------------- 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 395 drrgqrsraqEVASRLRIrMRDVDQAARDLSGGNQQKIVFgrwVLAGSR---VLLLDEPTRGVDVGARV 460
Cdd:PRK13409 436 ----------EIIKPLQL-ERLLDKNVKDLSGGELQRVAI---AACLSRdadLYLLDEPSAHLDVEQRL 490
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
311-502 |
1.29e-10 |
|
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: 61.05 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 311 GVAGLVG---AGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAVAAGIGHVPEDrkgQGLVLDASVAENLGYATLAa 387
Cdd:cd03264 26 GMYGLLGpngAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKLRRRIGYLPQE---FGVYPNFTVREFLDYIAWL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 388 tsrAGFADRRgQRSRAQEVASRLRIRMRdVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELIn 467
Cdd:cd03264 100 ---KGIPSKE-VKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL- 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 502628485 468 aVAAAGGAVLLVSSDLPE-VLGVSDRVLVMSGGRLT 502
Cdd:cd03264 174 -SELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
296-504 |
1.71e-10 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 61.06 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAgighvpedRKGQGLV---- 371
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA--------RRRIGMIfqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 372 --LDA-SVAENLGYA-TLAATSRAgfadrrgqrsraqEVASRLRIRMRDVDQAAR------DLSGGNQQKIVFGRWVLAG 441
Cdd:cd03258 92 nlLSSrTVFENVALPlEIAGVPKA-------------EIEERVLELLELVGLEDKadaypaQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 442 SRVLLLDEPTRGVDVGARVEIYELInavaaaggavllvsSDLPEVLGVS---------------DRVLVMSGGRLTGE 504
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALL--------------RDINRELGLTivlithemevvkricDRVAVMEKGEVVEE 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
258-466 |
1.74e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 258 DELVRLMVGRDITEQYPRRTHTPGDEVLlDVRGLS------RTgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAD 331
Cdd:COG4178 336 AGFEEALEAADALPEAASRIETSEDGAL-ALEDLTlrtpdgRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 332 PYDAGTVHV-DGQR---------LPPRSVGSAVA--AGIGHVPEDRkgqglVLDASVAENLGYatlaatsragfadrrgq 399
Cdd:COG4178 414 PYGSGRIARpAGARvlflpqrpyLPLGTLREALLypATAEAFSDAE-----LREALEAVGLGH----------------- 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 400 rsraqevasrLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI 466
Cdd:COG4178 472 ----------LAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL 528
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
293-499 |
1.89e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 293 RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPR-----------------SVGS 352
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARdrkvgfvfqhyalfrhmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 353 AVAAGIGHVPEDRKGQGLVLDASVAENLGYATLAatsragfadRRGQRSRAQevasrlrirmrdvdqaardLSGGNQQKI 432
Cdd:PRK10851 94 NIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLA---------HLADRYPAQ-------------------LSGGQKQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 433 VFGRWVLAGSRVLLLDEPTRGVDVGARVEIYE-LINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGG 499
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRwLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
42-246 |
2.00e-10 |
|
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: 60.81 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 42 SFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAE---RLGIATIHQEL 117
Cdd:cd03290 9 SWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 118 NLVpSMTVAENVLMGrlpsrGGFVSRRTmrrlaREALDRVRLDVSLD-------TPVGELGI----ARQQLVEIAKALSL 186
Cdd:cd03290 89 WLL-NATVEENITFG-----SPFNKQRY-----KAVTDACSLQPDIDllpfgdqTEIGERGInlsgGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 187 NARVLILDEPTAALTGSETEVLF--GVVEELRRDDVAMVFISHHLEEIAAiGDEVSVLRDGA 246
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
289-455 |
3.30e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 59.49 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 289 RGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAG--ADPYDAGTVHVDGQRLPPRSVGSAvaagIGHVPEDrk 366
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 367 gqgLVLDAS--VAENLGYAtlaatsragfADRRGqrsraqevasrlrirmrdvdqaardLSGGNQQKIVFGRWVLAGSRV 444
Cdd:cd03213 91 ---DILHPTltVRETLMFA----------AKLRG-------------------------LSGGERKRVSIALELVSNPSL 132
|
170
....*....|.
gi 502628485 445 LLLDEPTRGVD 455
Cdd:cd03213 133 LFLDEPTSGLD 143
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
296-467 |
4.28e-10 |
|
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: 60.10 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAD-PYDAGTVHVDGQRLpprsvgsavaaGIGHVPEDRKGQGLVlDA 374
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERR-----------GGEDVWELRKRIGLV-SP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAENL-GYATLAATSRAGFADRRG--------QRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:COG1119 86 ALQLRFpRDETVLDVVLSGFFDSIGlyreptdeQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180
....*....|....*....|..
gi 502628485 446 LLDEPTRGVDVGARVEIYELIN 467
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLD 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
297-500 |
4.59e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgsavaagigHVPEDRKGQGLVL---D 373
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV---------KLSDIRKKVGLVFqypE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAENLGYATLA-ATSRAGFADrrgqrsraQEVASRLRIRMRDV--------DQAARDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:PRK13637 94 YQLFEETIEKDIAfGPINLGLSE--------EEIENRVKRAMNIVgldyedykDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 445 LLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
34-196 |
4.91e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.40 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSF-GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVhlGSVRDAERlGIAT 112
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEPADR-DIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQELNLVPSMTVAENVLMGrLPSRGgfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLI 192
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYG-LKIRG--MPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
....
gi 502628485 193 LDEP 196
Cdd:PRK11650 158 FDEP 161
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-197 |
5.21e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVdGKPVHLGSV---RDAerlg 109
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAYVdqsRDA---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 iatihqelnLVPSMTVAENV-------LMGR--LPSRgGFVSRRTMRrlareALDRVRldvsldtPVGEL-GIARQQlVE 179
Cdd:PRK11819 399 ---------LDPNKTVWEEIsggldiiKVGNreIPSR-AYVGRFNFK-----GGDQQK-------KVGVLsGGERNR-LH 455
|
170
....*....|....*...
gi 502628485 180 IAKALSLNARVLILDEPT 197
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPT 473
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
296-466 |
6.00e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.10 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpprsvgSAVAAGIGHVPEDrkgQGLVLDAS 375
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAERGVVFQN---EGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYA-TLAATSRAgfadrrGQRSRAQEVASRLrirmrDVDQAAR----DLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK11248 87 VQDNVAFGlQLAGVEKM------QRLEIAHQMLKKV-----GLEGAEKryiwQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170
....*....|....*.
gi 502628485 451 TRGVDVGARVEIYELI 466
Cdd:PRK11248 156 FGALDAFTREQMQTLL 171
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
296-466 |
6.33e-10 |
|
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: 58.48 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVGSAVAAGIGHVPEdrkgQGLVLDAS 375
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV--PVSDLEKALSSLISVLNQ----RPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaaRDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:cd03247 91 LRNNLG----------------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170
....*....|.
gi 502628485 456 VGARVEIYELI 466
Cdd:cd03247 131 PITERQLLSLI 141
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
296-455 |
8.74e-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: 58.82 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDA---GTVHVDGQRLPPRSVGSAVAagigHVPEDRKgqgLVL 372
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKCVA----YVRQDDI---LLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLGYatlAATSRAGFADRRGQRSRAQEVASRLRIRMRDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPT 451
Cdd:cd03234 95 GLTVRETLTY---TAILRLPRKSSDAIRKKRVEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
....
gi 502628485 452 RGVD 455
Cdd:cd03234 172 SGLD 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-227 |
9.50e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGK----------PVHL-GSV 102
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpPRNVeGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 103 RD--AErlGIATI-------HQELNLVPSMTVAENV-----LMGRLPSRGG--FVSRrtmrrlAREALDRVRLDVslDTP 166
Cdd:PRK11147 84 YDfvAE--GIEEQaeylkryHDISHLVETDPSEKNLnelakLQEQLDHHNLwqLENR------INEVLAQLGLDP--DAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 167 VGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRddvAMVFISH 227
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISH 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
33-254 |
9.98e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFG----PVDVLKDITVHVRPGRVQVLLGENGAGKS-TLIKMMSGIYQPdgGRVVVDG---KPVHLGSVRD 104
Cdd:PRK11022 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKlefNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 105 AER---LG--IATIHQE--LNLVPSMTVAENVLMGRLPSRGGfvSRRTMRRLAREALDRV-------RLDVSLDtpvgEL 170
Cdd:PRK11022 81 KERrnlVGaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVgipdpasRLDVYPH----QL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 171 GIARQQLVEIAKALSLNARVLILDEPTAALTGS-ETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVA 249
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
....*
gi 502628485 250 EVPAS 254
Cdd:PRK11022 235 TGKAH 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
286-509 |
1.20e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.99 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHV-----DGQRlpprsvgsAVAA 356
Cdd:PRK11264 4 IEVKNLVKKfhgqTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTAR--------SLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 357 GIGHVPEDRKGQGLVLDA-------SVAENL--GYATLAATSRAGFAdrrgqrSRAQEVASRLRIRMRDvDQAARDLSGG 427
Cdd:PRK11264 76 QKGLIRQLRQHVGFVFQNfnlfphrTVLENIieGPVIVKGEPKEEAT------ARARELLAKVGLAGKE-TSYPRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPA 507
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
..
gi 502628485 508 AT 509
Cdd:PRK11264 229 KA 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
296-455 |
1.20e-09 |
|
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: 58.78 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSaVAAGIGHVPEDRkgqgLVLDAS 375
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDV----FLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYATLAATSRAgfADRRGQRSRAQEVASRL------RIRMRDVDqaardLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:cd03251 92 VAENIAYGRPGATREE--VEEAARAANAHEFIMELpegydtVIGERGVK-----LSGGQRQRIAIARALLKDPPILILDE 164
|
....*.
gi 502628485 450 PTRGVD 455
Cdd:cd03251 165 ATSALD 170
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
44-97 |
1.32e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 1.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 44 GPVDVlkditvHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPV 97
Cdd:COG4615 349 GPIDL------TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
297-465 |
1.72e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.88 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDA---GTVHVDGQRlpprsvgsavaagIGHVPEDRKGQGLVL- 372
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRR-------------LTALPAEQRRIGILFq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DA------SVAENLGYATLAATSRAgfaDRRGQRSRAQEVASRLRIRMRDVDQaardLSGGNQQKIVFGRWVLAGSRVLL 446
Cdd:COG4136 84 DDllfphlSVGENLAFALPPTIGRA---QRRARVEQALEEAGLAGFADRDPAT----LSGGQRARVALLRALLAEPRALL 156
|
170
....*....|....*....
gi 502628485 447 LDEPTRGVDVGARVEIYEL 465
Cdd:COG4136 157 LDEPFSKLDAALRAQFREF 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
308-501 |
1.85e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 308 EVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLppRSVGSAVAAGIGHVPEDRKgqgLVLDASVAEN-LGYATLa 386
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNI---LFHHLTVAEHiLFYAQL- 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 387 atsragfadrrgqRSRAQEVAS-RLRIRMRDV------DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGAR 459
Cdd:TIGR01257 1031 -------------KGRSWEEAQlEMEAMLEDTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502628485 460 VEIYE-LINAVAAAGGAVLLVSSDLPEVLGvsDRVLVMSGGRL 501
Cdd:TIGR01257 1098 RSIWDlLLKYRSGRTIIMSTHHMDEADLLG--DRIAIISQGRL 1138
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-459 |
2.05e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpvhlGSVRDA---ERLG 109
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG-----GDMADArhrRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 110 --IATIHQEL--NLVPSMTVAENV-LMGRLPSRGGFVSRRTMRRLareaLDRVRLDVSLDTPVGEL-GIARQQLvEIAKA 183
Cdd:NF033858 76 prIAYMPQGLgkNLYPTLSVFENLdFFGRLFGQDAAERRRRIDEL----LRATGLAPFADRPAGKLsGGMKQKL-GLCCA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 184 LSLNARVLILDEPTAaltgsetevlfGV-----------VEELRRDDVAM-VFIS-HHLEE------IAAIgDEVSVLRD 244
Cdd:NF033858 151 LIHDPDLLILDEPTT-----------GVdplsrrqfwelIDRIRAERPGMsVLVAtAYMEEaerfdwLVAM-DAGRVLAT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 245 G---ALVAEVPASTHEDELVRLMvGRDITEQY-----PRRTHTPGDEVLLDVRGLSR-----TGVLHdIDVQVRAGEVVG 311
Cdd:NF033858 219 GtpaELLARTGADTLEAAFIALL-PEEKRRGHqpvviPPRPADDDDEPAIEARGLTMrfgdfTAVDH-VSFRIRRGEIFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 312 VAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVgsavaagighvpEDRKGQG-------LVLDASVAENLG-YA 383
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI------------ATRRRVGymsqafsLYGELTVRQNLElHA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 384 TLaatsragF---ADRRGQrsRAQEVASRLRIrmRDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGAR 459
Cdd:NF033858 365 RL-------FhlpAAEIAA--RVAEMLERFDL--ADVaDALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-200 |
2.12e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 15 GRASGPARSRTSVPAPAPVLTLDSVSKSfgpvdVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGiYQPDG----GRV 90
Cdd:TIGR00955 12 GRVAQDGSWKQLVSRLRGCFCRERPRKH-----LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 91 VVDGKPVHlgsvRDAERLGIATIHQELNLVPSMTVAENVL---MGRLPsrggfvsRRTMRRLAREALDRVRLDVSL---- 163
Cdd:TIGR00955 86 LLNGMPID----AKEMRAISAYVQQDDLFIPTLTVREHLMfqaHLRMP-------RRVTKKEKRERVDEVLQALGLrkca 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502628485 164 DTPVGELGIAR------QQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:TIGR00955 155 NTRIGVPGRVKglsggeRKRLAFASELLTDPPLLFCDEPTSGL 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
297-456 |
2.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDG-------QRLPPR----SVGSAVAAGIGHVPEDR 365
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlQQDPPRnvegTVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 366 KGQGLVLDaSVAENLGYATLAatsragfadrrgQRSRAQEV-----ASRLRIRMRDV--------DQAARDLSGGNQQKI 432
Cdd:PRK11147 99 KRYHDISH-LVETDPSEKNLN------------ELAKLQEQldhhnLWQLENRINEVlaqlgldpDAALSSLSGGWLRKA 165
|
170 180
....*....|....*....|....
gi 502628485 433 VFGRWVLAGSRVLLLDEPTRGVDV 456
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
296-455 |
3.31e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.72 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgsavAAGIGHVPEDRKGQGLVLDA- 374
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSK-----TPSDKAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ------SVAENLgyatLAATSRAGFADRRGQRSRAQEVASRLRIRmrdvDQAAR---DLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:PRK11124 92 nlwphlTVQQNL----IEAPCRVLGLSKDQALARAEKLLERLRLK----PYADRfplHLSGGQQQRVAIARALMMEPQVL 163
|
170
....*....|
gi 502628485 446 LLDEPTRGVD 455
Cdd:PRK11124 164 LFDEPTAALD 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-241 |
3.41e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 22 RSRTSVPAPAPVLTLDSVSKSFGpvdvlkDITVHVRPGRV---QVL--LGENGAGKSTLIKMMSGIYQPDGGRVVVDGKp 96
Cdd:COG1245 330 HAPRREKEEETLVEYPDLTKSYG------GFSLEVEGGEIregEVLgiVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 97 vhlgsvrdaerlgIATIHQELNLVPSMTVAEnVLMGRLPSR--GGFVSRRTMRRLAREALdrvrldvsLDTPVGELGIAR 174
Cdd:COG1245 403 -------------ISYKPQYISPDYDGTVEE-FLRSANTDDfgSSYYKTEIIKPLGLEKL--------LDKNVKDLSGGE 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 175 QQLVEIAKALSLNARVLILDEPTAALTGSE----TEVLFGVVEElrRDDVAMVfISHHLEEIAAIGDEVSV 241
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLDVEQrlavAKAIRRFAEN--RGKTAMV-VDHDIYLIDYISDRLMV 528
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
44-261 |
3.48e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 44 GPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQpDGGRVVVDG------KPVHLgSVRDAERL---GIATIH 114
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRmrfddiDLLRL-SPRERRKLvghNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 115 QELN--LVPSMTVAENvLMGRLPS---RGGFVSRRTMR-RLAREALDRVRL----DVSLDTPVgELGIARQQLVEIAKAL 184
Cdd:PRK15093 96 QEPQscLDPSERVGRQ-LMQNIPGwtyKGRWWQRFGWRkRRAIELLHRVGIkdhkDAMRSFPY-ELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 185 SLNARVLILDEPTAALTGSETEVLFGVVEELRRDD-VAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAstheDELV 261
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKINVLYCGQTVETAPS----KELV 247
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
48-232 |
4.53e-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: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAeRLGIATIHQE---------LN 118
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDpvlfsgslrMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 119 LVP-SMTVAENVLMG-RLPSRGGFVSrrtmrrlarealdrvRLDVSLDTPVGE----LGIARQQLVEIAKALSLNARVLI 192
Cdd:TIGR00957 1380 LDPfSQYSDEEVWWAlELAHLKTFVS---------------ALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502628485 193 LDEPTAALTgSETEVLFGVVEELRRDDVAMVFISHHLEEI 232
Cdd:TIGR00957 1445 LDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
285-501 |
6.11e-09 |
|
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: 57.76 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLS-----RTGVLH---DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADP---YDAGTVHVDGQ---RLPPRSV 350
Cdd:COG0444 1 LLEVRNLKvyfptRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEdllKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 351 GSAVAAGIGHVPED---------RKGQglvldaSVAENLgyatlaatSRAGFADRRGQRSRAQEVASRLRIRmrDVDQAA 421
Cdd:COG0444 81 RKIRGREIQMIFQDpmtslnpvmTVGD------QIAEPL--------RIHGGLSKAEARERAIELLERVGLP--DPERRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 422 RD----LSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYEL--------------InavaaaggavllvSSDL 483
Cdd:COG0444 145 DRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLlkdlqrelglailfI-------------THDL 211
|
250
....*....|....*...
gi 502628485 484 PEVLGVSDRVLVMSGGRL 501
Cdd:COG0444 212 GVVAEIADRVAVMYAGRI 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
296-467 |
8.01e-09 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAdpYD--AGTVHVDGQRLppRSVG-SAVAAGIGHVPEDrkgqgLVL 372
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF--YDvsSGSILIDGQDI--REVTlDSLRRAIGVVPQD-----TVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 -DASVAENLGYATLAATSRagfadrrgQRSRAQEVAS--RLRIRMRD-----VDQAARDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:cd03253 87 fNDTIGYNIRYGRPDATDE--------EVIEAAKAAQihDKIMRFPDgydtiVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180
....*....|....*....|...
gi 502628485 445 LLLDEPTRGVDVGARVEIYELIN 467
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALR 181
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
267-342 |
8.55e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.24 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 267 RDITEQYPRRtHTPGDEVLLDVRGLSRTG-----VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVD 341
Cdd:COG1134 8 ENVSKSYRLY-HEPSRSLKELLLRRRRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
.
gi 502628485 342 G 342
Cdd:COG1134 87 G 87
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
299-501 |
1.22e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 55.19 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 299 DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlpprSVGSAVaagighvPEDRKGQGLVLDASVAE 378
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAP-------PADRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 379 NLGYATLAATSRA-GFADRRGQRSRAQEVASRLRIRMRDVdQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVG 457
Cdd:cd03298 84 HLTVEQNVGLGLSpGLKLTAEDRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502628485 458 ARVEIYELINAVAAAGGAVLLVSSDLPE-VLGVSDRVLVMSGGRL 501
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
296-363 |
1.26e-08 |
|
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: 55.62 E-value: 1.26e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlpprsVGSAVAAGIGHVPE 363
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLGGGFNPE 98
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
48-228 |
1.36e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.08 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVvvdGKPVHlgsvrdaerlgiatihqelnlvpsmtvaE 127
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEG----------------------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMgrLPSRgGFVSRRTMRRLAREALDRVrldVSLdtpvGElgiarQQLVEIAKALSLNARVLILDEPTAALTgseTEV 207
Cdd:cd03223 65 DLLF--LPQR-PYLPLGTLREQLIYPWDDV---LSG----GE-----QQRLAFARLLLHKPKFVFLDEATSALD---EES 126
|
170 180
....*....|....*....|.
gi 502628485 208 LFGVVEELRRDDVAMVFISHH 228
Cdd:cd03223 127 EDRLYQLLKELGITVISVGHR 147
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
297-505 |
1.47e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVgSAVAAGIGHVPEDRKgqgLVLD 373
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditRLKNREV-PFLRRQIGMIFQDHH---LLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAENLGYATLAATsrAGFADRRGQRSRAQEVASRLrirmrdvDQAAR---DLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK10908 94 RTVYDNVAIPLIIAG--ASGDDIRRRVSAALDKVGLL-------DKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 451 TRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGEL 505
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
39-250 |
1.48e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 39 VSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGK--PVHLGSVRDAERLGIATIHQE 116
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 117 LNLVPSMTVAENVLM-----GRLPSrggfvsrRTMRRLAREALDRVRLDVSLDTPVGEL--GIARQqlVEIAKALSLNAR 189
Cdd:PRK11831 93 GALFTDMNVFDNVAYplrehTQLPA-------PLLHSTVMMKLEAVGLRGAAKLMPSELsgGMARR--AALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 190 VLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
296-455 |
1.49e-08 |
|
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: 55.57 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPprSVGSA-VAAGIGHVPEDrkgqGLVLDA 374
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA--LADPAwLRRQVGVVLQE----NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAENLGYATLAATSR-----AGFADrrgqrsrAQEVASRLRIRMRD-VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:cd03252 91 SIRDNIALADPGMSMErvieaAKLAG-------AHDFISELPEGYDTiVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
....*..
gi 502628485 449 EPTRGVD 455
Cdd:cd03252 164 EATSALD 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
296-464 |
1.53e-08 |
|
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: 55.31 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlPPRSVG-SAVAAGIGHVPEDRkgqgLVLDA 374
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI--DIRDISrKSLRSMIGVVLQDT----FLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAENLGYATLAATsragfaDRRGQRSRAQEVASRLRIRMRD-----VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:cd03254 92 TIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPNgydtvLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170
....*....|....*
gi 502628485 450 PTRGVDVGARVEIYE 464
Cdd:cd03254 166 ATSNIDTETEKLIQE 180
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
48-248 |
1.53e-08 |
|
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: 55.11 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKpvhlgsvrDAERLGIATIHQELNLVPSMTVae 127
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--------DISTIPLEDLRSSLTIIPQDPT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 nVLMGRLpsrggfvsRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:cd03369 93 -LFSGTI--------RSNLDPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502628485 208 LFGVVEELRRdDVAMVFISHHLEEIAAIgDEVSVLRDGALV 248
Cdd:cd03369 164 IQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-200 |
1.56e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 8 PASEPSGGRASGPARSRTSVPApapvltldsvsksFGPVDVlkditvHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG 87
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPV-------------FGPLDF------HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVES 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 88 GRVVVDGKPvhlgsVRDAERLG-IATIHQELNLVPSMTVAENV-----LMGRLPsrggfvsrrtmRRLAREALDRVRLDV 161
Cdd:PRK13543 66 GQIQIDGKT-----ATRGDRSRfMAYLGHLPGLKADLSTLENLhflcgLHGRRA-----------KQMPGSALAIVGLAG 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 502628485 162 SLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:PRK13543 130 YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
40-242 |
1.62e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 40 SKSFGPVDvlkDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRD--AERLGIATIHQE- 116
Cdd:PRK15079 31 PKTLKAVD---GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 117 -LNLVPSMTVAEnVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDVSLdtpvgelgIARQ---------QLVEIAKALSL 186
Cdd:PRK15079 108 lASLNPRMTIGE-IIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNL--------INRYphefsggqcQRIGIARALIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 187 NARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVL 242
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
180-455 |
1.62e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 180 IAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAevpASTHEDE 259
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE---TGEREEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 260 LVRLMVG--------RDI----TEQYPRRTHTPGDEVLLDVR-GLSRTG---VLHDIDVQVRAGEVVGVAGLVGAGRTEL 323
Cdd:PRK10938 223 LQQALVAqlahseqlEGVqlpePDEPSARHALPANEPRIVLNnGVVSYNdrpILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 324 LRAIAGADP--YdAGTVHVDGQRlppRSVGSAV---AAGIGHVpedrkGQGLVLDASVAENLGYATLaatsrAGFADRRG 398
Cdd:PRK10938 303 LSLITGDHPqgY-SNDLTLFGRR---RGSGETIwdiKKHIGYV-----SSSLHLDYRVSTSVRNVIL-----SGFFDSIG 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 399 --------QRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:PRK10938 369 iyqavsdrQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
297-512 |
1.67e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 55.16 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRL----PPRSVgsaVAAGIGHVPEdrkgqglvl 372
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgPDRMV---VFQNYSLLPW--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 dASVAENLGYATLAAtsragfadRRGQRSRAQEVASRLRIRMRDVDQAAR----DLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:TIGR01184 69 -LTVRENIALAVDRV--------LPDLSKSERRAIVEEHIALVGLTEAADkrpgQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 449 EPTRGVDVGARVEIYE-LINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGrltgelPAATATQ 512
Cdd:TIGR01184 140 EPFGALDALTRGNLQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG------PAANIGQ 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
296-466 |
1.92e-08 |
|
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: 54.73 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAvaagIGHVPEDRkgqgLVL 372
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdisTIPLEDLRSS----LTIIPQDP----TLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLgyatlaatsragfaDRRGQRSRAQEVASrLRIRmrdvdQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTR 452
Cdd:cd03369 95 SGTIRSNL--------------DPFDEYSDEEIYGA-LRVS-----EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170
....*....|....
gi 502628485 453 GVDVGARVEIYELI 466
Cdd:cd03369 155 SIDYATDALIQKTI 168
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
297-504 |
1.96e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.79 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSaVAAGIGHVPEDRKGQ--GLVLDA 374
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQNPDNQfvGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVA---ENLGYATLAATSRAGFADRRgqrsraqevasrlrIRMRD-VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK13635 102 DVAfglENIGVPREEMVERVDQALRQ--------------VGMEDfLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 451 TRGVDVGARVEIYELINAVAAAGGAVLLV-SSDLPEVLGvSDRVLVMSGGRLTGE 504
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-242 |
2.12e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.13 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 29 APAPVLTLDSVSKS-------FGP---VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVh 98
Cdd:PRK11308 1 SQQPLLQAIDLKKHypvkrglFKPerlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 99 LGSVRDAERLgiatIHQELNLV---------PSMTV----AENVLMGRLPSRGgfvSRRT-----MRR--LAREALDRVR 158
Cdd:PRK11308 80 LKADPEAQKL----LRQKIQIVfqnpygslnPRKKVgqilEEPLLINTSLSAA---ERREkalamMAKvgLRPEHYDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 159 LDVSldtpvgelGIARQQlVEIAKALSLNARVLILDEPTAALTGS-ETEVLfGVVEELRRD-DVAMVFISHHLEEIAAIG 236
Cdd:PRK11308 153 HMFS--------GGQRQR-IAIARALMLDPDVVVADEPVSALDVSvQAQVL-NLMMDLQQElGLSYVFISHDLSVVEHIA 222
|
....*.
gi 502628485 237 DEVSVL 242
Cdd:PRK11308 223 DEVMVM 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
48-252 |
2.34e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIY--QPDGGRVVVDGKPvhlgsvrdaerlgiatIHQELNLVPSmtv 125
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGREASLIDA--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 aenvlmgrLPSRGGFVsrrtmrrLAREALDRVRLD--VSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGS 203
Cdd:COG2401 106 --------IGRKGDFK-------DAVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 204 ETEVL-FGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVP 252
Cdd:COG2401 171 TAKRVaRNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGYGGVPEEK 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
275-462 |
2.51e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 275 RRTHTPGDEVLldvrglsrtGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAV 354
Cdd:PRK10535 11 RRSYPSGEEQV---------EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 355 AAGIGHVPEDRKGQGLVLDASVAENLGYATLAATSragfaDRRGQRSRAQEVASRLRIRMRdVDQAARDLSGGNQQKIVF 434
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGL-----ERKQRLLRAQELLQRLGLEDR-VEYQPSQLSGGQQQRVSI 155
|
170 180
....*....|....*....|....*...
gi 502628485 435 GRWVLAGSRVLLLDEPTRGVDVGARVEI 462
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEV 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-248 |
2.69e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHL--GSVRDAERLGIATIHQE--LNLVP 121
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlsPGKLQALRRDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 122 SMTVAENVlMGRLPSRGGFVSRRTMRRLArEALDRVRL--DVSLDTPVGELGIARQQLVeIAKALSLNARVLILDEPTAA 199
Cdd:PRK10261 417 RQTVGDSI-MEPLRVHGLLPGKAAAARVA-WLLERVGLlpEHAWRYPHEFSGGQRQRIC-IARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 200 LTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-100 |
2.76e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 2.76e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 30 PAPVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVdGKPVHLG 100
Cdd:PRK10636 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLG 378
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
32-248 |
3.54e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 32 PVLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSG--IYQPDGGRVVVDGKpvhlgSVRDAE--- 106
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE-----SILDLEpee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 --RLGIATIHQELNLVPSMTvAENVLMGRLPSRGGFVSRRTMRRLA-----REALDRVRLDVS-LDTPVGElGIA--RQQ 176
Cdd:CHL00131 81 raHLGIFLAFQYPIEIPGVS-NADFLRLAYNSKRKFQGLPELDPLEfleiiNEKLKLVGMDPSfLSRNVNE-GFSggEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 177 LVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHH---LEEIaaIGDEVSVLRDGALV 248
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYI--KPDYVHVMQNGKII 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
46-245 |
3.81e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSG-IYQ---PDGGRVVVDGKPVHlgSVRDAERLGIATIHQELNLVP 121
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPE--EIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 122 SMTVAEN-VLMGRLPS---RGGFVSRRTMRRLAREALDRVR-LDVSLDTPVGE---LGIA--RQQLVEIAKALSLNARVL 191
Cdd:TIGR00956 152 HLTVGETlDFAARCKTpqnRPDGVSREEYAKHIADVYMATYgLSHTRNTKVGNdfvRGVSggERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 192 ILDEPTAALTGSETevlFGVVEELRR-----DDVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:TIGR00956 232 CWDNATRGLDSATA---LEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
296-455 |
4.08e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpPRSVGSAVAAGIGHVPedrkgqGLVLDAS 375
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA-TRGDRSRFMAYLGHLP------GLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYATlaatsraGFADRRGQRSRAQEVASrlrIRMRDVDQA-ARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:PRK13543 99 TLENLHFLC-------GLHGRRAKQMPGSALAI---VGLAGYEDTlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
.
gi 502628485 455 D 455
Cdd:PRK13543 169 D 169
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
286-506 |
4.73e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVhvdgqrlpprsvgSAVAAGIGHV 361
Cdd:PRK11247 13 LLLNAVSKRygerTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-------------LAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PEDRKGqgLVLDA------SVAENLGY--------ATLAATSRAGFADRRGQRSRAqevasrlrirmrdvdqaardLSGG 427
Cdd:PRK11247 80 REDTRL--MFQDArllpwkKVIDNVGLglkgqwrdAALQALAAVGLADRANEWPAA--------------------LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR----LT 502
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeSLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKigldLT 217
|
....
gi 502628485 503 GELP 506
Cdd:PRK11247 218 VDLP 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
296-458 |
4.95e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.34 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAgIGHvpedrkgqglvLDA- 374
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-LGH-----------RNAm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ----SVAENLgyatlaatsrAGFADRRGQRSRAQEVASRlRIRMRDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:PRK13539 85 kpalTVAENL----------EFWAAFLGGEELDIAAALE-AVGLAPLaHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*....
gi 502628485 450 PTRGVDVGA 458
Cdd:PRK13539 154 PTAALDAAA 162
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
296-466 |
5.87e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvGSAVAAGIGHVPED-RKGQGLVLDA 374
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQQlPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAenLG-YATLAATSRAGFADRRgqrsRAQEVASRLRIR---MRDVDQaardLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK10575 105 LVA--IGrYPWHGALGRFGAADRE----KVEEAISLVGLKplaHRLVDS----LSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170
....*....|....*.
gi 502628485 451 TRGVDVGARVEIYELI 466
Cdd:PRK10575 175 TSALDIAHQVDVLALV 190
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
48-200 |
5.88e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG--GRVVVDGKPVHLGSVRdaeRLGIATihQELNLVPSMTV 125
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK---RTGFVT--QDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVL---MGRLPSRggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGI-----ARQQLVEIAKALSLNARVLILDEPT 197
Cdd:PLN03211 158 RETLVfcsLLRLPKS---LTKQEKILVAESVISELGLTKCENTIIGNSFIrgisgGERKRVSIAHEMLINPSLLILDEPT 234
|
...
gi 502628485 198 AAL 200
Cdd:PLN03211 235 SGL 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
296-466 |
5.96e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.10 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVaagighVPEDrkgQGLVLDAS 375
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV------VFQK---DALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYA-TLAATSRAgfadrrgQRsraQEVASRL--RIRMRDVDQAARD-LSGGNQQKIVFGRWVLAGSRVLLLDEPT 451
Cdd:COG4525 93 VLDNVAFGlRLRGVPKA-------ER---RARAEELlaLVGLADFARRRIWqLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170
....*....|....*
gi 502628485 452 RGVDVGARVEIYELI 466
Cdd:COG4525 163 GALDALTREQMQELL 177
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-200 |
6.36e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 53.24 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 40 SKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGkpvhlgsvrdaerlGIATIHQELNL 119
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 120 VpSMTVAENVLMGrlpsrggfvSRRTMRRLaREALDRVRLDVSLD-------TPVGELGIA----RQQLVEIAKALSLNA 188
Cdd:cd03250 78 Q-NGTIRENILFG---------KPFDEERY-EKVIKACALEPDLEilpdgdlTEIGEKGINlsggQKQRISLARAVYSDA 146
|
170
....*....|..
gi 502628485 189 RVLILDEPTAAL 200
Cdd:cd03250 147 DIYLLDDPLSAV 158
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
253-466 |
6.38e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 53.63 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 253 ASTHEDELVRLmvgRDITEQYPRRTHTPgdevlldvrglsrtgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADP 332
Cdd:cd03248 4 APDHLKGIVKF---QNVTFAYPTRPDTL---------------VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 333 YDAGTVHVDGQRLPP------RSVGSAVaagighvpedrkGQGLVLDA-SVAENLGY--ATLAATSRAGFADRRGQRSRA 403
Cdd:cd03248 66 PQGGQVLLDGKPISQyehkylHSKVSLV------------GQEPVLFArSLQDNIAYglQSCSFECVKEAAQKAHAHSFI 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 404 QEVASRLRirmRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI 466
Cdd:cd03248 134 SELASGYD---TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
48-248 |
9.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRV----------------------VVDGKPVH--LGSVR 103
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvlekLVIQKTRFkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 104 DA-ERLGIATIHQELNLVPSmTVAENVLMGRLpSRGgfVSRRTMRRLAREALDRVRLDVS-LDTPVGELGIARQQLVEIA 181
Cdd:PRK13651 102 EIrRRVGVVFQFAEYQLFEQ-TIEKDIIFGPV-SMG--VSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 182 KALSLNARVLILDEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
296-455 |
9.86e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.43 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpprsvgsavaagigHVPEDRKGQGLVLDA- 374
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI--------------NLVRDKDGQLKVADKn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 ----------------------SVAENLGYATLAATSRAgfadRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKI 432
Cdd:PRK10619 86 qlrllrtrltmvfqhfnlwshmTVLENVMEAPIQVLGLS----KQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180
....*....|....*....|...
gi 502628485 433 VFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALD 184
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-132 |
9.89e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGP-VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVdgkpvhlgsvrdAERLGIA 111
Cdd:PRK11819 6 IYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------------APGIKVG 73
|
90 100
....*....|....*....|.
gi 502628485 112 TIHQELNLVPSMTVAENVLMG 132
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEEG 94
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
51-200 |
1.02e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 51 DITVHVRPGR-VQVLlGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHlgSVRDAerlgiatIHQEL-------NLVPS 122
Cdd:PRK13538 19 GLSFTLNAGElVQIE-GPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRDE-------YHQDLlylghqpGIKTE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502628485 123 MTVAENVLMgrLPSRGGFVSRRTMrrlaREALDRVRLDVSLDTPVGELGIARQQLVEIAKaLSLNARVL-ILDEPTAAL 200
Cdd:PRK13538 89 LTALENLRF--YQRLHGPGDDEAL----WEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAI 160
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
48-228 |
1.02e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGrvQVLL--GENGAGKSTLIKMMSGIYQPDGGRVVV-DG--------KP-VHLGSVRDAerlgiatihq 115
Cdd:COG4178 378 LLEDLSLSLKPG--ERLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGarvlflpqRPyLPLGTLREA---------- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 116 elnLVpsmtvaenvlmgrLPSRGGFVSRRTMrrlaREALDRVRLDV---SLDT--------PVGElgiarQQLVEIAKAL 184
Cdd:COG4178 446 ---LL-------------YPATAEAFSDAEL----REALEAVGLGHlaeRLDEeadwdqvlSLGE-----QQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502628485 185 SLNARVLILDEPTAAL-TGSETEVLFGVVEELRrdDVAMVFISHH 228
Cdd:COG4178 501 LHKPDWLFLDEATSALdEENEAALYQLLREELP--GTTVISVGHR 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
275-502 |
1.05e-07 |
|
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: 54.95 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 275 RRTHTPGDEVLLDVRGLSRT------GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlppr 348
Cdd:TIGR00957 626 RRTIKPGEGNSITVHNATFTwardlpPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 349 svgsavaagIGHVPEdrkgQGLVLDASVAENLGYATLAATSRagfadrrgQRSRAQEVASRLRIRM------RDVDQAAR 422
Cdd:TIGR00957 701 ---------VAYVPQ----QAWIQNDSLRENILFGKALNEKY--------YQQVLEACALLPDLEIlpsgdrTEIGEKGV 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 423 DLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI-----NAVAAAGGAVLLVSSDLPEVlgvsDRVLVMS 497
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpegVLKNKTRILVTHGISYLPQV----DVIIVMS 835
|
....*
gi 502628485 498 GGRLT 502
Cdd:TIGR00957 836 GGKIS 840
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
44-245 |
1.15e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 44 GPVDVLKDITVHVRPGRVQVLLGENGAGKS-TLIKMMsGIYQPDG---GRVVVDGKPV------HLGSVRdAERlgIATI 113
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGrigGSATFNGREIlnlpekELNKLR-AEQ--ISMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 114 HQE--LNLVPSMTVAEN---VLM--GRLPSRGGFVSRRTMRRLAR--EALDRVRLdvsldTPVGELGIARQQlVEIAKAL 184
Cdd:PRK09473 103 FQDpmTSLNPYMRVGEQlmeVLMlhKGMSKAEAFEESVRMLDAVKmpEARKRMKM-----YPHEFSGGMRQR-VMIAMAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 185 SLNARVLILDEPTAALTGSETEVLFGVVEELRRD-DVAMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
296-501 |
1.26e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.54 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAvaagighvpedRKGQGLV- 371
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERELRAA-----------RRKIGMIf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 372 -----LDA-SVAENLGYA-TLAATSRagfADRrgqRSRAQEVASR--LRirmrdvDQAAR---DLSGGNQQKIVFGRwVL 439
Cdd:COG1135 89 qhfnlLSSrTVAENVALPlEIAGVPK---AEI---RKRVAELLELvgLS------DKADAypsQLSGGQKQRVGIAR-AL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 440 AGS-RVLLLDEPTRGVDVGARVEIYELInavaaaggavllvsSDLPEVLGVS---------------DRVLVMSGGRL 501
Cdd:COG1135 156 ANNpKVLLCDEATSALDPETTRSILDLL--------------KDINRELGLTivlithemdvvrricDRVAVLENGRI 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-248 |
1.43e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKpvhlgsvrDAERLGIATIHQELNLVPSMTVae 127
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGC--------DISKFGLMDLRKVLGIIPQAPV-- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 nvlmgrLPSrgGFVsRRTMRRLAR-------EALDRVRL-DV------SLDTPVGELG----IARQQLVEIAKALSLNAR 189
Cdd:PLN03130 1324 ------LFS--GTV-RFNLDPFNEhndadlwESLERAHLkDVirrnslGLDAEVSEAGenfsVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 190 VLILDEPTAAL-TGSETEVLFGVVEELRrdDVAMVFISHHLEEIAAIgDEVSVLRDGALV 248
Cdd:PLN03130 1395 ILVLDEATAAVdVRTDALIQKTIREEFK--SCTMLIIAHRLNTIIDC-DRILVLDAGRVV 1451
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
296-516 |
1.46e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.71 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAVAAGIGH--VPEDRKGQGL 370
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpisMLSSRQLARRLALLPQHhlTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 371 VLDASVAENLGYATLAATSRAgFADRRGQRSRAQEVAsrlrirmrdvDQAARDLSGGNQQKiVFGRWVLA-GSRVLLLDE 449
Cdd:PRK11231 97 VAYGRSPWLSLWGRLSAEDNA-RVNQAMEQTRINHLA----------DRRLTDLSGGQRQR-AFLAMVLAqDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 450 PTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTgelpaATATQDQVM 516
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM-----AQGTPEEVM 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
297-501 |
1.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSaVAAGIGHVPEDRKGQ--GLVLDA 374
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPDNQfvGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVA---ENLGyatlaatsragfADRRGQRSRAQEvASRLrIRMRDVD--QAARdLSGGNQQKIVFGRWVLAGSRVLLLDE 449
Cdd:PRK13650 102 DVAfglENKG------------IPHEEMKERVNE-ALEL-VGMQDFKerEPAR-LSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 450 PTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVlGVSDRVLVMSGGRL 501
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIkGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
291-501 |
1.83e-07 |
|
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: 52.65 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 291 LSRTGV---LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlpprSVGSAVAAGIGHVPEDRKG 367
Cdd:cd03294 31 LKKTGQtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ-----DIAAMSRKELRELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 368 Q-----GLVLDASVAENLGYATlaatSRAGfADRRGQRSRAQEVASRLRIRmRDVDQAARDLSGGNQQKIVFGRWVLAGS 442
Cdd:cd03294 106 MvfqsfALLPHRTVLENVAFGL----EVQG-VPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 443 RVLLLDEPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
48-230 |
1.84e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVvdgkpVHLGSVRDAERLGIATIHQELNLVPSMTVAE 127
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMgrlpsrggFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEV 207
Cdd:PRK13541 90 NLKF--------WSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|...
gi 502628485 208 LFGVVeELRRDDVAMVFISHHLE 230
Cdd:PRK13541 162 LNNLI-VMKANSGGIVLLSSHLE 183
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
286-456 |
2.08e-07 |
|
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: 51.72 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGL--SRTG--VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLP-PRSVGSAVAAGIGH 360
Cdd:cd03231 1 LEADELtcERDGraLFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 VPedrkgqGLVLDASVAENLGyatlaatsragFADRRGQRSRAQEVASRLRIRMRDvDQAARDLSGGNQQKIVFGRWVLA 440
Cdd:cd03231 81 AP------GIKTTLSVLENLR-----------FWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLS 142
|
170
....*....|....*.
gi 502628485 441 GSRVLLLDEPTRGVDV 456
Cdd:cd03231 143 GRPLWILDEPTTALDK 158
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
298-456 |
2.25e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 298 HDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLppRSVGSAVAAG---IGHVPedrkgqGLVLDA 374
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEYHQDllyLGHQP------GIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 375 SVAENLGYAtlAATSRAGFADRRGQRSRAQEVASRLrirmrdvDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEP---- 450
Cdd:PRK13538 90 TALENLRFY--QRLHGPGDDEALWEALAQVGLAGFE-------DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftai 160
|
....*..
gi 502628485 451 -TRGVDV 456
Cdd:PRK13538 161 dKQGVAR 167
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
283-455 |
2.38e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAdpydagtvhVDGQRLPPRSV---GSAVA 355
Cdd:PRK09984 2 QTIIRVEKLAKTfnqhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---------ITGDKSAGSHIellGRTVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 356 AGiGHVPED-RKGQG----------LVLDASVAENLGYATLAATS--RAGFA-DRRGQRSRAQEVASRLRIrMRDVDQAA 421
Cdd:PRK09984 73 RE-GRLARDiRKSRAntgyifqqfnLVNRLSVLENVLIGALGSTPfwRTCFSwFTREQKQRALQALTRVGM-VHFAHQRV 150
|
170 180 190
....*....|....*....|....*....|....
gi 502628485 422 RDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
45-255 |
2.97e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 45 PVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPD----GGRVVVDGKPVHLGSVRDAErlgIATIHQElnlv 120
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRGRK---IATIMQN---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 121 psmtvaenvlmgrlpSRGGFVSRRTMRRLARE---ALDRVRLDVSLDTPVGELGIARQ----------------QLVEIA 181
Cdd:PRK10418 88 ---------------PRSAFNPLHTMHTHAREtclALGKPADDATLTAALEAVGLENAarvlklypfemsggmlQRMMIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 182 KALSLNARVLILDEPTAALTG-SETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAEVPAST 255
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVvAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
288-467 |
2.98e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 288 VRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHVPe 363
Cdd:NF033858 4 LEGVShrygKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 364 drkgQG----LVLDASVAENLGY-----------------ATLAATSRAGFADRrgqrsraqevasrlrirmrdvdqAAR 422
Cdd:NF033858 83 ----QGlgknLYPTLSVFENLDFfgrlfgqdaaerrrridELLRATGLAPFADR-----------------------PAG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502628485 423 DLSGGNQQKIvfGrwvLAGSRV-----LLLDEPTRGVDVGARVEIYELIN 467
Cdd:NF033858 136 KLSGGMKQKL--G---LCCALIhdpdlLILDEPTTGVDPLSRRQFWELID 180
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
296-455 |
3.90e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 52.80 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDG---QRLPPRSVGSAVAagighvpedRKGQGLVL 372
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLASLRRQVA---------LVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 -DASVAENLGYATLAATSRAGFaDRRGQRSRAQEVASRLRIRMR-DVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:TIGR02203 418 fNDTIANNIAYGRTEQADRAEI-ERALAAAYAQDFVDKLPLGLDtPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
....*
gi 502628485 451 TRGVD 455
Cdd:TIGR02203 497 TSALD 501
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
48-200 |
4.47e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.93 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGiyQPDGGrvVVDGKPVHLGSVRDAERLGIATIHQELNLV--PSMTV 125
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDIRISGFPKKQETFARISGYCEQNDIhsPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 126 AENVLMG---RLPSRggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIA------RQQLVeIAKALSLNARVLILDEP 196
Cdd:PLN03140 971 RESLIYSaflRLPKE---VSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTglsteqRKRLT-IAVELVANPSIIFMDEP 1046
|
....
gi 502628485 197 TAAL 200
Cdd:PLN03140 1047 TSGL 1050
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
42-108 |
4.75e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 4.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 42 SFGPVDvlkdITVHvrPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERL 108
Cdd:PRK10522 338 SVGPIN----LTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-90 |
5.47e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 5.47e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 34 LTLDSVSKSFGPVDVLKDITVHVRPG-RVQVLlGENGAGKSTLIKMMSGIYQPDGGRV 90
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGeRLAII-GENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
296-506 |
5.69e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.23 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPP----------RSVGSAVAAGIGHV-PED 364
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrRDIQMVFQDSISAVnPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 365 RKGqglvldASVAENLGYATLaatsragfADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:PRK10419 107 TVR------EIIREPLRHLLS--------LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502628485 445 LLLDEPTRGVDVGARVEIYELINAVAAAGGAV-LLVSSDLPEVLGVSDRVLVMSGGRLTGELP 506
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-245 |
5.96e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 1 MTAAAPVPASEPSGGRASGPARSRTSVPAPAPVLTLDSVSKSFG--PVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKM 78
Cdd:PTZ00243 626 TDYGSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFElePKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQS 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 79 MSGIYQPDGGRVVvdgkpvhlgsvrdAERlGIATIHQElNLVPSMTVAENVLMgrlpsrggFVSRRTMR-----RLAREA 153
Cdd:PTZ00243 706 LLSQFEISEGRVW-------------AER-SIAYVPQQ-AWIMNATVRGNILF--------FDEEDAARladavRVSQLE 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 154 LDRVRLDVSLDTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTAALtgsETEVLFGVVEELRRDDVA---MVFIS 226
Cdd:PTZ00243 763 ADLAQLGGGLETEIGEKGVnlsgGQKARVSLARAVYANRDVYLLDDPLSAL---DAHVGERVVEECFLGALAgktRVLAT 839
|
250
....*....|....*....
gi 502628485 227 HHLeEIAAIGDEVSVLRDG 245
Cdd:PTZ00243 840 HQV-HVVPRADYVVALGDG 857
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-455 |
6.07e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 43 FGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDgKPVHLG------------SVRDAERLGi 110
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-PNERLGklrqdqfafeefTVLDTVIMG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 111 atiHQELNLV----------PSMT------VAEnvLMGRLPSRGGFV--SRrtmrrlAREALDRVRLDVSLDT-PVGELG 171
Cdd:PRK15064 89 ---HTELWEVkqerdriyalPEMSeedgmkVAD--LEVKFAEMDGYTaeAR------AGELLLGVGIPEEQHYgLMSEVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 172 IARQQLVEIAKALSLNARVLILDEPTAAL---TGSETEvlfgvvEELRRDDVAMVFISH----------HL--------- 229
Cdd:PRK15064 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLdinTIRWLE------DVLNERNSTMIIISHdrhflnsvctHMadldygelr 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 230 ----------------------------EEIAAIGDEVSvlRDGA------------------LVAEVPASTHEDELVRL 263
Cdd:PRK15064 232 vypgnydeymtaatqarerlladnakkkAQIAELQSFVS--RFSAnaskakqatsrakqidkiKLEEVKPSSRQNPFIRF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 264 mvgrditEQyprrthtpgDEVL----LDVRGLSRT---GVL-HDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDA 335
Cdd:PRK15064 310 -------EQ---------DKKLhrnaLEVENLTKGfdnGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 336 GTVHvdgqrlpprsvgSAVAAGIGHVPEDRKgqglvldASVAENLGYATLAATSRAGFADRRGQRSraqeVASRLRIRMR 415
Cdd:PRK15064 374 GTVK------------WSENANIGYYAQDHA-------YDFENDLTLFDWMSQWRQEGDDEQAVRG----TLGRLLFSQD 430
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502628485 416 DVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:PRK15064 431 DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
296-501 |
6.68e-07 |
|
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: 50.18 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPPRSVGSAvaagIGHVPEDrkgqGLVL 372
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdisKIGLHDLRSR----ISIIPQD----PVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENL---GYAT----LAATSRAGFadrrgqRSRAQEVASRLRIRmrdVDQAARDLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:cd03244 91 SGTIRSNLdpfGEYSdeelWQALERVGL------KEFVESLPGGLDTV---VEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 446 LLDEPTRGVDVGARVEIYELINAVAaaggavllvsSD---------LPEVLGvSDRVLVMSGGRL 501
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAF----------KDctvltiahrLDTIID-SDRILVLDKGRV 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-197 |
8.67e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRvvvdgkpVHLGSvrdaeRLGIAT 112
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-------IHCGT-----KLEVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 113 IHQ-ELNLVPSMTVAENVLMGRLPSRGGFVSRRTMRRLaREAL---DRVRldvsldTPVGEL-GIARQQLVeIAKALSLN 187
Cdd:PRK11147 387 FDQhRAELDPEKTVMDNLAEGKQEVMVNGRPRHVLGYL-QDFLfhpKRAM------TPVKALsGGERNRLL-LARLFLKP 458
|
170
....*....|
gi 502628485 188 ARVLILDEPT 197
Cdd:PRK11147 459 SNLLILDEPT 468
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
33-237 |
9.96e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 33 VLTLDSVSKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI------YQPDGgRVVVDGKPVHLGSVRDAE 106
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVEG-KVTFHGKNLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 107 -RLGIATIHQELNLVPSmTVAENVLMG-RLPSRGGFVSRRTMRRLAREAL-DRVRlDvSLDTPVGELGIARQQLVEIAKA 183
Cdd:PRK14243 89 vRRRIGMVFQKPNPFPK-SIYDNIAYGaRINGYKGDMDELVERSLRQAALwDEVK-D-KLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628485 184 LSLNARVLILDEPTAALTGSETEVLFGVVEELRRdDVAMVFISHHLEEIAAIGD 237
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSD 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
283-500 |
9.99e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLSRTGVLHDIDV--------QVRAGEVVGVAGLVGAGRTELLRAIAG---ADPYDAGTVHVDGQR---LPPR 348
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVtavndlnfSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREilnLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 349 SVGSAVAAGIGHVPED---------RKGQGLVLDASVAENLGYATlaatsraGFADRRGQRSRAQEVASRLRIRMRdvdq 419
Cdd:PRK09473 90 ELNKLRAEQISMIFQDpmtslnpymRVGEQLMEVLMLHKGMSKAE-------AFEESVRMLDAVKMPEARKRMKMY---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 420 aARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAA-GGAVLLVSSDLPEVLGVSDRVLVMSG 498
Cdd:PRK09473 159 -PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYA 237
|
..
gi 502628485 499 GR 500
Cdd:PRK09473 238 GR 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
294-500 |
1.14e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 294 TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVG-SAVAAGIGHVPEDRKGQglVL 372
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlMKLRESVGMVFQDPDNQ--LF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRirmrdvDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTR 452
Cdd:PRK13636 97 SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK------DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 453 GVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGR 500
Cdd:PRK13636 171 GLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
296-465 |
1.29e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQR---LPPRSVGSAVA----AGIGHVpedrkgq 368
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvneLEPADRDIAMVfqnyALYPHM------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 369 glvldaSVAENLGYA-TLAATSRAGFadrrgqRSRAQEVASRLRIrMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLL 447
Cdd:PRK11650 92 ------SVRENMAYGlKIRGMPKAEI------EERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180
....*....|....*....|..
gi 502628485 448 DEPTRGVD----VGARVEIYEL 465
Cdd:PRK11650 159 DEPLSNLDaklrVQMRLEIQRL 180
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
297-501 |
1.29e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVdgqrlpprsvGSAVAAGIGHVPED---RKGQGLVLD 373
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV----------GDIVVSSTSKQKEIkpvRKKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAEnLGYATLAATSRAGFADRRGQRSRAQEVASRlRIRMRDV-----DQAARDLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:PRK13643 92 FPESQ-LFEETVLKDVAFGPQNFGIPKEKAEKIAAE-KLEMVGLadefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 449 EPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
286-455 |
1.50e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLSRT------GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDaGTVHVDGQRLPPRSVGSAVAAgIG 359
Cdd:TIGR01271 1218 MDVQGLTAKyteagrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKA-FG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 360 HVPEdrkgQGLVLDASVAENLG-YATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDvdqAARDLSGGNQQKIVFGRWV 438
Cdd:TIGR01271 1296 VIPQ----KVFIFSGTFRKNLDpYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVD---GGYVLSNGHKQLMCLARSI 1368
|
170
....*....|....*..
gi 502628485 439 LAGSRVLLLDEPTRGVD 455
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLD 1385
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
274-500 |
1.68e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.22 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 274 PRRTHTPgdevLLDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLpprs 349
Cdd:PRK11607 12 TRKALTP----LLEIRNLTKSfdgqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 350 vgsavaagiGHVPEDRKGQGLVLDAsvaenlgYAT---LAATSRAGFADRRGQRSRAqEVASRLR-----IRMRDVdqAA 421
Cdd:PRK11607 84 ---------SHVPPYQRPINMMFQS-------YALfphMTVEQNIAFGLKQDKLPKA-EIASRVNemlglVHMQEF--AK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 422 R---DLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEI-YELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMS 497
Cdd:PRK11607 145 RkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
...
gi 502628485 498 GGR 500
Cdd:PRK11607 225 RGK 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
297-504 |
1.90e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.71 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSaVAAGIGHVPEDRKGQglVLDASV 376
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPDNQ--FVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 377 AENLGYatlaATSRAGFAdRRGQRSRAQEvaSRLRIRMRDVD--QAARdLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:PRK13642 100 EDDVAF----GMENQGIP-REEMIKRVDE--ALLAVNMLDFKtrEPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 455 DVGARVEIYELINAVAAA-GGAVLLVSSDLPEVlGVSDRVLVMSGGRLTGE 504
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKE 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
285-504 |
1.92e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 285 LLDVRGLSRT----GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAgigh 360
Cdd:PRK11831 7 LVDMRGVSFTrgnrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 vpedRK-------GQGLVLDASVAENLGYATlaatsragfadRRGQRSRAQEVASRLRIRMRDVD--QAAR----DLSGG 427
Cdd:PRK11831 83 ----RKrmsmlfqSGALFTDMNVFDNVAYPL-----------REHTQLPAPLLHSTVMMKLEAVGlrGAAKlmpsELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVD---VGARVEIYELINavAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDpitMGVLVKLISELN--SALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
289-500 |
1.98e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.80 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 289 RGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDA---GTVHVDG------QRLPPRSVgSAVAAGIG 359
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGipykefAEKYPGEI-IYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 360 HVPEdrkgqglvldASVAENLGYAtlaatsragfADRRGqrsraqevasrlrirmrdvDQAARDLSGGNQQKIVFGRWVL 439
Cdd:cd03233 94 HFPT----------LTVRETLDFA----------LRCKG-------------------NEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 440 AGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVS----SDlpEVLGVSDRVLVMSGGR 500
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSD--EIYDLFDKVLVLYEGR 197
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
292-456 |
2.23e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.34 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 292 SRTGVlHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGA-DPyDAGTVHVDGQRLppRSVG-SAVAAGIGHVPEDrkgqG 369
Cdd:PRK13657 347 SRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfDP-QSGRILIDGTDI--RTVTrASLRRNIAVVFQD----A 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 370 LVLDASVAENLGYATLAATSragfADRRGQRSRAQE---VASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLL 446
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPDATD----EEMRAAAERAQAhdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170
....*....|
gi 502628485 447 LDEPTRGVDV 456
Cdd:PRK13657 495 LDEATSALDV 504
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
290-534 |
2.53e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 290 GLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSavaagIGHVPEDRKGQG 369
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFN-----YRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 370 LVLD------ASVAENLgyatLAATSRAGFADRRGQRSRAQ----EVASRLRIRMRDVDQAARdLSGGNQQKIVFGRWVL 439
Cdd:PRK14271 105 MLFQrpnpfpMSIMDNV----LAGVRAHKLVPRKEFRGVAQarltEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 440 AGSRVLLLDEPTRGVDVGARVEIYELINaVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAatatqDQVMAlA 519
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIR-SLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT-----EQLFS-S 252
|
250
....*....|....*
gi 502628485 520 VKHADDDDHVAPSHG 534
Cdd:PRK14271 253 PKHAETARYVAGLSG 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
417-491 |
2.57e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 417 VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSD 491
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
296-460 |
2.84e-06 |
|
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: 48.23 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGqrlpprsvgsavaaGIGHVPEdrkgQGLVLDAS 375
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQ----EPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLgyatLaatsragFADRRGQRsRAQEV--ASRLRirmRDVDQ-AARD----------LSGGNQQKIVFGRWVLAGS 442
Cdd:cd03250 82 IRENI----L-------FGKPFDEE-RYEKVikACALE---PDLEIlPDGDlteigekginLSGGQKQRISLARAVYSDA 146
|
170 180
....*....|....*....|
gi 502628485 443 RVLLLDEPTRGVD--VGARV 460
Cdd:cd03250 147 DIYLLDDPLSAVDahVGRHI 166
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
287-466 |
2.86e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.89 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 287 DVRGLSR-------TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAG-ADPYDAgTVHVDGQRLP-PRSVGSAVAAG 357
Cdd:PRK14246 9 DVFNISRlylyindKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlIEIYDS-KIKVDGKVLYfGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 358 IghvpedRKGQGLVLDA-------SVAENLGYATlaatSRAGFADRRGQRSRAQEVASRLRIRMRDVDQ---AARDLSGG 427
Cdd:PRK14246 88 L------RKEVGMVFQQpnpfphlSIYDNIAYPL----KSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnsPASQLSGG 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 502628485 428 NQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI 466
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLI 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
294-505 |
4.05e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 294 TGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHVPEDRKGQGLVLD 373
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAENLGYATLAATSRAGFAdrrgqRSRAQEVASRLRIRMRdVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRG 453
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEI-----NSRALEMLAAVGLEHR-ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502628485 454 VDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGEL 505
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
275-536 |
6.85e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 275 RRTHTPGDEVLLDVRGLSR----TGVLHDIDVQVRAGEVVGVAGLVGAGRTEllraiaGADPydAGTVHVDGQRLPPR-- 348
Cdd:NF000106 3 RKTISNGARNAVEVRGLVKhfgeVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALP--AHV*GPDAGRRPWRf* 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 349 ---SVGSAVAAGIGHVPEDRKGQGLVLDasvaenlGYATLAATSRAGFADRRGQRSRAQEVASRLRIrMRDVDQAARDLS 425
Cdd:NF000106 75 twcANRRALRRTIG*HRPVR*GRRESFS-------GRENLYMIGR*LDLSRKDARARADELLERFSL-TEAAGRAAAKYS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 426 GGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGEl 505
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD- 225
|
250 260 270
....*....|....*....|....*....|.
gi 502628485 506 paatatqDQVMALAVKHADDDDHVAPSHGPE 536
Cdd:NF000106 226 -------GKVDELKTKVGGRTLQIRPAHAAE 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
41-250 |
7.48e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 41 KSFGPVDVLKDITVHVRPGRVQVLLGENGAG--KSTLIKMMSGiyqPDGGRvvvdgKPVHLGSVRDAERLGIATI--HQE 116
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR-----RPWRF*TWCANRRALRRTIg*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 117 LNL--VPSMTVAENVLM-GRLPSrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLIL 193
Cdd:NF000106 93 VR*grRESFSGRENLYMiGR*LD----LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVLRDGALVAE 250
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
48-200 |
7.48e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGiyQPDGGrVVVDGKPVHLGSVRD---AERLGIATiHQELNLvPSMT 124
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRLVNGRPLDssfQRSIGYVQ-QQDLHL-PTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 125 VAENVLMG---RLPSRggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIA-----RQQLVeIAKALSLNARVLI-LDE 195
Cdd:TIGR00956 853 VRESLRFSaylRQPKS---VSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveqRKRLT-IGVELVAKPKLLLfLDE 928
|
....*
gi 502628485 196 PTAAL 200
Cdd:TIGR00956 929 PTSGL 933
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
302-499 |
7.82e-06 |
|
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: 48.86 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 302 VQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgSAVAAGIGHVPEdrkgqglvLDASVAENLG 381
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNI--SDVHQNMGYCPQ--------FDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 382 YATLAATSRAgfadrRGQRSRAQEVASRLRIRMRDV----DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVG 457
Cdd:TIGR01257 2030 REHLYLYARL-----RGVPAEEIEKVANWSIQSLGLslyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502628485 458 ARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGG 499
Cdd:TIGR01257 2105 ARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
296-456 |
8.39e-06 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 48.58 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGsAVAAGIGHVPEDRkgqgLVLDAS 375
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH-TLRQFINYLPQEP----YIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLgyatLAATSRAGFADRRGQRSRAQEVASRLRiRMR-----DVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:TIGR01193 564 ILENL----LLGAKENVSQDEIWAACEIAEIKDDIE-NMPlgyqtELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*.
gi 502628485 451 TRGVDV 456
Cdd:TIGR01193 639 TSNLDT 644
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
297-501 |
1.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.13 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSvgsavaaGIGHVPEDRKGQGLVL---- 372
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPET-------GNKNLKKLRKKVSLVFqfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 ----DASVAENLGYATLaatsRAGFADRRGqRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:PRK13641 96 aqlfENTVLKDVEFGPK----NFGFSEDEA-KEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 449 EPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
49-203 |
1.28e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.08 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLI------KMMSGIyqpdGGRVVVDGKPvhlgsVRDAERLGIATIHQELNLVPS 122
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLdvlagrKTAGVI----TGEILINGRP-----LDKNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 123 MTVaenvlmgrlpsrggfvsrrtmrrlaREALdrvRLDVSLDtpvgELGIARQQLVEIAKALSLNARVLILDEPTAALTG 202
Cdd:cd03232 94 LTV-------------------------REAL---RFSALLR----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
.
gi 502628485 203 S 203
Cdd:cd03232 142 Q 142
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
296-514 |
1.31e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGS-AVAAGIGHVPEDRKGQGLV--L 372
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVATVFQDPEQQIFYtdI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVA---ENLGYATlaatsragfadrrgqrsraQEVASRLRIRMRDVD------QAARDLSGGNQQKIVFGRWVLAGSR 443
Cdd:PRK13638 96 DSDIAfslRNLGVPE-------------------AEITRRVDEALTLVDaqhfrhQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 444 VLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL-----TGELPAATATQDQ 514
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIlthgaPGEVFACTEAMEQ 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
281-467 |
1.53e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.90 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 281 GDEVLLdvrGLSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPpRSVGSAVAAGIGH 360
Cdd:PRK10253 10 GEQLTL---GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 361 VPEDRKGQGlvlDASVAEnlgyatLAATSRAG----FADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGR 436
Cdd:PRK10253 86 LAQNATTPG---DITVQE------LVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190
....*....|....*....|....*....|.
gi 502628485 437 WVLAGSRVLLLDEPTRGVDVGARVEIYELIN 467
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
301-466 |
1.57e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.50 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 301 DVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPP--RSVGS-----------AVAAGIG---Hv 361
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtTTPPsrRPVSMlfqennlfshlTVAQNIGlglN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 362 PedrkgqGLVLDASvaenlgyatlaatsragfadrrgQRSRAQEVASRLRIRmrdvDQAAR---DLSGGNQQKIVFGRWV 438
Cdd:PRK10771 98 P------GLKLNAA-----------------------QREKLHAIARQMGIE----DLLARlpgQLSGGQRQRVALARCL 144
|
170 180
....*....|....*....|....*...
gi 502628485 439 LAGSRVLLLDEPTRGVDVGARVEIYELI 466
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLV 172
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
297-466 |
2.22e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQrlpprSVGSAVAAG-IGHVPE----DRKGQGLV 371
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQALQKNlVAYVPQseevDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 372 LDASVAENLGYAtlaatsraGFADRRGQRSRAQEVASRLRIRMRDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK15056 98 EDVVMMGRYGHM--------GWLRRAKKRDRQIVTAALARVDMVEFrHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170
....*....|....*.
gi 502628485 451 TRGVDVGARVEIYELI 466
Cdd:PRK15056 170 FTGVDVKTEARIISLL 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
56-242 |
2.42e-05 |
|
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: 46.21 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 56 VRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRvvVDGKP---------------VHLGSVRDAErLGIATIHQELNLV 120
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrgselqNYFTKLLEGD-VKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 121 PSmTVAENVlmgrlpsrGGFVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAAL 200
Cdd:cd03236 100 PK-AVKGKV--------GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502628485 201 TGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAIGDEVSVL 242
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
297-455 |
2.52e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGadpydagtvhvdgqRLPPRSVGSAVAAG-IGHVPEdrkgQGLVLDAS 375
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHAETSSVVIRGsVAYVPQ----VSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYATLAATSRAGFA-DRRGQRSRAQEVASRLRIrmrDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGV 454
Cdd:PLN03232 695 VRENILFGSDFESERYWRAiDVTALQHDLDLLPGRDLT---EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
.
gi 502628485 455 D 455
Cdd:PLN03232 772 D 772
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
297-345 |
2.80e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.33 E-value: 2.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRL 345
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL 69
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
274-500 |
2.91e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.96 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 274 PRRTHTPGDEVLLDVRGLS-------RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYD---AGTVHVDGQ 343
Cdd:TIGR00955 11 FGRVAQDGSWKQLVSRLRGcfcrerpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 344 RLPPRSVgSAVAAgigHVPEDrkgQGLVLDASVAENLGYATLAATSRAGFADRRgqRSRAQEVASRLRIR-MRD----VD 418
Cdd:TIGR00955 91 PIDAKEM-RAISA---YVQQD---DLFIPTLTVREHLMFQAHLRMPRRVTKKEK--RERVDEVLQALGLRkCANtrigVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 419 QAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD---VGARVEI-YELINAVAAAGGAVLLVSSDLPEVLgvsDRVL 494
Cdd:TIGR00955 162 GRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmAYSVVQVlKGLAQKGKTIICTIHQPSSELFELF---DKII 238
|
....*.
gi 502628485 495 VMSGGR 500
Cdd:TIGR00955 239 LMAEGR 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
49-216 |
3.01e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQP-DGGRVVVDGKpvhlgsvrdaerlgIATIHQeLNLVPSMTVAE 127
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGS--------------VAYVPQ-VSWIFNATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrlpsrGGFVSRRTMRrlareALDRVRLDVSLD-------TPVGELGI----ARQQLVEIAKALSLNARVLILDEP 196
Cdd:PLN03232 698 NILFG-----SDFESERYWR-----AIDVTALQHDLDllpgrdlTEIGERGVnisgGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180
....*....|....*....|..
gi 502628485 197 TAALTGSETEVLFG--VVEELR 216
Cdd:PLN03232 768 LSALDAHVAHQVFDscMKDELK 789
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
48-248 |
3.45e-05 |
|
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: 45.67 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG-----KPVHlgSVRdaERLGIatIHQE------ 116
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLH--TLR--SRLSI--ILQDpilfsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 117 ---LNLVPSMTVAENVLMGRLPsrggFVSRRTMRRLAREALDRVRLDVSLDTPVGElgiarQQLVEIAKALSLNARVLIL 193
Cdd:cd03288 110 sirFNLDPECKCTDDRLWEALE----IAQLKNMVKSLPGGLDAVVTEGGENFSVGQ-----RQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 194 DEPTAALTGSETEVLFGVVEELRRDDvAMVFISHHLEEIAAiGDEVSVLRDGALV 248
Cdd:cd03288 181 DEATASIDMATENILQKVVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
86-260 |
3.81e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 86 DGGRVVVDGKPVHLGSVRDAERLgIATIHQELNLVpSMTVAENVLMGRLPSrggfvSRRTMRRLAR-EALDRV--RLDVS 162
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKEDA-----TREDVKRACKfAAIDEFieSLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 163 LDTPVGELGIA----RQQLVEIAKALSLNARVLILDEPTAAL-TGSETEVLFGVVEELRRDDVAMVFISHHLEEIAAiGD 237
Cdd:PTZ00265 1348 YDTNVGPYGKSlsggQKQRIAIARALLREPKILLLDEATSSLdSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SD 1426
|
170 180
....*....|....*....|....*..
gi 502628485 238 EVSVL----RDGALVAEvpASTHEDEL 260
Cdd:PTZ00265 1427 KIVVFnnpdRTGSFVQA--HGTHEELL 1451
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
296-467 |
4.71e-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: 44.07 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHvdgqrLPPRsvgsavaAGIGHVPEdrkgQGLVLDAS 375
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----MPEG-------EDLLFLPQ----RPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 VAENLGYAtlaatsragfadrrgqrsraqevasrlrirMRDVdqaardLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:cd03223 80 LREQLIYP------------------------------WDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170
....*....|..
gi 502628485 456 VGARVEIYELIN 467
Cdd:cd03223 124 EESEDRLYQLLK 135
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
299-501 |
4.86e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 44.98 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 299 DIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQ---RLPP----RSVGSAVAAgIGHVPEdrkgqglv 371
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdirEQDPvelrRKIGYVIQQ-IGLFPH-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 372 ldASVAENLGYA-TLAATSRAgfadRRgqRSRAQEVasrlrIRMRDVDQAA------RDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:cd03295 90 --MTVEENIALVpKLLKWPKE----KI--RERADEL-----LALVGLDPAEfadrypHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 445 LLLDEPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQeEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
65-228 |
8.42e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 65 LGENGAGKSTLIKMMSGIYQPDGGRVVVDGKPVHLGSVRDAERLGIATihQELNLVPSMTVAEN-VLMGRLpsrggF-VS 142
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMS--QAFSLYGELTVRQNlELHARL-----FhLP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 143 RRTMRRLAREALDRVRLDVSLDTPVGEL--GIaRQQLvEIAKALSLNARVLILDEPTAaltgsetevlfGV--------- 211
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDSLplGI-RQRL-SLAVAVIHKPELLILDEPTS-----------GVdpvardmfw 437
|
170
....*....|....*....
gi 502628485 212 --VEELRRDDVAMVFISHH 228
Cdd:NF033858 438 rlLIELSREDGVTIFISTH 456
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
40-248 |
8.48e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 43.79 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 40 SKSFGPVDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDG---GRVVVDGKPVH-LGSVRDAErlgIATIHQ 115
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKeFAEKYPGE---IIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 116 ELNLVPSMTVaenvlmgrlpsrggfvsRRTMRRLAREALDRVRLDVSldtpVGElgiarQQLVEIAKALSLNARVLILDE 195
Cdd:cd03233 91 EDVHFPTLTV-----------------RETLDFALRCKGNEFVRGIS----GGE-----RKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 196 PTAALTGSET----EVLFGVVEELRRddVAMVFISHHLEEIAAIGDEVSVLRDGALV 248
Cdd:cd03233 145 STRGLDSSTAleilKCIRTMADVLKT--TTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
286-509 |
9.00e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGLS--RTGVL-HDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADP----YDAGTVHVDGQRLPPRSVGSAVAAGI 358
Cdd:PRK10418 5 IELRNIAlqAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 359 GHVPEDRKGQGLVLDASVAEnlgyaTLAATSRAGFADRRGQRSRAQEVASRLRIrmrdVDQAARDLSGGNQQKIVFGRWV 438
Cdd:PRK10418 85 MQNPRSAFNPLHTMHTHARE-----TCLALGKPADDATLTAALEAVGLENAARV----LKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 439 LAGSRVLLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAAT 509
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLeSIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-232 |
1.20e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 46 VDVLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG----KPVHLG--------------------- 100
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKwwrskigvvsqdpllfsnsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 101 --------SVRDAERL-------GIATiHQELNLVPSMTVAE----NVLMGRLPSRGGFVSRRTMRRLAREALDRVRLDV 161
Cdd:PTZ00265 478 nnikyslySLKDLEALsnyynedGNDS-QENKNKRNSCRAKCagdlNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 162 SL-----------DTPVG----ELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVEELR-RDDVAMVFI 225
Cdd:PTZ00265 557 LIhdfvsalpdkyETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIII 636
|
....*..
gi 502628485 226 SHHLEEI 232
Cdd:PTZ00265 637 AHRLSTI 643
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
49-200 |
1.47e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQP-DGGRVVVDGKpvhlgsvrdaerlgIATIHQeLNLVPSMTVAE 127
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT--------------VAYVPQ-VSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrLPsrggFVSRRTMRRLAREALDRvrlDVSL-----DTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:PLN03130 698 NILFG-SP----FDPERYERAIDVTALQH---DLDLlpggdLTEIGERGVnisgGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
..
gi 502628485 199 AL 200
Cdd:PLN03130 770 AL 771
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-465 |
1.60e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 43.36 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 286 LDVRGL----SRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAG-----ADPYDAGTVHVDGQ---RLPPRSVGSA 353
Cdd:PRK14247 4 IEIRDLkvsfGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQdifKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 354 VAAgIGHVPEDRKGqgLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQ---EVASRLrirmrdvDQAARDLSGGNQQ 430
Cdd:PRK14247 84 VQM-VFQIPNPIPN--LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQlwdEVKDRL-------DAPAGKLSGGQQQ 153
|
170 180 190
....*....|....*....|....*....|....*
gi 502628485 431 KIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYEL 465
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESL 188
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
297-501 |
1.63e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.84 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPprsvgsAVAAGIGHVPEDRKGQGLVLD--- 373
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP------ANLKKIKEVKRLRKEIGLVFQfpe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 -----ASVAENLGYATLAATsragfADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLD 448
Cdd:PRK13645 101 yqlfqETIEKDIAFGPVNLG-----ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 449 EPTRGVDVGAR---VEIYELINAVAAAGGAVLLVSSDlpEVLGVSDRVLVMSGGRL 501
Cdd:PRK13645 176 EPTGGLDPKGEedfINLFERLNKEYKKRIIMVTHNMD--QVLRIADEVIVMHEGKV 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
296-456 |
1.72e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.66 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDA--------GTVHVDGQrlPPRSVGSAVAAGIGHVPEDRKG 367
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGE--PLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 368 QGLVLDASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQaardLSGGNQQKIVFGRwVLA------- 440
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTT----LSGGELARVQFAR-VLAqlwpphd 168
|
170
....*....|....*....
gi 502628485 441 ---GSRVLLLDEPTRGVDV 456
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDL 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-455 |
1.80e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.07 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 300 IDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDaGTVHVDGQ---RLPPRSVGSAVAaGIGHVPedrkgqgLVLDASV 376
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIelrELDPESWRKHLS-WVGQNP-------QLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 377 AENLGYATLAATSRAgfADRRGQRSRAQEVASRL------RIRmrdvDQAARdLSGGNQQKIVFGRWVLAGSRVLLLDEP 450
Cdd:PRK11174 440 RDNVLLGNPDASDEQ--LQQALENAWVSEFLPLLpqgldtPIG----DQAAG-LSVGQAQRLALARALLQPCQLLLLDEP 512
|
....*
gi 502628485 451 TRGVD 455
Cdd:PRK11174 513 TASLD 517
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
294-504 |
1.85e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 43.44 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 294 TGVLHDIDVQVRAGEVVGVAGLVGAGRTELlraiagadpydagTVHVDGQRLPPRsvGSAVAAGI-----GHVPEDRKGQ 368
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTL-------------ALHLNGLLRPQK--GKVLVSGIdtgdfSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 369 GLVLD--------ASVAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRmrdvdqAARDLSGGNQQKIVFGRWVLA 440
Cdd:PRK13644 80 GIVFQnpetqfvgRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHR------SPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 441 GSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEvLGVSDRVLVMSGGRLTGE 504
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
48-95 |
2.12e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGI--YQPDGGRVVVDGK 95
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGK 65
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
61-245 |
2.46e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.59 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 61 VQVLLGENGAGKSTLIKMMS----GIYQPDGGRVVVDGKPVhlgsvRDAERLGIATIHQELN------LVPSMTVAENVL 130
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLI-----REGEVRAQVKLAFENAngkkytITRSLAILENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 131 mgrlpsrggFVSRRTMRRLAREALDRV----RLDVSLdtpvgelgIARqqlVEIAKALSLNARVLILDEPTAAL-TGSET 205
Cdd:cd03240 99 ---------FCHQGESNWPLLDMRGRCsggeKVLASL--------IIR---LALAETFGSNCGILALDEPTTNLdEENIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502628485 206 EVLFGVVEELRRDDV-AMVFISHHLEEIAAIGDEVSVLRDG 245
Cdd:cd03240 159 ESLAEIIEERKSQKNfQLIVITHDEELVDAADHIYRVEKDG 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
296-462 |
2.91e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGAdpydagTVHVDgqrlppRSVGSAVAAGiGHVPEDRKGQ--GLVLD 373
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASN------TDGFH------IGVEGVITYD-GITPEEIKKHyrGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAEN-LGYATLAATsrAGFADR-RGQRSRAQEVASRLRI-RMRDVDQAA----------------RDLSGGNQQKIVF 434
Cdd:TIGR00956 143 NAETDVhFPHLTVGET--LDFAARcKTPQNRPDGVSREEYAkHIADVYMATyglshtrntkvgndfvRGVSGGERKRVSI 220
|
170 180
....*....|....*....|....*...
gi 502628485 435 GRWVLAGSRVLLLDEPTRGVDVGARVEI 462
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEF 248
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
49-232 |
3.16e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKpvhlgsvrdaerLGIATIHQELNlvPSMTVAEN 128
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------VSVIAISAGLS--GQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 129 VLMGRLPSrgGFvSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVL 208
Cdd:PRK13546 106 IEFKMLCM--GF-KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|....
gi 502628485 209 FGVVEELRRDDVAMVFISHHLEEI 232
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQV 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
296-467 |
3.26e-04 |
|
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: 40.89 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGqrlpprsvgsavAAGIGHVPEdrkgqglvldas 375
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 vaenlgyatlaatsragfadrrgqrsraqevasrlrirmrdvdqaardLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170
....*....|..
gi 502628485 456 VGARVEIYELIN 467
Cdd:cd03221 103 LESIEALEEALK 114
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
283-455 |
3.99e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.46 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYD-----AGTVHVDGQRL-PPRSvgs 352
Cdd:PRK14239 3 EPILQVSDLSvyynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIySPRT--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 353 avaagigHVPEDRKGQGLVLDA------SVAENLGYA-TLAATSRAGFADRRGQRSRAQ-----EVASRLRirmrdvdQA 420
Cdd:PRK14239 80 -------DTVDLRKEIGMVFQQpnpfpmSIYENVVYGlRLKGIKDKQVLDEAVEKSLKGasiwdEVKDRLH-------DS 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 502628485 421 ARDLSGGNQQKIVFGRwVLAGS-RVLLLDEPTRGVD 455
Cdd:PRK14239 146 ALGLSGGQQQRVCIAR-VLATSpKIILLDEPTSALD 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
424-501 |
4.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.53 E-value: 4.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502628485 424 LSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
56-94 |
5.17e-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: 41.02 E-value: 5.17e-04
10 20 30
....*....|....*....|....*....|....*....
gi 502628485 56 VRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDG 94
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG 60
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
277-466 |
5.76e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 41.95 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 277 THTPGDEVLLDVRGLS----RTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRA-------IAGAdpYDAGTVHVDGQRL 345
Cdd:COG1117 3 APASTLEPKIEVRNLNvyygDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGA--RVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 346 PPRSVgsavaagigHVPEDRKGQGLV------LDASVAENLGYAtlaatsragfADRRGQRSRAQ--------------- 404
Cdd:COG1117 81 YDPDV---------DVVELRRRVGMVfqkpnpFPKSIYDNVAYG----------LRLHGIKSKSEldeiveeslrkaalw 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502628485 405 -EVASRLrirmrdvDQAARDLSGGNQQKIVFGRwVLAGS-RVLLLDEPTRGVDVGARVEIYELI 466
Cdd:COG1117 142 dEVKDRL-------KKSALGLSGGQQQRLCIAR-ALAVEpEVLLMDEPTSALDPISTAKIEELI 197
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
58-232 |
6.67e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 58 PGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDgkpvhlgsvrDAERLgiatihqelnlvpsmtvaenvlmgrlpsr 137
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI----------DGEDI----------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 138 ggfvsrrtmrrlaREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETEVLFGVVE---- 213
Cdd:smart00382 42 -------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180
....*....|....*....|.
gi 502628485 214 --ELRRDDVAMVFISHHLEEI 232
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDL 129
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
296-466 |
7.64e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLppRSVGSA-VAAGIGHVPedrkgQGLVL-D 373
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI--SKFGLMdLRKVLGIIP-----QAPVLfS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 374 ASVAENL------GYATL-AATSRAGFAD--RRGQRSRAQEVAsrlrirmrdvdQAARDLSGGNQQKIVFGRWVLAGSRV 444
Cdd:PLN03130 1327 GTVRFNLdpfnehNDADLwESLERAHLKDviRRNSLGLDAEVS-----------EAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180
....*....|....*....|..
gi 502628485 445 LLLDEPTRGVDVGARVEIYELI 466
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTI 1417
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
267-465 |
9.75e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.02 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 267 RDITEQYPRRTHTPgdevlldvrglsrtgVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLP 346
Cdd:TIGR00958 482 QDVSFSYPNRPDVP---------------VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 347 P---RSVGSAVAAgIGHVPedrkgqgLVLDASVAENLGY-------ATLAATSRAGFADrrgqrSRAQEVASRLRIrmrD 416
Cdd:TIGR00958 547 QydhHYLHRQVAL-VGQEP-------VLFSGSVRENIAYgltdtpdEEIMAAAKAANAH-----DFIMEFPNGYDT---E 610
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502628485 417 VDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYEL 465
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES 659
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
283-501 |
1.17e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.56 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 283 EVLLDVRGLSrTGVlHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSAVAAGIGHVP 362
Cdd:PRK10070 32 EQILEKTGLS-LGV-KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 363 EDRKGQGLVLDASVAENLGYATlaatSRAGFAdrrGQRSRAQEVASRLRIRMRDVDQAARD-LSGGNQQKIVFGRWVLAG 441
Cdd:PRK10070 110 MVFQSFALMPHMTVLDNTAFGM----ELAGIN---AEERREKALDALRQVGLENYAHSYPDeLSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502628485 442 SRVLLLDEPTRGVDVGARVEIY-ELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
297-504 |
1.21e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.92 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSavaagigHVPEDRKGQGLVLDASV 376
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDK-------YIRPVRKRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 377 AEnLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRM---RDV-DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTR 452
Cdd:PRK13646 96 SQ-LFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfsRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502628485 453 GVDVGARVEIYELINAVAAAGGAV-LLVSSDLPEVLGVSDRVLVMSGGRLTGE 504
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTiILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
58-237 |
1.22e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 58 PGRVQVLLGENGAGKSTLIKMMSgiyqpdggrVVVDGKPVHLGSVRDAerlgiatihqelnlvpsmtvaenvlmgrlpSR 137
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGV------------------------------KA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 138 GGFVsrrtmrrlAREALDRVRLDVSLDTpvGElgiarQQLVEIAKALSLNAR----VLILDEPTAALTGSETEVLFGVVE 213
Cdd:cd03227 61 GCIV--------AAVSAELIFTRLQLSG--GE-----KELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....
gi 502628485 214 ElRRDDVAMVFISHHLEEIAAIGD 237
Cdd:cd03227 126 E-HLVKGAQVIVITHLPELAELAD 148
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
300-508 |
1.59e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 300 IDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYD----AGTVHVDG---QRLPPRSVGSAVAAGIGHVPEDRkgqglVL 372
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgrvmAEKLEFNGqdlQRISEKERRNLVGAEVAMIFQDP-----MT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 373 DASVAENLGYATLAATSRAGFADRRGQRSRAQEV---------ASRLrirmrdvDQAARDLSGGNQQKIVFGRWVLAGSR 443
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLlnqvgipdpASRL-------DVYPHQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502628485 444 VLLLDEPTRGVDVGARVEIYE-LINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLTGELPAA 508
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIElLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-324 |
1.69e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 139 GFVSRRTMrrLAREALDRVRLDVSLDTPVGelgiARQQLVEIAKAL--SLNARVLILDEPTAALTGSETEVLFGVVEELr 216
Cdd:PRK00635 452 GLKSRLSI--LIDLGLPYLTPERALATLSG----GEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKKL- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 217 RDDVAMVFISHHLEEIAAIGDEVSVLRDGALV--AEVPASTHEDELvrLMVGRDITEQYPR----------RTHTPGDEV 284
Cdd:PRK00635 525 RDQGNTVLLVEHDEQMISLADRIIDIGPGAGIfgGEVLFNGSPREF--LAKSDSLTAKYLRqeltipipekRTNSLGTLT 602
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502628485 285 LLDvrglSRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELL 324
Cdd:PRK00635 603 LSK----ATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLI 638
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
48-200 |
2.18e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.05 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 48 VLKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDggrvvvDGKPVHLGSvrdaerlgIATIHQELNLVPSmTVAE 127
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS------EGKIKHSGR--------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 128 NVLMGrlpsrggfVSRRTMRRLAREALDRVRLDVSL-----DTPVGELGI----ARQQLVEIAKALSLNARVLILDEPTA 198
Cdd:TIGR01271 506 NIIFG--------LSYDEYRYTSVIKACQLEEDIALfpekdKTVLGEGGItlsgGQRARISLARAVYKDADLYLLDSPFT 577
|
..
gi 502628485 199 AL 200
Cdd:TIGR01271 578 HL 579
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
41-122 |
2.21e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.95 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 41 KSFGPVdvlKDITVHVRPgrVQVLLGENGAGKSTLIKMMSGIYQpdggrvvvdGKPVHLGsvrdAERLGIATIHQELNLV 120
Cdd:COG4938 7 KNFGPF---KEAELELKP--LTLLIGPNGSGKSTLIQALLLLLQ---------SNFIYLP----AERSGPARLYPSLVRE 68
|
..
gi 502628485 121 PS 122
Cdd:COG4938 69 LS 70
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
268-467 |
2.56e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.58 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 268 DITEQ-----YPRRTHTPGDEVLLDVRGLSRT------GVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGA-DPyDA 335
Cdd:PRK11160 316 EITEQkpevtFPTTSTAAADQVSLTLNNVSFTypdqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAwDP-QQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 336 GTVHVDGQRLPPRSvGSAVAAGIGHVPedrkgQGL-VLDASVAENLGYATLAATSragfadrrgqrSRAQEVASRLRIR- 413
Cdd:PRK11160 395 GEILLNGQPIADYS-EAALRQAISVVS-----QRVhLFSATLRDNLLLAAPNASD-----------EALIEVLQQVGLEk 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502628485 414 MRDVDQA--------ARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELIN 467
Cdd:PRK11160 458 LLEDDKGlnawlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA 519
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
49-232 |
2.63e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKMMSGIYQPDGGRVVVDGKP--VHLGSVRDAERLGIATIhqELnlvpsmtva 126
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTGIENI--EL--------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 127 ENVLMGrlpsrggfVSRRTMRRLAREALDRVRLDVSLDTPVGELGIARQQLVEIAKALSLNARVLILDEPTAALTGSETE 206
Cdd:PRK13545 109 KGLMMG--------LTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|....*.
gi 502628485 207 VLFGVVEELRRDDVAMVFISHHLEEI 232
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
418-517 |
3.63e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.40 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 418 DQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSS-DLPEVLGVSDRVLVM 496
Cdd:PRK13652 132 DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSThQLDLVPEMADYIYVM 211
|
90 100
....*....|....*....|..
gi 502628485 497 SGGRLTGE-LPAATATQDQVMA 517
Cdd:PRK13652 212 DKGRIVAYgTVEEIFLQPDLLA 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
296-501 |
4.37e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 39.30 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 296 VLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTV-------HVDGQRLPPRSVGSAVAAG------IGHVP 362
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKEKVLEKLVIQktrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 363 EDRKGQGLVLdaSVAEnlgYATLAATSRAGFAdrRGQRS------RAQEVASRLrIRMRDVDQ-----AARDLSGGnqQK 431
Cdd:PRK13651 102 EIRRRVGVVF--QFAE---YQLFEQTIEKDII--FGPVSmgvskeEAKKRAAKY-IELVGLDEsylqrSPFELSGG--QK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502628485 432 ivfGRWVLAG-----SRVLLLDEPTRGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRL 501
Cdd:PRK13651 172 ---RRVALAGilamePDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
297-502 |
5.30e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 38.96 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDGQRLPPRSVGSavaagigHVPEDRKGQGLVLdaSV 376
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNK-------DIKQIRKKVGLVF--QF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 377 AENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQAARD-----LSGGNQQKIVFGRWVLAGSRVLLLDEPT 451
Cdd:PRK13649 94 PESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEknpfeLSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502628485 452 RGVDVGARVEIYELINAVAAAGGAVLLVSSDLPEVLGVSDRVLVMSGGRLT 502
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
292-501 |
5.77e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 39.01 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 292 SRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAG---ADPYDAGTVHVDGQRLPPRSVGSaVAAGIGHVPEDRKGQ 368
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTAKTVWD-IREKVGIVFQNPDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 369 glVLDASVAENLGYatlaatsraGFADRRGQRSRAQEVASRL--RIRMRD-VDQAARDLSGGNQQKIVFGRWVLAGSRVL 445
Cdd:PRK13640 97 --FVGATVGDDVAF---------GLENRAVPRPEMIKIVRDVlaDVGMLDyIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502628485 446 LLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLGvSDRVLVMSGGRL 501
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIrKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKL 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
49-230 |
7.48e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 37.69 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 49 LKDITVHVRPGRVQVLLGENGAGKSTLIKmmSGIYQpDGGRVVVDGKPVhlgsvrdAERLGIATIHQELNLVpsmtvaeN 128
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA-SGKARLISFLPK-------FSRNKLIFIDQLQFLI-------D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 129 VLMGRLPsrggfvsrrtmrrlarealdrvrldvsLDTPVGELGIARQQLVEIAKALSLNAR--VLILDEPTAALTGSETE 206
Cdd:cd03238 74 VGLGYLT---------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....
gi 502628485 207 VLFGVVEELRRDDVAMVFISHHLE 230
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
304-458 |
8.27e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 304 VRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDG--------QRLPPRSVgSAVAAGIGHVPEDRKGQGLVLDAS 375
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQ-PALEYVIDGDREYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 376 vAENLGYATLAATSRAGFADRRGQRSRAQEVASRLRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVD 455
Cdd:PRK10636 103 -ERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
...
gi 502628485 456 VGA 458
Cdd:PRK10636 182 LDA 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
263-500 |
8.59e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 38.41 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 263 LMVGRDITEQYPRRthtpgdevlldvRGL----SRTGVLHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTV 338
Cdd:PRK11308 5 LLQAIDLKKHYPVK------------RGLfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 339 HVDGQRL--PPRSVGSAVAAGIGHVPED-------RKGQGLVLDASVAENlgyATLAATSRagfadrrgqRSRAQEVASR 409
Cdd:PRK11308 73 YYQGQDLlkADPEAQKLLRQKIQIVFQNpygslnpRKKVGQILEEPLLIN---TSLSAAER---------REKALAMMAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628485 410 LRIRMRDVDQAARDLSGGNQQKIVFGRWVLAGSRVLLLDEPTRGVDVGARVEIYELI-NAVAAAGGAVLLVSSDLPEVLG 488
Cdd:PRK11308 141 VGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVFISHDLSVVEH 220
|
250
....*....|..
gi 502628485 489 VSDRVLVMSGGR 500
Cdd:PRK11308 221 IADEVMVMYLGR 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
297-342 |
9.18e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 9.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 502628485 297 LHDIDVQVRAGEVVGVAGLVGAGRTELLRAIAGADPYDAGTVHVDG 342
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| |
