|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-496 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 732.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDnIDPRVAVESLDVGYWQMVEIAKALSQDA 161
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLDA 241
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 242 AAKTSFERVERnfeQSGDPVLRVRDFAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEP- 320
Cdd:COG1129 240 ELEDLFPKRAA---APGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPv 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 321 -IKSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLS 399
Cdd:COG1129 317 rIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 400 GGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKEL 479
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
490
....*....|....*..
gi 1054755845 480 SGREIESEEVLHHAIQG 496
Cdd:COG1129 477 DREEATEEAIMAAATGG 493
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-496 |
1.94e-177 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 507.93 E-value: 1.94e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVY---TKDaGQIRIDGQEADLHSVEDA 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HKKGIAMIYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDnIDPRVAVESLDVGYWQMVEIAKAL 157
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 158 SQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDK 237
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 238 MLDAAAKTSFERVERNFeqsGDPVLRVRDF-AYG------NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRN- 309
Cdd:PRK13549 239 MVGRELTALYPREPHTI---GEVILEVRNLtAWDpvnphiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGr 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 310 WTGDVAMRGEP--IKSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIK 387
Cdd:PRK13549 316 WEGEIFIDGKPvkIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 388 ADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRI 467
Cdd:PRK13549 396 TASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRV 475
|
490 500
....*....|....*....|....*....
gi 1054755845 468 LVLYNRTVNKELSGREIESEEVLHHAIQG 496
Cdd:PRK13549 476 LVMHEGKLKGDLINHNLTQEQVMEAALRS 504
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-489 |
6.30e-177 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 506.49 E-value: 6.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKK 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDnIDPRVAVESLDVGYWQMVEIAKALSQD 160
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLD 240
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 241 AAAKTSFERVERnfeQSGDPVLRVRDFAY-----GNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVA 315
Cdd:COG3845 240 REVLLRVEKAPA---EPGEVVLEVENLSVrddrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 316 MRGEPI--KSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQ--MRKGFLIDDKKGADISREYIEKLSIKADSI 391
Cdd:COG3845 317 LDGEDItgLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRppFSRGGFLDRKAIRAFAEELIEEFDVRTPGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 392 KQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLY 471
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMY 476
|
490
....*....|....*...
gi 1054755845 472 NRTVNKELSGREIESEEV 489
Cdd:COG3845 477 EGRIVGEVPAAEATREEI 494
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-470 |
1.61e-167 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 482.49 E-value: 1.61e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMI 85
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDnIDPRVAVESLDVGYWQMVEIAKALSQDAKILV 165
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVES-RDTTMEEIIDKMldaaak 244
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRDQLVQAM------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 245 tsferVERNFE--------QSGDPVLRVRDFAyGNKLA-DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVA 315
Cdd:PRK11288 238 -----VGREIGdiygyrprPLGEVRLRLDGLK-GPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 316 MRGEP--IKSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVR-QMRKGFLIDDKKGADISREYIEKLSIKADSIK 392
Cdd:PRK11288 312 LDGKPidIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRhHLRAGCLINNRWEAENADRFIRSLNIKTPSRE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 393 QMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-494 |
7.74e-159 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 460.41 E-value: 7.74e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVY---TKDaGQIRIDGQEADLHSVEDAHKKG 81
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphgSYE-GEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDnIDPRVAVESLDVGYWQMVEIAKALSQDA 161
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLD-ESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESR--DTTMEEIIDKML 239
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRadEVTEDRIIRGMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 240 DAAAKTSFERVERNFeqsGDPVLRVRDF-AY-----GNK-LADVSFDLYPGEILGLAGLMGSGRTELVESIFGiR---RN 309
Cdd:NF040905 239 GRDLEDRYPERTPKI---GEVVFEVKNWtVYhplhpERKvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG-RsygRN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 310 WTGDVAMRGEPI--KSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIK 387
Cdd:NF040905 315 ISGTVFKDGKEVdvSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 388 ADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRI 467
Cdd:NF040905 395 TPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRI 474
|
490 500
....*....|....*....|....*..
gi 1054755845 468 LVLYNRTVNKELSGREIeSEEVLHHAI 494
Cdd:NF040905 475 YVMNEGRITGELPREEA-SQERIMRLI 500
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-493 |
5.21e-149 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 435.63 E-value: 5.21e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAM 84
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYItrewkkgGLIDDRKNMKKAEELLKWLEIdNIDPRVAVESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILF-------GLPKRQASMQKMKQLLAALGC-QLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLDAAAK 244
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAARE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 245 TSFERVE---------RNFEQSGDPVLRVRDFAyGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVA 315
Cdd:PRK15439 243 KSLSASQklwlelpgnRRQQAAGAPVLTVEDLT-GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 316 MRGEPIK--SKKDAMNKGIALVPEDRRQEGLILQHSIKSNfmLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQ 393
Cdd:PRK15439 322 LNGKEINalSTAQRLARGLVYLPEDRQSSGLYLDAPLAWN--VCALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 394 MAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNR 473
Cdd:PRK15439 400 AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
490 500
....*....|....*....|
gi 1054755845 474 TVNKELSGREIESEEVLHHA 493
Cdd:PRK15439 480 EISGALTGAAINVDTIMRLA 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-494 |
8.32e-148 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 432.12 E-value: 8.32e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKG 81
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENIYITREWKKG-GLIDDRKNMKKAEELLKWLEIDNiDPRVAVESLDVGYWQMVEIAKALSQD 160
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNRfGRIDWKKMYAEADKLLARLNLRF-SSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLD 240
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 241 AAAKTSFERVERnfeQSGDPVLRVRDFAyGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEP 320
Cdd:PRK10762 240 RKLEDQYPRLDK---APGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 321 I--KSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQM-RKGFLIDDKKGADISREYIEKLSIKADSIKQMAML 397
Cdd:PRK10762 316 VvtRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFsRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNK 477
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
|
490
....*....|....*..
gi 1054755845 478 ELSGREIESEEVLHHAI 494
Cdd:PRK10762 476 EFTREQATQEKLMAAAV 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-493 |
8.21e-145 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 424.14 E-value: 8.21e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 8 MHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMIYQ 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 88 EFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDnIDPRVAVESLDVGYWQMVEIAKALSQDAKILVMD 167
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDID-IDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 168 EPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLdaaAKTSF 247
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMV---GRSLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 248 ERVERNFEQSGDPVLRVRDFAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKK 325
Cdd:PRK10982 237 QRFPDKENKPGEVILEVRNLTSLRQpsIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 326 --DAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQMRKGF-LIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGN 402
Cdd:PRK10982 317 anEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVgLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 403 QQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGR 482
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTK 476
|
490
....*....|.
gi 1054755845 483 EIESEEVLHHA 493
Cdd:PRK10982 477 TTTQNEILRLA 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-488 |
3.04e-144 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 423.43 E-value: 3.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKK 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIYITREWKKG----GLIDDRKNMKKAEELLKWLEIdNIDPRVAVESLDVGYWQMVEIAKA 156
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 157 LSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIID 236
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 237 KMLDAAAKTSFERVERNFEQ-SGDPVLRVRDFAY--GNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGD 313
Cdd:PRK09700 240 LMVGRELQNRFNAMKENVSNlAHETVFEVRNVTSrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 314 VAMRGEPI--KSKKDAMNKGIALVPEDRRQEGLILQHSIKSNF-MLPSVRQMR-KGF--LIDDKKGADISREYIEKLSIK 387
Cdd:PRK09700 320 IRLNGKDIspRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMaISRSLKDGGyKGAmgLFHEVDEQRTAENQRELLALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 388 ADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRI 467
Cdd:PRK09700 400 CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
|
490 500
....*....|....*....|.
gi 1054755845 468 LVLYNRTVNKELSGREIESEE 488
Cdd:PRK09700 480 AVFCEGRLTQILTNRDDMSEE 500
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-494 |
3.34e-131 |
|
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: 389.95 E-value: 3.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDA--GQIRIDGQEADLHSVEDAHKKGI 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMIYQEFSLLPAMSVAENIYITREWK-KGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALSQDA 161
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITlPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLDA 241
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 242 AAKTSFERVErnfEQSGDPVLRVRDFA-------YGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRN-WTGD 313
Cdd:TIGR02633 241 EITSLYPHEP---HEIGDVILEARNLTcwdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGkFEGN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 314 VAMRGEP--IKSKKDAMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSI 391
Cdd:TIGR02633 318 VFINGKPvdIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 392 KQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLY 471
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIG 477
|
490 500
....*....|....*....|...
gi 1054755845 472 NRTVNKELSGREIESEEVLHHAI 494
Cdd:TIGR02633 478 EGKLKGDFVNHALTQEQVLAAAL 500
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
258-472 |
1.56e-82 |
|
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: 253.51 E-value: 1.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 258 GDPVLRVRDFAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPI--KSKKDAMNKGIALV 335
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEDRRQEGLILQHSIKSNFMLPSvrqmrkgfliddkkgadisreyieklsikadsikqmamLLSGGNQQKIVLGKWLARG 415
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSS--------------------------------------LLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 416 PRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-223 |
3.52e-80 |
|
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: 246.57 E-value: 3.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMI 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQefsllpamsvaeniyitrewkkggliddrknmkkaeellkwleidnidprvavesLDVGYWQMVEIAKALSQDAKILV 165
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVAT 223
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-492 |
1.65e-69 |
|
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: 230.56 E-value: 1.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNG--VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDA---GQIRIDGQEADLHSVEDA 77
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HKKgIAMIYQEF--SLLPaMSVAENIyitREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAK 155
Cdd:COG1123 82 GRR-IGMVFQDPmtQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVAtvesrDTTMEEI 234
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE-----DGPPEEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 235 ID--KMLDAA-AKTSFERVERNFEQSGDPVLRVRD--FAYGNK-------LADVSFDLYPGEILGLAGLMGSGRTELVES 302
Cdd:COG1123 231 LAapQALAAVpRLGAARGRAAPAAAAAEPLLEVRNlsKRYPVRgkggvraVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 303 IFGIRRNWTGDVAMRGEPIKSKKDAMnkgialVPEDRRQEGLILQHSIKSNFMLPSVRQ-----MRKGFLIDDKKGADIS 377
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRS------LRELRRRVQMVFQDPYSSLNPRMTVGDiiaepLRLHGLLSRAERRERV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 378 REYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSE 456
Cdd:COG1123 385 AELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1054755845 457 LSeLVAA-CDRILVLYNrtvnkelsGREIES---EEVLHH 492
Cdd:COG1123 465 LA-VVRYiADRVAVMYD--------GRIVEDgptEEVFAN 495
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-242 |
4.07e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 4.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAMI 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE--DVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIdPRVAVESLDVGYWQMVEIAKALSQDAKILV 165
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYG---LPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVAtvesrDTTMEEIIDKMLDAA 242
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVA-----DGTPDELKARLLEDV 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-242 |
5.39e-52 |
|
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: 176.59 E-value: 5.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAM 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE--DVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENI-YITREWKkgglIDDRKNMKKAEELLKWLEIDNI-DPRvaVESLDVGYWQMVEIAKALSQDAK 162
Cdd:COG4555 79 LPDERGLYDRLTVRENIrYFAELYG----LFDEELKKRIEELIELLGLEEFlDRR--VGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 163 ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVAtVESRDTTMEEIIDKMLDAA 242
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVA-QGSLDELREEIGEENLEDA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-215 |
3.32e-51 |
|
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: 174.16 E-value: 3.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMI 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMK-------KAEELLKWLEIDNIDPRVAvESLDVGYWQMVEIAKALS 158
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARReereareRAEELLERVGLADLADRPA-GELSYGQQRRLEIARALA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 159 QDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-215 |
2.23e-48 |
|
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: 167.14 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENIYITREWKKGGLI------------DDRKNMKKAEELLKWLEIDNIDPRVAvESLDVGYWQ 149
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPA-GNLSYGQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-218 |
3.57e-45 |
|
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: 156.02 E-value: 3.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAMI 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITrewkKGgliddrknMKKaeellkwleidnidpRVAvesldvgywqmveIAKALSQDAKILV 165
Cdd:cd03230 79 PEEPSLYENLTVRENLKLS----GG--------MKQ---------------RLA-------------LAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-218 |
5.65e-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: 151.52 E-value: 5.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEdAHKKGIAMI 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--DVTGVP-PERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYItrewkkgGLidDRKNMKKAE------ELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQ 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAF-------GL--KLRGVPKAEirarvrELLELVGLEGLLNR-YPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 160 DAKILVMDEPTSSL---SKTETKALFKVIrqLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03259 148 EPSLLLLDEPLSALdakLREELREELKEL--QRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-222 |
9.51e-41 |
|
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: 145.50 E-value: 9.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeadlHSVEDAHKKGIAMI 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAEN-IYITRewkkggliddRKNMKKAE---ELLKWLEIDNIDPR--VAVESLDVGYWQMVEIAKALSQ 159
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQ----------LKGLKKEEarrRIDEWLERLELSEYanKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-245 |
1.01e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.87 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIekqfNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGI 82
Cdd:COG1129 254 EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMI---YQEFSLLPAMSVAENIYIT--REWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKAL 157
Cdd:COG1129 330 AYVpedRKGEGLVLDLSIRENITLAslDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 158 SQDAKILVMDEPTSSL---SKTEtkaLFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEI 234
Cdd:COG1129 410 ATDPKVLILDEPTRGIdvgAKAE---IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAI 486
|
250
....*....|.
gi 1054755845 235 IDKMLDAAAKT 245
Cdd:COG1129 487 MAAATGGAAAA 497
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-218 |
6.28e-40 |
|
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: 142.33 E-value: 6.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVED-AHKKGIAM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIyitrewkkggliddrknmkkaeellkwleidnidprvaVESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:cd03229 81 VFQDFALFPHLTVLENI--------------------------------------ALGLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
3.91e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.71 E-value: 3.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlhsVEDAHKKGIAM 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-----LDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENI-YITRewkkggliddRKNMKKAE---ELLKWLEIDNIDPR--VAVESLDVGYWQMVEIAKALS 158
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvYLAR----------LKGLSKAEakrRADEWLERLGLGDRanKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 159 QDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-171 |
5.81e-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: 138.55 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeADLHSVEDAHKKGIAMIYQEFSLLPAMSVAEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ-DLTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 101 IYITREwkKGGLIDDRKNMkKAEELLKWLEIDNIDPRVAVE---SLDVGYWQMVEIAKALSQDAKILVMDEPTS 171
Cdd:pfam00005 80 LRLGLL--LKGLSKREKDA-RAEEALEKLGLGDLADRPVGErpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-218 |
1.48e-37 |
|
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: 137.24 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNG----VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAH-- 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEI-DNIDPRVAveSLDVGYWQMVEIAKAL 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLgDRLNHYPS--ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 158 SQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMaEVFEICDRVTILRDG 218
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
2.08e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.62 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEdAHKK 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR--DVTGLP-PEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENI-YitrewkkgGLidDRKNMKKAEellkwleidnIDPRVAvESLDV-------------- 145
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVaF--------GL--RMRGVPKAE----------IRARVA-ELLELvglegladryphql 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 146 --GYWQMVEIAKALSQDAKILVMDEPTSSLSK-------TETKALfkvirqLKEKGISIIYISHRMAEVFEICDRVTILR 216
Cdd:COG3842 137 sgGQQQRVALARALAPEPRVLLLDEPLSALDAklreemrEELRRL------QRELGITFIYVTHDQEEALALADRIAVMN 210
|
...
gi 1054755845 217 DGV 219
Cdd:COG3842 211 DGR 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-218 |
3.03e-37 |
|
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: 136.06 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNG--VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAM 84
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQ---------------EFSLlpamsvaENIYITREWKKggliddrknmKKAEELLKWLEIDNIDPRVaVESLDVGYWQ 149
Cdd:cd03225 80 VFQnpddqffgptveeevAFGL-------ENLGLPEEEIE----------ERVEEALELVGLEGLRDRS-PFTLSGGQKQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-218 |
1.47e-36 |
|
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: 134.77 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIYQ-------- 87
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQnpddqlfa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 88 -------EFSLlpamsvaENIYITREWkkgglIDDRknmkkAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQD 160
Cdd:COG1122 91 ptveedvAFGP-------ENLGLPREE-----IRER-----VEEALELVGLEHLADR-PPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-492 |
2.82e-36 |
|
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: 140.98 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNG----VPVLKKMNFSLKKGEVHALLGGNGAGKS----TLMKILNGVYTKDAGQIRIDGQ----- 67
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 68 -EADLHSVedahkKG--IAMIYQE--FSLLPAMSVAENIYITREWKKGglIDDRKNMKKAEELLKWLEIDniDPRVAVES 142
Cdd:COG4172 82 sERELRRI-----RGnrIAMIFQEpmTSLNPLHTIGKQIAEVLRLHRG--LSGAAARARALELLERVGIP--DPERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 143 ----LDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRD 217
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 218 GvnvATVESRDTtmEEIID-------KMLDAAAKTsfeRVERNFEQSGDPVLRVRDF---------------AYGNKLAD 275
Cdd:COG4172 233 G---EIVEQGPT--AELFAapqhpytRKLLAAEPR---GDPRPVPPDAPPLLEARDLkvwfpikrglfrrtvGHVKAVDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 276 VSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNwTGDVAMRGEPIkskkDAMNKGiALVPEdRRQ-------------- 341
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDL----DGLSRR-ALRPL-RRRmqvvfqdpfgslsp 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 ---------EGLILqHSIKsnfmlPSVRQMRkgfliddkkgaDISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWL 412
Cdd:COG4172 378 rmtvgqiiaEGLRV-HGPG-----LSAAERR-----------ARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARAL 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 413 ARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSeLVAA-CDRILVLYNrtvnkelsGREIES---E 487
Cdd:COG4172 441 ILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLA-VVRAlAHRVMVMKD--------GKVVEQgptE 511
|
....*
gi 1054755845 488 EVLHH 492
Cdd:COG4172 512 QVFDA 516
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
5.47e-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: 133.57 E-value: 5.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVE-DAH 78
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDiTGLSEKElYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQEFSLLPAMSVAENI-YITREWKKgglIDDRKNMKKAEELLKWLEIDNIDP------------RVAvesldv 145
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVaFPLREHTD---LSEAEIRELVLEKLELVGLPGAADkmpselsggmrkRVA------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 146 gywqmveIAKALSQDAKILVMDEPTSSL---SKTETKALfkvIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDGVNV 221
Cdd:COG1127 152 -------LARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*
gi 1054755845 222 AtvesrDTTMEEIID 236
Cdd:COG1127 222 A-----EGTPEELLA 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-219 |
7.08e-36 |
|
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: 132.27 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVE-DAHKKGIAM 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWKKGglIDDRKNMKKAEELLKwleidnidpRVAVE--------SLDVGYWQMVEIAKA 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLE---------KVGLAdkadaypaQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 157 LSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
259-493 |
1.84e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRD--FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnKGIAL 334
Cdd:COG1121 4 MPAIELENltVSYGGRPVleDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR----RRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 335 VPedrrQeglilQHSIKSNFMLpSVRQM-------RKGFL-IDDKKGADISREYIEKLSI--KADsiKQMAMLlSGGNQQ 404
Cdd:COG1121 80 VP----Q-----RAEVDWDFPI-TVRDVvlmgrygRRGLFrRPSRADREAVDEALERVGLedLAD--RPIGEL-SGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 405 KIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLyNRTVNKELSGREI 484
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEV 225
|
....*....
gi 1054755845 485 ESEEVLHHA 493
Cdd:COG1121 226 LTPENLSRA 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-215 |
3.48e-35 |
|
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: 130.73 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSvedahkKGIAMIY 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 87 QEFSLLPAM--SVAENIYITREWKKGGL-IDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKI 163
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGLFrRLSKADKAKVDEALERVGLSELADR-QIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 164 LVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-218 |
5.57e-35 |
|
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: 130.78 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHS---VEDA 77
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HKKgIAMIYQEFSLLPAMSVAENIYITRE---WKKggliDDRKnmKKAEELLKWLEI-DNIDPRVAveSLDVGYWQMVEI 153
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEiagVPK----AEIE--ERVLELLELVGLeDKADAYPA--QLSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 154 AKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-218 |
6.50e-35 |
|
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: 130.36 E-value: 6.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAHkKGIAM 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLPMHKRAR-LGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIDPRVAVeSLDVGYWQMVEIAKALSQDAKIL 164
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
8.05e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 8.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEAdlhsveDAHKK 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSL---LPaMSVAENIYITReWKKGGLID--DRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAK 155
Cdd:COG1121 76 RIGYVPQRAEVdwdFP-ITVRDVVLMGR-YGRRGLFRrpSRADREAVDEALERVGLEDLADR-PIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 156 ALSQDAKILVMDEPTSSL-SKTEtKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVdAATE-EALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-222 |
8.69e-35 |
|
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: 130.55 E-value: 8.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAHKkgIA 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRELARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYITRE-WKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAK 162
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYpHLGLFGRPSAEDREAVEEALERTGLEHLADR-PVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 163 ILVMDEPTSSL---SKTEtkaLFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:COG1120 158 LLLLDEPTSHLdlaHQLE---VLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-471 |
2.32e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 136.52 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNIEKQFNG----VPVLKKMNFSLKKGEVHALLGGNGAGKS----TLMKILNgvytKDAGQIRIDG------- 66
Cdd:PRK10261 9 ARDVLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLE----QAGGLVQCDKmllrrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 67 -QEADLHSVEDAHKKG-----IAMIYQE--FSLLPAMSVAENIYITREWKKGglIDDRKNMKKAEELLKWLEIDNIDPRV 138
Cdd:PRK10261 85 rQVIELSEQSAAQMRHvrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVRIPEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 139 A--VESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:PRK10261 163 SryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 216 RDG--VNVATVESRDTTMEEIIDKMLDAA-------------------AKTSFERVERNFEQ----SGDPVLRVRDFAYG 270
Cdd:PRK10261 243 YQGeaVETGSVEQIFHAPQHPYTRALLAAvpqlgamkgldyprrfpliSLEHPAKQEPPIEQdtvvDGEPILQVRNLVTR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 271 ---------------NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIK----SKKDAMNKG 331
Cdd:PRK10261 323 fplrsgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 332 IALVPEDrRQEGLILQHSIKSNFMLPsvrqMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKW 411
Cdd:PRK10261 403 IQFIFQD-PYASLDPRQTVGDSIMEP----LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 412 LARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLY 471
Cdd:PRK10261 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMY 538
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-219 |
3.03e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.24 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDA- 77
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQ--DISSLSERe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 ----HKKGIAMIYQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDN-IDPRVAveSLDVGYWQMVE 152
Cdd:COG1136 80 larlRRRHIGFVFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDrLDHRPS--QLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 153 IAKALSQDAKILVMDEPTSSL-SKTeTKALFKVIRQL-KEKGISIIYISHRMaEVFEICDRVTILRDGV 219
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLdSKT-GEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-218 |
3.13e-34 |
|
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: 126.73 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNG--VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIA 83
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLpAMSVAENIyitrewkkggliddrknmkkaeellkwleidnidprvavesLDVGYWQMVEIAKALSQDAKI 163
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 164 LVMDEPTSSL-SKTEtKALFKVIRQLKeKGISIIYISHRMAEVfEICDRVTILRDG 218
Cdd:cd03228 118 LILDEATSALdPETE-ALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-218 |
3.84e-34 |
|
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: 128.51 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVeDAHKKGIAMI 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK--DITNL-PPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPrvavESLDVGYWQMVEIAKALSQDAKILV 165
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP----SQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-218 |
8.14e-34 |
|
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: 125.05 E-value: 8.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIY 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-IGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 87 QefsllpamsvaeniyitrewkkggliddrknmkkaeellkwleidnidprvavesLDVGYWQMVEIAKALSQDAKILVM 166
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 167 DEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-222 |
1.97e-33 |
|
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: 126.01 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMI 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKGGLIDDRknMKKAEELLkwleidnidPRVA------VESLDVGYWQMVEIAKALSQ 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKAR--LERVYELF---------PRLKerrkqlAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-218 |
2.57e-33 |
|
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: 125.41 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADlHSVEDAHKKGIAMI 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFslLPAMSVAENIYItrewkKGGLIDDRKnmKKAEELLKWLEIDNIdPRVAVESLDVGYWQMVEIAKALSQDAKILV 165
Cdd:cd03268 80 APGF--YPNLTARENLRL-----LARLLGIRK--KRIDEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-222 |
3.66e-33 |
|
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: 125.17 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeADLHSVEDAHKKG 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENI-YITREWkkgGLidDRKNMKKA-EELLKWLEI-DNIDPRVavESLDVGYWQMVEIAKALS 158
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeYFAGLY---GL--KGDELTARlEELADRLGMeELLDRRV--GGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 159 QDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
267-475 |
6.14e-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: 124.57 E-value: 6.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkdAMNKGIALVPEdrrqegl 344
Cdd:cd03235 7 VSYGGHPVleDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQ------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ilQHSIKSNFMLpSVRQM--------RKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLlSGGNQQKIVLGKWLARGP 416
Cdd:cd03235 76 --RRSIDRDFPI-SVRDVvlmglyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGEL-SGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 417 RVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLyNRTV 475
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-466 |
1.44e-32 |
|
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: 130.31 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV--YTKDAGQI--------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 63 -------RIDGQEADLHSVEDAHK----KGIAMIYQE-FSLLPAMSVAENIyiTREWKKGGLiDDRKNMKKAEELLKWLE 130
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRrrirKRIAIMLQRtFALYGDDTVLDNV--LEALEEIGY-EGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 131 IDNIDPRVAVEsLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEIC 209
Cdd:TIGR03269 158 LSHRITHIARD-LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 210 DRVTILRDGVNVatvesRDTTMEEIIDKMLDAAakTSFERvERNFEQsGDPVLRVRDFA--YGN------KLAD-VSFDL 280
Cdd:TIGR03269 237 DKAIWLENGEIK-----EEGTPDEVVAVFMEGV--SEVEK-ECEVEV-GEPIIKVRNVSkrYISvdrgvvKAVDnVSLEV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 281 YPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMR-GEPI--KSKKDAMNKGIAlvpedRRQEGLILQH-------SI 350
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWvdMTKPGPDGRGRA-----KRYIGILHQEydlyphrTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 KSNFM------LPSVRQMRKGFLIDDKKGADisreyiEKlsiKADSI-KQMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:TIGR03269 383 LDNLTeaigleLPDELARMKAVITLKMVGFD------EE---KAEEIlDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDR 466
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDR 497
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-218 |
5.30e-32 |
|
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: 122.68 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF-NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE--ADLHSVEDAHKKGI 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMIYQEFSLLPAMSVAENIYITR-----EWKKGGLIDDRKNMKKAEELLKWLEI-DNIDPRVAveSLDVGYWQMVEIAKA 156
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALERVGLlDKAYQRAD--QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 157 LSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-222 |
1.09e-31 |
|
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: 119.85 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeadlhSVEDAHKKGIAmiy 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK-----DLASLSPKELA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 87 QEFSLLPamsvaeniyitrewkkggliddrknmkkaeELLKWLEIDNIDPRVaVESLDVGYWQMVEIAKALSQDAKILVM 166
Cdd:cd03214 73 RKIAYVP------------------------------QALELLGLAHLADRP-FNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 167 DEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-219 |
1.23e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.80 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHsvedAHKKGIAM 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvTDLP----PKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENI-YitrewkkgGLidDRKNMKKAEellkwleidnIDPRV--AVESLDVGYW------------- 148
Cdd:COG3839 80 VFQSYALYPHMTVYENIaF--------PL--KLRKVPKAE----------IDRRVreAAELLGLEDLldrkpkqlsggqr 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 149 QMVEIAKALSQDAKILVMDEPTSSL---SKTETKALfkvIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLdakLRVEMRAE---IKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
262-472 |
2.34e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.94 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPE 337
Cdd:COG1131 1 IEVRGltKRYGDKTAldGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DrrqeglilqhsiksnFMLP---SVRQ----MRKGFLIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGK 410
Cdd:COG1131 81 E---------------PALYpdlTVREnlrfFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 411 WLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-218 |
3.13e-31 |
|
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: 120.52 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDahkKGIAMI 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMK-KAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALSQDAKIL 164
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRaKVHELLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-219 |
4.17e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 119.28 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLhsveDAHKKGIAM 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvTDL----PPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvaveSLDVGYWQMVEIAKALSQDAKIL 164
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK----QLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 165 VMDEPTSSL-SKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:cd03301 153 LMDEPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-218 |
2.75e-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: 117.61 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDA--- 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK--DLLKLSRRlrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 -HKKGIAMIYQE--FSLLPAMSVAENIyitRE--WKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVE 152
Cdd:cd03257 79 iRRKEIQMVFQDpmSSLNPRMTIGEQI---AEplRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 153 IAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-237 |
4.19e-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: 124.18 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH-KKGIAMIYQEFSLLPA 94
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI--DLRQIDPASlRRQIGVVLQDVFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 mSVAENIYITREWkkgglIDDrknmkkaEELLKWLEIDNIDPrvAVESLDVGY---------------WQMVEIAKALSQ 159
Cdd:COG2274 564 -TIRENITLGDPD-----ATD-------EEIIEAARLAGLHD--FIEALPMGYdtvvgeggsnlsggqRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKeKGISIIYISHRMAeVFEICDRVTILRDGVNVAtvesrDTTMEEIIDK 237
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLS-TIRLADRIIVLDKGRIVE-----DGTHEELLAR 699
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-218 |
6.22e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.41 E-value: 6.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNG----VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVED----A 77
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGV--DLTALSErelrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HKKGIAMIYQEFSLLPAMSVAENI----YITReWKKggliDDRKnmKKAEELLKW--LEiDNID--P---------RVAv 140
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENValplEIAG-VPK----AEIR--KRVAELLELvgLS-DKADayPsqlsggqkqRVG- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 141 esldvgywqmveIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG1135 151 ------------IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
9.08e-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: 115.65 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAM 84
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE--PIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWKKGGLIDDRknmkkAEELLKWLEIDnidprvAVESLDVGYW-----QMVEIAKALSQ 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREA-----IDEALEAVGLA------GLADLPVRQLsagqkRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH 200
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-218 |
1.53e-29 |
|
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: 115.74 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVY-----TKDAGQIRIDGQE-ADLHSVEDAHK 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KGIAMIYQEFSLLPaMSVAENIYITRewKKGGLIDDRKNMKKAEELLK----WleiDNIDPRVAVESLDVGYWQMVEIAK 155
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL--RLHGIKLKEELDERVEEALRkaalW---DEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
262-487 |
1.89e-29 |
|
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: 115.22 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRDF--AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKK--DAMNKGIALV 335
Cdd:cd03224 1 LEVENLnaGYGKSqiLFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPphERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEDRRqegLILQHSIKSNFMLPSVRqmrkgfLIDDKKGADISREYiEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARG 415
Cdd:cd03224 81 PEGRR---IFPELTVEENLLLGAYA------RRRAKRKARLERVY-ELFPRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 416 PRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESE 487
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-470 |
2.18e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.97 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKS----TLMKILNG---VYTkdAGQIRIDGQEAdLHSVEDA--HKKG--IAMIYQ 87
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESL-LHASEQTlrGVRGnkIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 88 E--FSLLPAMSVAENIY--------ITREWKKGGLID--DRKNMKKAEELLkwleidNIDPrvavESLDVGYWQMVEIAK 155
Cdd:PRK15134 100 EpmVSLNPLHTLEKQLYevlslhrgMRREAARGEILNclDRVGIRQAAKRL------TDYP----HQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTILRDGvnvATVESRDTTMeei 234
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVRKLADRVAVMQNG---RCVEQNRAAT--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 235 idkmLDAAAKTSFERVERNFEQSGDPV---------LRVRDF---------------AYGNKLADVSFDLYPGEILGLAG 290
Cdd:PRK15134 244 ----LFSAPTHPYTQKLLNSEPSGDPVplpepasplLDVEQLqvafpirkgilkrtvDHNVVVKNISFTLRPGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 291 LMGSGRTElvesifgirrnwTGDVAMRgePIKSKKDAMNKGIALVPEDRRQEgLILQHSIKSNFMLP--------SVRQM 362
Cdd:PRK15134 320 ESGSGKST------------TGLALLR--LINSQGEIWFDGQPLHNLNRRQL-LPVRHRIQVVFQDPnsslnprlNVLQI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 363 -RKGFLIDDKKGADISRE-----YIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEI 436
Cdd:PRK15134 385 iEEGLRVHQPTLSAAQREqqviaVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
490 500 510
....*....|....*....|....*....|....*
gi 1054755845 437 LRIIRQL-ADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK15134 465 LALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-218 |
2.38e-29 |
|
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: 114.91 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNG--VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIA 83
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYI-TRewKKGglIDDRKNMKKAEELLKWLEI-DNIDPRvaVESLDVGYWQMVEIAKALSQDA 161
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyAR--LKG--LPKSEIKEEVELLLRVLGLtDKANKR--ARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKeKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
269-472 |
2.63e-29 |
|
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: 113.26 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDRRqeglil 346
Cdd:cd03230 10 YGKKTAldDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPS------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 qhsiksnfmlpsvrqmrkgfLIDDKKGadisREYIEklsikadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:cd03230 84 --------------------LYENLTV----RENLK---------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 427 GVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-218 |
3.37e-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: 114.31 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 25 NFSLK-----KGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDG-------QEADLHSvedaHKKGIAMIYQEFSLL 92
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPP----QQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 93 PAMSVAENIYItrewkkgGLIDDRKNMKK--AEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPT 170
Cdd:cd03297 88 PHLNVRENLAF-------GLKRKRNREDRisVDELLDLLGLDHLLNR-YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1054755845 171 SSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
261-471 |
4.00e-29 |
|
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: 114.53 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRDF--AYGNK------LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKgi 332
Cdd:cd03257 1 LLEVKNLsvSFPTGggsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 333 alvpeDRRQE-GLILQHSIKS-NFMLPSVRQMRKGFLI--DDKKGADISREYIEKLSIKADSIKQMAML---LSGGNQQK 405
Cdd:cd03257 79 -----IRRKEiQMVFQDPMSSlNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEVLNRYpheLSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 406 IVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSeLVAA-CDRILVLY 471
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLG-VVAKiADRVAVMY 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-228 |
5.60e-29 |
|
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: 114.52 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHSVED-AHKK 80
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP--VTRRRRkAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQ--EFSLLPAMSV----AENIYITRewkkgglIDDRKnmkkaEELLKWLEIDNIDPRVA---VESLDVGYWQMV 151
Cdd:COG1124 80 RVQMVFQdpYASLHPRHTVdrilAEPLRIHG-------LPDRE-----ERIAELLEQVGLPPSFLdryPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 152 EIAKALSQDAKILVMDEPTSSL---SKTETKALFKVIRQlkEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRD 228
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALdvsVQAEILNLLKDLRE--ERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-475 |
7.78e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 8 MHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDG--------QEADLHS------ 73
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQEPPLDDdltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 74 -VEDAHKKGIAMI--YQEFSLLPAMSVAENIYITR-----EWKKGGLIDDRknmkkAEELLKWLEIDNIDPRVAVESLDV 145
Cdd:COG0488 81 tVLDGDAELRALEaeLEELEAKLAEPDEDLERLAElqeefEALGGWEAEAR-----AEEILSGLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 146 GyWQM-VEIAKALSQDAKILVMDEPT-----SSLSKTEtkalfkviRQLKEKGISIIYISH----------RMAEVfeic 209
Cdd:COG0488 156 G-WRRrVALARALLSEPDLLLLDEPTnhldlESIEWLE--------EFLKNYPGTVLVVSHdryfldrvatRILEL---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 210 DRVTI---------------LRDGVNVATVESRDTT---MEEIIDKMLDAAAKTS--------FERVER----------- 252
Cdd:COG0488 223 DRGKLtlypgnysayleqraERLEQEAAAYAKQQKKiakEEEFIRRFRAKARKAKqaqsrikaLEKLEReepprrdktve 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 253 -NFEQ---SGDPVLRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAmRGEPIKsk 324
Cdd:COG0488 303 iRFPPperLGKKVLELEGlsKSYGDKtlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVK-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 325 kdamnkgIALVPEDrrQEGL-----ILQH--SIKSNFMLPSVRQMRKGFLiddkkgadISREYIEKlSIKAdsikqmaml 397
Cdd:COG0488 380 -------IGYFDQH--QEELdpdktVLDElrDGAPGGTEQEVRGYLGRFL--------FSGDDAFK-PVGV--------- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKaEILriIRQLAD-EGvAVLMIS--SELSELVaaCDRILVLYNRT 474
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVShdRYFLDRV--ATRILEFEDGG 506
|
.
gi 1054755845 475 V 475
Cdd:COG0488 507 V 507
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-219 |
9.24e-29 |
|
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: 111.54 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeADLHSV-EDAHKKGIAMIYQEFSLLPAmSV 97
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWdPNELGDHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIyitrewkkggliddrknmkkaeellkwleidnidprvavesLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTE 177
Cdd:cd03246 93 AENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1054755845 178 TKALFKVIRQLKEKGISIIYISHRMaEVFEICDRVTILRDGV 219
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-218 |
1.19e-28 |
|
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: 111.75 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNI--EKQFNGVpvlkkmNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHK 79
Cdd:cd03215 1 GEPVLEVRGLsvKGAVRDV------SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KGIAMI---YQEFSLLPAMSVAENIYITReWKKGGliddrkNMKKaeellkwleidnidprvavesldvgywqmVEIAKA 156
Cdd:cd03215 75 AGIAYVpedRKREGLVLDLSVAENIALSS-LLSGG------NQQK-----------------------------VVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 157 LSQDAKILVMDEPTSSLSkTETKA-LFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03215 119 LARDPRVLILDEPTRGVD-VGAKAeIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-218 |
1.92e-28 |
|
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: 112.78 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGV-PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEdaHKKGIA 83
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVE--LRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYIT---REWKKggliddRKNMKKAEELLKW--LEIDNIDPRVAVEsLDVGYWQMVEIAKALS 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVpklLKWPK------EKIRERADELLALvgLDPAEFADRYPHE-LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 159 QDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-226 |
2.27e-28 |
|
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: 112.43 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVpVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEdahKKGIAMI 85
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKggliDDRKNM-KKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRK----VDKKEIeRKVLEIAEMLGIDHLLNR-KPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 165 VMDEPTSSLS-KTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG--VNVATVES 226
Cdd:cd03299 152 LLDEPFSALDvRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGklIQVGKPEE 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
259-493 |
2.99e-28 |
|
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: 112.38 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRDF--AYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKK--DAMNKGI 332
Cdd:COG0410 1 MPMLEVENLhaGYGGIHVlhGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 333 ALVPEDRRqegLILQHSIKSNFMLPsvrqmrkGFLIDDKKGADISREYI--------EKLsikadsiKQMAMLLSGGNQQ 404
Cdd:COG0410 81 GYVPEGRR---IFPSLTVEENLLLG-------AYARRDRAEVRADLERVyelfprlkERR-------RQRAGTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 405 KIVLGKWLARGPRVLILDEPTIGvdVAAK--AEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGR 482
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLG--LAPLivEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
250
....*....|.
gi 1054755845 483 EIESEEVLHHA 493
Cdd:COG0410 222 ELLADPEVREA 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-218 |
3.01e-28 |
|
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: 112.21 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVED--AHKKGIA 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENI-YITREWKKG--GLIDDRKNMKKAEELLKwlEIDNIDPrvavESLDVGYWQMVEIAKALSQD 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVaFPLREHTRLseEEIREIVLEKLEAVGLR--GAEDLYP----AELSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-218 |
3.32e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH---- 78
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ--DLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQEFSLLPAMSVAENIYITRE---WKKggliDDRKnmKKAEELLKWLEIDniDPRVAVES-LDVGYWQMVEIA 154
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLElagTPK----AEIK--ARVTELLELVGLS--DKADRYPAqLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 155 KALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-228 |
3.79e-28 |
|
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: 112.00 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGI 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMIYQEFSLLPAMSVAENIYItrewkkGGLIddRKNMKKAEELLKWleIDNIDPRVAvESLDV-------GYWQMVEIAK 155
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLL------GAYA--RRDRAEVRADLER--VYELFPRLK-ERRRQragtlsgGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRD 228
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-235 |
3.89e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 117.19 E-value: 3.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVpvLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGI 82
Cdd:PRK09700 263 ETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMIYQ---EFSLLPAMSVAENIYITREWKKG------GLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEI 153
Cdd:PRK09700 341 AYITEsrrDNGFFPNFSIAQNMAISRSLKDGgykgamGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 154 AKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEE 233
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
..
gi 1054755845 234 II 235
Cdd:PRK09700 501 EI 502
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-252 |
4.77e-28 |
|
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: 112.74 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 11 IEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDA-----HKKGIAMI 85
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ--DIAAMSRKelrelRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALSQDAKILV 165
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVATvesrdTTMEEIIDKMLDAAAK 244
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQV-----GTPEEILTNPANDYVR 258
|
....*...
gi 1054755845 245 TSFERVER 252
Cdd:cd03294 259 EFFRGVDR 266
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-218 |
6.30e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEdahKK 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ---QR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENI-YITREWKKGGliDDRKnmKKAEELLKWLEIDNIDPRVaVESLDVGYWQMVEIAKALSQ 159
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVgYGLKMLGVPK--EERK--QRVKEALELVDLAGFEDRY-VDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-222 |
1.10e-27 |
|
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: 110.15 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEAdlhsVEDAHK--KGIA 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREvrRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYItrewkKGGL--IDDRKNMKKAEELLKWLEI-DNIDPRVAVESldVGYWQMVEIAKALSQD 160
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI-----HARLygVPGAERRERIDELLDFVGLlEAADRLVKTYS--GGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-218 |
2.07e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIYQEFSLLpAM 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLF-SG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIYITREWkkgglIDDrknmkkaEELLKWLEIDNIDPRvaVESLDVGY---------------WQMVEIAKALSQD 160
Cdd:COG1132 429 TIRENIRYGRPD-----ATD-------EEVEEAAKAAQAHEF--IEALPDGYdtvvgergvnlsggqRQRIAIARALLKD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 161 AKILVMDEPTSSL-SKTEtKALFKVIRQLKEKGISIIyISHRMAEVfEICDRVTILRDG 218
Cdd:COG1132 495 PPILILDEATSALdTETE-ALIQEALERLMKGRTTIV-IAHRLSTI-RNADRILVLDDG 550
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-218 |
7.63e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.58 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE---ADLHsvEDAhKKG 81
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithLPMH--KRA-RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIDPRVAVeSLDVGYWQMVEIAKALSQDA 161
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRK---LSKKEREERLEELLEEFGITHLRKSKAY-SLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 162 KILVMDEPtsslsktetkalF------------KVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG1137 156 KFILLDEP------------FagvdpiavadiqKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEG 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-235 |
7.77e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 113.47 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 25 NFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMI---YQEFSLLPAMSVAENI 101
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCpedRKAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 102 YIT-REW--KKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSL---SK 175
Cdd:PRK11288 353 NISaRRHhlRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIdvgAK 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 176 TEtkaLFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEII 235
Cdd:PRK11288 433 HE---IYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQAL 489
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
267-470 |
9.31e-27 |
|
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: 107.17 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialVPEDRRQE 342
Cdd:cd03225 7 FSYPDGarpaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---------LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 GLILQHSiKSNFMLPSVRQ-----MRKgFLIDDKKGADISREYIEKLSIKA---DSIKQmamlLSGGNQQKIVLGKWLAR 414
Cdd:cd03225 78 GLVFQNP-DDQFFGPTVEEevafgLEN-LGLPEEEIEERVEEALELVGLEGlrdRSPFT----LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-218 |
1.14e-26 |
|
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: 106.96 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGVP-VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAM- 84
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK--PIKAKERRKSIGYVMq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 --IYQEFSllpaMSVAENIYITREwkkggLIDDRKNmkKAEELLKWLEIDNID---PRvaveSLDVGYWQMVEIAKALSQ 159
Cdd:cd03226 79 dvDYQLFT----DSVREELLLGLK-----ELDAGNE--QAETVLKDLDLYALKerhPL----SLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
267-472 |
1.35e-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: 107.64 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDRrqeGL 344
Cdd:COG4555 9 KKYGKVPAlkDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDER---GL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQHSIKSNfmlpsVRQMRKGFLIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:COG4555 86 YDRLTVREN-----IRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 425 TIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-218 |
1.56e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.70 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEdAHKKGIAM 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLSHVP-PYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYItrewkkgGLIDDRknMKKAE------ELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALS 158
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAF-------GLKQDK--LPKAEiasrvnEMLGLVHMQEFAKR-KPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 159 QDAKILVMDEPTSSLSKT-ETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-218 |
1.60e-26 |
|
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: 106.72 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF-NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAH-KKGI 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvSDLRGRAIPYlRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMIYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPrvavESLDVGYWQMVEIAKALSQDAK 162
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP----AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 163 ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
265-470 |
3.72e-26 |
|
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: 105.83 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 265 RDFAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkDAMNKGIALVPEDRrqeGL 344
Cdd:cd03269 8 KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPEER---GL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQHSIKSNFM-LPSVRQMRKgfliddKKGADISREYIEKLSI---KADSIKQmamlLSGGNQQKIVLGKWLARGPRVLI 420
Cdd:cd03269 82 YPKMKVIDQLVyLAQLKGLKK------EEARRRIDEWLERLELseyANKRVEE----LSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1054755845 421 LDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-222 |
4.05e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.52 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAM 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNmkKAEELLKWLEIDNIDPRVAvESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQRED--RANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-218 |
1.74e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAH-----KK 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKairelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIyITREWKKGGLiDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALSQD 160
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNL-IEAPCRVLGL-SKDQALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-203 |
2.16e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.40 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEA-DLHSVEDAHKKGIA 83
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYItrewkkgGLIDDRKNMKK-----AEELLKwleidnidpRVAVES--------LDVGYWQM 150
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMF-------GPLRVRGASKEeaekqARELLA---------KVGLAErahhypseLSGGQQQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 151 VEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMA 203
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-215 |
2.32e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 103.71 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlhsVEDAHKKg 81
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNID---PRvaveSLDVGYWQMVEIAKALS 158
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFEnayPH----QLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 159 QDAKILVMDEPTSSL---SKTETKALfkVIRQLKEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:cd03293 148 VDPDVLLLDEPFSALdalTREQLQEE--LLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-218 |
2.70e-25 |
|
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: 103.84 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH-KKGIAMIYQEFSLLPA 94
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI--DIRDISRKSlRSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 mSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEiDNIDPRV--AVESLDVGYWQMVEIAKALSQDAKILVMDEPTSS 172
Cdd:cd03254 92 -TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLP-NGYDTVLgeNGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 173 L-SKTEtKALFKVIRQLKEKGISIIyISHRMAEVFEiCDRVTILRDG 218
Cdd:cd03254 170 IdTETE-KLIQEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
273-472 |
5.96e-25 |
|
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: 101.95 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKkdamnkgialvpEDRRQEGLILQHSiKS 352
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK------------ERRKSIGYVMQDV-DY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVR-QMRKGFLIDDKKGADIsREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVA 431
Cdd:cd03226 83 QLFTDSVReELLLGLKELDAGNEQA-ETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 432 AKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
1.14e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKK 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIYIT--REWKKG---GLIDD----RKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQM- 150
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAqhQQLKTGlfsGLLKTpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQr 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 151 -VEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTILRDGVNVAT 223
Cdd:PRK11300 161 rLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-222 |
1.25e-24 |
|
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: 101.51 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAhKKGIAMIYQEFSLLpAMSV 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYItrewkKGGLIDDrknmkkaEELLKWLEIDNIDPRVAV-------------ESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:cd03245 95 RDNITL-----GAPLADD-------ERILRAAELAGVTDFVNKhpngldlqigergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEkGISIIYISHRMAeVFEICDRVTILRDGVNVA 222
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVA 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
262-470 |
1.27e-24 |
|
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: 100.34 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRDFA--YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkdamNKGIALVPE 337
Cdd:cd03229 1 LELKNVSkrYGQKTVlnDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-------TDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DRRQEGLILQHSIKsnFMLPSVRQmrkgfliddkkgadisreyieklsikadsikQMAMLLSGGNQQKIVLGKWLARGPR 417
Cdd:cd03229 74 LRRRIGMVFQDFAL--FPHLTVLE-------------------------------NIALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVL 174
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
261-472 |
1.34e-24 |
|
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: 102.43 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKD-AMNKGIALV 335
Cdd:COG1120 1 MLEAENlsVGYGGRpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PedrrqeglilQHSIkSNFMLpSVRQM--------RKGFLIDDKKGADISREYIEKLSI--KAD-SIKQmamlLSGGNQQ 404
Cdd:COG1120 81 P----------QEPP-APFGL-TVRELvalgryphLGLFGRPSAEDREAVEEALERTGLehLADrPVDE----LSGGERQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 405 KIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYN 472
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
273-470 |
1.42e-24 |
|
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: 99.81 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEP--IKSKKDAMNKGIALVPEdrrqeglilqhsi 350
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEvsFASPRDARRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 ksnfmlpsvrqmrkgfliddkkgadisreyieklsikadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDV 430
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 431 AAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
267-472 |
1.56e-24 |
|
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: 99.63 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialVPEDRRQEGL 344
Cdd:cd00267 7 FRYGGRtaLDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---------LEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQhsiksnfmlpsvrqmrkgfliddkkgadisreyieklsikadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:cd00267 78 VPQ--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 425 TIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-218 |
2.28e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.01 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHsvedAHKKGIAM 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvSRLH----ARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYI------TREWKKGGLIDdrknmKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALS 158
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFgltvlpRRERPNAAAIK-----AKVTQLLEMVQLAHLADRYPAQ-LSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 159 QDAKILVMDEPTSSLSKTETKALFKVIRQLKE--KGISiIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTS-VFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-218 |
2.79e-24 |
|
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: 101.25 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAMIY-QEFSLLPAMS 96
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL--VPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIdPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKT 176
Cdd:cd03267 112 VIDSFYLLAAIYD---LPPARFKKRLDELSELLDLEEL-LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 177 ETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03267 188 AQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
262-475 |
4.43e-24 |
|
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: 100.65 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIalvpe 337
Cdd:cd03261 1 IELRGltKSFGGRtvLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 dRRQEGLILQH-------SIKSNFMLPsvrqMRKGFLIDDKKGADISREYIEKLSIKADsIKQMAMLLSGGNQQKIVLGK 410
Cdd:cd03261 76 -RRRMGMLFQSgalfdslTVFENVAFP----LREHTRLSEEEIREIVLEKLEAVGLRGA-EDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 411 WLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-219 |
6.49e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.10 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVeDAHKK 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHV-PAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIYItrewkkgGLiddrkNMKKAEEllkwleiDNIDPRVA---------------VESLDV 145
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAF-------GL-----RMQKTPA-------AEITPRVMealrmvqleefaqrkPHQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 146 GYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
1.12e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeADLHSVEDAHKK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIYITREWKkggliddRKNMKKAEE----LLKWLEIDN-IDPRVAveSLDVGYWQMVEIAK 155
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYF-------GMSTREIEAvipsLLEFARLESkADARVS--DLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEI 234
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-222 |
1.28e-23 |
|
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: 99.39 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQ-IRIDGQEADLHSVEDaHKKG 81
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWE-LRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQEFSL-LPAMSVAENIYITrewkkgGLID--------DRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVE 152
Cdd:COG1119 80 IGLVSPALQLrFPRDETVLDVVLS------GFFDsiglyrepTDEQRERARELLELLGLAHLADR-PFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 153 IAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-218 |
1.64e-23 |
|
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: 103.68 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH-KKGIAMIYQEfSLLPA 94
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV--DLSDLDPASwRRQIAWVPQN-PYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 MSVAENIYITREwkkggLIDDrknmkkaEELLKWLEIDNIDPRVAveSLDVGY---------------WQMVEIAKALSQ 159
Cdd:COG4988 425 GTIRENLRLGRP-----DASD-------EELEAALEAAGLDEFVA--ALPDGLdtplgeggrglsggqAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 160 DAKILVMDEPTSSL-SKTEtKALFKVIRQLKeKGISIIYISHRMAEVfEICDRVTILRDG 218
Cdd:COG4988 491 DAPLLLLDEPTAHLdAETE-AEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDG 547
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
2.04e-23 |
|
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: 98.28 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNEnVLEMHNIEKQF-----NGV--PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRI--DGQEADL 71
Cdd:COG4778 1 MTT-LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 72 HSVEDAH-----KKGIAMIYQEFSLLPAMS----VAENIyitREWkkGglIDDRKNMKKAEELLKWLEIDnidprvavES 142
Cdd:COG4778 80 AQASPREilalrRRTIGYVSQFLRVIPRVSaldvVAEPL---LER--G--VDREEARARARELLARLNLP--------ER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 143 LdvgyW------------QMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICD 210
Cdd:COG4778 145 L----WdlppatfsggeqQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
....*...
gi 1054755845 211 RVTILRDG 218
Cdd:COG4778 221 RVVDVTPF 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-223 |
2.84e-23 |
|
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: 97.56 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 24 MNFSLK--KGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlHSVEDAHKKGIAMIYQEFSLLPAMSVAENI 101
Cdd:cd03298 15 MHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 102 YITREWKKGGLIDDRKNMKKAeelLKWLEIDNIDPRVAvESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLS---KTET 178
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVA---LARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1054755845 179 KALFKVIRQlkEKGISIIYISHRMAEVFEICDRVTILRDGVNVAT 223
Cdd:cd03298 168 LDLVLDLHA--ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
267-475 |
2.86e-23 |
|
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: 96.74 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPedrrqeg 343
Cdd:cd03214 7 VGYGGRtvLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVP------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 344 lilqhsiksnfmlpsvrQMRKGFLIDDKKGADISReyieklsikadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:cd03214 80 -----------------QALELLGLAHLADRPFNE-------------------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-212 |
5.04e-23 |
|
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: 99.36 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNG----VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVY---TKDAGQIRIDGQeaDLHSVEDA 77
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGE--DLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 H-----KKGIAMIYQEF--SLLPAMSV----AENIYITREWKKggliDDRKnmKKAEELLKWLEIDNidprvAVESLDV- 145
Cdd:COG0444 79 ElrkirGREIQMIFQDPmtSLNPVMTVgdqiAEPLRIHGGLSK----AEAR--ERAIELLERVGLPD-----PERRLDRy 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 146 ------GYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRV 212
Cdd:COG0444 148 phelsgGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-218 |
5.38e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 96.88 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGeVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEaDLHSVEDAHKKgIAMI 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENI-YITreWKKGglIDDRKNMKKAEELlkwLEIDNIDPRV--AVESLDVGYWQMVEIAKALSQDAK 162
Cdd:cd03264 78 PQEFGVYPNFTVREFLdYIA--WLKG--IPSKEVKARVDEV---LELVNLGDRAkkKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 163 ILVMDEPTSSLSKTETKALFKVIRQLKEKGIsIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKG 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
262-484 |
7.38e-23 |
|
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: 97.02 E-value: 7.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialVP 336
Cdd:COG1122 1 IELENlsFSYPGGtpaLDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---------LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 337 EDRRQEGLILQ---HSIksnFMlPSVRQ------MRKGfliddkkgadISREYIEKLSIKAdsIKQMAM---------LL 398
Cdd:COG1122 72 ELRRKVGLVFQnpdDQL---FA-PTVEEdvafgpENLG----------LPREEIRERVEEA--LELVGLehladrpphEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 399 SGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKE 478
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
....*.
gi 1054755845 479 LSGREI 484
Cdd:COG1122 216 GTPREV 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
9.63e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIamIYQEFSLLPAMSVAENIYITREWKKGGLIDDRKNMKKaeeLLKWLEIDN-IDPRVAveSLDVGYWQMVEIAKALSQ 159
Cdd:PRK13537 83 GV--VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPP---LLEFAKLENkADAKVG--ELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEI 234
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
262-475 |
1.10e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 95.65 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkDAMNkgialVPE 337
Cdd:COG4619 1 LELEGlsFRVGGKpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMP-----PPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DRRQEGLILQHSIksnFMLPSVRQ-MRKGFLIDDKKG-ADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARG 415
Cdd:COG4619 72 WRRQVAYVPQEPA---LWGGTVRDnLPFPFQLRERKFdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 416 PRVLILDEPTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-218 |
1.26e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.89 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQF-NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVED----AHK 79
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ--DLSRLKRreipYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KGIAMIYQEFSLLPAMSVAENIY----ITREwkkgglidDRKNMKK-AEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIA 154
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVAlplrVTGK--------SRKEIRRrVREVLDLVGLSDKAKALPHE-LSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 155 KALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-218 |
2.39e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.21 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAhkkGIAMIY--QEFSLLPA 94
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRHIGYlpQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 mSVAENIyiTRewkkggliddrknmkkaeellkwleIDNIDPRVAVE------------SLDVGY--------------- 147
Cdd:COG4618 421 -TIAENI--AR-------------------------FGDADPEKVVAaaklagvhemilRLPDGYdtrigeggarlsggq 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 148 WQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAeVFEICDRVTILRDG 218
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDG 542
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
273-472 |
2.53e-22 |
|
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: 96.03 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKD-AMNKGIALVPED-------RRQEGL 344
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQMVFQDpyaslhpRHTVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQHSIKSNFMLPSVRQMRKgfLIDDkkgADISREYIEKLSIKadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:COG1124 101 ILAEPLRIHGLPDREERIAE--LLEQ---VGLPPSFLDRYPHQ----------LSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1054755845 425 TIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELsELVAA-CDRILVLYN 472
Cdd:COG1124 166 TSALDVSVQAEILNLLKDLrEERGLTYLFVSHDL-AVVAHlCDRVAVMQN 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
273-492 |
4.46e-22 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 94.81 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialvPEDRRQEGL-------- 344
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----------PHEIARLGIgrtfqipr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQH-SIKSNFMLPsvRQMRKGFLIDDKKGADISREYIEK---------LSIKADsikQMAMLLSGGNQQKIVLGKWLAR 414
Cdd:cd03219 86 LFPElTVLENVMVA--AQARTGSGLLLARARREEREARERaeellervgLADLAD---RPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYnrtvnkelSGREIES---EEVLH 491
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLD--------QGRVIAEgtpDEVRN 232
|
.
gi 1054755845 492 H 492
Cdd:cd03219 233 N 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-218 |
5.09e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.44 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPvlkkMNFSL--KKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlHSVEDAHKKGIA 83
Cdd:COG3840 2 LRLDDLTYRYGDFP----LRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYItrewkkgGLIDDRK----NMKKAEELLKWLEIDNIDPRVAvESLDVGYWQMVEIAKALSQ 159
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGL-------GLRPGLKltaeQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 160 DAKILVMDEPTSSLS---KTETKALfkvIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG3840 147 KRPILLLDEPFSALDpalRQEMLDL---VDELcRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
1.56e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.29 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIYQ----EFSllpA 94
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK-IGIIFQnpdnQFI---G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 MSVAENIYITREWKKggliDDRKNMKK-AEELLKWLEIDNI---DPrvavESLDVGYWQMVEIAKALSQDAKILVMDEPT 170
Cdd:PRK13632 99 ATVEDDIAFGLENKK----VPPKKMKDiIDDLAKKVGMEDYldkEP----QNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 171 SSLSKTETKALFKVIRQLKEKGI-SIIYISHRMAEVFeICDRVTILRDGVNVATVESRDT-TMEEIIDKM 238
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIlNNKEILEKA 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
262-470 |
2.06e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 90.91 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIAL 334
Cdd:cd03228 1 IEFKNvsFSYPGRpkpvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 335 VPedrrQEGLILQHSIKSNfmlpsvrqmrkgfliddkkgadisreyieklsikadsikqmamLLSGGNQQKIVLGKWLAR 414
Cdd:cd03228 81 VP----QDPFLFSGTIREN-------------------------------------------ILSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADeGVAVLMISSELSeLVAACDRILVL 470
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS-TIRDADRIIVL 167
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-227 |
2.24e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADlHSVEDAHKKG---- 81
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID-TARSLSQQKGlirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 ----IAMIYQEFSLLPAMSVAENIYITREWKKGglIDDRKNMKKAEELLKWLEI---DNIDPRvaveSLDVGYWQMVEIA 154
Cdd:PRK11264 83 lrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLagkETSYPR----RLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 155 KALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESR 227
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-218 |
3.71e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMI 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITREWKKGGLI----DDRKNMKKAeelLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDA 161
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDtwteTDRAAVERA---MERTGVAQFADR-PVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-223 |
4.41e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNG--VYTKDAGQIRIDGQE-ADLhSVEDAHKKGI 82
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDiLEL-SPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 83 AMIYQ---EFsllPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLeidNIDPRVAVESLDVGY----WQMVEIAK 155
Cdd:COG0396 80 FLAFQypvEI---PGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKEL---GLDEDFLDRYVNEGFsggeKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH--RMAEvFEICDRVTILRDGVNVAT 223
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqRILD-YIKPDFVHVLVDGRIVKS 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
6.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQF-NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADlHSVEDAHK 79
Cdd:PRK13636 1 MEDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 --KGIAMIYQE-FSLLPAMSVAENIYItrewkkGGLiddrkNMKKAEELLKwLEIDNIDPRVAVE--------SLDVGYW 148
Cdd:PRK13636 80 lrESVGMVFQDpDNQLFSASVYQDVSF------GAV-----NLKLPEDEVR-KRVDNALKRTGIEhlkdkpthCLSFGQK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 149 QMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-218 |
9.59e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.00 E-value: 9.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGV--PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAH 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKgIAMIYQE---------------FSLlpamsvaENIYITREwkkggliDDRKNMKKAEELLKWLEIDNIDPrvavESL 143
Cdd:PRK13635 81 RQ-VGMVFQNpdnqfvgatvqddvaFGL-------ENIGVPRE-------EMVERVDQALRQVGMEDFLNREP----HRL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 144 DVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-218 |
2.12e-20 |
|
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: 88.76 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNG--VYTKDAGQIRIDGQEADLHSVedahKKGIAMIYQEFSLLPAMS 96
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSF----RKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITREWKK--GGlidDRKnmkkaeellkwleidnidpRVAvesldvgywqmveIAKALSQDAKILVMDEPTSSLS 174
Cdd:cd03213 99 VRETLMFAAKLRGlsGG---ERK-------------------RVS-------------IALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1054755845 175 KTETKALFKVIRQLKEKGISIIYISHR-MAEVFEICDRVTILRDG 218
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-218 |
3.23e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDagqiRIDGQEADL--HSVEDAHKK 80
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD----KSAGSHIELlgRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 G---------IAMIYQEFSLLPAMSVAENIYI-----TREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVG 146
Cdd:PRK09984 78 ArdirksranTGYIFQQFNLVNRLSVLENVLIgalgsTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQ-RVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 147 YWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
235-470 |
3.33e-20 |
|
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: 93.67 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 235 IDKMLDAAAKTSfERVERNFEQSGDPVLRVRD--FAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRN 309
Cdd:COG4988 311 IFALLDAPEPAA-PAGTAPLPAAGPPSIELEDvsFSYPGGrpaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 310 WTGDVAMRGEPIKS-KKDAMNKGIALVPedrrQEGLILQHSIKSNFML----PSVRQMRKgflIDDKKGADisrEYIEKL 384
Cdd:COG4988 390 YSGSILINGVDLSDlDPASWRRQIAWVP----QNPYLFAGTIRENLRLgrpdASDEELEA---ALEAAGLD---EFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 385 SIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSeLVAA 463
Cdd:COG4988 460 PDGLDTpLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA-LLAQ 537
|
....*..
gi 1054755845 464 CDRILVL 470
Cdd:COG4988 538 ADRILVL 544
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-246 |
4.21e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEAdlhsvedahkkgiAMIyqEFS--LLPAM 95
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS-------------ALL--ELGagFHPEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIYItrewkkGGLIddrKNMKKAEellkwleidnIDPRVAvesldvgywqmvEIAK-------------------- 155
Cdd:COG1134 104 TGRENIYL------NGRL---LGLSRKE----------IDEKFD------------EIVEfaelgdfidqpvktyssgmr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 156 -------ALSQDAKILVMDEPTS----SLSKtetKAlFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVAtv 224
Cdd:COG1134 153 arlafavATAVDPDILLVDEVLAvgdaAFQK---KC-LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM-- 226
|
250 260
....*....|....*....|..
gi 1054755845 225 esrDTTMEEIIDKMLDAAAKTS 246
Cdd:COG1134 227 ---DGDPEEVIAAYEALLAGRE 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
6.77e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 4 NVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVY-----TKDAGQIRIDGQEADLHSVEDAH 78
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKgIAMIYQEFSLLPAMSVAENIYItrewkkgGLIDDR--KNMKKAEELLKW-LE----IDNIDPRVAVE--SLDVGYWQ 149
Cdd:PRK14247 82 RR-VQMVFQIPNPIPNLSIFENVAL-------GLKLNRlvKSKKELQERVRWaLEkaqlWDEVKDRLDAPagKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKeKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRD 228
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-237 |
9.97e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.96 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVyTKD-----AGQIRIDGQEADLHSVEDAHK---KGIAMIYQE- 88
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDnwhvtADRFRWNGIDLLKLSPRERRKiigREIAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 -FSLLPAMSV----AENIyitREWKKGGLIDDRKNMKK--AEELLKWLEIDniDPRVAVES----LDVGYWQMVEIAKAL 157
Cdd:COG4170 99 sSCLDPSAKIgdqlIEAI---PSWTFKGKWWQRFKWRKkrAIELLHRVGIK--DHKDIMNSypheLTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 158 SQDAKILVMDEPTSSLSKTeTKA-LFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGvnvATVESrdTTMEEII 235
Cdd:COG4170 174 ANQPRLLIADEPTNAMEST-TQAqIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCG---QTVES--GPTEQIL 247
|
..
gi 1054755845 236 DK 237
Cdd:COG4170 248 KS 249
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-219 |
1.74e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKK 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 ------------GIAMIYQEFSLLPAMSVAENIyITREWKKGGLiddrKNMKKAEELLKWLEIDNIDPRVAVE---SLDV 145
Cdd:PRK10619 81 vadknqlrllrtRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGL----SKQEARERAVKYLAKVGIDERAQGKypvHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 146 GYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
257-475 |
1.75e-19 |
|
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: 87.34 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 257 SGDPVLRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPI-KSKKDAMNkg 331
Cdd:COG1127 1 MSEPMIEVRNltKSFGDRvvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItGLSEKELY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 332 ialvpEDRRQEGLILQH-------SIKSNFMLPsvrqMRKGFLIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGnQQ 404
Cdd:COG1127 79 -----ELRRRIGMLFQGgalfdslTVFENVAFP----LREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGG-MR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 405 KIVlGkwLARG----PRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:COG1127 148 KRV-A--LARAlaldPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
259-470 |
2.05e-19 |
|
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: 91.19 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVR--DFAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGI 332
Cdd:TIGR02857 319 ASSLEFSgvSVAYPGRrpaLRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 333 ALVPedrrQEGLILQHSIKSNfmlpsVRQMRKgflidDKKGADISR--------EYIEKLSIKADSI--KQMAMlLSGGN 402
Cdd:TIGR02857 399 AWVP----QHPFLFAGTIAEN-----IRLARP-----DASDAEIREaleragldEFVAALPQGLDTPigEGGAG-LSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 403 QQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELsELVAACDRILVL 470
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-215 |
3.33e-19 |
|
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: 90.42 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGV-PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADlHSVEDAHKKGIAM 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-DADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAmSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEiDNIDPRV--AVESLDVGYWQMVEIAKALSQDAK 162
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALP-QGLDTPIgeGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 163 ILVMDEPTSSLSKTETKALFKVIRQLKEkGISIIYISHRMAeVFEICDRVTIL 215
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA-LAALADRIVVL 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
243-470 |
3.38e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 91.05 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 243 AKTSFER--------VERNFEQSGDPV------LRVRD--FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVES 302
Cdd:COG2274 441 AKIALERlddildlpPEREEGRSKLSLprlkgdIELENvsFRYPGDsppvLDNISLTIKPGERVAIVGRSGSGKSTLLKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 303 IFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPedrrQEGLILQHSIKSNFMLpsvrqmrkgfliddkKGADISREYI 381
Cdd:COG2274 521 LLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVL----QDVFLFSGTIRENITL---------------GDPDATDEEI 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 382 EKLSIKA---DSIKQMAM-----------LLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEG 447
Cdd:COG2274 582 IEAARLAglhDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KG 660
|
250 260
....*....|....*....|...
gi 1054755845 448 VAVLMISSELSeLVAACDRILVL 470
Cdd:COG2274 661 RTVIIIAHRLS-TIRLADRIIVL 682
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
262-472 |
3.48e-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: 86.02 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD----FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALV 335
Cdd:cd03263 1 LQIRNltktYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PedrrqeglilQHSIKSNFMlpSVRQ-MR-----KGflIDDKKGADISREYIEKLSIKaDSIKQMAMLLSGGNQQKIVLG 409
Cdd:cd03263 81 P----------QFDALFDEL--TVREhLRfyarlKG--LPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSD 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-218 |
3.81e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQ----EADLHSVEDAH 78
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 -KKGIAMIYQEFSLLPAMSVAENIyiTREWKKGGLIDDRKNMKKAEELLK----WLEI-DNIDPrvAVESLDVGYWQMVE 152
Cdd:PRK14246 88 lRKEVGMVFQQPNPFPHLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRkvglWKEVyDRLNS--PASQLSGGQQQRLT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 153 IAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
260-493 |
3.87e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.90 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRDFA--YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGepikskKDAMNKGIALV 335
Cdd:PRK11701 5 PLLSVRGLTklYGPRKGcrDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM------RDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEDRRQE------GLILQHSiksnfmlpsvrqmRKGFLIDDKKGADIS--------REY----------IEKLSIKADSI 391
Cdd:PRK11701 79 SEAERRRllrtewGFVHQHP-------------RDGLRMQVSAGGNIGerlmavgaRHYgdiratagdwLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 392 KQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELS--ELVAacDRIL 468
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAvaRLLA--HRLL 223
|
250 260 270
....*....|....*....|....*....|.
gi 1054755845 469 VLYnrtvnkelSGREIES---EEVL---HHA 493
Cdd:PRK11701 224 VMK--------QGRVVESgltDQVLddpQHP 246
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-218 |
4.06e-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: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF--NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeADLHSVEDAHKKGIA 83
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--VPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLpAMSVAENIyitrewkkGgliddrknmkkaeellkwleidnidprvavESLDVGYWQMVEIAKALSQDAKI 163
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNL--------G------------------------------RRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 164 LVMDEPTSSLS-KTETKALFKVIRQLKEKgiSIIYISHRMAEVfEICDRVTILRDG 218
Cdd:cd03247 120 VLLDEPTVGLDpITERQLLSLIFEVLKDK--TLIWITHHLTGI-EHMDKILFLENG 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-218 |
5.22e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF-NG---VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDA--H 78
Cdd:PRK10535 5 LELKDIRRSYpSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALAqlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQEFSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEI-DNIDPRVAveSLDVGYWQMVEIAKAL 157
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAG---LERKQRLLRAQELLQRLGLeDRVEYQPS--QLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 158 SQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRmAEVFEICDRVTILRDG 218
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDG 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-218 |
5.43e-19 |
|
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: 84.89 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV--YTKDAGQIRIDGQEADLHSVEDAHKKGIAMIYQEFSLLP 93
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 AMSVAENIYITREWKKGGlidDRKNmkkaeellkwleidnidprvavesldvgywqmVEIAKALSQDAKILVMDEPTSSL 173
Cdd:cd03217 91 GVKNADFLRYVNEGFSGG---EKKR--------------------------------NEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 174 SKTETKALFKVIRQLKEKGISIIYISH--RMAEvFEICDRVTILRDG 218
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHyqRLLD-YIKPDRVHVLYDG 181
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-218 |
5.44e-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: 86.13 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQ---EADLHSVedahKKGIAMIYQEFSLLP 93
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirEVTLDSL----RRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 AmSVAENIYITR---------EWKKGGLIDDR-KNMKKA------EELLKwleidnidprvavesLDVGYWQMVEIAKAL 157
Cdd:cd03253 89 D-TIGYNIRYGRpdatdeeviEAAKAAQIHDKiMRFPDGydtivgERGLK---------------LSGGEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 158 SQDAKILVMDEPTSSLSKTETKALFKVIRQLKeKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDG 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
257-457 |
6.56e-19 |
|
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: 89.34 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 257 SGDPVLRVRDFAYG-----NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNK 330
Cdd:TIGR02868 330 LGKPTLELRDLSAGypgapPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 331 GIALVPEDRRqeglILQHSIKSNFMLPsvrqmrKGFLIDDKKGADISR----EYIEKLSIKADS-IKQMAMLLSGGNQQK 405
Cdd:TIGR02868 410 RVSVCAQDAH----LFDTTVRENLRLA------RPDATDEELWAALERvglaDWLRALPDGLDTvLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 406 IVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSEL 457
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-221 |
6.95e-19 |
|
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: 85.67 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVE-DAHKKGIAMIYQEFSLLpAM 95
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLNlRWLRSQIGLVSQEPVLF-DG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIyitrewkkgGLIDDRKNMKKAEELLKWLEIDNIdprvaVESLDVGYWQMV---------------EIAKALSQD 160
Cdd:cd03249 92 TIAENI---------RYGKPDATDEEVEEAAKKANIHDF-----IMSLPDGYDTLVgergsqlsggqkqriAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 161 AKILVMDEPTSSL-SKTET---KALFKVIrqlkeKGISIIYISHRMAEVfEICDRVTILRDGVNV 221
Cdd:cd03249 158 PKILLLDEATSALdAESEKlvqEALDRAM-----KGRTTIVIAHRLSTI-RNADLIAVLQNGQVV 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-218 |
7.58e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.78 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQ---EADLHSVedaHKKgIAMIYQEfSLLPA 94
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvQYDHHYL---HRQ-VALVGQE-PVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 MSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEiDNIDPRVAVES--LDVGYWQMVEIAKALSQDAKILVMDEPTSS 172
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFP-NGYDTEVGEKGsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 173 LSkTETKALFKVIRQLKEKgiSIIYISHRMAEVfEICDRVTILRDG 218
Cdd:TIGR00958 648 LD-AECEQLLQESRSRASR--TVLLIAHRLSTV-ERADQILVLKKG 689
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
262-471 |
7.69e-19 |
|
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: 85.29 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRDFA--YGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskKDAMNK----GIA 333
Cdd:cd03218 1 LRAENLSkrYGKRkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT--KLPMHKrarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 LVPedrrQEGLILQH-SIKSNFMLpsVRQMRKgfliDDKKGADISREY-IEKLSIKAdSIKQMAMLLSGGNQQKIVLGKW 411
Cdd:cd03218 79 YLP----QEASIFRKlTVEENILA--VLEIRG----LSKKEREEKLEElLEEFHITH-LRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 412 LARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLY 471
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIY 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
261-492 |
9.43e-19 |
|
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: 87.03 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRD----FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFG-IRRNW--TGDVAMRGEPI-KSKKDAM 328
Cdd:COG0444 1 LLEVRNlkvyFPTRRGvvkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGlLPPPGitSGEILFDGEDLlKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 329 N----KGIALVPED-----------RRQ--EGLILQHSIksnfmlpsvrqmrkgflidDKKGA-DISREYIEKLSIkADS 390
Cdd:COG0444 81 RkirgREIQMIFQDpmtslnpvmtvGDQiaEPLRIHGGL-------------------SKAEArERAIELLERVGL-PDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 391 IKQMAML---LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSelVAA--C 464
Cdd:COG0444 141 ERRLDRYpheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLG--VVAeiA 218
|
250 260 270
....*....|....*....|....*....|.
gi 1054755845 465 DRILVLYnrtvnkelSGREIE---SEEVLHH 492
Cdd:COG0444 219 DRVAVMY--------AGRIVEegpVEELFEN 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
14-265 |
1.15e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.37 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 14 QFNGVPV---LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVyTKDAGQIRIDGQE-ADLHSVEDAHKKgiAMIYQEF 89
Cdd:PRK03695 2 QLNDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPlEAWSAAELARHR--AYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 90 SLLPAMSVAEniYITREWKKGGLIDDRKnmKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQ-------DAK 162
Cdd:PRK03695 79 TPPFAMPVFQ--YLTLHQPDKTRTEAVA--SALNEVAEALGLDDKLGR-SVNQLSGGEWQRVRLAAVVLQvwpdinpAGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 163 ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATvESRDTTMEEiidKMLDAA 242
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS-GRRDEVLTP---ENLAQV 229
|
250 260
....*....|....*....|...
gi 1054755845 243 AKTSFERVERNfeqsGDPVLRVR 265
Cdd:PRK03695 230 FGVNFRRLDVE----GHPMLIST 248
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
260-470 |
1.25e-18 |
|
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: 84.07 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALV 335
Cdd:COG4133 1 MMLEAENlsCRRGERllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEdrrqeglilQHSIKSNFmlpSVR------QMRKGFLIDDkkgADIsREYIEKLSIkADSIKQMAMLLSGGNQQKIVLG 409
Cdd:COG4133 81 GH---------ADGLKPEL---TVRenlrfwAALYGLRADR---EAI-DEALEAVGL-AGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSElsELVAACDRILVL 470
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ--PLELAAARVLDL 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-222 |
1.27e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.59 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAhkKGIA 83
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPlADWSPAELA--RRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYItrewkkgGLIDDRKNMKKAEELL-KWLEidnidpRVAVE--------SLDVGYWQMVEIA 154
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAM-------GRAPHGLSRAEDDALVaAALA------QVDLAhlagrdypQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 155 KALSQ------DAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISH--RMAEVFeiCDRVTILRDGVNVA 222
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHdlNLAARY--ADRIVLLHQGRLVA 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
273-496 |
1.33e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDA--MNKGIALVPEDRRqegLILQHSI 350
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRR---VFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 KSNFMLpsvrqmrKGFLIDDKKGAD-ISREYiEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:PRK11614 98 EENLAM-------GGFFAERDQFQErIKWVY-ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 430 VAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESEEVLHHAIQG 496
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
262-473 |
1.37e-18 |
|
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: 84.45 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK------LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKkdamNKGIA 333
Cdd:cd03293 1 LEVRNvsKTYGGGggavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP----GPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 LVPedrrQEGLILQH-SIKSNFMLPsvRQMRKgflIDDKKGADISREYIEKLSIK--ADS-IKQmamlLSGGNQQKIVLG 409
Cdd:cd03293 77 YVF----QQDALLPWlTVLDNVALG--LELQG---VPKAEARERAEELLELVGLSgfENAyPHQ----LSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKA----EILRIIRQladEGVAVLMISSELSELVAACDRILVLYNR 473
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREqlqeELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSAR 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-218 |
1.40e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGIAMIYQE-FSLLPA 94
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 MSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvaveSLDVGYWQMVEIAKALSQDAKILVMDEPTSSLS 174
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPK----TLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 175 KTETKALFKVIRQLKEKGISIIYISHRMAEVfEICDRVTILRDG 218
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
269-470 |
1.98e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.55 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamNKGIALVPEDRrqeGLil 346
Cdd:COG4152 11 FGDKTAvdDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLPEER---GL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 qhsiksnfmLPSVR---QMR-----KGFlidDKKGADIS-REYIEKLSIKA---DSIKQmamlLSGGNQQKIVLGKWLAR 414
Cdd:COG4152 83 ---------YPKMKvgeQLVylarlKGL---SKAEAKRRaDEWLERLGLGDranKKVEE----LSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMiSSELSELVAA-CDRILVL 470
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF-SSHQMELVEElCDRIVII 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-218 |
2.22e-18 |
|
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: 83.74 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLhsvedahkKGIAMiyqefSLLPAMSV 97
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGG-----GFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYITREWKkgGLidDRKNMK-KAEELLKWLEI-DNIDPRVAVESldVGYWQMVEIAKALSQDAKILVMDEptsSLS- 174
Cdd:cd03220 102 RENIYLNGRLL--GL--SRKEIDeKIDEIIEFSELgDFIDLPVKTYS--SGMKARLAFAIATALEPDILLIDE---VLAv 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 175 ---KTETKALfKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03220 173 gdaAFQEKCQ-RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-251 |
2.53e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 25 NFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKdAGQIRIDGQE-ADLHSVEDAHKKgiAMIYQEFSLLPAMSVAEniYI 103
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPlSDWSAAELARHR--AYLSQQQSPPFAMPVFQ--YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 104 TREWKKGGliDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQ-------DAKILVMDEPTSSLSKT 176
Cdd:COG4138 91 ALHQPAGA--SSEAVEQLLAQLAEALGLEDKLSR-PLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 177 ETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIidkmLDAAAKTSFERVE 251
Cdd:COG4138 168 QQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN----LSEVFGVKFRRLE 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
262-489 |
2.65e-18 |
|
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: 83.77 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRT-------ELVESIFGIRrnWTGDVAMRGEPIKSKKDAmnk 330
Cdd:cd03260 1 IELRDlnVYYGDKhaLKDISLDIPKGEITALIGPSGCGKStllrllnRLNDLIPGAP--DEGEVLLDGKDIYDLDVD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 331 gialVPEDRRQEGLILQH------SIKSNFML-PSVRQMRKGFLIDDK-----KGADISREyiEKLSIKADSikqmamlL 398
Cdd:cd03260 76 ----VLELRRRVGMVFQKpnpfpgSIYDNVAYgLRLHGIKLKEELDERveealRKAALWDE--VKDRLHALG-------L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 399 SGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEgVAVLMISSELSELVAACDRILVLYNrtvnke 478
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLN------ 215
|
250
....*....|.
gi 1054755845 479 lsGREIESEEV 489
Cdd:cd03260 216 --GRLVEFGPT 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
273-470 |
2.67e-18 |
|
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: 83.69 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAmnkgiALVPEDRRQEGLILQH---- 348
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK-----ELAAFRRRHIGFVFQSfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSNFMLPSVRQMRKGFLIDDKkgadiSREYIEKLSIKaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPT 425
Cdd:cd03255 95 pdlTALENVELPLLLAGVPKKERRER-----AEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 426 IGVDVAAKAEILRIIRQLADE-GVAVLMISSELsELVAACDRILVL 470
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
2.68e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKK 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFSLLPAMSVAENIYItrewkkGGLIDDRKNMKKAEEllkwlEIDNIDPRVA------VESLDVGYWQMVEIA 154
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAM------GGFFAERDQFQERIK-----WVYELFPRLHerriqrAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 155 KALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-218 |
3.09e-18 |
|
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: 83.67 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIYQEfSLLPAMSV 97
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQE-PVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYITREWKKGGLIDDRKNMKKAEELLKWLEiDNIDPRVAVES--LDVGYWQMVEIAKALSQDAKILVMDEPTSSLSK 175
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELA-SGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 176 TETKALFKVIRQLKEKGiSIIYISHRMAEVfEICDRVTILRDG 218
Cdd:cd03248 184 ESEQQVQQALYDWPERR-TVLVIAHRLSTV-ERADQILVLDGG 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
273-491 |
3.75e-18 |
|
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: 84.09 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIalvpedRRQEGLILQHSIKS 352
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF------RRDVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVRQ-----MRKgfLIDDKKGADISR--EYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPT 425
Cdd:TIGR02769 101 VNPRMTVRQiigepLRH--LTSLDESEQKARiaELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 426 IGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNrtvnkelsGREIESEEVLH 491
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDK--------GQIVEECDVAQ 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
273-470 |
3.82e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGepikskkdamNKGIALVPedrrqeglilQHSIKS 352
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVP----------QRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVRQM-------RKGFL----IDDKKGADisrEYIEKLSIKADSIKQMAMLlSGGNQQKIVLGKWLARGPRVLIL 421
Cdd:NF040873 68 DSLPLTVRDLvamgrwaRRGLWrrltRDDRAAVD---DALERVGLADLAGRQLGEL-SGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1054755845 422 DEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELsELVAACDRILVL 470
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
273-425 |
3.98e-18 |
|
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: 81.16 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSK-KDAMNKGIALVPEDrrqEGLILQHSIK 351
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDeRKSLRKEIGYVFQD---PQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 352 SNFMLPsvrqMRKGFLIDDKKGADISrEYIEKLSIK---ADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPT 425
Cdd:pfam00005 78 ENLRLG----LLLKGLSKREKDARAE-EALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-251 |
4.28e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.24 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeADLHSVEDAH-----KKGIAMIYQEFSLLPAM 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAElrevrRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSK 175
Cdd:PRK10070 122 TVLDNTAFGMELAG---INAEERREKALDALRQVGLENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 176 -TETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVATvesrdTTMEEIIDKMLDAAAKTSFERVE 251
Cdd:PRK10070 198 lIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV-----GTPDEILNNPANDYVRTFFRGVD 269
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-218 |
5.49e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGV-PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH-KKGIAM 84
Cdd:PRK13657 336 EFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT--DIRTVTRASlRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEfSLLPAMSVAENIYITREwkkgglidDRKNmkkaEELLKWLEI----DNIDPR------VAVE---SLDVGYWQMV 151
Cdd:PRK13657 414 VFQD-AGLFNRSIEDNIRVGRP--------DATD----EEMRAAAERaqahDFIERKpdgydtVVGErgrQLSGGERQRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 152 EIAKALSQDAKILVMDEPTSSLSkTETKAlfKVIRQLKE--KGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALD-VETEA--KVKAALDElmKGRTTFIIAHRLSTVRN-ADRILVFDNG 545
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-237 |
5.59e-18 |
|
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: 83.30 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 20 VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH-KKGIAMIYQEfSLLPAMSVA 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH--DLALADPAWlRRQVGVVLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 99 ENIYITREWKKGGLIDDRKNMKKAEELLKWLEI--DNIDPRVAVeSLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKT 176
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFISELPEgyDTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 177 ETKALFKVIRQLKeKGISIIYISHRMAEVfEICDRVTILRDGvnvATVEsrDTTMEEIIDK 237
Cdd:cd03252 173 SEHAIMRNMHDIC-AGRTVIIIAHRLSTV-KNADRIIVMEKG---RIVE--QGSHDELLAE 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-218 |
6.71e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAMIY-QEFSLLPAMS 96
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY--VPFKRRKEFARRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITRE-WKkgglIDDRKNMKKAEELLKWLEIDNIdPRVAVESLDVGywQ-M-VEIAKALSQDAKILVMDEPTSSL 173
Cdd:COG4586 113 AIDSFRLLKAiYR----IPDAEYKKRLDELVELLDLGEL-LDTPVRQLSLG--QrMrCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1054755845 174 ---SKtetKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG4586 186 dvvSK---EAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-232 |
7.35e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNG---VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHK 79
Cdd:PRK13650 2 SNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KgIAMIYQ----EFSllpAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPrvavESLDVGYWQMVEIAK 155
Cdd:PRK13650 82 K-IGMVFQnpdnQFV---GATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREP----ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVfEICDRVTILRDGvnvaTVESRDTTME 232
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG----QVESTSTPRE 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-218 |
8.22e-18 |
|
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: 82.16 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVeDAHK--KGIAMIYQEFSLLP 93
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV--DISKI-GLHDlrSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 AmSVAENIYITREWKKGGLIDDRKNMKKAEELLKwlEIDNIDPRVAV--ESLDVGYWQMVEIAKALSQDAKILVMDEPTS 171
Cdd:cd03244 92 G-TIRSNLDPFGEYSDEELWQALERVGLKEFVES--LPGGLDTVVEEggENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 172 SLSKTETKALFKVIRQlKEKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:cd03244 169 SVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-218 |
9.08e-18 |
|
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: 82.28 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDG---QEADLHSVedahKKGIAMIYQEfSLLP 93
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASL----RRQIGLVSQD-VFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 AMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEiDNIDPRVAVE--SLDVGYWQMVEIAKALSQDAKILVMDEPTS 171
Cdd:cd03251 89 NDTVAENIAYGRPGATREEVEEAARAANAHEFIMELP-EGYDTVIGERgvKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 172 SLSkTETKALF-KVIRQLKEKGISIIyISHRMAEVfEICDRVTILRDG 218
Cdd:cd03251 168 ALD-TESERLVqAALERLMKNRTTFV-IAHRLSTI-ENADRIVVLEDG 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-218 |
1.03e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.86 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVED-AHKKgiAM 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRR--AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREwkkGGLIDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQ----- 159
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRA---PHGSSAAQDRQIVREALALVGLAHLAGR-SYQTLSGGEQQRVQLARVLAQlwepv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 160 --DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH--RMAEVFeiCDRVTILRDG 218
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlNLAAQY--ADRILLLHQG 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-222 |
1.04e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAhkKGIAM 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPiSMLSSRQLA--RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITRE-----WKKGGlIDDRKNMKKAEELLkwlEIDNIDPRvAVESLDVGYWQMVEIAKALSQ 159
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSpwlslWGRLS-AEDNARVNQAMEQT---RINHLADR-RLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 160 DAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
275-470 |
1.49e-17 |
|
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: 84.00 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkDAmNKGIALVPEDRR-----QEGLILQHs 349
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ---DS-ARGIFLPPHRRRigyvfQEARLFPH- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 iksnfmLpSVRQ-----MRKGFLIDDKKGADisrEYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:COG4148 92 ------L-SVRGnllygRKRAPRAERRISFD---EVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 425 TIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLL 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
273-490 |
1.83e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKK-DAMNKGIALVPEDRrqeglilqhSIK 351
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaRAASRRVASVPQDT---------SLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SNFMLPSVRQM-----RKGFLIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:PRK09536 90 FEFDVRQVVEMgrtphRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 427 GVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKelSGReieSEEVL 490
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA--AGP---PADVL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-218 |
1.93e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFN-GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEA--DLHSVEDAHKKg 81
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQE-FSLLPAMSVAENIYItrewkkGGL---IDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKAL 157
Cdd:PRK13639 80 VGIVFQNpDDQLFAPTVEEDVAF------GPLnlgLSKEEVEKRVKEALKAVGMEGFENK-PPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 158 SQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
269-470 |
2.07e-17 |
|
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: 83.62 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnKGIALVPEDRR-----QEG 343
Cdd:TIGR02142 9 LGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSR----KGIFLPPEKRRigyvfQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 344 LILQH-SIKSNfmlpsvrqMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILD 422
Cdd:TIGR02142 85 RLFPHlSVRGN--------LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1054755845 423 EPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
273-470 |
2.08e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMnkgialVPEDRRQEGLILQ----- 347
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE------VPFLRRQIGMIFQdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 348 --HSIKSNFMLPsvrqmrkgFLIDDKKGADISREY---IEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILD 422
Cdd:PRK10908 92 mdRTVYDNVAIP--------LIIAGASGDDIRRRVsaaLDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 423 EPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTL 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
275-470 |
2.70e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.42 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLyPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkDAMNKGIALVPEDRR-----QEGLILQH- 348
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL----FDSRKKINLPPQQRKiglvfQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 SIKSN--FMLPSVRQMRKGFLIDdkkgadisrEYIEKLSIkaDSIKQMAML-LSGGNQQKIVLGKWLARGPRVLILDEPT 425
Cdd:cd03297 91 NVRENlaFGLKRKRNREDRISVD---------ELLDLLGL--DHLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 426 IGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-222 |
2.94e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAHKkgIAMIYQEFSLLPAM 95
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPlESWSSKAFARK--VAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIYITREWKKGGL----IDDRknmKKAEELLKWLEIDNIDPRVaVESLDVGYWQMVEIAKALSQDAKILVMDEPTS 171
Cdd:PRK10575 101 TVRELVAIGRYPWHGALgrfgAADR---EKVEEAISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 172 SLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-242 |
3.04e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 4 NVLEMHNIEKQFNGV---------PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSV 74
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE--PLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 75 EDAHKKG----IAMIYQE-FSLL-PAMSVAEniyITREWKKGGL-IDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGY 147
Cdd:PRK10419 80 NRAQRKAfrrdIQMVFQDsISAVnPRKTVRE---IIREPLRHLLsLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 148 WQMVEIAKALSQDAKILVMDEPTSSLS---KTETKALFKVIRQlkEKGISIIYISH--RMAEVFeiCDRVTILRDG--VN 220
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQQ--QFGTACLFITHdlRLVERF--CQRVMVMDNGqiVE 232
|
250 260
....*....|....*....|..
gi 1054755845 221 VATVeSRDTTMEEIIDKMLDAA 242
Cdd:PRK10419 233 TQPV-GDKLTFSSPAGRVLQNA 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
262-470 |
4.23e-17 |
|
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: 78.80 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIAL 334
Cdd:cd03246 1 LEVENvsFRYPGAeppvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 335 VPedrrQEGLILQHSIksnfmlpsvrqmrkgfliddkkgadisreyieklsikADSIkqmamlLSGGNQQKIVLGKWLAR 414
Cdd:cd03246 81 LP----QDDELFSGSI-------------------------------------AENI------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELsELVAACDRILVL 470
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
273-470 |
4.41e-17 |
|
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: 80.46 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEpikskkDAMNKGIalvpeDRRQEGLILQH---- 348
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE------DATDVPV-----QERNVGFVFQHyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSN--FMLpsvrQMRKGFLIDDKkgADISReyieklsiKADSIKQMAML----------LSGGNQQKIVLGKWLA 413
Cdd:cd03296 87 rhmTVFDNvaFGL----RVKPRSERPPE--AEIRA--------KVHELLKLVQLdwladrypaqLSGGQRQRVALARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 414 RGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVM 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
273-491 |
6.16e-17 |
|
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: 79.93 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkGIALVPEdRRQEGLILQH---- 348
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS-----GKELRKA-RRRIGMIFQHfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSNFMLPSvrqmrkgfliddkKGADISREYIEK----------LSIKADS-IKQmamlLSGGNQQKIVLGKWLAR 414
Cdd:cd03258 95 ssrTVFENVALPL-------------EIAGVPKAEIEErvlellelvgLEDKADAyPAQ----LSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNrtvnkelsGREIESEEVLH 491
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEK--------GEVVEEGTVEE 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
259-470 |
6.22e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 79.70 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRD--FAYGNK------LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDamnK 330
Cdd:COG1136 2 SPLLELRNltKSYGTGegevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 331 GIALVpedRRQE-GLILQH-------SIKSNFMLPsvrQMRKGflIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGN 402
Cdd:COG1136 79 ELARL---RRRHiGFVFQFfnllpelTALENVALP---LLLAG--VSRKERRERARELLERVGL-GDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 403 QQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELsELVAACDRILVL 470
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRL 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-218 |
8.06e-17 |
|
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: 82.93 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVP--VLKKMN---FSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQ--IRIDGQEADLHSV- 74
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDrgVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 75 ---EDAHKKGIAMIYQEFSLLPAMSVAENIYitrewKKGGL-IDDRKNMKKAEELLKWLEID-----NIDPRVAVEsLDV 145
Cdd:TIGR03269 357 pdgRGRAKRYIGILHQEYDLYPHRTVLDNLT-----EAIGLeLPDELARMKAVITLKMVGFDeekaeEILDKYPDE-LSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 146 GYWQMVEIAKALSQDAKILVMDEPTSSLSK-TETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
273-470 |
8.34e-17 |
|
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: 78.99 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPedrrQEGLILQHSIK 351
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIP----QDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SNFmlpsvrqmrkgfliddkkgaDISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVA 431
Cdd:cd03369 100 SNL--------------------DPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1054755845 432 AKAEILRIIRQLAdEGVAVLMISSELSElVAACDRILVL 470
Cdd:cd03369 160 TDALIQKTIREEF-TNSTILTIAHRLRT-IIDYDKILVM 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
235-470 |
9.50e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 82.89 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 235 IDKMLDAAAKTSFERVERnfEQSGDPVLRVRD--FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRR 308
Cdd:COG4987 309 LNELLDAPPAVTEPAEPA--PAPGGPSLELEDvsFRYPGAgrpvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 309 NWTGDVAMRGEPIKS-KKDAMNKGIALVPedrrQEGLILQHSIKSNFML----PSVRQMRK--------GFLIDDKKGAD 375
Cdd:COG4987 387 PQSGSITLGGVDLRDlDEDDLRRRIAVVP----QRPHLFDTTLRENLRLarpdATDEELWAalervglgDWLAALPDGLD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 376 isreyieklsikaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISS 455
Cdd:COG4987 463 -------------TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITH 528
|
250
....*....|....*
gi 1054755845 456 ELSELvAACDRILVL 470
Cdd:COG4987 529 RLAGL-ERMDRILVL 542
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-224 |
9.92e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 10 NIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHSVEDAhKKGIAMIYQEF 89
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR--MNDVPPA-ERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 90 SLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvaveSLDVGYWQMVEIAKALSQDAKILVMDEP 169
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 170 TSSLSktetkALFKV-----IRQLKEK-GISIIYISHRMAEVFEICDRVTILrDGVNVATV 224
Cdd:PRK11000 161 LSNLD-----AALRVqmrieISRLHKRlGRTMIYVTHDQVEAMTLADKIVVL-DAGRVAQV 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-218 |
1.38e-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: 83.14 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 10 NIEKQFN--GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGIAMIYQ 87
Cdd:TIGR01257 933 NLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 88 EFSLLPAMSVAENIYITREWKKggliddrKNMKKAE-ELLKWLEIDNIDPRVAVESLDV--GYWQMVEIAKALSQDAKIL 164
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKG-------RSWEEAQlEMEAMLEDTGLHHKRNEEAQDLsgGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQLKEkGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
260-484 |
1.58e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRD--FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgia 333
Cdd:PRK13635 4 EIIRVEHisFRYPDAatyaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 lVPEDRRQEGLILQHSiKSNFMLPSVRqmrkgfliDD------KKGadISR-EYIEKLSikaDSIKQMAML--------- 397
Cdd:PRK13635 76 -VWDVRRQVGMVFQNP-DNQFVGATVQ--------DDvafgleNIG--VPReEMVERVD---QALRQVGMEdflnrephr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSElVAACDRILVLYNRTVN 476
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDE-AAQADRVIVMNKGEIL 219
|
....*...
gi 1054755845 477 KELSGREI 484
Cdd:PRK13635 220 EEGTPEEI 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-470 |
2.31e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 268 AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEdrrQEGLI 345
Cdd:PRK13536 50 SYGDKavVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ---FDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LQHSIKSNFMLPSvrqmrKGFLIDDKKGADISREYIE--KLSIKADSikqMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:PRK13536 127 LEFTVRENLLVFG-----RYFGMSTREIEAVIPSLLEfaRLESKADA---RVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-470 |
2.60e-16 |
|
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: 77.79 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDRR-QEGLilqhsiksn 353
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGlYDRL--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 354 fmlpSVRQMRKGF--LIDDKKGADISR--EYIEKLSIKaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:cd03266 94 ----TARENLEYFagLYGLKGDELTARleELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 430 VAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-218 |
2.63e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH 78
Cdd:PRK10584 4 ENIVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ--PLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 K-----KGIAMIYQEFSLLPAMSVAENIYITrewkkgGLI---DDRKNMKKAEELLKWLEI-DNIDPRVAveSLDVGYWQ 149
Cdd:PRK10584 82 RaklraKHVGFVFQSFMLIPTLNALENVELP------ALLrgeSSRQSRNGAKALLEQLGLgKRLDHLPA--QLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRmAEVFEICDRVTILRDG 218
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNG 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
269-470 |
2.90e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 77.26 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEdrrqEGLIL 346
Cdd:cd03268 10 YGKKrvLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA----PGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 QHSIKSNFmlpsvRQMRKGFLIDDKkgadISREYIEKLSIKADSiKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:cd03268 86 NLTARENL-----RLLARLLGIRKK----RIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 427 GVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGII 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
267-470 |
2.92e-16 |
|
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: 77.90 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK-----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPedrr 340
Cdd:cd03248 19 FAYPTRpdtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVG---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 341 QEGLILQHSIKSN--FMLPSVRQMRKGFLiDDKKGADisrEYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPR 417
Cdd:cd03248 95 QEPVLFARSLQDNiaYGLQSCSFECVKEA-AQKAHAH---SFISELASGYDTeVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSELSeLVAACDRILVL 470
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLS-TVERADQILVL 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
3.27e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.62 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQF-NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKg 81
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 IAMIYQE-----FSLLPAMSVA---ENIYITREwkkggLIDDRknmkkAEELLKWLEIDNIDPRvAVESLDVGYWQMVEI 153
Cdd:PRK13647 81 VGLVFQDpddqvFSSTVWDDVAfgpVNMGLDKD-----EVERR-----VEEALKAVRMWDFRDK-PPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 154 AKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDGVNVA 222
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
273-470 |
4.28e-16 |
|
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: 77.61 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIalvpedRRQEGLILQH---- 348
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL------RRQIGMIFQQfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSNFM------LPSVRQMRKGFLIDDKKGAdisREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVL 419
Cdd:cd03256 91 erlSVLENVLsgrlgrRSTWRSLFGLFPKEEKQRA---LAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 420 ILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGL 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
268-468 |
4.45e-16 |
|
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: 76.80 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 268 AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNkgialvpEDRRQEGLI 345
Cdd:cd03262 9 SFGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIN-------ELRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LQH-------SIKSNFMLP--SVRQMRKgfliddKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGP 416
Cdd:cd03262 82 FQQfnlfphlTVLENITLApiKVKGMSK------AEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 417 RVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRIL 468
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
275-466 |
4.68e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.63 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIK--SKKDAMNKGIALVPedrrQEGLILQH-SIK 351
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP----QEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SNFMlpSVRQMRKGFLIDDKKgaDISREYIEKLSIK--ADSIKQMamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:PRK10895 97 DNLM--AVLQIRDDLSAEQRE--DRANELMEEFHIEhlRDSMGQS---LSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 1054755845 430 VAAKAEILRIIRQLADEGVAVLMISSELSELVAACDR 466
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCER 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-218 |
6.86e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.93 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 23 KMNFSL--KKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlHSVEDAHKKGIAMIYQEFSLLPAMSVAEN 100
Cdd:PRK10771 15 PMRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRPVSMLFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 101 IYItrewkkG---GLIDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTE 177
Cdd:PRK10771 92 IGL------GlnpGLKLNAAQREKLHAIARQMGIEDLLARLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1054755845 178 TKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK10771 165 RQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-218 |
7.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.78 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVE--DAHKK-GIAMIYQEFSLLpamsv 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKvGLVFQYPEYQLF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIY--ITREWKKGGLIDD--RKNMKKAEELLKwLEIDNIDPRVAVEsLDVGYWQMVEIAKALSQDAKILVMDEPTSSL 173
Cdd:PRK13637 98 EETIEkdIAFGPINLGLSEEeiENRVKRAMNIVG-LDYEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 174 SKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13637 176 DPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-206 |
9.12e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEdahkKGIamI 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGV--V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYItrewkkgGL----IDDRKNMKKAEELLKWLEIDNIDPRVaVESLDVGYWQMVEIAKALSQDA 161
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAF-------GLqlagVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAE-VF 206
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEaVF 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-218 |
9.47e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.48 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHK---KGIAMIYQ-------E 88
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqirKKVGLVFQfpesqlfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 FSLLPAMSVA-ENIYITREwkkggliddrKNMKKAEELLKWLEID-NIDPRVAVEsLDVGYWQMVEIAKALSQDAKILVM 166
Cdd:PRK13649 101 ETVLKDVAFGpQNFGVSQE----------EAEALAREKLALVGISeSLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 167 DEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
273-470 |
9.66e-16 |
|
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: 76.16 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNW---TGDVAMRGEPikSKKDAMNKGIALVPE-DRRQEGLILQH 348
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP--RKPDQFQKCVAYVRQdDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 SIKSNFMLPSVRQMRKGflIDDKKGADISREYIEKLSIKADSIKQmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGV 428
Cdd:cd03234 101 TLTYTAILRLPRKSSDA--IRKKRVEDVLLRDLALTRIGGNLVKG----ISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 429 DVAAKAEILRIIRQLADEGVAVLM-ISSELSELVAACDRILVL 470
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLL 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-237 |
1.02e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFN-GVP----VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDL-HSVEDAHK 79
Cdd:COG1101 2 LELKNLSKTFNpGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVtKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KGIAMIYQEFSL--LPAMSVAENIYI------TREWKKGGLIDDRKNMKkaeELLKWLEI---DNIDprVAVESLDVGYW 148
Cdd:COG1101 80 KYIGRVFQDPMMgtAPSMTIEENLALayrrgkRRGLRRGLTKKRRELFR---ELLATLGLgleNRLD--TKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 149 QMVEIAKALSQDAKILVMDEPTSSLS-KTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG---VNVATV 224
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGriiLDVSGE 234
|
250
....*....|...
gi 1054755845 225 ESRDTTMEEIIDK 237
Cdd:COG1101 235 EKKKLTVEDLLEL 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
273-463 |
1.28e-15 |
|
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: 75.52 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMnkgialVPEDRRQEGLILQHS--- 349
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA------IPYLRRKIGVVFQDFrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 ----IKSNFMLPsvrqMRkgflIDDKKGADISREYIEKLSIK--ADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:cd03292 91 pdrnVYENVAFA----LE----VTGVPPREIRKRVPAALELVglSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADEGVAVLMiSSELSELVAA 463
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVV-ATHAKELVDT 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-210 |
1.28e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFN----GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHSVED 76
Cdd:PRK11629 1 MNKILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP--MSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 77 AHK-----KGIAMIYQEFSLLPAMSVAENIYITRewkkggLIDDRKNMKKAEELLKWLEIDNIDPRVAVES--LDVGYWQ 149
Cdd:PRK11629 79 AAKaelrnQKLGFIYQFHHLLPDFTALENVAMPL------LIGKKKPAEINSRALEMLAAVGLEHRANHRPseLSGGERQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISH------RMAEVFEICD 210
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHdlqlakRMSRQLEMRD 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-218 |
1.85e-15 |
|
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: 75.14 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIYQEFSLLpAMSVA 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS-LTIIPQDPTLF-SGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 99 ENIyitrewkkgglidDRKNMKKAEELLKWLEIDNidprvAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTET 178
Cdd:cd03369 100 SNL-------------DPFDEYSDEEIYGALRVSE-----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 179 KALFKVIRQLKeKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:cd03369 162 ALIQKTIREEF-TNSTILTIAHRLRTIID-YDKILVMDAG 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
256-492 |
2.02e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 256 QSGDPVLRVRD----FAY--GNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGI-RRNW--TGDVAMRGEPIKS- 323
Cdd:PRK09473 7 QQADALLDVKDlrvtFSTpdGDVTAvnDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlAANGriGGSATFNGREILNl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 324 KKDAMNKGIAlvpedrRQEGLILQHSIKS-N-FM-----LPSVRQMRKGFliddkKGADISREYIEKL-SIK-ADSIKQM 394
Cdd:PRK09473 87 PEKELNKLRA------EQISMIFQDPMTSlNpYMrvgeqLMEVLMLHKGM-----SKAEAFEESVRMLdAVKmPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 395 AML---LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:PRK09473 156 KMYpheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 235
|
250 260
....*....|....*....|....*
gi 1054755845 471 YnrtvnkelSGREIE---SEEVLHH 492
Cdd:PRK09473 236 Y--------AGRTMEygnARDVFYQ 252
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-221 |
2.29e-15 |
|
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: 75.39 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 13 KQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDA---GQIRIDGQEADLHSVedahKKGIAMIYQEF 89
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF----QKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 90 SLLPAMSVAENIYITREWKKGGLIDDRKNMKKAE-ELLKWLEIDNIDPRVaVESLDVGYWQMVEIAKALSQDAKILVMDE 168
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 169 PTSSLSKTETKALFKVIRQLKEKG-ISIIYISHRMAEVFEICDRVTILRDGVNV 221
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNrIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-223 |
3.00e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.45 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNG--VYTKDAGQIRIDGQE-ADLHSVEDA 77
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESiLDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HkKGIAMIYQEFSLLPAMSVAENIYITREWKkggliddRKNMKKAE-------ELLK-WLEIDNIDP----RVAVESLDV 145
Cdd:CHL00131 83 H-LGIFLAFQYPIEIPGVSNADFLRLAYNSK-------RKFQGLPEldpleflEIINeKLKLVGMDPsflsRNVNEGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 146 GYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH--RMAEvFEICDRVTILRDGVNVAT 223
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLD-YIKPDYVHVMQNGKIIKT 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
273-484 |
3.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.02 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDamNKGIAlvpEDRRQEGLILQHS--- 349
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETG--NKNLK---KLRKKVSLVFQFPeaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 IKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:PRK13641 98 LFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 430 VAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGREI 484
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-218 |
3.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQF--NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDA---GQIRIDGQEADLHSVE 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 76 DAHKK-GIAMIYQEFSLLPAM---SVA---ENIYITREWKKggliddrKNMKKAEELLKWLEIDNIDPrvavESLDVGYW 148
Cdd:PRK13640 81 DIREKvGIVFQNPDNQFVGATvgdDVAfglENRAVPRPEMI-------KIVRDVLADVGMLDYIDSEP----ANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 149 QMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVfEICDRVTILRDG 218
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDG 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-200 |
4.05e-15 |
|
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: 72.48 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlhsvedahkkgiami 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 yqEFSLLPAMSvaeniyitrewkkGGliddrknmkkaeellkwleidnidprvavesldvgyWQM-VEIAKALSQDAKIL 164
Cdd:cd03221 64 --KIGYFEQLS-------------GG------------------------------------EKMrLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*.
gi 1054755845 165 VMDEPTSSLSkTETKALfkVIRQLKEKGISIIYISH 200
Cdd:cd03221 93 LLDEPTNHLD-LESIEA--LEEALKEYPGTVILVSH 125
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-228 |
4.54e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 76.38 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQF----NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVyTKD-----AGQIRIDgqEADLHSVE 75
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDnwrvtADRMRFD--DIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 76 DAHKK-----GIAMIYQE--FSLLPAMSVAENI--------YITREWKKGGLiddRKnmKKAEELLKWLEIDniDPRVAV 140
Cdd:PRK15093 80 PRERRklvghNVSMIFQEpqSCLDPSERVGRQLmqnipgwtYKGRWWQRFGW---RK--RRAIELLHRVGIK--DHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 141 ES----LDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:PRK15093 153 RSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL 232
|
250
....*....|...
gi 1054755845 216 RDGVNVATVESRD 228
Cdd:PRK15093 233 YCGQTVETAPSKE 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-218 |
5.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIdgqeADLHSVEDAHKKGIAMIYQEFSLL---PAMSV 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI----AGYHITPETGNKNLKKLRKKVSLVfqfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIyITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVES---LDVGYWQMVEIAKALSQDAKILVMDEPTSSLS 174
Cdd:PRK13641 99 FENT-VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 175 KTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
273-497 |
6.05e-15 |
|
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: 74.44 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkdamnkGIALVPEDRRQEGLILQH---- 348
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL---------ALADPAWLRRQVGVVLQEnvlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 --SIKSNFML----PSVRQmrkgfLIDDKKGADiSREYIEKLSIKADSI-KQMAMLLSGGNQQKIVLGKWLARGPRVLIL 421
Cdd:cd03252 89 nrSIRDNIALadpgMSMER-----VIEAAKLAG-AHDFISELPEGYDTIvGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 422 DEPTIGVDVAAKAEILRIIRQLADeGVAVLMISSELSELVAAcDRILVLYNRTVNKELSGREIESEEVLHHAIQGL 497
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
260-470 |
6.36e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRDFA--YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAM--NKGIA 333
Cdd:PRK11300 4 PLLSVSGLMmrFGGLLAvnNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 LVPEDRRqegLILQHSIKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAML---------LSGGNQQ 404
Cdd:PRK11300 84 RTFQHVR---LFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLehanrqagnLAYGQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 405 KIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
268-470 |
7.28e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 268 AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVaMRGEPIKskkdamnkgIALVPEDRRQEG-- 343
Cdd:PRK09544 13 SFGQRrvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLR---------IGYVPQKLYLDTtl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 344 -------LILQHSIKSNFMLPSVRQMRKGFLIDdkkgadisreyieklsikadsikQMAMLLSGGNQQKIVLGKWLARGP 416
Cdd:PRK09544 83 pltvnrfLRLRPGTKKEDILPALKRVQAGHLID-----------------------APMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 417 RVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
8.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVP--VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAh 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQ----EF--SLLpAMSVA---ENIYITREwkkggliDDRKNMKKAEELLKWLEIDNIDPrvavESLDVGYWQ 149
Cdd:PRK13648 82 RKHIGIVFQnpdnQFvgSIV-KYDVAfglENHAVPYD-------EMHRRVSEALKQVDMLERADYEP----NALSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
262-470 |
8.62e-15 |
|
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: 73.32 E-value: 8.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRDF--AYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdamnkgialVPE 337
Cdd:cd03259 1 LELKGLskTYGSVRAldDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----------VPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DRRQEGLILQHSIksnfMLP--SVRQ-----MRKGfLIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGK 410
Cdd:cd03259 70 ERRNIGMVFQDYA----LFPhlTVAEniafgLKLR-GVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 411 WLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVM 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
269-475 |
9.27e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.55 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamNKGIALVpedRRQEGLI 345
Cdd:COG2884 11 YPGGreaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK---RREIPYL---RRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LQ-------HSIKSNFMLPsvrqMRkgflIDDKKGADISR---EYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARG 415
Cdd:COG2884 85 FQdfrllpdRTVYENVALP----LR----VTGKSRKEIRRrvrEVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 416 PRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELsELVAACD-RILVLYNRTV 475
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL-ELVDRMPkRVLELEDGRL 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-218 |
9.86e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAHKkgIAMI 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvATTPSRELAKR--LAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYITR-EWKKGGL-IDDRknmKKAEELLKWLEIDNIDPRVaVESLDVGYWQMVEIAKALSQDAKI 163
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRfPYSKGRLtAEDR---EIIDEAIAYLDLEDLADRY-LDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 164 LVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISH--RMAEVFeiCDRVTILRDG 218
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHdiNFASCY--ADHIVAMKDG 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
1.37e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 4 NVLEMHNIEKQFNG-VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQ---EADLHSVedahK 79
Cdd:PRK13652 2 HLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitKENIREV----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KGIAMIYQE-----FSLLPAMSVA---ENIyitrewkkgGLiDDRKNMKKAEELLKWLEIDNIDPRVAvESLDVGYWQMV 151
Cdd:PRK13652 78 KFVGLVFQNpddqiFSPTVEQDIAfgpINL---------GL-DEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 152 EIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDGVNVAtvesrDTT 230
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA-----YGT 221
|
....
gi 1054755845 231 MEEI 234
Cdd:PRK13652 222 VEEI 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
273-470 |
1.44e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIalvpedRRQEGLILQHSIKS 352
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF------RRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVRQ-----MRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIG 427
Cdd:PRK10419 102 VNPRKTVREiirepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 428 VDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVM 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-218 |
1.46e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAH-KKGIAMIYQEFSLLPA 94
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDiTRLKNREVPFlRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 MSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvaveSLDVGYWQMVEIAKALSQDAKILVMDEPTSSLS 174
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 175 KTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-221 |
1.48e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADL-HSVedaHKKGIAMIYQEFSLLpAMS 96
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlSSLsHSV---LRQGVAMVQQDPVVL-ADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITREWKKGGLIDDRKNMKKAeELLKWLEiDNIDPRVAVE--SLDVGYWQMVEIAKALSQDAKILVMDEPTSSL- 173
Cdd:PRK10790 431 FLANVTLGRDISEEQVWQALETVQLA-ELARSLP-DGLYTPLGEQgnNLSVGQKQLLALARVLVQTPQILILDEATANId 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 174 SKTEtKALFKVIRQLKEKgISIIYISHRMAEVFEiCDRVTILRDGVNV 221
Cdd:PRK10790 509 SGTE-QAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-212 |
1.92e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.15 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 15 FNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILN-------GVYTKdaGQIRIDGQeaDLHS----VEDAHKKgIA 83
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmndlipGARVE--GEILLDGE--DIYDpdvdVVELRRR-VG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPaMSVAENI---YITREWKKGGLIDDRknmkkAEELLK----WLEI-DNIDPRVAveSLDVGYWQMVEIAK 155
Cdd:COG1117 96 MVFQKPNPFP-KSIYDNVaygLRLHGIKSKSELDEI-----VEESLRkaalWDEVkDRLKKSAL--GLSGGQQQRLCIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRV 212
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYT 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
266-490 |
1.93e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 266 DFAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKD-AMNKGIALVPEdrrqe 342
Cdd:PRK11231 9 TVGYGTKriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 glilQHsiksnfMLP---SVRQM----RKGFLiddkkgadisrEYIEKLSIKADSIKQMAML--------------LSGG 401
Cdd:PRK11231 84 ----HH------LTPegiTVRELvaygRSPWL-----------SLWGRLSAEDNARVNQAMEqtrinhladrrltdLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 402 NQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSG 481
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
....*....
gi 1054755845 482 REIESEEVL 490
Cdd:PRK11231 223 EEVMTPGLL 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-218 |
1.98e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.89 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV-----YTKDAGQIRIDGqeADLHS-- 73
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNG--HNIYSpr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 74 ---VEdaHKKGIAMIYQEFSLLPaMSVAEN-IYITRewKKGglIDDRKNMKKA-EELLK----WLEIDNIDPRVAVeSLD 144
Cdd:PRK14239 79 tdtVD--LRKEIGMVFQQPNPFP-MSIYENvVYGLR--LKG--IKDKQVLDEAvEKSLKgasiWDEVKDRLHDSAL-GLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 145 VGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
273-470 |
2.06e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 72.75 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDRRQegLILQHSIKS 352
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQ--LWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLpsvrqMRKGFLIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAA 432
Cdd:cd03267 115 SFYL-----LAAIYDLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1054755845 433 KAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03267 189 QENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
273-470 |
2.38e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKD---AMNKGIALVPEDRRQEglILQHS 349
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVFQDPEQQ--IFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 IKSNFMLpSVRQMrkgflidDKKGADISREYIEKLS-IKADSIKQMAM-LLSGGNQQKIVLGKWLARGPRVLILDEPTIG 427
Cdd:PRK13638 95 IDSDIAF-SLRNL-------GVPEAEITRRVDEALTlVDAQHFRHQPIqCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 428 VDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
273-470 |
3.14e-14 |
|
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: 71.04 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNW--TGDVAMRGEPikSKKDAMNKGIALVPEDrrqEGLILQHSI 350
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRP--LDKRSFRKIIGYVPQD---DILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 KSNFMlpsvrqmrkgfliddkkgadisreYIEKLSIkadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDV 430
Cdd:cd03213 100 RETLM------------------------FAAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 431 AAKAEILRIIRQLADEGVAVLM-ISSELSELVAACDRILVL 470
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTIICsIHQPSSEIFELFDKLLLL 185
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
269-470 |
3.49e-14 |
|
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: 71.63 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDRR------ 340
Cdd:cd03265 10 YGDFEAvrGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSvddelt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 341 -QEGLILQHSIksnFMLPSVRQmrkgfliddKKGADISREYIEkLSIKADsikQMAMLLSGGNQQKIVLGKWLARGPRVL 419
Cdd:cd03265 90 gWENLYIHARL---YGVPGAER---------RERIDELLDFVG-LLEAAD---RLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 420 ILDEPTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-218 |
3.58e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKS----TLMKIL--NGVYTkdaGQIRIDGQEAdLHSVEDAHKK----GIAMIYQ 87
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGRIG---GSATFNGREI-LNLPEKELNKlraeQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 88 E--FSLLPAMSVAENIYITREWKKGgliddrknMKKA---EELLKWLEIDNIdP------RVAVESLDVGYWQMVEIAKA 156
Cdd:PRK09473 105 DpmTSLNPYMRVGEQLMEVLMLHKG--------MSKAeafEESVRMLDAVKM-PearkrmKMYPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 157 LSQDAKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
273-465 |
3.67e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdAMNKG-IALVPEDRRQEgLILQHSIK 351
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNlVAYVPQSEEVD-WSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SNFMLPSVRQMrkGFL-IDDKKGADISREYIEKLSIKADSIKQMAMLlSGGNQQKIVLGKWLARGPRVLILDEPTIGVDV 430
Cdd:PRK15056 99 DVVMMGRYGHM--GWLrRAKKRDRQIVTAALARVDMVEFRHRQIGEL-SGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1054755845 431 AAKAEILRIIRQLADEGVAVLMISSELSELVAACD 465
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-238 |
3.82e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 20 VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKgIAMIYQEFSLLPAMSVAE 99
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 100 NIYITR--------EWKKggliDDRKNMKKAeelLKWLEIDNIdPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTS 171
Cdd:PRK10253 101 LVARGRyphqplftRWRK----EDEEAVTKA---MQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 172 SLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKM 238
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
260-470 |
4.12e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIAL 334
Cdd:PRK13548 1 AMLEARNlsVRLGGRtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 335 VPedrrqeglilQHSIKSnFMLpSVRQ---M-RKGFLIDDKKGADISREYIEKLSIkadsikqmAML-------LSGGNQ 403
Cdd:PRK13548 81 LP----------QHSSLS-FPF-TVEEvvaMgRAPHGLSRAEDDALVAAALAQVDL--------AHLagrdypqLSGGEQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 404 QKIVLGKWLAR------GPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMIsseLSEL-VAA--CDRILVL 470
Cdd:PRK13548 141 QRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVV---LHDLnLAAryADRIVLL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-218 |
4.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE-ADLHSVEDAHKKG 81
Cdd:PRK13633 8 KNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 iAMIYQE-FSLLPAMSVAENIYITREwKKGglIDDRKNMKKAEELLKWLEIDNIDpRVAVESLDVGYWQMVEIAKALSQD 160
Cdd:PRK13633 88 -GMVFQNpDNQIVATIVEEDVAFGPE-NLG--IPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSG 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-218 |
5.37e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 28 LKKGEVHALLGGNGAGKSTLMKILNGVYTKD---AGQIRIDGQEADLhsveDAHKKGIAMIYQEFSLLPAMSVAENIYIT 104
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA----KEMRAISAYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 105 REWKKGGLIDDRKNMKKAEELLKWLEIDN-----IDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETK 179
Cdd:TIGR00955 124 AHLRMPRRVTKKEKRERVDEVLQALGLRKcantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 180 ALFKVIRQLKEKGISIIYISHR-MAEVFEICDRVTILRDG 218
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEG 243
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-218 |
6.62e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.41 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVY-----TKDAGQIRIDGQE---ADLHSV 74
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 75 EdaHKKGIAMIYQEFSLLPAMSVAENIYITreWKKGGLIDDRKNM-KKAEELLK----WLEI-DNIDPRVAveSLDVGYW 148
Cdd:PRK14267 82 E--VRREVGMVFQYPNPFPHLTIYDNVAIG--VKLNGLVKSKKELdERVEWALKkaalWDEVkDRLNDYPS--NLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 149 QMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLG 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-218 |
7.13e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDG---QEADLHSVedahKKGIAMIYQEFSLLPAm 95
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASL----RNQVALVSQNVHLFND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENI-YITREWKKGGLIDDRKNMKKAEELLKWLE--IDNIDPRVAVeSLDVGYWQMVEIAKALSQDAKILVMDEPTSS 172
Cdd:PRK11176 432 TIANNIaYARTEQYSREQIEEAARMAYAMDFINKMDngLDTVIGENGV-LLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 173 LSKTETKALFKVIRQLKEKGISIIyISHRMAEVfEICDRVTILRDG 218
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSLV-IAHRLSTI-EKADEILVVEDG 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-218 |
7.38e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV--YTkdaGQIRIDGQEadLHSVEDAH-KKGIAMIYQEfSLL 92
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIE--LRELDPESwRKHLSWVGQN-PQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 93 PAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEiDNIDPRVAVES--LDVGYWQMVEIAKALSQDAKILVMDEPT 170
Cdd:PRK11174 435 PHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLP-QGLDTPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 171 SSL-SKTETkalfKVIRQLKE--KGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PRK11174 514 ASLdAHSEQ----LVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDG 559
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-246 |
7.64e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEdAHKKGIAMIYQEFSLLpamsvaen 100
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-DYRKLFSAVFTDFHLF-------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 101 iyiTRewkkggLIDDRKNMKKAEELLKWLEIDNIDPRVAVE-------SLDVGYWQMVEIAKALSQDAKILVMDEPTSSL 173
Cdd:PRK10522 410 ---DQ------LLGPEGKPANPALVEKWLERLKMAHKLELEdgrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 174 SKTETKALFKV-IRQLKEKGISIIYISHRMAeVFEICDRVTILRDGvnvatvESRDTTMEEIIDKMLDAAAKTS 246
Cdd:PRK10522 481 DPHFRREFYQVlLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNG------QLSELTGEERDAASRDAVARTA 547
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-233 |
9.69e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.22 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVyTKDAGQIRIDGQ-EADLHSVEDAH------ 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRvEFFNQNIYERRvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQEFSLLPaMSVAENIYITRE---WKKGGLIDD-RKNMKKAEELlkWLEIDNIDPRVAVEsLDVGYWQMVEIA 154
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKivgWRPKLEIDDiVESALKDADL--WDEIKHKIHKSALD-LSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 155 KALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKG-ISIIYISHRMAEVFEICDRVTILRDGvnvatvESRDTTMEE 233
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGN------ENRIGQLVE 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-218 |
1.18e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 14 QFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADlHSVED--AHKKGIAMIYQE--- 88
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGllALRQQVATVFQDpeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 ------------FSLlPAMSVAENiYITREwkkgglIDDRKNMKKAEELLKwleidniDPrvaVESLDVGYWQMVEIAKA 156
Cdd:PRK13638 89 qifytdidsdiaFSL-RNLGVPEA-EITRR------VDEALTLVDAQHFRH-------QP---IQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 157 LSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-218 |
1.25e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQF---------NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHS 73
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP--LHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 74 VEDAHK-KGIAMIYQEfsllPAMSVAENIYItrewkkGGLID-------DRKNMKKAEELLKWLEIDNIDPRVAV---ES 142
Cdd:PRK15112 80 GDYSYRsQRIRMIFQD----PSTSLNPRQRI------SQILDfplrlntDLEPEQREKQIIETLRQVGLLPDHASyypHM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 143 LDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-218 |
1.32e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIdGqeadlHSVEdahkkgIAM 84
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G-----ETVK------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLL-PAMSVAENIyitREWKKGGliddrkNMKKAEELLKWLEIDNIDPRVAVESLDVGywqmvE-----IAKALS 158
Cdd:COG0488 383 FDQHQEELdPDKTVLDEL---RDGAPGG------TEQEVRGYLGRFLFSGDDAFKPVGVLSGG-----EkarlaLAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 159 QDAKILVMDEPTSSLSkTETKALfkVIRQLKE-KGiSIIYISHRMAEVFEICDRVTILRDG 218
Cdd:COG0488 449 SPPNVLLLDEPTNHLD-IETLEA--LEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDG 505
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
1.62e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNI-----EKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRID----GQEADLH 72
Cdd:PRK13631 18 DDIILRVKNLycvfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 73 SVEDAH-----------KKGIAMIYQ--EFSLLPAmSVAENIYITREWKKGGLIDDRKnmkKAEELLKWLEIDNIDPRVA 139
Cdd:PRK13631 98 ELITNPyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKK---LAKFYLNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 140 VESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
260-451 |
1.62e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRDFA--YGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskKDAMNK----G 331
Cdd:COG1137 2 MTLEAENLVksYGKRtvVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT--HLPMHKrarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 332 IALVPedrrQEGLILQH-SIKSNFMLpsVRQMRKgflIDDKKGADISREYIEKLSIkaDSI-KQMAMLLSGGNQQKIVLG 409
Cdd:COG1137 80 IGYLP----QEASIFRKlTVEDNILA--VLELRK---LSKKEREERLEELLEEFGI--THLrKSKAYSLSGGERRRVEIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVL 451
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVL 190
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-240 |
2.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.51 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNEnVLEMHNIEKQF---NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDA 77
Cdd:PRK13642 1 MNK-ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HKKgIAMIYQE-FSLLPAMSVAENIYITREWKKgglIDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKA 156
Cdd:PRK13642 80 RRK-IGMVFQNpDNQFVGATVEDDVAFGMENQG---IPREEMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 157 LSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEiCDRVTILRDG--VNVATVESRDTTMEE 233
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGeiIKEAAPSELFATSED 233
|
....*..
gi 1054755845 234 IIDKMLD 240
Cdd:PRK13642 234 MVEIGLD 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
272-472 |
2.25e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 69.67 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 272 KLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMnKGIALVPEDRrqeGLILQHSIK 351
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RDISYVPQNY---ALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SN--FMLPSVRQMRKGfliDDKKGADISreyiEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:cd03299 90 KNiaYGLKKRKVDKKE---IERKVLEIA----EMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 430 VAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd03299 162 VRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLN 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
269-470 |
2.31e-13 |
|
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: 69.14 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLA--DVSFDLYPGeILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDRRqeglil 346
Cdd:cd03264 10 YGKKRAldGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFG------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 qhsIKSNFmlPSVRQMR-----KGflIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLIL 421
Cdd:cd03264 83 ---VYPNF--TVREFLDyiawlKG--IPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1054755845 422 DEPTIGVDVAAKAEILRIIRQLADEgvAVLMISSELSELVAA-CDRILVL 470
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESlCNQVAVL 202
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
276-492 |
2.39e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.99 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 276 VSFDLYPGEILGLAGLMGSGRTELVESIFGIRR-NW--TGDvAMRGEPIKSkkdamnkgIALVPEDRRQeglILQHSIKS 352
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdNWrvTAD-RMRFDDIDL--------LRLSPRERRK---LVGHNVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSV---------RQMRKGFLIDDKKGADISR---------EYIEKLSIKA--DSIKQMAMLLSGGNQQKIVLGKWL 412
Cdd:PRK15093 94 IFQEPQScldpservgRQLMQNIPGWTYKGRWWQRfgwrkrraiELLHRVGIKDhkDAMRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 413 ARGPRVLILDEPTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVLYnrtvnkelSGREIES---EE 488
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLY--------CGQTVETapsKE 245
|
....*..
gi 1054755845 489 VL---HH 492
Cdd:PRK15093 246 LVttpHH 252
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-215 |
2.63e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.36 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNEN--VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEdAH 78
Cdd:PRK10247 1 MQENspLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGIAMIYQEFSLLpAMSVAENIYITREWKKgglidDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALS 158
Cdd:PRK10247 80 RQQVSYCAQTPTLF-GDTVYDNLIFPWQIRN-----QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 159 QDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEiCDRVTIL 215
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-218 |
2.88e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 20 VLKKMNFSLKKGEVHALLGGNGAGKST----LMKILNGvytkdAGQIRIDGQEadLHSVEDAH----KKGIAMIYQE--F 89
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQP--LHNLNRRQllpvRHRIQVVFQDpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 90 SLLPAMSVAEniyITREwkkgGLIDDRKNMKKAE---ELLKWLEIDNIDP----RVAVEsLDVGYWQMVEIAKALSQDAK 162
Cdd:PRK15134 374 SLNPRLNVLQ---IIEE----GLRVHQPTLSAAQreqQVIAVMEEVGLDPetrhRYPAE-FSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 163 ILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-218 |
3.72e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 10 NIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTK-----DAGQIRIDGQEADLHSVEDAHKKGIAM 84
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPaMSVAENIYITREWKKggLIDDRKNMKKAEELLKWLEI-DNIDPRVAVE--SLDVGYWQMVEIAKALSQDA 161
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDG 238
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-201 |
3.87e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVedAHKKGIAM 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC--TYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWKKGGL-IDDRKNMKKAEELLKWleidnidprvAVESLDVGYWQMVEIAKALSQDAKI 163
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVgITELCRLFSLEHLIDY----------PCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1054755845 164 LVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHR 201
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
268-470 |
3.93e-13 |
|
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: 68.80 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 268 AYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkdamnkgiALVPEDRRQEGLI 345
Cdd:cd03300 9 FYGGFVAldGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----------TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LQH-------SIKSNFMLPsvRQMRKgfliddKKGADISREYIEKLsikadsiKQMAML---------LSGGNQQKIVLG 409
Cdd:cd03300 78 FQNyalfphlTVFENIAFG--LRLKK------LPKAEIKERVAEAL-------DLVQLEgyanrkpsqLSGGQQQRVAIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-218 |
4.31e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQI-----RIDGQEADLHSVEDAHKK-GIAMIYQEFSLLpa 94
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyAIPANLKKIKEVKRLRKEiGLVFQFPEYQLF-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 95 msvAENIYITREWKKGGLIDDRKNM-KKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSL 173
Cdd:PRK13645 105 ---QETIEKDIAFGPVNLGENKQEAyKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1054755845 174 S-KTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13645 182 DpKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-218 |
4.40e-13 |
|
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: 71.37 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 25 NFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEdAHKKGIAMIYQEFSLLpamsvaENIYit 104
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNRE-AYRQLFSAVFSDFHLF------DRLL-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 105 rewkkgGLiDDRKNMKKAEELLKWLEIDNidpRVAVE-----SLDvgywqmveiakaLSQ--------------DAKILV 165
Cdd:COG4615 423 ------GL-DGEADPARARELLERLELDH---KVSVEdgrfsTTD------------LSQgqrkrlallvalleDRPILV 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 166 MDE------PtsslsktETKALF--KVIRQLKEKGISIIYISH--RMaevFEICDRVTILRDG 218
Cdd:COG4615 481 FDEwaadqdP-------EFRRVFytELLPELKARGKTVIAISHddRY---FDLADRVLKMDYG 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-215 |
5.29e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 13 KQFNGVpvlkkmNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAH----KKGIAMIYQE 88
Cdd:PRK15079 35 KAVDGV------TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK--DLLGMKDDEwravRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 --FSLLPAMSVAENI-----YITREWKKGGLIDDRKNMKKAEELLKwleidNIDPRVAVEsLDVGYWQMVEIAKALSQDA 161
Cdd:PRK15079 107 plASLNPRMTIGEIIaeplrTYHPKLSRQEVKDRVKAMMLKVGLLP-----NLINRYPHE-FSGGQCQRIGIARALILEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-201 |
5.55e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.85 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeADLHSV-EDAHKKGIAMIYQEFSLLpAMSV 97
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLdQDEVRRRVSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYITREwkkGGLIDDRKNMKKAEELLKWLE--IDNIDPRVA--VESLDVGYWQMVEIAKALSQDAKILVMDEPTSSL 173
Cdd:TIGR02868 426 RENLRLARP---DATDEELWAALERVGLADWLRalPDGLDTVLGegGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 1054755845 174 SKTETKALFKVIRQLKEkGISIIYISHR 201
Cdd:TIGR02868 503 DAETADELLEDLLAALS-GRTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
266-470 |
5.61e-13 |
|
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: 68.00 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 266 DFAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdamnkgiaLVPEDRRQ 341
Cdd:cd03245 9 SFSYPNQeipaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ----------LDPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 E-GLILQH------SIKSNFML--PSV---RQMRKG-------FLIDDKKGADISreyieklsikadsIKQMAMLLSGGN 402
Cdd:cd03245 79 NiGYVPQDvtlfygTLRDNITLgaPLAddeRILRAAelagvtdFVNKHPNGLDLQ-------------IGERGRGLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 403 QQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSeLVAACDRILVL 470
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVM 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
275-492 |
5.96e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKgialvpEDRRQEGLILQHSIKSnf 354
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR------AVRSDIQMIFQDPLAS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 355 MLPsvrQMRKGFLIddkkgADISREYIEKLS---IKaDSIKQMAM---LL-----------SGGNQQKIVLGKWLARGPR 417
Cdd:PRK15079 111 LNP---RMTIGEII-----AEPLRTYHPKLSrqeVK-DRVKAMMLkvgLLpnlinryphefSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYnrtvnkelSGREIE---SEEVLHH 492
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY--------LGHAVElgtYDEVYHN 252
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
261-488 |
6.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.95 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRDFAYG-----NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGialv 335
Cdd:PRK13639 1 ILETRDLKYSypdgtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 pedRRQEGLILQHSIKSNFMlPSVRQ------MRKGFliddkkgadiSREYIEKLSikADSIKQMAML---------LSG 400
Cdd:PRK13639 77 ---RKTVGIVFQNPDDQLFA-PTVEEdvafgpLNLGL----------SKEEVEKRV--KEALKAVGMEgfenkpphhLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 401 GNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLmISSELSELVAA-CDRILVLYNRTVNKEL 479
Cdd:PRK13639 141 GQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITII-ISTHDVDLVPVyADKVYVMSDGKIIKEG 219
|
....*....
gi 1054755845 480 SGREIESEE 488
Cdd:PRK13639 220 TPKEVFSDI 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
273-470 |
6.56e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVamRGEPIKSKKDAMNKGIALVpedRRQEGLILQHSIKS 352
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQKEIKPV---RKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NF---MLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:PRK13643 97 LFeetVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 430 VAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
259-455 |
6.73e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.65 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRDFA--YGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIfgirrNWTGD----VAMRGEPIKSKKDAMNK 330
Cdd:PRK14239 3 EPILQVSDLSvyYNKKkaLNSVSLDFYPNEITALIGPSGSGKSTLLRSI-----NRMNDlnpeVTITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 331 GIALVpEDRRQEGLILQH------SIKSNFmlpsVRQMR-KGflIDDKKGADisrEYIEKlSIKADSI--------KQMA 395
Cdd:PRK14239 78 RTDTV-DLRKEIGMVFQQpnpfpmSIYENV----VYGLRlKG--IKDKQVLD---EAVEK-SLKGASIwdevkdrlHDSA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 396 MLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISS 455
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRS 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
269-484 |
9.36e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 9.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEdrrQEGLIL 346
Cdd:PRK13537 17 YGDKLVvdGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ---FDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 QHSIKSN-------FMLPS--VRQMRKGFLiddkkgadisrEYiEKLSIKADSikqMAMLLSGGNQQKIVLGKWLARGPR 417
Cdd:PRK13537 94 DFTVRENllvfgryFGLSAaaARALVPPLL-----------EF-AKLENKADA---KVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNrtvnkelsGREI 484
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEE--------GRKI 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
276-492 |
1.02e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 276 VSFDLYPGEILGLAGLMGSGRTELVESIFGI-RRNWT--------GDVAMRGEPIKSKKDAMNKGIALV---------PE 337
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGItKDNWHvtadrfrwNGIDLLKLSPRERRKIIGREIAMIfqepsscldPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DRRQEGL---ILQHSIKSNFMlpSVRQMRKGFLIddkkgadisrEYIEKLSIKaDSIKQMAML---LSGGNQQKIVLGKW 411
Cdd:COG4170 106 AKIGDQLieaIPSWTFKGKWW--QRFKWRKKRAI----------ELLHRVGIK-DHKDIMNSYpheLTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 412 LARGPRVLILDEPTIGVDVAAKAEILRIIRQLAD-EGVAVLMISSELSELVAACDRILVLYnrtvnkelSGREIES---E 487
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLY--------CGQTVESgptE 244
|
....*...
gi 1054755845 488 EVL---HH 492
Cdd:COG4170 245 QILkspHH 252
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-256 |
1.10e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDgqeaDLHSVEDAHKK----GIAMIYQEfSLLP 93
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDINLKwwrsKIGVVSQD-PLLF 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 AMSVAENI-----------YITREW-------------------KKGGLIDDRKN---------MKKAEELLKWLEIDNI 134
Cdd:PTZ00265 473 SNSIKNNIkyslyslkdleALSNYYnedgndsqenknkrnscraKCAGDLNDMSNttdsnelieMRKNYQTIKDSEVVDV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 135 DPRVAVE-------------------SLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLK--EKGI 193
Cdd:PTZ00265 553 SKKVLIHdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRI 632
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 194 SIIyISHRMAEVfeicdrvtilRDGVNVATVESRDTTMEEIIDKMLDAAAKTSFERVERNFEQ 256
Cdd:PTZ00265 633 TII-IAHRLSTI----------RYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKD 684
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-196 |
1.17e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 4 NVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDA-----H 78
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 79 KKGiamiyqefsLLPAMSVAENIYITREWKKGGLIDdrknmkkAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAKALS 158
Cdd:PRK13539 81 RNA---------MKPALTVAENLEFWAAFLGGEELD-------IAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 159 QDAKILVMDEPTSSLSKTeTKALFK--VIRQLKEKGISII 196
Cdd:PRK13539 144 SNRPIWILDEPTAALDAA-AVALFAelIRAHLAQGGIVIA 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
273-484 |
1.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSK-KDAMNKGIalvpedRRQEGLILQHSIK 351
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtKDKYIRPV------RKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SNFMLPSVRQMR---KGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGV 428
Cdd:PRK13646 97 QLFEDTVEREIIfgpKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 429 DVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGREI 484
Cdd:PRK13646 177 DPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-219 |
1.29e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.10 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQF-NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAhKKGIAM 84
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR--VVNELEPA-DRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIyitrEWkkgGLiddrKN--MKKAE------ELLKWLEIDNI---DPRvaveSLDVGYWQMVEI 153
Cdd:PRK11650 81 VFQNYALYPHMSVRENM----AY---GL----KIrgMPKAEieervaEAARILELEPLldrKPR----ELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 154 AKALSQDAKILVMDEPTSSLSktetkALFKV-----IRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGV 219
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD-----AKLRVqmrleIQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
273-490 |
1.34e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkDAMNKgialvPEDRRQEGLILQHSikS 352
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI----TDDNF-----EKLRKHIGIVFQNP--D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVRQMRKGFLIDDKkgadiSREYIEKLSIKADSIKQMAML---------LSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:PRK13648 94 NQFVGSIVKYDVAFGLENH-----AVPYDEMHRRVSEALKQVDMLeradyepnaLSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 424 PTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAAcDRILVLYNRTVNKELSGREI-ESEEVL 490
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTEIfDHAEEL 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
273-488 |
1.73e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNkgialvpEDRRQEGLILQ---HS 349
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS-------DIRKKVGLVFQypeYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 IKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAML-LSGGNQQKIVLGKWLARGPRVLILDEPTIGV 428
Cdd:PRK13637 96 LFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 429 DVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVnkELSG------REIESEE 488
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC--ELQGtprevfKEVETLE 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
273-457 |
1.78e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDamnKGIALVPEDRRQEGL-------I 345
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRD---KDGQLKVADKNQLRLlrtrltmV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LQHSIKSNFM--LPSVRQMRKGFLIDDKKGA-DISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILD 422
Cdd:PRK10619 98 FQHFNLWSHMtvLENVMEAPIQVLGLSKQEArERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1054755845 423 EPTIGVDVAAKAEILRIIRQLADEGVAVLMISSEL 457
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-218 |
2.46e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeadlhsveDAHKKGIAMIYQEFSLLP----- 93
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--------DVAKFGLTDLRRVLSIIPqspvl 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 -AMSVAENIYITREWKKGGLID--DRKNMKKAeellkwleIDN----IDPRVAV--ESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:PLN03232 1322 fSGTVRFNIDPFSEHNDADLWEalERAHIKDV--------IDRnpfgLDAEVSEggENFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 165 VMDEPTSSLSKTETKALFKVIRQlKEKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSG 1445
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
267-478 |
2.63e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNKLADVSFDLYPGEILGLAGLMGSGRTELV-------ESIFGIRrnWTGDVAMRGEPIKSKKDAMnkgialvpEDR 339
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYR--YSGDVLLGGRSIFNYRDVL--------EFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 340 RQEGLILQH------SIKSNfMLPSVRQMRkgfLIDDKKGADISREYIEKLSI---KADSIKQMAMLLSGGNQQKIVLGK 410
Cdd:PRK14271 101 RRVGMLFQRpnpfpmSIMDN-VLAGVRAHK---LVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 411 WLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEgVAVLMISSELSELVAACDRILVLYNRTVNKE 478
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
262-472 |
2.76e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 65.03 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIfgiRRNW---TGDVAMRGEPIKSKKDAMNKGI 332
Cdd:cd03247 1 LSINNvsFSYPEQeqqvLKNLSLELKQGEKIALLGRSGSGKSTLLQLL---TGDLkpqQGEITLDGVPVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 333 ALVPEdrrqeglilqhsiksnfmlpsvrqmrKGFLIDDKKGADISREyieklsikadsikqmamlLSGGNQQKIVLGKWL 412
Cdd:cd03247 78 SVLNQ--------------------------RPYLFDTTLRNNLGRR------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 413 ARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSElVAACDRILVLYN 472
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTG-IEHMDKILFLEN 171
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-218 |
3.01e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRidGQEADLHSVEDahkkGIAMI 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--AGTAPLAEARE----DTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIYItrewkkgGLIDDRKnmkkaEELLKWLEIDNIDPRvAVE---SLDVGYWQMVEIAKALSQDAK 162
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGL-------GLKGQWR-----DAALQALAAVGLADR-ANEwpaALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 163 ILVMDEP---TSSLSKTETKALFKVIRQlkEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11247 154 LLLLDEPlgaLDALTRIEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-218 |
3.24e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 23 KMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHSVED-----AHKKGIAMIYQEFSLLPAMSV 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV--LFDAEKgiclpPEKRRIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENI-YITREwKKGGLIDDRKNMKKAEELLKWLEIdnidprvaveSLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKT 176
Cdd:PRK11144 94 RGNLrYGMAK-SMVAQFDKIVALLGIEPLLDRYPG----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 177 ETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11144 163 RKRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
262-470 |
3.27e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALV 335
Cdd:COG1132 340 IEFENvsFSYPGDrpvLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PedrrQEGLILQHSIKSNfmlpsVRQMRKgfliddkkgaDISREYIEKLSIKA---DSIKQM-----------AMLLSGG 401
Cdd:COG1132 420 P----QDTFLFSGTIREN-----IRYGRP----------DATDEEVEEAAKAAqahEFIEALpdgydtvvgerGVNLSGG 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 402 NQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSeLVAACDRILVL 470
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLS-TIRNADRILVL 547
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-229 |
3.61e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeadlhSVEDAHKKG-IAMIYQ------E 88
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQALQKNlVAYVPQseevdwS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 FSLLPAMSVAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNidprVAVESLDVGYWQMVEIAKALSQDAKILVMDE 168
Cdd:PRK15056 93 FPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRH----RQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 169 PTSSLS-KTETKaLFKVIRQLKEKGISIIYISHRMAEVFEICDrVTILRDGVNVATVESRDT 229
Cdd:PRK15056 169 PFTGVDvKTEAR-IISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETT 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
257-470 |
3.81e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 257 SGDPVLRVRDFA--YGNK-------LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDA 327
Cdd:PRK13631 17 SDDIILRVKNLYcvFDEKqenelvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 328 MNKGIALVPED-------RRQEGLILQH--------SIKSNFMLPSVrqmrkGFLIDDKKGADISREYIEKLSIKADSIK 392
Cdd:PRK13631 97 HELITNPYSKKiknfkelRRRVSMVFQFpeyqlfkdTIEKDIMFGPV-----ALGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 393 QMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-200 |
3.83e-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: 65.21 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHSVEDAHKKGIAMI 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 86 YQEFSLLPAMSVAENIyitREWKKgglIDDRKNMKKAeellkwleIDNIDPR----VAVESLDVGYWQMVEIAKALSQDA 161
Cdd:cd03231 79 GHAPGIKTTLSVLENL---RFWHA---DHSDEQVEEA--------LARVGLNgfedRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH 200
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
267-490 |
3.95e-12 |
|
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: 65.71 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPedrrQE 342
Cdd:cd03254 10 FSYDEKkpvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVL----QD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 GLILQHSIKSNFMLPSVRQMRKGFLIDDK-KGADisrEYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRVLI 420
Cdd:cd03254 86 TFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAH---DFIMKLPNGYDTvLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 421 LDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELVAAcDRILVLYNrtvnkelsGREIES---EEVL 490
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNA-DKILVLDD--------GKIIEEgthDELL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-228 |
4.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.73 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEAdLHSVEDAH----KKGIAMIYQefslLPAMS 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKDKYirpvRKRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENiYITREwkkggLIDDRKNMKkaeellkwLEIDNIDPRVAVESLDVGY---------WQM-------VEIAKALSQD 160
Cdd:PRK13646 98 LFED-TVERE-----IIFGPKNFK--------MNLDEVKNYAHRLLMDLGFsrdvmsqspFQMsggqmrkIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 161 AKILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRD 228
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
262-490 |
4.63e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRDFAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNwTGDVAMRGEPIKSkkdamnkgiALVPEDRRQ 341
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEA---------WSAAELARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 EGLILQHSiKSNFMLPsVRQMRKGFLIDDKKGADIS---REYIEKLSIkADSIKQMAMLLSGGNQQKI-----VLGKWLA 413
Cdd:PRK03695 71 RAYLSQQQ-TPPFAMP-VFQYLTLHQPDKTRTEAVAsalNEVAEALGL-DDKLGRSVNQLSGGEWQRVrlaavVLQVWPD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 414 RGP--RVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESEEVL 490
Cdd:PRK03695 148 INPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-235 |
5.48e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYT----------------------------------------- 56
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 57 -------------KDAGQIRIDGQEADLHSVEDAhKKGIAMIYQEfSLLPAMSVAENIYITREwkkGGLIDDRKNMKKAE 123
Cdd:PTZ00265 1261 tkeggsgedstvfKNSGKILLDGVDICDYNLKDL-RNLFSIVSQE-PMLFNMSIYENIKFGKE---DATREDVKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 124 ELLKWLEI--DNIDPRVAV--ESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKG-ISIIYI 198
Cdd:PTZ00265 1336 AIDEFIESlpNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITI 1415
|
250 260 270
....*....|....*....|....*....|....*..
gi 1054755845 199 SHRMAEVfEICDRVTILRDGVNVATVESRDTTMEEII 235
Cdd:PTZ00265 1416 AHRIASI-KRSDKIVVFNNPDRTGSFVQAHGTHEELL 1451
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
246-470 |
6.06e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 65.21 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 246 SFERVERNFEQSGDPVLRvrdfaygnklaDVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-- 323
Cdd:cd03244 4 EFKNVSLRYRPNLPPVLK-----------NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKig 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 324 KKDAMNKgIALVPedrrQEGLILQHSIKSNfmlpsvrqmrkgflID------DKKGADI-----SREYIEKLSIKADS-I 391
Cdd:cd03244 73 LHDLRSR-ISIIP----QDPVLFSGTIRSN--------------LDpfgeysDEELWQAlervgLKEFVESLPGGLDTvV 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 392 KQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSELsELVAACDRILVL 470
Cdd:cd03244 134 EEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL-DTIIDSDRILVL 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
238-473 |
6.45e-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: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 238 MLDAAAKTSFERVERNFEQSGDPVlRVrdfaygnkLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMR 317
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTGGGGV-TA--------LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 318 GEPIKSKkdamNKGIALVPedrrQEGLILQH-SIKSNFMLP-SVRQMRKgfliddKKGADISREYIEK--LSIKADS-IK 392
Cdd:COG1116 72 GKPVTGP----GPDRGVVF----QEPALLPWlTVLDNVALGlELRGVPK------AERRERARELLELvgLAGFEDAyPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 393 QmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKA----EILRIIRQladEGVAVLMISSELSELVAACDRIL 468
Cdd:COG1116 138 Q----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQE---TGKTVLFVTHDVDEAVFLADRVV 210
|
....*
gi 1054755845 469 VLYNR 473
Cdd:COG1116 211 VLSAR 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-218 |
7.12e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeaDLHSvedahkkgiamiYQEFSLLPAMS-V 97
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ--PIAD------------YSEAALRQAISvV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYITrewkKGGLiddRKNMKKA------EELLKWLEidnidpRVAVESL---DVGY--W------QM-------VEI 153
Cdd:PRK11160 420 SQRVHLF----SATL---RDNLLLAapnasdEALIEVLQ------QVGLEKLledDKGLnaWlgeggrQLsggeqrrLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 154 AKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKgiSIIYISHRMAEVfEICDRVTILRDG 218
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaQNK--TVLMITHRLTGL-EQFDRICVMDNG 549
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-469 |
8.79e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.50 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 28 LKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIridGQEADLHSVEDaHKKGIAMiYQEFSLLPA--MSVAENI-YI- 103
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLK-RFRGTEL-QDYFKKLANgeIKVAHKPqYVd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 104 ---------TREWKKGglIDDRknmKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLS 174
Cdd:COG1245 171 lipkvfkgtVRELLEK--VDER---GKLDELAEKLGLENILDR-DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 175 KTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTIL----------------RDGVNV--------ATVESRDtt 230
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygepgvygvvskpksvRVGINQyldgylpeENVRIRD-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 231 mEEIidkmldaaaktSFERVERNFEQSGDPVLRVRDF--AYGN-KLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIr 307
Cdd:COG1245 323 -EPI-----------EFEVHAPRREKEEETLVEYPDLtkSYGGfSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGV- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 308 rnwtgdvamrgepIKSKKDAMNKGIALvpedrrqeglilqhSIKSNFMLP----SVRQMRKGFLIDDKKGADISREYIEK 383
Cdd:COG1245 390 -------------LKPDEGEVDEDLKI--------------SYKPQYISPdydgTVEEFLRSANTDDFGSSYYKTEIIKP 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 384 LSIKaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVA 462
Cdd:COG1245 443 LGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDY 521
|
....*..
gi 1054755845 463 ACDRILV 469
Cdd:COG1245 522 ISDRLMV 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
273-472 |
1.04e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIAL---------------VPE 337
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLeklviqktrfkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DRRQEGLILQ--------HSIKSNFMLPSVrqmrkGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLG 409
Cdd:PRK13651 103 IRRRVGVVFQfaeyqlfeQTIEKDIIFGPV-----SMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN 472
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-217 |
1.06e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHS---VEDAHK 79
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 80 KgIAMIYQEFSLLPAMSVAENI-YITREwkkggliddrkNMKKAEELLK---WLEIDNIDPRVAVE----SLDVGYWQMV 151
Cdd:PRK11831 85 R-MSMLFQSGALFTDMNVFDNVaYPLRE-----------HTQLPAPLLHstvMMKLEAVGLRGAAKlmpsELSGGMARRA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 152 EIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRD 217
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVAD 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
271-484 |
1.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 271 NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialVPEDRRQEGLILQHSi 350
Cdd:PRK13642 21 NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN---------VWNLRRKIGMVFQNP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 kSNFMLPSVRQMRKGFLIDDKkgaDISREYIEKLSIKA-------DSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:PRK13642 91 -DNQFVGATVEDDVAFGMENQ---GIPREEMIKRVDEAllavnmlDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSElVAACDRILVLYNRTVNKELSGREI 484
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDE-AASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-218 |
1.33e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDG----QEADLHSVEDAHKK-GIAMIYQEFSLLPAM 95
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKPVRKKvGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIYITREWKkgglIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSK 175
Cdd:PRK13643 102 VLKDVAFGPQNFG----IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 176 TETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
270-470 |
1.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.15 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 270 GNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkDAMNKGIALVpedRRQEGLILQHS 349
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS--TSKNKDIKQI---RKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 IKSNF---MLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:PRK13649 95 ESQLFeetVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 427 GVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVL 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
273-470 |
1.78e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.49 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkSKKDAMNkgialvpedrRQEGLILQH---- 348
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARD----------RKVGFVFQHyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSNF-----MLPsvRQMRKgfliddkkgadiSREYIEKLSIKADSIKQMAML-------LSGGNQQKIVLGKWLA 413
Cdd:PRK10851 87 rhmTVFDNIafgltVLP--RRERP------------NAAAIKAKVTQLLEMVQLAHLadrypaqLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 414 RGPRVLILDEPTIGVDVAAKAEILRIIRQLADE----GVAVLMISSELSElVAacDRILVL 470
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkftSVFVTHDQEEAME-VA--DRVVVM 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
273-484 |
1.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMN-KGIALvpedRRQEGLILQH--- 348
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQiDAIKL----RKEVGMVFQQpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ----SIKSNFMLPsvrqMRKGFLIDDKKGADISREYIEKLSIKA---DSIKQMAMLLSGGNQQKIVLGKWLARGPRVLIL 421
Cdd:PRK14246 102 fphlSIYDNIAYP----LKSHGIKEKREIKKIVEECLRKVGLWKevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 422 DEPTIGVDVAAKAEILRIIRQLADEgVAVLMISSELSELVAACDRILVLYNRTVNKELSGREI 484
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
273-458 |
2.02e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.96 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgiALVPEDRRQEGLILQH---- 348
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK-------VDERLIRQEAGMVFQQfylf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSNFML-P-SVRQMRKgfliddKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:PRK09493 90 phlTALENVMFgPlRVRGASK------EEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADEGVAVLMISSELS 458
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
259-470 |
2.35e-11 |
|
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: 63.95 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRD--FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGirRNW---TGDVAMRGEPikskkdamnKG 331
Cdd:COG1119 1 DPLLELRNvtVRRGGKtiLDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPptyGNDVRLFGER---------RG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 332 IALVPEDRRQEGLI---LQHSIKSNfmlPSVRQM-RKGFLiddkKGADISREYIEKLSIKADSIkqMAML---------- 397
Cdd:COG1119 70 GEDVWELRKRIGLVspaLQLRFPRD---ETVLDVvLSGFF----DSIGLYREPTDEQRERAREL--LELLglahladrpf 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 --LSGGnQQKIVLgkwLAR----GPRVLILDEPTIGVDVAAKAEILRIIRQLADEG-VAVLMISSELSELVAACDRILVL 470
Cdd:COG1119 141 gtLSQG-EQRRVL---IARalvkDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-218 |
2.52e-11 |
|
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: 66.58 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 4 NVLEMHNIEKQFNGV--PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEAdLHSVEDAHkkg 81
Cdd:TIGR01257 1936 DILRLNELTKVYSGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVH--- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 82 iamiyQEFSLLPAMSVAENIYITREWKkggLIDDRKNMKKAEELLK---WlEIDNIDPRVAVESLDVGYW----QMVEIA 154
Cdd:TIGR01257 2012 -----QNMGYCPQFDAIDDLLTGREHL---YLYARLRGVPAEEIEKvanW-SIQSLGLSLYADRLAGTYSggnkRKLSTA 2082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 155 KALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
230-470 |
2.69e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 230 TMEEIIDKMLDA--AAKTSFERVER--NFEQSG-------DPVLRVRD--FAYGNK-----LADVSFDLYPGEILGLAGL 291
Cdd:TIGR00958 436 VLSYVYSGMMQAvgASEKVFEYLDRkpNIPLTGtlaplnlEGLIEFQDvsFSYPNRpdvpvLKGLTFTLHPGEVVALVGP 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 292 MGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVpedrRQEGLILQHSIKSNFmlpsvrqmrkGFLIDD 370
Cdd:TIGR00958 516 SGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALV----GQEPVLFSGSVRENI----------AYGLTD 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 371 KKGADI--------SREYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDvaakAEILRIIR 441
Cdd:TIGR00958 582 TPDEEImaaakaanAHDFIMEFPNGYDTeVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQ 657
|
250 260 270
....*....|....*....|....*....|
gi 1054755845 442 QLAD-EGVAVLMISSELSeLVAACDRILVL 470
Cdd:TIGR00958 658 ESRSrASRTVLLIAHRLS-TVERADQILVL 686
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-215 |
3.19e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 4 NVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIridgqeadlhsvEDAHKKGIA 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAM--SVAENIYITREWKKGGLIDDRKNMkKAEELLKwleidnidprVAVESLDVGYWQMVEIAKALSQDA 161
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRPGTKKEDILPALKRV-QAGHLID----------APMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 162 KILVMDEPTSSLSKTETKALFKVIRQLK-EKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-201 |
3.98e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.40 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 16 NGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlhsvedahkkGIAMIYQEfSLLPAM 95
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------DLLFLPQR-PYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIyitrewkkggliddrknmkkaeeLLKWLEIdnidprvavesLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSK 175
Cdd:cd03223 79 TLREQL-----------------------IYPWDDV-----------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*.
gi 1054755845 176 TETKALFkviRQLKEKGISIIYISHR 201
Cdd:cd03223 125 ESEDRLY---QLLKELGITVISVGHR 147
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
273-472 |
4.25e-11 |
|
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: 62.87 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSK-KDAMN--KGIALVPEDRRQEGLILqhS 349
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMVvfQNYSLLPWLTVRENIAL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 IKSnfmlpSVRQMRKGfliddkKGADISREYIEKLSIKADSIKQMAMLlSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:TIGR01184 79 VDR-----VLPDLSKS------ERRAIVEEHIALVGLTEAADKRPGQL-SGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 430 VAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYN 472
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
257-471 |
4.39e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.98 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 257 SGDPVLRVRD----F-----------AYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPI 321
Cdd:COG4608 3 MAEPLLEVRDlkkhFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 322 -KSKKDAMNKgiaLvpedRRQEGLILQHSIKS-NfmlP--SVRQM-RKGFLIDDKKGADISREYIEKLsikadsikqMAM 396
Cdd:COG4608 83 tGLSGRELRP---L----RRRMQMVFQDPYASlN---PrmTVGDIiAEPLRIHGLASKAERRERVAEL---------LEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 397 L-------------LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELS--EL 460
Cdd:COG4608 144 VglrpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSvvRH 223
|
250
....*....|.
gi 1054755845 461 VaaCDRILVLY 471
Cdd:COG4608 224 I--SDRVAVMY 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
273-470 |
5.28e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 62.45 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkDAMNkgialvpED------RRQEGLIL 346
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL----FALD-------EDararlrARHVGFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 Q--HSIKS-----NFMLP-SVRQMRkgfliDDKKGAdisREYIEK--LSIKADSI-KQmamlLSGGNQQKIVLGKWLARG 415
Cdd:COG4181 97 QsfQLLPTltaleNVMLPlELAGRR-----DARARA---RALLERvgLGHRLDHYpAQ----LSGGEQQRVALARAFATE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 416 PRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELsELVAACDRILVL 470
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDP-ALAARCDRVLRL 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-173 |
5.77e-11 |
|
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: 64.57 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIdGQEADLHSVEDAHKK-- 80
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAld 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 GIAMIYQEFS------LLPAMSVAENIYITREWKKGGliDDRKNmkkaeellkwleidnidprvaVESLDVGYWQMVEIA 154
Cdd:TIGR03719 399 PNKTVWEEISggldiiKLGKREIPSRAYVGRFNFKGS--DQQKK---------------------VGQLSGGERNRVHLA 455
|
170
....*....|....*....
gi 1054755845 155 KALSQDAKILVMDEPTSSL 173
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDL 474
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-218 |
6.29e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRI---DGQEADLHSVEDA 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 78 HKK-------GIAMIYQEFSLLPAMSVAENI---YITREWKKGGLIDDrknmkKAEELLKWLEID--NID--PRvaveSL 143
Cdd:PRK11701 82 ERRrllrtewGFVHQHPRDGLRMQVSAGGNIgerLMAVGARHYGDIRA-----TAGDWLERVEIDaaRIDdlPT----TF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 144 DVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
273-470 |
6.62e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRG----EPikSKKDAMNKGIALVPEDRRQE--GLIL 346
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDF--SKLQGIRKLVGIVFQNPETQfvGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 QHSIK---SNFMLPSVrQMRKGFlidDKKGADISREYIEKLSIKAdsikqmamlLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:PRK13644 96 EEDLAfgpENLCLPPI-EIRKRV---DRALAEIGLEKYRHRSPKT---------LSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAAcDRILVL 470
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVM 208
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-223 |
6.77e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQfNGVPVLKKMNFSLKKGEVHALLGGNGAGKS----TLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHkk 80
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRK-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 81 gIAMIYQE----FSLLPAMSVAeniyiTRE-WKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVEsLDVGYWQMVEIAK 155
Cdd:PRK10418 81 -IATIMQNprsaFNPLHTMHTH-----AREtCLALGKPADDATLTAALEAVGLENAARVLKLYPFE-MSGGMLQRMMIAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 156 ALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVAT 223
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
273-458 |
6.78e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdAMNKGIALVPEDRRQEGLILQhsiks 352
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR-SLSQQKGLIRQLRQHVGFVFQ----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVR----QMRKGFLIDDKKGAD----ISREYIEK--LSIKADSIKQMamlLSGGNQQKIVLGKWLARGPRVLILD 422
Cdd:PRK11264 93 NFNLFPHRtvleNIIEGPVIVKGEPKEeataRARELLAKvgLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1054755845 423 EPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELS 458
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-254 |
7.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.12 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQ-------EADLHSVedahKKGIAMIYQ--EFSL 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkkNKKLKPL----RKKVGIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 92 LPAmSVAENIYItrewkkGGL---IDDRKNMKKAEELLKWLeidNIDPRVAVES-LDVGYWQM--VEIAKALSQDAKILV 165
Cdd:PRK13634 99 FEE-TVEKDICF------GPMnfgVSEEDAKQKAREMIELV---GLPEELLARSpFELSGGQMrrVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 166 MDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRD--TTMEEIIDKMLDAA 242
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREifADPDELEAIGLDLP 248
|
250
....*....|...
gi 1054755845 243 AKTSFER-VERNF 254
Cdd:PRK13634 249 ETVKFKRaLEEKF 261
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
259-446 |
7.82e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 62.36 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRD--FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELV-------ESIFGIRrnWTGDVAMRGEPIKSKKda 327
Cdd:COG1117 9 EPKIEVRNlnVYYGDKQAlkDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLDGEDIYDPD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 328 MNkgialVPEDRRQEGLILQ------HSIKSNF-MLPSVRQMRKGFLIDDK-----KGADISREyieklsIKaDSIKQMA 395
Cdd:COG1117 85 VD-----VVELRRRVGMVFQkpnpfpKSIYDNVaYGLRLHGIKSKSELDEIveeslRKAALWDE------VK-DRLKKSA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 396 MLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE 446
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-237 |
8.48e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 20 VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDA--------GQIRIDGQE-ADLHSVEDAHKKgiAMIYQEFS 90
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPlAAIDAPRLARLR--AVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 91 LLPAMSVAENIYITR--EWKKGG--LIDDRKNMKKAeellkwLEIDNIDPRVA--VESLDVGYWQMVEIAKALSQ----- 159
Cdd:PRK13547 94 PAFAFSAREIVLLGRypHARRAGalTHRDGEIAWQA------LALAGATALVGrdVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 160 ----DAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEI 234
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAH 247
|
...
gi 1054755845 235 IDK 237
Cdd:PRK13547 248 IAR 250
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-218 |
9.33e-11 |
|
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: 64.07 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQ---EADLHSVEDAhkkgIAMIYQEFSLLPAm 95
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirDVTQASLRAA----IGIVPQDTVLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENI-Y----ITRewkkggliddrknmkkaEELLKWLEIDNIDPrvAVESLDVGY---------------WQMVEIAK 155
Cdd:COG5265 447 TIAYNIaYgrpdASE-----------------EEVEAAARAAQIHD--FIESLPDGYdtrvgerglklsggeKQRVAIAR 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 156 ALSQDAKILVMDEPTSSL-SKTEtKALFKVIRQLKEKGISIIyISHRMAEVFEiCDRVTILRDG 218
Cdd:COG5265 508 TLLKNPPILIFDEATSALdSRTE-RAIQAALREVARGRTTLV-IAHRLSTIVD-ADEILVLEAG 568
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
262-475 |
9.76e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.69 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRD--FAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkdamnkgIALVPEDR 339
Cdd:COG3840 2 LRLDDltYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----------TALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 340 R-----QEGLILQH-SIKSNFML---PSVRqmrkgfliddkkgadISREYIEKLsikADSIKQM---AML------LSGG 401
Cdd:COG3840 72 PvsmlfQENNLFPHlTVAQNIGLglrPGLK---------------LTAEQRAQV---EQALERVglaGLLdrlpgqLSGG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 402 NQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-203 |
1.38e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIdgqEADL-------------- 71
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---EQDLivarlqqdpprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 72 HSVEDAHKKGIAMI------YQEFSLLPAMSVAEniyitrewkkggliddrKNMKKAEELLKWLEIDN------------ 133
Cdd:PRK11147 81 GTVYDFVAEGIEEQaeylkrYHDISHLVETDPSE-----------------KNLNELAKLQEQLDHHNlwqlenrinevl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 134 ----IDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVirqLKEKGISIIYISH------RMA 203
Cdd:PRK11147 144 aqlgLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGF---LKTFQGSIIFISHdrsfirNMA 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-438 |
1.41e-10 |
|
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: 63.42 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFN-GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDgqeadlhsvedahkKGIA 83
Cdd:TIGR03719 4 IYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------------PGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIY--QEFSLLPAMSVAENIYITREWKKGGLidDRKN---MKKAEE------LLKWL-----EID-----NIDPRVA--- 139
Cdd:TIGR03719 70 VGYlpQEPQLDPTKTVRENVEEGVAEIKDAL--DRFNeisAKYAEPdadfdkLAAEQaelqeIIDaadawDLDSQLEiam 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 140 -----------VESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSkTETKALFKviRQLKEKGISIIYISH------RM 202
Cdd:TIGR03719 148 dalrcppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPGTVVAVTHdryfldNV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 203 AE-VFEIcDRVT-ILRDGVNVATVESRDTTMEE----------IIDKMLD---AAAK----------TSFERV------E 251
Cdd:TIGR03719 225 AGwILEL-DRGRgIPWEGNYSSWLEQKQKRLEQeekeesarqkTLKRELEwvrQSPKgrqakskarlARYEELlsqefqK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 252 RNFEQS---------GDPVLRVRDF--AYGNKL--ADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMrG 318
Cdd:TIGR03719 304 RNETAEiyippgprlGDKVIEAENLtkAFGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-G 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 319 EPIKskkdamnkgialvpedrrqeglilqhsiksnfmLPSVRQMRKGflIDDKK--------GADI---------SREYI 381
Cdd:TIGR03719 383 ETVK---------------------------------LAYVDQSRDA--LDPNKtvweeisgGLDIiklgkreipSRAYV 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 382 EKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVaakaEILR 438
Cdd:TIGR03719 428 GRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLR 480
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-228 |
1.51e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.45 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 23 KMNFSLKKGEVHALLGGNGAGKS----TLMKILNGVYTKDAGQIRIDGQeaDLHSVEDAHKKGI-----AMIYQE--FSL 91
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQ--DLQRISEKERRNLvgaevAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 92 LPAMSVAENIYITREWKKGGLIDDRKnmKKAEELLKWLEIDNIDPRVAV--ESLDVGYWQMVEIAKALSQDAKILVMDEP 169
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRR--QRAIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 170 TSSLSKTETKALFKVIRQLKEK-GISIIYISHRMAEVFEICDRVTILRDGVNVATVESRD 228
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
259-470 |
2.13e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.50 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRDFAY---GNK-LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkdamnkgiAL 334
Cdd:PRK10247 5 SPLLQLQNVGYlagDAKiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS----------TL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 335 VPEDRRQE-------GLILQHSIKSNFMLPsvRQMRKGFLIDDKKGADISR----EYIEKLSIKAdsikqmamlLSGGNQ 403
Cdd:PRK10247 75 KPEIYRQQvsycaqtPTLFGDTVYDNLIFP--WQIRNQQPDPAIFLDDLERfalpDTILTKNIAE---------LSGGEK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 404 QKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLA-DEGVAVLMISSELSElVAACDRILVL 470
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
382-490 |
2.31e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 382 EKLSIKADSIKQMAML---------LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLA-DEGVAVL 451
Cdd:PRK13640 119 EMIKIVRDVLADVGMLdyidsepanLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVI 198
|
90 100 110
....*....|....*....|....*....|....*....
gi 1054755845 452 MISSELSELVAAcDRILVLYNRTVNKELSGREIESEEVL 490
Cdd:PRK13640 199 SITHDIDEANMA-DQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-218 |
2.41e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 18 VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVE--DAHKKGIAMIYQE--FSLLP 93
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 AMSVAENiyITREWKKGGLIDDRKNMKKAEELLKWLeidNIDPRVAV---ESLDVGYWQMVEIAKALSQDAKILVMDEPT 170
Cdd:PRK10261 417 RQTVGDS--IMEPLRVHGLLPGKAAAARVAWLLERV---GLLPEHAWrypHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1054755845 171 SSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
261-470 |
2.48e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 60.78 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRDF--AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIfgirrNW-----TGDVAMRGEPIKSKKDAMNKg 331
Cdd:COG1126 1 MIEIENLhkSFGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-----NLleepdSGTITVDGEDLTDSKKDINK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 332 ialvpeDRRQEGLILQH-------SIKSNFMLP--SVRQMRKgfliddKKGADISREYIEK--LSIKADsikQMAMLLSG 400
Cdd:COG1126 75 ------LRRKVGMVFQQfnlfphlTVLENVTLApiKVKKMSK------AEAEERAMELLERvgLADKAD---AYPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 401 GNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFM 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-207 |
3.07e-10 |
|
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: 60.50 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 27 SLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIridgqEADLHSVedAHKKGIAMIYQEFS---LLpaMSVAENIYI 103
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTV--SYKPQYIKADYEGTvrdLL--SSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 104 TREWKKggliddrknmkkaeELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFK 183
Cdd:cd03237 92 HPYFKT--------------EIAKPLQIEQILDR-EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1054755845 184 VIRQLKEKG-----------ISIIYISHRMAeVFE 207
Cdd:cd03237 157 VIRRFAENNektafvvehdiIMIDYLADRLI-VFE 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
273-458 |
3.16e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkSKKDAMNKGialvpEDRRQE-GLILQ-HSI 350
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-SKLSSAAKA-----ELRNQKlGFIYQfHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 KSNFMlpSVRQMRKGFLIDDKKGADISREYIEKLsiKADSIKQMAML----LSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:PRK11629 99 LPDFT--ALENVAMPLLIGKKKPAEINSRALEML--AAVGLEHRANHrpseLSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|...
gi 1054755845 427 GVDVAAKAEILRIIRQL-ADEGVAVLMISSELS 458
Cdd:PRK11629 175 NLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
276-452 |
3.23e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 276 VSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEdrrqeglilQHSIKSnfM 355
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH---------APGIKT--T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 356 LPSVRQMRkgFLIDDKkgadiSREYIEklsikaDSIKQMAM---------LLSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:cd03231 88 LSVLENLR--FWHADH-----SDEQVE------EALARVGLngfedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*.
gi 1054755845 427 GVDVAAKAEILRIIRQLADEGVAVLM 452
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVL 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
273-470 |
3.23e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.37 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWT---GDVAMRGEPIKSKKdaMNKGIALVPED-------RRQE 342
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKE--MRAISAYVQQDdlfiptlTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 GLILQhsikSNFMLPsvRQMRKgflidDKKGADISrEYIEKLSIK--ADSIKQMAML---LSGGNQQKIVLGKWLARGPR 417
Cdd:TIGR00955 119 HLMFQ----AHLRMP--RRVTK-----KEKRERVD-EVLQALGLRkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMI----SSELSELVaacDRILVL 470
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILM 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
282-470 |
3.63e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 282 PGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPE-DRRQEGLILQHSIksnfmlpsvr 360
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQfDAIDDLLTGREHL---------- 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 361 qmrkgFLIDDKKGadISREYIEK----------LSIKADsikQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDV 430
Cdd:TIGR01257 2034 -----YLYARLRG--VPAEEIEKvanwsiqslgLSLYAD---RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 431 AAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
261-490 |
4.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRDFAY---GNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialV 335
Cdd:PRK13652 3 LIETRDLCYsysGSKeaLNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---------I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEDRRQEGLILQHSIKSNFMlPSVRQ------MRKGflIDDKKGADISREYIEKLSIKaDSIKQMAMLLSGGNQQKIVLG 409
Cdd:PRK13652 74 REVRKFVGLVFQNPDDQIFS-PTVEQdiafgpINLG--LDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESEE 488
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
..
gi 1054755845 489 VL 490
Cdd:PRK13652 230 DL 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
273-470 |
4.30e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.32 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEpikskkDAMnkgIALVPEDRRQeGLILQHsiks 352
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR------DLF---TNLPPRERRV-GFVFQH---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 nFML-P--SVRQ-----MRKGFLIDDKKGADIsREYIEKLsikadsikQMAML-------LSGGNQQKIVLGKWLARGPR 417
Cdd:COG1118 84 -YALfPhmTVAEniafgLRVRPPSKAEIRARV-EELLELV--------QLEGLadrypsqLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVM 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-226 |
4.88e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.25 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMK-ILNGVYTKdaGQIRIDGQEADLHSVEDaHKKGIAMIYQEFSLLPAm 95
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLNTE--GDIQIDGVSWNSVPLQK-WRKAFGVIPQKVFIFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVAENIYITREWKkgglidDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYW------QMVEIAKALSQDAKILVMDEP 169
Cdd:cd03289 92 TFRKNLDPYGKWS------DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVlshghkQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 170 TSSLSKTETKALFKVIRQlKEKGISIIYISHRMAEVFEiCDRVTILRDGvNVATVES 226
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEEN-KVRQYDS 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
273-490 |
5.31e-10 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 61.69 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPedrrQEGLILQHSIK 351
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLP----QDVELFDGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 352 SNF-MLPSVrqmrkgfliDDKK--------GADisrEYIEKLsikAD----SIKQMAMLLSGGNQQKIVLGKWLARGPRV 418
Cdd:COG4618 424 ENIaRFGDA---------DPEKvvaaaklaGVH---EMILRL---PDgydtRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 419 LILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSeLVAACDRILVLYNRTVnkELSGreiESEEVL 490
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRV--QAFG---PRDEVL 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
267-472 |
5.36e-10 |
|
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: 59.55 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPEDRrqe 342
Cdd:cd03253 8 FAYDPGrpvLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 gLILQHSIKSN--FMLPSVRQMRkgfLIDDKKGADISREyIEKLSIKADSI-KQMAMLLSGGNQQKIVLGKWLARGPRVL 419
Cdd:cd03253 85 -VLFNDTIGYNirYGRPDATDEE---VIEAAKAAQIHDK-IMRFPDGYDTIvGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 420 ILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSElVAACDRILVLYN 472
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLST-IVNADKIIVLKD 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
267-490 |
5.79e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.00 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYG----NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialVPEDRRQE 342
Cdd:PRK13632 15 FSYPnsenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---------LKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 GLILQHSiKSNFMLPSVR-------QMRKgflIDDKKGADISREYIEKLSIKaDSIKQMAMLLSGGNQQKIVLGKWLARG 415
Cdd:PRK13632 86 GIIFQNP-DNQFIGATVEddiafglENKK---VPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 416 PRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLM-ISSELSELVAAcDRILVLYNRTVNKELSGREI-ESEEVL 490
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAILA-DKVIVFSEGKLIAQGKPKEIlNNKEIL 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-470 |
6.46e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRG-EPIKSKKdAMNKGIALVPEDRRQegLILQHSIKSN 353
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRRK-EFARRIGVVFGQRSQ--LWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 354 FMLpsvrqMRKGFLIDDKKGADISREYIEKLSIKaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAK 433
Cdd:COG4586 117 FRL-----LKAIYRIPDAEYKKRLDELVELLDLG-ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 1054755845 434 AEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVL 470
Cdd:COG4586 191 EAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
249-492 |
8.83e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.23 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 249 RVERNFEQSGDPVLRVRDF--AYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEpiksk 324
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLtkSFDGQHAvdDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 325 kdamnkGIALVPEDRRQEGLILQhsikSNFMLP--SVRQMRKGFLIDDK-KGADISREYIEKLSI--KADSIKQMAMLLS 399
Cdd:PRK11607 82 ------DLSHVPPYQRPINMMFQ----SYALFPhmTVEQNIAFGLKQDKlPKAEIASRVNEMLGLvhMQEFAKRKPHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 400 GGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEI-LRIIRQLADEGVAVLMISSELSELVAACDRILVLyNRTVNKE 478
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM-NRGKFVQ 230
|
250
....*....|....
gi 1054755845 479 LSgreiESEEVLHH 492
Cdd:PRK11607 231 IG----EPEEIYEH 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-203 |
9.27e-10 |
|
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: 59.30 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 29 KKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIridGQEADLHSVEDAHKKGIAMIYQEFSLLPAMSVA------ENIY 102
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIvkpqyvDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 103 ITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALF 182
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDELVDQLELRHVLDR-NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180
....*....|....*....|.
gi 1054755845 183 KVIRQLKEKGISIIYISHRMA 203
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHDLA 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
399-470 |
9.91e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.60 E-value: 9.91e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 399 SGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVL 470
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
259-493 |
1.06e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.48 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRDFAYG-----NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkDAMNKGIA 333
Cdd:PRK13636 3 DYILKVEELNYNysdgtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI----DYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 lvpEDRRQEGLILQhSIKSNFMLPSVRQMRKGFLIDDKKGADISREYIEKlSIKADSIKQM----AMLLSGGNQQKIVLG 409
Cdd:PRK13636 79 ---KLRESVGMVFQ-DPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDN-ALKRTGIEHLkdkpTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 410 KWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESE- 487
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEk 233
|
....*.
gi 1054755845 488 EVLHHA 493
Cdd:PRK13636 234 EMLRKV 239
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-102 |
1.16e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeadlHSVEDAHK-KGIA 83
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-----KTATRGDRsRFMA 85
|
90
....*....|....*....
gi 1054755845 84 MIYQEFSLLPAMSVAENIY 102
Cdd:PRK13543 86 YLGHLPGLKADLSTLENLH 104
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-221 |
1.47e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 7 EMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKD--AGQIRIDG---------------QEA 69
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkkqetfarisgycEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 70 DLHSVEDAHKKgiAMIYQEFSLLPAmsvaeniYITREWKkggliddrknMKKAEELLKWLEIDNIDPRV----AVESLDV 145
Cdd:PLN03140 962 DIHSPQVTVRE--SLIYSAFLRLPK-------EVSKEEK----------MMFVDEVMELVELDNLKDAIvglpGVTGLST 1022
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 146 GYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMA-EVFEICDRVTILRDGVNV 221
Cdd:PLN03140 1023 EQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQV 1099
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-218 |
1.55e-09 |
|
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: 57.66 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 10 NIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV---YTKDAGQIRIDGQEADlhsvEDA--HKKGIAM 84
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYK----EFAekYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLPAMSVAENIYITREWK--------KGGlidDRKNMKKAEELLKwleidnidprvavesldvgywqmveiaka 156
Cdd:cd03233 88 VSEEDVHFPTLTVRETLDFALRCKgnefvrgiSGG---ERKRVSIAEALVS----------------------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 157 lsqDAKILVMDEPTSSLSKTETKALFKVIRQL--KEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:cd03233 136 ---RASVLCWDNSTRGLDSSTALEILKCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
269-472 |
1.57e-09 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 58.04 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEpikskkdAMNKgialVPEDRRQEGLIL 346
Cdd:cd03301 10 FGNVTAldDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-------DVTD----LPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 QhsiksNFML-P--SVRQ-MRKGFliddkKGADISREYIEKLSIKADSIKQMAMLL-------SGGNQQKIVLGKWLARG 415
Cdd:cd03301 79 Q-----NYALyPhmTVYDnIAFGL-----KLRKVPKDEIDERVREVAELLQIEHLLdrkpkqlSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 416 PRVLILDEPTIGVD----VAAKAEILRIIRQLadeGVAVLMISSELSELVAACDRILVLYN 472
Cdd:cd03301 149 PKVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-212 |
1.79e-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: 60.18 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGvpvlkkmnFSL-------KKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRID---------- 65
Cdd:COG1245 339 ETLVEYPDLTKSYGG--------FSLeveggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyi 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 66 GQEADLhSVEDahkkgiamiyqefsLLpaMSVAENIYITREWKkggliddrknmkkaEELLKWLEIDNIDPRvAVESLDV 145
Cdd:COG1245 411 SPDYDG-TVEE--------------FL--RSANTDDFGSSYYK--------------TEIIKPLGLEKLLDK-NVKDLSG 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 146 GYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQL-KEKGISIIYISHRMAEVFEICDRV 212
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-469 |
2.18e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 28 LKKGEVHALLGGNGAGKSTLMKILngvytkdAGQIR----IDGQEADLHSVEDaHKKGIAMiYQEFSLLPA--MSVAENI 101
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIpnlgDYEEEPSWDEVLK-RFRGTEL-QNYFKKLYNgeIKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 102 -YI----------TREWKKGglIDDRknmKKAEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPT 170
Cdd:PRK13409 167 qYVdlipkvfkgkVRELLKK--VDER---GKLDEVVERLGLENILDR-DISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 171 SSLSKTETKALFKVIRQLKEkGISIIYISHRMAEVFEICDRVTIL----------------RDGVNV--------ATVES 226
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIAygepgaygvvskpkgvRVGINEylkgylpeENMRI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 227 RDttmEEIidkmldaaaktSFE-RVERNfEQSGDPVLRVRDF--AYGN-KLADVSFDLYPGEILGLAGLMGSGRTELVES 302
Cdd:PRK13409 320 RP---EPI-----------EFEeRPPRD-ESERETLVEYPDLtkKLGDfSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 303 IFGIRR------NWTGDVAMRGEPIKSKKDAmnkgialvpedRRQEGLilqHSIKSNFMLPSVRQmrkgfliddkkgadi 376
Cdd:PRK13409 385 LAGVLKpdegevDPELKISYKPQYIKPDYDG-----------TVEDLL---RSITDDLGSSYYKS--------------- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 377 srEYIEKLSIKaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISS 455
Cdd:PRK13409 436 --EIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDH 512
|
490
....*....|....*.
gi 1054755845 456 ELS--ELVAacDRILV 469
Cdd:PRK13409 513 DIYmiDYIS--DRLMV 526
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
258-470 |
2.20e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 59.75 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 258 GDPVLRVRDFAYG---NKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIA 333
Cdd:TIGR01193 472 GDIVINDVSYSYGygsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 LVPedrrQEGLILQHSIKSNFMLPSVRQMRKGFLIDDKKGADISREyIEKLSIKAD-SIKQMAMLLSGGNQQKIVLGKWL 412
Cdd:TIGR01193 552 YLP----QEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDD-IENMPLGYQtELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 413 ARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEgvAVLMISSELSeLVAACDRILVL 470
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLS-VAKQSDKIIVL 681
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-207 |
2.44e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 25 NFSL-------KKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDgqeadlhsVEDAHKKgiamiyQEFSLLPAMSV 97
Cdd:PRK13409 352 DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------LKISYKP------QYIKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYitrewKKGGLIDDrkNMKKaEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTE 177
Cdd:PRK13409 418 EDLLR-----SITDDLGS--SYYK-SEIIKPLQLERLLDK-NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 178 TKALFKVIRQL---KEKGISII--------YISHRMAeVFE 207
Cdd:PRK13409 489 RLAVAKAIRRIaeeREATALVVdhdiymidYISDRLM-VFE 528
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
270-470 |
2.46e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.47 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 270 GNKLAD-VSFDLYPGEILGLAGLMGSGRTELVESIFGIRrNWTGDVAMRGEPIKSkkdamnkgiaLVPEDRR-------Q 341
Cdd:PRK11174 362 GKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRE----------LDPESWRkhlswvgQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 EGLILQHSIKSNFML--PSVRQMRKGFLIDDkkgADISrEYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRV 418
Cdd:PRK11174 431 NPQLPHGTLRDNVLLgnPDASDEQLQQALEN---AWVS-EFLPLLPQGLDTpIGDQAAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 419 LILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSELSELvAACDRILVL 470
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDL-AQWDQIWVM 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
256-471 |
3.42e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.35 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 256 QSGDPVLRVRDFAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKG 331
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDnlvLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 332 IALVpedrRQEGLILQHSIKSNFMLpsvrqmrkgfliddkkGADISREYI----EKLSIkADSIKQM-----AML----- 397
Cdd:PRK10790 417 VAMV----QQDPVVLADTFLANVTL----------------GRDISEEQVwqalETVQL-AELARSLpdglyTPLgeqgn 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 398 -LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEI---LRIIRqladEGVAVLMISSELSELVAAcDRILVLY 471
Cdd:PRK10790 476 nLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIqqaLAAVR----EHTTLVVIAHRLSTIVEA-DTILVLH 548
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
235-470 |
3.59e-09 |
|
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: 58.96 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 235 IDKMLdAAAKTSFERVERNFEQS--GDPVLRVR--------DFAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELV 300
Cdd:TIGR02203 297 MQRGL-AAAESLFTLLDSPPEKDtgTRAIERARgdvefrnvTFRYPGRdrpaLDSISLVIEPGETVALVGRSGSGKSTLV 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 301 ESIFGIRRNWTGDVAMRGEPIKSKK-DAMNKGIALVPedrrQEGLILQHSIKSNFMLPSVRQMRKGfLIDDKKGADISRE 379
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTlASLRRQVALVS----QDVVLFNDTIANNIAYGRTEQADRA-EIERALAAAYAQD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 380 YIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDvaakAEILRIIRQLAD---EGVAVLMISS 455
Cdd:TIGR02203 451 FVDKLPLGLDTpIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD----NESERLVQAALErlmQGRTTLVIAH 526
|
250
....*....|....*
gi 1054755845 456 ELSELVAAcDRILVL 470
Cdd:TIGR02203 527 RLSTIEKA-DRIVVM 540
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
273-484 |
3.61e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkgialVPEDRRQEGLILQHSiKS 352
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN---------VWDIRHKIGMVFQNP-DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLPSVRqmrkgfliDD------KKGadISREYIEKLSIKADSIKQMAML-------LSGGNQQKIVLGKWLARGPRVL 419
Cdd:PRK13650 93 QFVGATVE--------DDvafgleNKG--IPHEEMKERVNEALELVGMQDFkereparLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 420 ILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSElVAACDRILVLYNRTVNKELSGREI 484
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
273-478 |
3.67e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkdAMNKgialvpEDR-----RQEGLILQ 347
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH----QMDE------EARaklraKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 348 hsiksNFML-PSVRQMRKGFL------IDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLI 420
Cdd:PRK10584 96 -----SFMLiPTLNALENVELpallrgESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 421 LDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKE 478
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
246-470 |
3.76e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.07 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 246 SFERVERNFEQSGDPVLRvrdfaygnklaDVSFDLYPGEILGLAGLMGSGRTELVESIfgiRRNW---TGDVAMRGEPIK 322
Cdd:PRK11160 340 TLNNVSFTYPDQPQPVLK-----------GLSLQIKAGEKVALLGRTGCGKSTLLQLL---TRAWdpqQGEILLNGQPIA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 323 S-KKDAMNKGIALVPedrrQEGLILQHSIKSNFMLPS-----------VRQMRKGFLIDDKKGADisreyieklsikads 390
Cdd:PRK11160 406 DySEAALRQAISVVS----QRVHLFSATLRDNLLLAApnasdealievLQQVGLEKLLEDDKGLN--------------- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 391 ikqmAML------LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELvAAC 464
Cdd:PRK11160 467 ----AWLgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGL-EQF 540
|
....*.
gi 1054755845 465 DRILVL 470
Cdd:PRK11160 541 DRICVM 546
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
273-452 |
3.77e-09 |
|
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: 56.60 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEdrrQEGLILQHSIKS 352
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH---LPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMlpsvrqmrkgFLIDDKKGADISREyieklsikaDSIKQMAML---------LSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:TIGR01189 93 NLH----------FWAAIHGGAQRTIE---------DALAAVGLTgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180
....*....|....*....|....*....
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADEGVAVLM 452
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLL 182
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-226 |
4.05e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 3 ENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGqIRIDGQ---------EADLHS 73
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKvtfhgknlyAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 74 VEdaHKKGIAMIYQEFSLLPAmSVAENI-YITREWKKGGLIDD--RKNMKKAeelLKWLEI-DNIdpRVAVESLDVGYWQ 149
Cdd:PRK14243 87 VE--VRRRIGMVFQKPNPFPK-SIYDNIaYGARINGYKGDMDElvERSLRQA---ALWDEVkDKL--KQSGLSLSGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 150 MVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKgISIIYISHRMAEVFEICDRVTILrdgvNVATVES 226
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFF----NVELTEG 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
273-470 |
4.97e-09 |
|
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: 57.27 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkdAMNKGiALVPEDRRQEGLILQH---- 348
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA----AMSRK-ELRELRRKKISMVFQSfall 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 ---SIKSNFMLP-SVRQMRKgfliddKKGADISREYIEKLSIKaDSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:cd03294 115 phrTVLENVAFGlEVQGVPR------AEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 425 TIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVL 470
Cdd:cd03294 188 FSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIM 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-215 |
4.98e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 13 KQFNGVpvlkkmNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAH--KKGIAMIYQE-- 88
Cdd:PRK11308 29 KALDGV------SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVFQNpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 FSLLPAMSV----AENIYITREWKKggliDDRKnmKKAEELLKwleidnidpRVAV--ESLDV-------GYWQMVEIAK 155
Cdd:PRK11308 103 GSLNPRKKVgqilEEPLLINTSLSA----AERR--EKALAMMA---------KVGLrpEHYDRyphmfsgGQRQRIAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 156 ALSQDAKILVMDEPTSSLS---KTETKALFKVIRQlkEKGISIIYISHRMAEVFEICDRVTIL 215
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDvsvQAQVLNLMMDLQQ--ELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
273-487 |
5.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDamnkgialVPEDRRQEGLILQHSiks 352
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--------LWDIRNKAGMVFQNP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 nfmlpsvrqmrkgfliDDKKGADISREYI----EKLSIKADSI--------KQMAM---------LLSGGNQQKIVLGKW 411
Cdd:PRK13633 95 ----------------DNQIVATIVEEDVafgpENLGIPPEEIrervdeslKKVGMyeyrrhaphLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 412 LARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAAcDRILVLYNRTVNKELSGREIESE 487
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
254-495 |
7.08e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 254 FEQSGDPVLRVRDFAYGNK-------LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkd 326
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKtpfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 327 AMNKGIALVPEDRRQEGLILQHSIKSNFMLPSVRQMRKG--FLIDDKKGA-DISREYIEKLSIKADSIKQMAMLLSGGNQ 403
Cdd:PRK13645 77 ANLKKIKEVKRLRKEIGLVFQFPEYQLFQETIEKDIAFGpvNLGENKQEAyKKVPELLKLVQLPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 404 QKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVNKELSGR 482
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
250
....*....|...
gi 1054755845 483 EIESEEVLHHAIQ 495
Cdd:PRK13645 237 EIFSNQELLTKIE 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
266-458 |
7.52e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.17 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 266 DFAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVpedRRQEG 343
Cdd:COG4161 9 NCFYGSHqaLFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLL---RQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 344 LILQH-------SIKSNFMLPSVRqmrkgFLIDDKKGADISREYIEK---LSIKADSikqMAMLLSGGNQQKIVLGKWLA 413
Cdd:COG4161 86 MVFQQynlwphlTVMENLIEAPCK-----VLGLSKEQAREKAMKLLArlrLTDKADR---FPLHLSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1054755845 414 RGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELS 458
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVE 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-201 |
8.44e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADlhsvedahkkgiam 84
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 85 IYQEFSLLpamsvaENIYItrewkkggliddRKNMKKAEELLKWLEI-DNIDPRVAVESLDVGYWQMVEIAKALSQDAKI 163
Cdd:COG2401 96 FGREASLI------DAIGR------------KGDFKDAVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1054755845 164 LVMDEPTSSLSKTETKAL-FKVIRQLKEKGISIIYISHR 201
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVaRNLQKLARRAGITLVVATHH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
260-443 |
8.58e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRDFAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRR-----NWTGDVAMRGEPIKSKKDAMNK 330
Cdd:PRK14258 6 PAIKVNNLSFYYDtqkiLEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 331 GialvpedRRQEGLILQhsiKSNFMLPSVRQ----------MRKGFLIDD-----KKGADISREYIEKlsikadsIKQMA 395
Cdd:PRK14258 86 L-------RRQVSMVHP---KPNLFPMSVYDnvaygvkivgWRPKLEIDDivesaLKDADLWDEIKHK-------IHKSA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 396 MLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQL 443
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSL 196
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-96 |
9.37e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV--YTKDAGQIRIDGQEADLHSVEDAHKKGI 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90
....*....|....
gi 1054755845 83 AMIYQEFSLLPAMS 96
Cdd:PRK09580 81 FMAFQYPVEIPGVS 94
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-63 |
1.19e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.19e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 1 MNENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIR 63
Cdd:PRK15064 315 LHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-218 |
1.29e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.02 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRidgqeadlhsvedaHKKGIAMIYQEFSLLPAmS 96
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------------HSGRISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKT 176
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 177 ETKALFK--VIRQLKEKgiSIIYISHRMaEVFEICDRVTILRDG 218
Cdd:cd03291 194 TEKEIFEscVCKLMANK--TRILVTSKM-EHLKKADKILILHEG 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-219 |
1.51e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 20 VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDG---QEADLHSVedahKKGIAMIYQEfSLLPAMS 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHDL----RFKITIIPQD-PVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIyitrewkkgglidDRKNMKKAEELLKWLEIDNIDPRVAV-------------ESLDVGYWQMVEIAKALSQDAKI 163
Cdd:TIGR00957 1376 LRMNL-------------DPFSQYSDEEVWWALELAHLKTFVSAlpdkldhecaeggENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 164 LVMDEPTSSLSkTETKALFKVIRQLKEKGISIIYISHRMAEVFEICdRVTILRDGV 219
Cdd:TIGR00957 1443 LVLDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1496
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
266-470 |
1.58e-08 |
|
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: 55.31 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 266 DFAYGNK----LADVSFDLYPGEILGLAGLMGSGRTELVESIfgiRRNW---TGDVAMRGEPIKSKK-DAMNKGIALVPe 337
Cdd:cd03251 7 TFRYPGDgppvLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRFYdvdSGRILIDGHDVRDYTlASLRRQIGLVS- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 drrQEGLILQHSIKSNFM--LPSVRQMRkgfLIDDKKGADiSREYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLAR 414
Cdd:cd03251 83 ---QDVFLFNDTVAENIAygRPGATREE---VEEAARAAN-AHEFIMELPEGYDTvIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELVAAcDRILVL 470
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVL 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
398-491 |
1.59e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNrtvn 476
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQ---- 244
|
90
....*....|....*...
gi 1054755845 477 kelsGREIES---EEVLH 491
Cdd:PRK10261 245 ----GEAVETgsvEQIFH 258
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
398-493 |
2.42e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNK 477
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|....*....
gi 1054755845 478 ELSGREIESEEV---LHHA 493
Cdd:PRK10938 216 TGEREEILQQALvaqLAHS 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-219 |
2.77e-08 |
|
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: 56.84 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRidgqeadlhsvedaHKKGIAMIYQEFSLLPAmS 96
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------------HSGRISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITREWKKGGLIDDRKNMKKAEELLKWLEIDNIDPRVAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKT 176
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1054755845 177 ETKALFK--VIRQLKEKgiSIIYISHRMaEVFEICDRVTILRDGV 219
Cdd:TIGR01271 583 TEKEIFEscLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEGV 624
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
398-484 |
2.84e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAD-EGVAVLMISSELSELVAACDRILVLYNRTVN 476
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*...
gi 1054755845 477 KELSGREI 484
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-218 |
3.00e-08 |
|
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: 53.79 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGvyTKDA----GQIRIDGQEadlhsVEDAHKKGIAMIYQEFSLLPAMS 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRP-----LDKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITrEWKKGGLIDDRKnmkkaeellkwleidnidprvavesldvgywqMVEIAKALSQDAKILVMDEPTSSLSKT 176
Cdd:cd03232 96 VREALRFS-ALLRGLSVEQRK--------------------------------RLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 177 ETKALFKVIRQLKEKGISII-YISHRMAEVFEICDRVTILRDG 218
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-218 |
3.68e-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: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 29 KKGEVHALLGGNGAGKSTLMKILN-----GVYTK----------DAGQIRIDG--QEADLHSVEDAHKKgiAMIYQEFSL 91
Cdd:TIGR00956 787 KPGTLTALMGASGAGKTTLLNVLAervttGVITGgdrlvngrplDSSFQRSIGyvQQQDLHLPTSTVRE--SLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 92 LPAmsvaeniYITREWKkggliddrknMKKAEELLKWLEIDNI-DPRVAV--ESLDVGYWQMVEIAKALSQDAKILV-MD 167
Cdd:TIGR00956 865 QPK-------SVSKSEK----------MEYVEEVIKLLEMESYaDAVVGVpgEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 168 EPTSSLSKTETKALFKVIRQLKEKGISIIYISHR-MAEVFEICDRVTILRDG 218
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpSAILFEEFDRLLLLQKG 979
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-218 |
4.17e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlhsvedahkkgiAMIYQEFSLLPAMSVAEN 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------------ALIAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 101 IyitrEWKkgGLIDDRKNMKKAEELLKWLEIDNIDPRV--AVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTET 178
Cdd:PRK13545 106 I----ELK--GLMMGLTKEKIKEIIPEIIEFADIGKFIyqPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1054755845 179 KALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
273-488 |
4.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRnwtgdvAMRGEPIKSKKDAMNKGIALVpedRRQEGLILQHSIks 352
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE------LEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPV-- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 nFMLPSVRqmrkgFLID---DKKGADIsREYIEKLSIKaDSIKQMAMLL-----------SGGNQQKIVLGKWLARGPRV 418
Cdd:PLN03232 1321 -LFSGTVR-----FNIDpfsEHNDADL-WEALERAHIK-DVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 419 LILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSELSELVaACDRILVLYNRTVNKELSGREIESEE 488
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTII-DCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
266-458 |
4.36e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 266 DFAYGNK--LADVSFDLYPGEILGLAGLMGSGRTEL--VESIFGIRRNWTGDVAMRGEPIKSKKDAmnKGIALVpedRRQ 341
Cdd:PRK11124 9 NCFYGAHqaLFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGTLNIAGNHFDFSKTPSD--KAIREL---RRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 EGLILQH-------SIKSNFMLPSVRQMRkgflIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLAR 414
Cdd:PRK11124 84 VGMVFQQynlwphlTVQQNLIEAPCRVLG----LSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELS 458
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-218 |
4.83e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeadlhsveDAHKKGIAMIYQEFSLLP----- 93
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGC--------DISKFGLMDLRKVLGIIPqapvl 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 94 -AMSVAENIYITREWKKGGLID--DRKNMKKAeellkwleIDN----IDPRV--AVESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:PLN03130 1325 fSGTVRFNLDPFNEHNDADLWEslERAHLKDV--------IRRnslgLDAEVseAGENFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 165 VMDEPTSSLSkTETKALF-KVIRQlKEKGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PLN03130 1397 VLDEATAAVD-VRTDALIqKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAG 1448
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
260-470 |
4.98e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 54.72 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRD--FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdamnkgialV 335
Cdd:COG3842 4 PALELENvsKRYGDVTAldDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEDRRQEGLILQhsiksNFML-P--SVRQ-------MRKgfliddKKGADISR---EYIEKLSIkADSIKQMAMLLSGGN 402
Cdd:COG3842 73 PPEKRNVGMVFQ-----DYALfPhlTVAEnvafglrMRG------VPKAEIRArvaELLELVGL-EGLADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 403 QQKIVLGKWLARGPRVLILDEPTIGVDVAAK----AEILRIIRQLadeGVAVLMISSELSELVAACDRILVL 470
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLReemrEELRRLQREL---GITFIYVTHDQEEALALADRIAVM 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
247-470 |
5.05e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.81 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 247 FERVERNFEQSGDPVlrvrdfaygNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKD 326
Cdd:PRK11153 4 LKNISKVFPQGGRTI---------HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 327 AmnkgiALVpEDRRQEGLILQH----SIKS---NFMLPSvrqmrkgfliddkKGADISREYIEK----------LSIKAD 389
Cdd:PRK11153 75 K-----ELR-KARRQIGMIFQHfnllSSRTvfdNVALPL-------------ELAGTPKAEIKArvtellelvgLSDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 390 SI-KQmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRI 467
Cdd:PRK11153 136 RYpAQ----LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRV 211
|
...
gi 1054755845 468 LVL 470
Cdd:PRK11153 212 AVI 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
273-492 |
5.36e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVPEDRRQ-EGLILQHsi 350
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAaEGMTVRE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 ksnfmLPSV-RQMRKGFLidDKKGADiSREYIEKlSIKADSIKQMAMLL----SGGNQQKIVLGKWLARGPRVLILDEPT 425
Cdd:PRK10575 105 -----LVAIgRYPWHGAL--GRFGAA-DREKVEE-AISLVGLKPLAHRLvdslSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 426 IGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESEEVLHH 492
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
398-470 |
6.42e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.53 E-value: 6.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-218 |
9.21e-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: 52.47 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 12 EKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeadlhsvedahkkGIAMIYQEFSL 91
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 92 LPAmSVAENIYITREWKKgglidDR-KNMKKAEELLKWLEI----DN-------IdprvaveSLDVGYWQMVEIAKALSQ 159
Cdd:cd03250 78 QNG-TIRENILFGKPFDE-----ERyEKVIKACALEPDLEIlpdgDLteigekgI-------NLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 160 DAKILVMDEPTSSL-SKTEtKALF-KVIRQLKEKGISIIYISHRMaEVFEICDRVTILRDG 218
Cdd:cd03250 145 DADIYLLDDPLSAVdAHVG-RHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
269-461 |
9.38e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.16 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 269 YGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKkdAMNKGIALvpedrRQEGLIL 346
Cdd:PRK11248 11 YGGKpaLEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP--GAERGVVF-----QNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 347 QHSIKSN--FMLpsvrQMRKgflIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:PRK11248 84 WRNVQDNvaFGL----QLAG---VEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1054755845 425 TIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELV 461
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAV 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-75 |
9.88e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 9.88e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 4 NVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIdGQEADLHSVE 75
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAYVD 393
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
273-471 |
1.01e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.82 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGE----PIKSKKDAMNKGIALVPED-------RRQ 341
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkADPEAQKLLRQKIQIVFQNpygslnpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 EGLILQHSIKSNFMLPsvRQMRKgfliddkkgaDISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLIL 421
Cdd:PRK11308 111 VGQILEEPLLINTSLS--AAERR----------EKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 422 DEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELS--ELVAacDRILVLY 471
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSvvEHIA--DEVMVMY 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
267-486 |
1.08e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK---LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKS-KKDAMNKGIALVpedrRQE 342
Cdd:PRK13657 342 FSYDNSrqgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVV----FQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 GLILQHSIKSNFML----PSVRQMRKGfliddKKGADISrEYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPR 417
Cdd:PRK13657 418 AGLFNRSIEDNIRVgrpdATDEEMRAA-----AERAQAH-DFIERKPDGYDTvVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSElVAACDRILVLYNrtvnkelsGREIES 486
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLST-VRNADRILVFDN--------GRVVES 550
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-218 |
1.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.55 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 6 LEMHNIEKQFN-GVP----VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQI-----------RIDGQEA 69
Cdd:PRK13651 3 IKVKNIVKIFNkKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 70 DLHSVEDAHKK--------------GIAMIYQEFSLLPAmSVAENIYItrewkkgGLIDDRKNMKKAEEL-LKWLEIDNI 134
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeirrrvGVVFQFAEYQLFEQ-TIEKDIIF-------GPVSMGVSKEEAKKRaAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 135 DPRVAVES---LDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMAEVFEICDR 211
Cdd:PRK13651 155 DESYLQRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
....*..
gi 1054755845 212 VTILRDG 218
Cdd:PRK13651 235 TIFFKDG 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
361-473 |
1.24e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 361 QMRKGF-LIDDKKGADISR-----EYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAK 433
Cdd:PTZ00265 536 EMRKNYqTIKDSEVVDVSKkvlihDFVSALPDKYETlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1054755845 434 AEILRIIRQL-ADEGVAVLMISSELSELVAAcDRILVLYNR 473
Cdd:PTZ00265 616 YLVQKTINNLkGNENRITIIIAHRLSTIRYA-NTIFVLSNR 655
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-430 |
1.38e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 31 GEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEAdlhsvedahkkgIAMIYQEfslLPAMSVAENIYIT---REW 107
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ------------LAWVNQE---TPALPQPALEYVIdgdREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 108 KK---------------------GGL--IDDRKNMKKAEELLKWLEIDNIDPRVAVESLDvGYWQM-VEIAKALSQDAKI 163
Cdd:PRK10636 92 RQleaqlhdanerndghaiatihGKLdaIDAWTIRSRAASLLHGLGFSNEQLERPVSDFS-GGWRMrLNLAQALICRSDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 164 LVMDEPTSSLsktETKALFKVIRQLKEKGISIIYISHRMAEVFEICDRV------TILRDGVNVATVESRDTT------- 230
Cdd:PRK10636 171 LLLDEPTNHL---DLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIihieqqSLFEYTGNYSSFEVQRATrlaqqqa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 231 -----------MEEIIDKMLDAAAKTS--------FERVE---------------RNFEQSGDPVLRVRDFA--YGNK-- 272
Cdd:PRK10636 248 myesqqervahLQSYIDRFRAKATKAKqaqsrikmLERMEliapahvdnpfhfsfRAPESLPNPLLKMEKVSagYGDRii 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMrgepikskkdamNKGIALvpedrrqeGLILQHSIKs 352
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------------AKGIKL--------GYFAQHQLE- 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 353 nFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIKADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDV 430
Cdd:PRK10636 387 -FLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
398-472 |
1.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYN 472
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
266-456 |
1.76e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 266 DFAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVPEDR---- 339
Cdd:PRK13540 8 DFDYHDQplLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSginp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 340 ----RQEGLILQHSIKSNFMLPS-VRQMRKGFLIDDKKGadisreyieklsikadsikqmamLLSGGNQQKIVLGKWLAR 414
Cdd:PRK13540 88 yltlRENCLYDIHFSPGAVGITElCRLFSLEHLIDYPCG-----------------------LLSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSE 456
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-207 |
1.91e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDaGQIRIDGQEADLHSVEdAHKKGIAMIYQEFSLLPAmS 96
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQ-TWRKAFGVIPQKVFIFSG-T 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 97 VAENIYITREWKkgglidDRKNMKKAEEL-LKWLeIDNIDPRVAVESLDVGYW------QMVEIAKALSQDAKILVMDEP 169
Cdd:TIGR01271 1308 FRKNLDPYEQWS------DEEIWKVAEEVgLKSV-IEQFPDKLDFVLVDGGYVlsnghkQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1054755845 170 TSSLSKTEtkalFKVIRQLKEKGIS---IIYISHRMAEVFE 207
Cdd:TIGR01271 1381 SAHLDPVT----LQIIRKTLKQSFSnctVILSEHRVEALLE 1417
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
246-490 |
3.57e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 246 SFERVERNFEQSGDPVLRVRDfaygnkladVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKK 325
Cdd:COG1135 3 ELENLSKTFPTKGGPVTALDD---------VSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 326 DAmnkgiALVPEdRRQEGLILQH-------SIKSNFMLPsvrqmrkgfLiddkKGADISREYIEK----------LSIKA 388
Cdd:COG1135 74 ER-----ELRAA-RRKIGMIFQHfnllssrTVAENVALP---------L----EIAGVPKAEIRKrvaellelvgLSDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 389 DS-IKQmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDR 466
Cdd:COG1135 135 DAyPSQ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDR 210
|
250 260
....*....|....*....|....
gi 1054755845 467 ILVLYNrtvnkelsGREIESEEVL 490
Cdd:COG1135 211 VAVLEN--------GRIVEQGPVL 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
255-470 |
3.69e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 255 EQSGDPVLRVRDFAY----GNKLADVSFDLYPGEILGLAGLMGSGRTELVESI---FGIRRnwtGDVAMRGEPI-KSKKD 326
Cdd:PRK10789 309 EGRGELDVNIRQFTYpqtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIqrhFDVSE---GDIRFHDIPLtKLQLD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 327 AMNKGIALVpedrRQEGLILQHSIKSNFML--PSVRQmrkgfliddkkgADIsrEYIEKLSIKADSIKQM---------- 394
Cdd:PRK10789 386 SWRSRLAVV----SQTPFLFSDTVANNIALgrPDATQ------------QEI--EHVARLASVHDDILRLpqgydtevge 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 395 -AMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELVAAcDRILVL 470
Cdd:PRK10789 448 rGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTEA-SEILVM 522
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
398-484 |
5.39e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVN 476
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
....*...
gi 1054755845 477 KELSGREI 484
Cdd:PRK13634 226 LQGTPREI 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
403-470 |
5.90e-07 |
|
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: 49.93 E-value: 5.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 403 QQKIV-LGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVL-MISSELSELVAACDRILVL 470
Cdd:cd03232 113 QRKRLtIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLL 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
267-475 |
6.51e-07 |
|
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: 50.18 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKskkdamnkgiALVPEDRR-----Q 341
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT----------AAPPADRPvsmlfQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 342 EGLILQH-SIKSNFMLPSVRQMRKgfliddkkgADISREYIEKLSIK---ADSIKQMAMLLSGGNQQKIVLGKWLARGPR 417
Cdd:cd03298 78 ENNLFAHlTVEQNVGLGLSPGLKL---------TAEDRQAIEVALARvglAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
273-478 |
6.98e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.83 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIR--RNWTGDVAMRGEPIKskkdamnkgiALVPEDRRQEGLIL--QH 348
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT----------DLPPEERARLGIFLafQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 349 SIKsnfmLPSVrqmrkgfliddkKGADISREYIEKLS---IKADSIKQMAMLlsggnqqkivlgkwlarGPRVLILDEPT 425
Cdd:cd03217 86 PPE----IPGV------------KNADFLRYVNEGFSggeKKRNEILQLLLL-----------------EPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 426 IGVDVAAKAEILRIIRQLADEGVAVLMIS--SELSELVAAcDRILVLYNRTVNKE 478
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYIKP-DRVHVLYDGRIVKS 186
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
250-468 |
7.53e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 250 VERNFeQSGDPVLRVrdfaygnkLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkdAMN 329
Cdd:PRK10535 10 IRRSY-PSGEEQVEV--------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-----ATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 330 KGIALVPEDRRQEGLILQH-------SIKSNFMLPSVRQMrkgflIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGN 402
Cdd:PRK10535 76 DADALAQLRREHFGFIFQRyhllshlTAAQNVEVPAVYAG-----LERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 403 QQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSElSELVAACDRIL 468
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVI 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
268-468 |
1.01e-06 |
|
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: 48.86 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 268 AYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGirrnwtgdvamrgepiKSKKDAMNKGIALVPEDRrqeglilq 347
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------------ASGKARLISFLPKFSRNK-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 348 hsiksnfmLPSVRQMRkgFLIDdkkgadISREYIeklsikadSIKQMAMLLSGGNQQKIVLGKWLARGPR--VLILDEPT 425
Cdd:cd03238 62 --------LIFIDQLQ--FLID------VGLGYL--------TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 426 IGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAAcDRIL 468
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSA-DWII 159
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
273-475 |
1.29e-06 |
|
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: 49.61 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKdamnkGIALvpedRRQEGLILQ----- 347
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD-----PVEL----RRKIGYVIQqiglf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 348 -H-SIKSNFMLpsVRQMRKgfliddkkgadISREYIEKlsiKADSIKQMAML------------LSGGNQQKIVLGKWLA 413
Cdd:cd03295 88 pHmTVEENIAL--VPKLLK-----------WPKEKIRE---RADELLALVGLdpaefadrypheLSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 414 RGPRVLILDEPTIGVDVAAKA----EILRIIRQLadeGVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDqlqeEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
260-451 |
1.34e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.10 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 260 PVLRVRDFA--YGNKL--ADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkskkdamnkgialv 335
Cdd:PRK13539 1 MMLEGEDLAcvRGGRVlfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 pEDRRQEGLI--LQHSiksNFMLP--SVR---QMRKGFLIDDKKGADISREYIEkLSIKADsIKqmAMLLSGGNQQKIVL 408
Cdd:PRK13539 67 -DDPDVAEAChyLGHR---NAMKPalTVAenlEFWAAFLGGEELDIAAALEAVG-LAPLAH-LP--FGYLSAGQKRRVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1054755845 409 GKWLARGPRVLILDEPTIGVDVAAKAEILRIIR-QLADEGVAVL 451
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIA 182
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-212 |
1.45e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 25 NFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHSVEDAHKKGiamiY--QEFSLLPAMSVAENIy 102
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVG----YmsQAFSLYGELTVRQNL- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 103 itrewkkggliddrknmkkaeEL---LKWLEIDNIDPRVAV---------------ESLDVGYWQMVEIAKALSQDAKIL 164
Cdd:NF033858 361 ---------------------ELharLFHLPAAEIAARVAEmlerfdladvadalpDSLPLGIRQRLSLAVAVIHKPELL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 165 VMDEPTS---------------SLSktetkalfkvirqlKEKGISiIYIS-HRMAEVfEICDRV 212
Cdd:NF033858 420 ILDEPTSgvdpvardmfwrlliELS--------------REDGVT-IFIStHFMNEA-ERCDRI 467
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-200 |
1.81e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 2 NENVLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNG----VYTKDA---GQIRIDGQeadlhSV 74
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqGYSNDLtlfGRRRGSGE-----TI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 75 EDAhKKGIAMIYQEFSLLPAMSV-AENIYITREWKKGGL---IDDRKNMKKAEellkWLEIDNIDPRVA---VESLDVGY 147
Cdd:PRK10938 332 WDI-KKHIGYVSSSLHLDYRVSTsVRNVILSGFFDSIGIyqaVSDRQQKLAQQ----WLDILGIDKRTAdapFHSLSWGQ 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 148 WQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQLKEKG-ISIIYISH 200
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGeTQLLFVSH 460
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-218 |
1.92e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 31 GEVHALLGGNGAGKSTLMKILNGVYTKD--AGQIRIDGQEADLHSVedahkKGIAMIYQEFSLLPAMSVAENIYITREWK 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL-----KRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 109 KGGLIDDRKNMKKAEELLKWLEIDNIDPRVA----VESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKV 184
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*
gi 1054755845 185 IRQLKEKGISIIYISHR-MAEVFEICDRVTILRDG 218
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
273-471 |
1.97e-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: 48.41 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNW---TGDVAMRGEPIKSKKDAMNKGIALVPEDrrqeglilqhs 349
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEE----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 350 iKSNFMLPSVRQmrkgfLID---DKKGADISREyieklsikadsikqmamlLSGGNQQKIVLGKWLARGPRVLILDEPTI 426
Cdd:cd03233 92 -DVHFPTLTVRE-----TLDfalRCKGNEFVRG------------------ISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1054755845 427 GVDVAAKAEILRIIRQLADEGVAVLMIS-SELS-ELVAACDRILVLY 471
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSlYQASdEIYDLFDKVLVLY 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
254-470 |
1.98e-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: 50.78 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 254 FEQSGDPVLrvrdfaygNKLaDVSFdlYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIA 333
Cdd:TIGR01257 938 FEPSGRPAV--------DRL-NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 LVPedrrQEGLILQHSIKSNFMLpsvrqmrkgfLIDDKKGADISREYIEKLSIKADS-----IKQMAMLLSGGNQQKIVL 408
Cdd:TIGR01257 1007 MCP----QHNILFHHLTVAEHIL----------FYAQLKGRSWEEAQLEMEAMLEDTglhhkRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054755845 409 GKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELVAACDRILVL 470
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAII 1133
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
273-475 |
2.17e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFG-----IRRNW---TGDVAMRGEPIkSKKDA--MNKGIALVPEDRRQE 342
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltggGAPRGarvTGDVTLNGEPL-AAIDAprLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 343 GLILQHSIKSNFMLPSVRqmRKGFL-IDDKKGADISREYIEKLSIKADSIKQmamlLSGGNQQKIVLGKWLA-------- 413
Cdd:PRK13547 96 FAFSAREIVLLGRYPHAR--RAGALtHRDGEIAWQALALAGATALVGRDVTT----LSGGELARVQFARVLAqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 414 -RGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-218 |
2.62e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 21 LKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQeadlhsvedahkkgIAMIYQEFSLLPAMSVAEN 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 101 IyitrEWKKGGLIDDRKNMKK-AEELLKWLEIDNIDPRvAVESLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETK 179
Cdd:PRK13546 106 I----EFKMLCMGFKRKEIKAmTPKIIEFSELGEFIYQ-PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1054755845 180 ALFKVIRQLKEKGISIIYISHRMAEVFEICDRVTILRDG 218
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
275-452 |
2.99e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 275 DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdamnkgialVPEDRRQEGLILQH--SIKS 352
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----------QRDEYHQDLLYLGHqpGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 --------NFMLPsvrqmrkgflIDDKKGADISREYIEKLSIK--AD-SIKQmamlLSGGNQQKIVLGK-WLARgPRVLI 420
Cdd:PRK13538 88 eltalenlRFYQR----------LHGPGDDEALWEALAQVGLAgfEDvPVRQ----LSAGQQRRVALARlWLTR-APLWI 152
|
170 180 190
....*....|....*....|....*....|..
gi 1054755845 421 LDEPTIGVDVAAKAEILRIIRQLADEGVAVLM 452
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-218 |
3.62e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadLHSVE-DAHKKGIAMIYQEfSLLPAMSV 97
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP--LTKLQlDSWRSRLAVVSQT-PFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 98 AENIYITREWKKGGLIDDRKNMKKA-EELLKWLEidNIDPRVAVES--LDVGYWQMVEIAKALSQDAKILVMDEPTSSLS 174
Cdd:PRK10789 406 ANNIALGRPDATQQEIEHVARLASVhDDILRLPQ--GYDTEVGERGvmLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1054755845 175 -KTETKALfKVIRQLKEkGISIIYISHRMAEVFEiCDRVTILRDG 218
Cdd:PRK10789 484 gRTEHQIL-HNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHG 525
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
393-470 |
4.57e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 393 QMAMLLSGGNQQKIVLGKWLAR---GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELsELVAACDRILV 469
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWIID 243
|
.
gi 1054755845 470 L 470
Cdd:cd03271 244 L 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
395-470 |
5.32e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.04 E-value: 5.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 395 AMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSElSELVAACDRILVL 470
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDRVLEL 556
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
268-470 |
5.95e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.49 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 268 AYGNKL--ADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEpikskkdAMNKgialVPEDRRQEGLI 345
Cdd:PRK11000 12 AYGDVVisKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-------RMND----VPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LQhsikSNFMLP--SVRQ-MRKGFliddkKGADISREYIEKLSIKADSIKQMAMLL-------SGGNQQKIVLGKWLARG 415
Cdd:PRK11000 81 FQ----SYALYPhlSVAEnMSFGL-----KLAGAKKEEINQRVNQVAEVLQLAHLLdrkpkalSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 416 PRVLILDEPTIGVD----VAAKAEILRIIRQLadeGVAVLMISSELSELVAACDRILVL 470
Cdd:PRK11000 152 PSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
370-471 |
6.71e-06 |
|
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: 48.63 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 370 DKKGAdiSREYIEKLSIKAdSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVA 449
Cdd:COG1245 188 DERGK--LDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKY 264
|
90 100
....*....|....*....|..
gi 1054755845 450 VLMISSELSELVAACDRILVLY 471
Cdd:COG1245 265 VLVVEHDLAILDYLADYVHILY 286
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
341-490 |
7.03e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 341 QEGLILQHSI-------KSNFMLPSVRQMRKGFLIDdkkgadisrEYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWL 412
Cdd:PTZ00265 1303 QEPMLFNMSIyenikfgKEDATREDVKRACKFAAID---------EFIESLPNKYDTnVGPYGKSLSGGQKQRIAIARAL 1373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 413 ARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESEEVL 490
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSFVQAHGTHEELL 1451
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
259-446 |
7.42e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 259 DPVLRVRDFA--YGNKLA--DVSFDLYPGEILGLAGLMGSGRTELV-------ESIFGIRRNwtGDVAMRGepikskKDA 327
Cdd:PRK14243 8 ETVLRTENLNvyYGSFLAvkNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVE--GKVTFHG------KNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 328 MNKGIALVpEDRRQEGLILQH------SIKSNFML-PSV------------RQMRKGFLIDDKKgadisreyieklsika 388
Cdd:PRK14243 80 YAPDVDPV-EVRRRIGMVFQKpnpfpkSIYDNIAYgARIngykgdmdelveRSLRQAALWDEVK---------------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 389 DSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE 446
Cdd:PRK14243 143 DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
389-455 |
7.85e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 7.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 389 DSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISS 455
Cdd:PRK14267 141 DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHS 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-65 |
9.53e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 9.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054755845 10 NIEKQFNGVPVLKkmNFSLKKGE--VHALLGGNGAGKSTLMKILNGVYTKDAGQIRID 65
Cdd:PRK15064 6 NITMQFGAKPLFE--NISVKFGGgnRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
267-472 |
9.62e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 46.76 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK-----LADVSFDLYPGEILGLAGLMGSGRT---ELVESIFGIRrnwTGDVAMRGEPIKSKK-DAMNKGIALVPe 337
Cdd:cd03249 8 FRYPSRpdvpiLKGLSLTIPPGKTVALVGSSGCGKStvvSLLERFYDPT---SGEILLDGVDIRDLNlRWLRSQIGLVS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 drrQEGLILQHSIKSNFML----PSVRQMrkgflIDDKKGADISrEYIEKLSIKADS-IKQMAMLLSGGNQQKIVLGKWL 412
Cdd:cd03249 84 ---QEPVLFDGTIAENIRYgkpdATDEEV-----EEAAKKANIH-DFIMSLPDGYDTlVGERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 413 ARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSElVAACDRILVLYN 472
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLST-IRNADLIAVLQN 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
398-454 |
1.01e-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: 45.61 E-value: 1.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRqlaDEGVAVLMIS 454
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVG 145
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
270-475 |
1.18e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 270 GNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdaMNKGIALVPEDRR-----QEGL 344
Cdd:PRK11144 11 GDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD----AEKGICLPPEKRRigyvfQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQH-SIKSNFMLPSVRQMRKGFliddkkgADIsreyIEKLSIKAdSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:PRK11144 87 LFPHyKVRGNLRYGMAKSMVAQF-------DKI----VALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 424 PTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
398-471 |
1.24e-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: 46.59 E-value: 1.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLY 471
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
261-491 |
1.53e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.54 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRV----RDFAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIrrnWTGD------VAMRGEPIKsKKDAMNK 330
Cdd:PRK09984 4 IIRVeklaKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDksagshIELLGRTVQ-REGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 331 GIAlvpEDRRQEGLILQH-------SIKSNFML------PSVRQMRKGFLIDDKKGAdisREYIEKLSIkADSIKQMAML 397
Cdd:PRK09984 80 DIR---KSRANTGYIFQQfnlvnrlSVLENVLIgalgstPFWRTCFSWFTREQKQRA---LQALTRVGM-VHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAK---AEILRIIRQlaDEGVAVLMISSELSELVAACDRILVLYNRT 474
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESArivMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
250
....*....|....*..
gi 1054755845 475 VNKELSGREIESEEVLH 491
Cdd:PRK09984 231 VFYDGSSQQFDNERFDH 247
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
273-470 |
1.59e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIkSKKDAMN--KGIALVPedrrQEGLILQHSI 350
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-SKFGLMDlrKVLGIIP----QAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 351 KSNfMLPsvrqmrkgflIDDKKGADIsREYIEKLSIKaDSIKQMAMLL-----------SGGNQQKIVLGKWLARGPRVL 419
Cdd:PLN03130 1330 RFN-LDP----------FNEHNDADL-WESLERAHLK-DVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 420 ILDEPTIGVDVAAKAEILRIIRQlADEGVAVLMISSELSELVaACDRILVL 470
Cdd:PLN03130 1397 VLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTII-DCDRILVL 1445
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
241-469 |
1.81e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.32 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 241 AAAKTSFERVERNFEQ----------SGDPVLRVRDFAYGNK----LADVSFDLYPGEILGLAGLMGSGRT---ELVESI 303
Cdd:PRK11176 313 AACQTLFAILDLEQEKdegkrvieraKGDIEFRNVTFTYPGKevpaLRNINFKIPAGKTVALVGRSGSGKStiaNLLTRF 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 304 FGIRRnwtGDVAMRGEPIKSKK-DAMNKGIALVpedrRQEGLILQHSIKSNFMLPSVRQMRKGFLIDDKKGAdISREYIE 382
Cdd:PRK11176 393 YDIDE---GEILLDGHDLRDYTlASLRNQVALV----SQNVHLFNDTIANNIAYARTEQYSREQIEEAARMA-YAMDFIN 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 383 KLSIKADS-IKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKaeilRIIRQLADE---GVAVLMISSELS 458
Cdd:PRK11176 465 KMDNGLDTvIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDElqkNRTSLVIAHRLS 540
|
250
....*....|.
gi 1054755845 459 ELVAAcDRILV 469
Cdd:PRK11176 541 TIEKA-DEILV 550
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-256 |
1.92e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 17 GVP-VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEADLHsvedahkkGIAMIYQEFSLLPAM 95
Cdd:PTZ00243 1321 GLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY--------GLRELRRQFSMIPQD 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 96 SVaeniyitrewkkggLIDD--RKNMK-----KAEELLKWLEIDNIDPRVAVES-------------LDVGYWQMVEIAK 155
Cdd:PTZ00243 1393 PV--------------LFDGtvRQNVDpfleaSSAEVWAALELVGLRERVASESegidsrvleggsnYSVGQRQLMCMAR 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 156 A-LSQDAKILVMDEPTSSLSktetKALFKVIRQLKEKGIS---IIYISHRMAEVFEiCDRVTILRDGVnVATVES-RDTT 230
Cdd:PTZ00243 1459 AlLKKGSGFILMDEATANID----PALDRQIQATVMSAFSaytVITIAHRLHTVAQ-YDKIIVMDHGA-VAEMGSpRELV 1532
|
250 260
....*....|....*....|....*...
gi 1054755845 231 M--EEIIDKMLDAAAKtsfeRVERNFEQ 256
Cdd:PTZ00243 1533 MnrQSIFHSMVEALGR----SEAKRFLQ 1556
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-68 |
2.03e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 2.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1054755845 25 NFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQE 68
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP 64
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
398-469 |
2.12e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 2.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILV 469
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
398-470 |
2.32e-05 |
|
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: 47.12 E-value: 2.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdEGVAVLMISSELSELVAAcDRILVL 470
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVDA-DEILVL 565
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
393-453 |
2.57e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 2.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 393 QMAMLLSGGNQQKIVLGKWLAR---GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMI 453
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVI 888
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
258-438 |
3.19e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 258 GDPVLRVRDF--AYGNKL--ADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMrGEPIKskkdamnkgia 333
Cdd:PRK11819 321 GDKVIEAENLskSFGDRLliDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 334 lvpedrrqeglilqhsiksnfmLPSVRQMRKGflIDDKK--------GADI---------SREYIEKLSIK-ADSIKQMA 395
Cdd:PRK11819 389 ----------------------LAYVDQSRDA--LDPNKtvweeisgGLDIikvgnreipSRAYVGRFNFKgGDQQKKVG 444
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1054755845 396 MLlSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVaakaEILR 438
Cdd:PRK11819 445 VL-SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLR 482
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
273-470 |
5.33e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 44.85 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdamnkgialvPEDRRqeGLILQHsiks 352
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------------PGADR--GVVFQK---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 353 NFMLP--SVR-------QMRKgflIDDKKGADISREYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDE 423
Cdd:COG4525 85 DALLPwlNVLdnvafglRLRG---VPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1054755845 424 PTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSELVAACDRILVL 470
Cdd:COG4525 161 PFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
267-474 |
5.83e-05 |
|
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: 43.21 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGirrnwtgdvamrgepikskkdamnkgialvpEDRRQEGL 344
Cdd:cd03221 8 KTYGGKllLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-------------------------------ELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 345 ILQHSiksnfmlpsvrqmrkgfliddkkGADISreYIEKLSikadsikqmamllsGGNQQKIVLGKWLARGPRVLILDEP 424
Cdd:cd03221 57 VTWGS-----------------------TVKIG--YFEQLS--------------GGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1054755845 425 TIGVDVAAkaeILRIIRQLADEGVAVLMISSELSELVAACDRILVLYNRT 474
Cdd:cd03221 98 TNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
261-484 |
6.19e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.52 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 261 VLRVRDF--AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVEsIFGIRRNWTGDVAMRGEPIKSKKDAMNKGIALVp 336
Cdd:PRK14247 3 KIEIRDLkvSFGQVevLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFKMDVIEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 337 edRRQEGLILQ-------HSIKSNFML-PSVRQMRKgfliDDKKGADISREYIEKLSI---KADSIKQMAMLLSGGNQQK 405
Cdd:PRK14247 81 --RRRVQMVFQipnpipnLSIFENVALgLKLNRLVK----SKKELQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 406 IVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEgVAVLMISSELSELVAACDRILVLYNRTVNKELSGREI 484
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-219 |
6.36e-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: 44.51 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 19 PVLKKMNFSLKKGEVHALLGGNGAGKSTL-MKILNGVYTKDaGQIRIDG---QEADLHSVedahKKGIAMIYQE------ 88
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGidiSKLPLHTL----RSRLSIILQDpilfsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 89 ---FSLLPAMSVAENiyitREWKkGGLIDDRKNMKKAEEllkwleiDNIDPRVAV--ESLDVGYWQMVEIAKALSQDAKI 163
Cdd:cd03288 110 sirFNLDPECKCTDD----RLWE-ALEIAQLKNMVKSLP-------GGLDAVVTEggENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 164 LVMDEPTSSLSKTETKALFKVIRQLKEKGiSIIYISHRMAEVFEiCDRVTILRDGV 219
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRGI 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
282-470 |
6.44e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 282 PGEILGLAGLMGSGRTELVESIFGIRR--NWTGDVAMRGEpiKSKKDAMnKGIALVPEDrrqeGLILQH-SIKSNFMLPS 358
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNR--KPTKQIL-KRTGFVTQD----DILYPHlTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 359 VRQMRKGFLIDDKkgADISREYIEKLSIK--ADSIKQMAML--LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKA 434
Cdd:PLN03211 166 LLRLPKSLTKQEK--ILVAESVISELGLTkcENTIIGNSFIrgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190
....*....|....*....|....*....|....*..
gi 1054755845 435 EILRIIRQLADEG-VAVLMISSELSELVAACDRILVL 470
Cdd:PLN03211 244 RLVLTLGSLAQKGkTIVTSMHQPSSRVYQMFDSVLVL 280
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
398-468 |
6.49e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 6.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 398 LSGGNQQKIVLGKWLarGPRVL----ILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSElSELVAACDRIL 468
Cdd:PRK00635 477 LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRII 548
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
253-472 |
6.81e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.85 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 253 NFEQSGDPVLRvrdfaygnklaDVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEpikskkdamnkgI 332
Cdd:cd03291 44 NLCLVGAPVLK-----------NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------I 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 333 ALVPedrrQEGLILQHSIKSNFMLP-SVRQMRKGFLIddkKGADIsREYIEKLSIKADSI-KQMAMLLSGGNQQKIVLGK 410
Cdd:cd03291 101 SFSS----QFSWIMPGTIKENIIFGvSYDEYRYKSVV---KACQL-EEDITKFPEKDNTVlGEGGITLSGGQRARISLAR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 411 WLARGPRVLILDEPTIGVDVAAKAEILR--IIRQLADEgvAVLMISSELSELVAAcDRILVLYN 472
Cdd:cd03291 173 AVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKKA-DKILILHE 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
237-475 |
7.71e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 237 KMLDAAAKTSFERVERNFeqSGDPVLRVRDFAYGNKlaDVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAM 316
Cdd:PRK10070 12 KIFGEHPQRAFKYIEQGL--SKEQILEKTGLSLGVK--DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 317 RGEPIKSKKDAMNKGIAlvpedRRQEGLILQhsikSNFMLPSVRqmrkgFLIDDKKGADISREYIEKLSIKA-DSIKQMA 395
Cdd:PRK10070 88 DGVDIAKISDAELREVR-----RKKIAMVFQ----SFALMPHMT-----VLDNTAFGMELAGINAEERREKAlDALRQVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 396 ML---------LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEIL-RIIRQLADEGVAVLMISSELSELVAACD 465
Cdd:PRK10070 154 LEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGD 233
|
250
....*....|
gi 1054755845 466 RILVLYNRTV 475
Cdd:PRK10070 234 RIAIMQNGEV 243
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
370-471 |
8.41e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 370 DKKGadISREYIEKLSIKA---DSIKQmamlLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLAdE 446
Cdd:PRK13409 188 DERG--KLDEVVERLGLENildRDISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-E 260
|
90 100
....*....|....*....|....*
gi 1054755845 447 GVAVLMISSELSELVAACDRILVLY 471
Cdd:PRK13409 261 GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
264-459 |
8.48e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 264 VRDFAYGNKLADVSFDLYPGEILGLAGLMGSG--RTELVESIFGI---RRNWtgdvamRGEPIKSKKDAMNKGIAL---V 335
Cdd:NF000106 20 VKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPdagRRPW------RF*TWCANRRALRRTIG*hrpV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 336 PEDRRQeglilQHSIKSN-FMLPSVRQMRKGfliDDKKGADisrEYIEKLSIkADSIKQMAMLLSGGNQQKIVLGKWLAR 414
Cdd:NF000106 94 R*GRRE-----SFSGRENlYMIGR*LDLSRK---DARARAD---ELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSE 459
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEE 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
262-470 |
9.44e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 43.62 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 262 LRVRDF--AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRR---NWTGDVAMRGEPIkskkdamnkgiAL 334
Cdd:COG4136 2 LSLENLtiTLGGRplLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRL-----------TA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 335 VPEDRRQEGLILQ------H-SIKSN--FMLPsvrqmrkgfliddkkgADISREyiEKLSIKADSIKQMAML-------- 397
Cdd:COG4136 71 LPAEQRRIGILFQddllfpHlSVGENlaFALP----------------PTIGRA--QRRARVEQALEEAGLAgfadrdpa 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 398 -LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIR-QLADEGVAVLMISSELSELVAAcDRILVL 470
Cdd:COG4136 133 tLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFeQIRQRGIPALLVTHDEEDAPAA-GRVLDL 206
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
404-470 |
9.86e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 9.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 404 QKIVLGKWLARGPRVLI-LDEPTIGVDVAAKAEILRIIRQLADEGVAVL-MISSELSELVAACDRILVL 470
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLL 976
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-63 |
1.04e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 1.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 5 VLEMHNIEKQFNGVPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIR 63
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
379-432 |
2.01e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 2.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 379 EYIEKLSIKADsikqmAML--LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAA 432
Cdd:PRK11147 141 EVLAQLGLDPD-----AALssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
257-484 |
2.33e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.40 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 257 SGDPVLRVRDF--AYGNK--LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIKSkkdamnkgi 332
Cdd:PRK09452 10 SLSPLVELRGIskSFDGKevISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 333 alVPEDRRQEGLILQH-------SIKSN--FMLpsvrQMRKgfliddKKGADISREYIEKLsiKADSIKQMA----MLLS 399
Cdd:PRK09452 81 --VPAENRHVNTVFQSyalfphmTVFENvaFGL----RMQK------TPAAEITPRVMEAL--RMVQLEEFAqrkpHQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 400 GGNQQKIVLGKWLARGPRVLILDEPTIGVD----VAAKAEILRIIRQLadeGVAVLMISSELSELVAACDRILVLYNRTV 475
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
....*....
gi 1054755845 476 NKELSGREI 484
Cdd:PRK09452 224 EQDGTPREI 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
264-478 |
2.39e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 43.64 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 264 VRDFAYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIR--RNWTGDVAMR----------------GEPIKS-- 323
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpskvGEPCPVcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 324 ------KKDAMNKGIALVPEDRRQEGLILQHSI---KSNFMLPSVRQMRKGFLIDDKKGADISREYIEKLSIkADSIKQM 394
Cdd:TIGR03269 87 gtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFalyGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL-SHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 395 AMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVA-ACDRILVLYNR 473
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENG 245
|
....*
gi 1054755845 474 TVNKE 478
Cdd:TIGR03269 246 EIKEE 250
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-245 |
3.04e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 28 LKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGqeadlhsvedahkkgIAMIYQefsllPAmsvaeniYItrew 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG---------------ITPVYK-----PQ-------YI---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 108 kkggliddrknmkkaeellkwleidnidprvaveSLDVGYWQMVEIAKALSQDAKILVMDEPTSSLSKTETKALFKVIRQ 187
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 188 LKEKGI-SIIYISHRMAEVFEICDRVTILRDGVNVATVESRDTTMEEIIDKMLDAAAKT 245
Cdd:cd03222 117 LSEEGKkTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLIT 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
398-470 |
3.19e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 42.78 E-value: 3.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVL 470
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
398-472 |
3.52e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 42.75 E-value: 3.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVD----VAAKAEILRIIRQLadeGVAVLMISSELSELVAACDRILVLYN 472
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
398-475 |
3.52e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.42 E-value: 3.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLYN-RTV 475
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEgRVL 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
273-451 |
3.62e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNW--TGDVAMRGEPIKSKKDAMNKGIA-----LVPEDRRQEGLI 345
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARISGYCeqndiHSPQVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 346 LqhsikSNFM-LP-SVRQMRKGFLIDDkkgadiSREYIEKLSIKaDSIKQMAML--LSGGNQQKIVLGKWLARGPRVLIL 421
Cdd:PLN03140 976 Y-----SAFLrLPkEVSKEEKMMFVDE------VMELVELDNLK-DAIVGLPGVtgLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190
....*....|....*....|....*....|
gi 1054755845 422 DEPTIGVDVAAKAEILRIIRQLADEGVAVL 451
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1073
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
142-200 |
5.19e-04 |
|
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: 40.77 E-value: 5.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054755845 142 SLDVGYWQMVEIAKALSQDAK--ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH 200
Cdd:cd03238 87 TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
267-463 |
5.55e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 41.55 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNKLA---DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDV----AMRGEPIKSKKDAMNKG-IALVPed 338
Cdd:cd03290 8 FSWGSGLAtlsNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYsVAYAA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 339 rrQEGLILQHSIKSN--FMLPSVRQMRKGFliddkkgadisreyIEKLSIKAD----------SIKQMAMLLSGGNQQKI 406
Cdd:cd03290 86 --QKPWLLNATVEENitFGSPFNKQRYKAV--------------TDACSLQPDidllpfgdqtEIGERGINLSGGQRQRI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 407 VLGKWLARGPRVLILDEPTIGVDVAAKAEILR--IIRQLADEGVAVLMISSELSELVAA 463
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHA 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-212 |
5.70e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 142 SLDVGYWQMVEIAKALSQDAK---ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMaEVFEICDRV 212
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYV 881
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
274-489 |
7.68e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 274 ADVSFDLYPGEILGLAGLMGSGRTELVESIFGIR----RNWTGDVAMRGEPIkskkdamnkgialVPEDRRQE--GLILQ 347
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPV-------------APCALRGRkiATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 348 HSiKSNFmlPSVRQMRkgfliddkkgaDISREYIEKLSIKADSIKQMAML------------------LSGGNQQKIVLG 409
Cdd:PRK10418 87 NP-RSAF--NPLHTMH-----------THARETCLALGKPADDATLTAALeavglenaarvlklypfeMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 410 -KWLARGPrVLILDEPTIGVDVAAKAEILRIIRQL-ADEGVAVLMISSELSeLVAAC-DRILVLYNrtvnkelsGREIES 486
Cdd:PRK10418 153 lALLCEAP-FIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMG-VVARLaDDVAVMSH--------GRIVEQ 222
|
...
gi 1054755845 487 EEV 489
Cdd:PRK10418 223 GDV 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
390-471 |
1.03e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.25 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 390 SIKQMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGV-AVLMISSELSELVAACDRIL 468
Cdd:cd03222 64 VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
...
gi 1054755845 469 VLY 471
Cdd:cd03222 144 VFE 146
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
267-497 |
1.29e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 40.74 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 267 FAYGNKLA--DVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAMRGEPIK---SKKDAMNKGI----ALVPE 337
Cdd:PRK10253 15 LGYGKYTVaeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaSKEVARRIGLlaqnATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 338 DRRQEGLILQHSIKSNfmlPSVRQMRKgfliDDKKGADisreyiekLSIKADSIKQMAM----LLSGGNQQKIVLGKWLA 413
Cdd:PRK10253 95 DITVQELVARGRYPHQ---PLFTRWRK----EDEEAVT--------KAMQATGITHLADqsvdTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 414 RGPRVLILDEPTIGVDVAAKAEILRIIRQLADE-GVAVLMISSELSELVAACDRILVLYNRTVNKELSGREIESEEVLHH 492
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
....*
gi 1054755845 493 aIQGL 497
Cdd:PRK10253 240 -IYGL 243
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
273-454 |
1.34e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 273 LADVSFDLYPGEILGLAGLMGSGRTELVESIFGiRRNWT---GDVAMRGEPIkskkdamnkgIALVPEDRRQEGLIL--Q 347
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEvtgGTVEFKGKDL----------LELSPEDRAGEGIFMafQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 348 HSIK----SN-FMLPS----VRQMRKGFLIDDKKGADISREYIEKLSIKADSI-KQMAMLLSGGNQQKIVLGKWLARGPR 417
Cdd:PRK09580 86 YPVEipgvSNqFFLQTalnaVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLtRSVNVGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1054755845 418 VLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMIS 454
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVT 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
415-467 |
1.64e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1054755845 415 GPRVLILDEPTIGVDVAAKAEILRIIRQLA-DEGVAVLmISSE-LSElvAA-CDRI 467
Cdd:NF033858 415 KPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIF-ISTHfMNE--AErCDRI 467
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-202 |
2.36e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054755845 142 SLDVGYWQMVEIAKALSQDAK---ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRM 202
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-54 |
3.22e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 3.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 1 MNENVLEMHNIEKQFNG-VPVLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGV 54
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 56
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
149-210 |
3.67e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 3.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 149 QMVEIAKALSQDAK---ILVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISHRMaEVFEICD 210
Cdd:cd03271 176 QRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCAD 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
398-429 |
4.60e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 4.60e-03
10 20 30
....*....|....*....|....*....|..
gi 1054755845 398 LSGGNQQKIVLGKWLARGPRVLILDEPTIGVD 429
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
5-200 |
4.64e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 5 VLEMHNIekQFNGVP-VLKKMNFSLKKGEVHALLGGNGAGKSTLMKILNGVYTKDAGQIRIDGQEadlhsVEDAHKKGIA 83
Cdd:PRK13541 1 MLSLHQL--QFNIEQkNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN-----INNIAKPYCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 84 MIYQEFSLLPAMSVAENIYItreWKKggLIDDRKNMKKAEELLKWLeiDNIDPRVAveSLDVGYWQMVEIAKALSQDAKI 163
Cdd:PRK13541 74 YIGHNLGLKLEMTVFENLKF---WSE--IYNSAETLYAAIHYFKLH--DLLDEKCY--SLSSGMQKIVAIARLIACQSDL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1054755845 164 LVMDEPTSSLSKTETKALFKVIRQLKEKGISIIYISH 200
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
244-471 |
4.72e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 244 KTSFERVERNFEQSGDPVLRVRDF-------AYGNKLADVSFDLYPGEILGLAGLMGSGRTELVESIFGIRRNWTGDVAM 316
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPFDKLKDLffrskdgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054755845 317 RGE----PIKSKKDAMNKGIalvpEDRRQEGLILQhsiksnfmlpsvrqmrkgflIDDKKGADISREYIEKLSIkADSIK 392
Cdd:PRK13545 84 KGSaaliAISSGLNGQLTGI----ENIELKGLMMG--------------------LTKEKIKEIIPEIIEFADI-GKFIY 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054755845 393 QMAMLLSGGNQQKIVLGKWLARGPRVLILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSELSELVAACDRILVLY 471
Cdd:PRK13545 139 QPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLH 217
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
395-467 |
6.97e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.01 E-value: 6.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054755845 395 AMLLSGGNQQKIVLGKWLARG-PRVL-ILDEPTIGVDVAAKAEILRIIRQLADEGVAVLMISSElSELVAACDRI 467
Cdd:cd03270 135 APTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| |
