|
Name |
Accession |
Description |
Interval |
E-value |
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-503 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 716.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDP----KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRL 156
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPtkggRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVGSDV 236
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 237 ASVSRATGEALGAPQIEVMGLSVAPRTPfAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVyNNDAIHLRGK 316
Cdd:COG3845 243 LLRVEKAPAEPGEVVLEVENLSVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP-ASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 317 PVGRIGINGRRLMGAGFVPEERHGHAAVPGMSLSDNLLLARARsdRKAFLTGGFLrivRGSVIKAAARRISETMDVRKSG 396
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYR--RPPFSRGGFL---DRKAIRAFAEELIEEFDVRTPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 397 ADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVI 476
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVM 475
|
490 500
....*....|....*....|....*..
gi 1609612952 477 SDGKLSDAHPVEKMTLEKIGLLMGGIH 503
Cdd:COG3845 476 YEGRIVGEVPAAEATREEIGLLMAGVK 502
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-506 |
9.61e-169 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 486.06 E-value: 9.61e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDPK----ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRL 156
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRrgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVGSDV 236
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGREL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 237 ASVSRATGEALGAPQIEVMGLSVAPRtpfavaLKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDaIHLRGK 316
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE-IRLDGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 317 PVgRIGiNGRRLMGAG--FVPEERHGHAAVPGMSLSDNLLLARarsdRKAFLTGGFLRIVRgsvIKAAARRISETMDVRK 394
Cdd:COG1129 315 PV-RIR-SPRDAIRAGiaYVPEDRKGEGLVLDLSIRENITLAS----LDRLSRGGLLDRRR---ERALAEEYIKRLRIKT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 395 SGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIA 474
Cdd:COG1129 386 PSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRIL 465
|
490 500 510
....*....|....*....|....*....|..
gi 1609612952 475 VISDGKLSDAHPVEKMTLEKIGLLMGGIHTSH 506
Cdd:COG1129 466 VMREGRIVGELDREEATEEAIMAAATGGAAAA 497
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-495 |
7.55e-102 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 315.33 E-value: 7.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL--APTEGDIIWQGQPVSVGSPSEARRL 78
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIGMVFQHFSLFEALTVAENIALSLDP----KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNP 154
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEItpggIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVGS 234
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 235 DVASVSRATGEALGAPQIEVMGLSV-APRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDAIHL 313
Cdd:PRK13549 243 ELTALYPREPHTIGEVILEVRNLTAwDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 314 RGKPVgRIGiNGRRLMGAG--FVPEERHGHAAVPGMSLSDNLLLARARsdrkafltggflRIVRGSVIKAAA-----RRI 386
Cdd:PRK13549 323 DGKPV-KIR-NPQQAIAQGiaMVPEDRKRDGIVPVMGVGKNITLAALD------------RFTGGSRIDDAAelktiLES 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 387 SETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEI 466
Cdd:PRK13549 389 IQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEV 468
|
490 500
....*....|....*....|....*....
gi 1609612952 467 FEVATNIAVISDGKLSDAHPVEKMTLEKI 495
Cdd:PRK13549 469 LGLSDRVLVMHEGKLKGDLINHNLTQEQV 497
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-482 |
2.22e-99 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 308.76 E-value: 2.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALS--------LDPKISLKEIAGQAEKLsrayGLPLDPNAHVADLSVGERQRIEIVRALLQ 152
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGqlphkggiVNRRLLNYEAREQLEHL----GVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 153 NPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETP-ASLARMM 231
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDrDQLVQAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 232 VGSDVASVSRATGEALGAPQIEVMGLSvAP--RTPfavalksISMTVRAGEVLAIAGVAGNGQGELFDALSGeypvynnd 309
Cdd:PRK11288 238 VGREIGDIYGYRPRPLGEVRLRLDGLK-GPglREP-------ISFSVRAGEIVGLFGLVGAGRSELMKLLYG-------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 310 AIHLRGkpvGRIGINGRRL--------MGAGFV--PEERHGHAAVPGMSLSDNLllarARSDRKAFLTGGFLrIVRGSVI 379
Cdd:PRK11288 302 ATRRTA---GQVYLDGKPIdirsprdaIRAGIMlcPEDRKAEGIIPVHSVADNI----NISARRHHLRAGCL-INNRWEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 380 KAAARRIsETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVI 459
Cdd:PRK11288 374 ENADRFI-RSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV 452
|
490 500
....*....|....*....|...
gi 1609612952 460 SQDLDEIFEVATNIAVISDGKLS 482
Cdd:PRK11288 453 SSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-495 |
5.17e-96 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 300.16 E-value: 5.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIG 81
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSLDPK--------ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQN 153
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTkkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVG 233
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 234 SDV----ASVSRATGEALGAPQIEVMGLSVAPRTpfavALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPvynnd 309
Cdd:PRK09700 244 RELqnrfNAMKENVSNLAHETVFEVRNVTSRDRK----KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK----- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 310 aihlrgKPVGRIGINGRRLM----------GAGFVPEERHGHAAVPGMSLSDNLLLARARSDRKaflTGGFLRIVRGSVI 379
Cdd:PRK09700 315 ------RAGGEIRLNGKDISprspldavkkGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGG---YKGAMGLFHEVDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 380 KAAARRISETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVI 459
Cdd:PRK09700 386 QRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
490 500 510
....*....|....*....|....*....|....*..
gi 1609612952 460 SQDLDEIFEVATNIAVISDGKLSDA-HPVEKMTLEKI 495
Cdd:PRK09700 466 SSELPEIITVCDRIAVFCEGRLTQIlTNRDDMSEEEI 502
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-513 |
1.28e-87 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 278.47 E-value: 1.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIG 81
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSLDPKISLKEiagQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPKRQASMQ---KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV--TGACDPRRE-------TPASLARMMV 232
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIalSGKTADLSTddiiqaiTPAAREKSLS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 233 GSDV----ASVSRATgEALGAPQIEVMGLSvaprtpfAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVyNN 308
Cdd:PRK15439 247 ASQKlwleLPGNRRQ-QAAGAPVLTVEDLT-------GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA-RG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 309 DAIHLRGKPVGRIGINGRRLMGAGFVPEERHGHAAVPGMSLSDNllLARARSDRKAFltggFLRIVRGSVIKAAARRIse 388
Cdd:PRK15439 318 GRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWN--VCALTHNRRGF----WIKPARENAVLERYRRA-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 389 tMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFE 468
Cdd:PRK15439 390 -LNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1609612952 469 VATNIAVISDGKLSDAHPVEKMTLEKIGLLMGGihtSHSGAAQHA 513
Cdd:PRK15439 469 MADRVLVMHQGEISGALTGAAINVDTIMRLAFG---EHQAQEASC 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-495 |
1.13e-86 |
|
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: 275.94 E-value: 1.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL--APTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSldPKISLK-------EIAGQAEKLSRAYGLPLDPNA-HVADLSVGERQRIEIVRALLQ 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLG--NEITLPggrmaynAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 153 NPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMV 232
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 233 GSDVASVSRATGEALGAPQIEVMGLSV-APRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDAI 311
Cdd:TIGR02633 239 GREITSLYPHEPHEIGDVILEARNLTCwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 312 HLRGKPVGRIGINGRRLMGAGFVPEERHGHAAVPGMSLSDNLLLARArsDRKAFLTggflRIVRGSVIKAAARRISEtMD 391
Cdd:TIGR02633 319 FINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVL--KSFCFKM----RIDAAAELQIIGSAIQR-LK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 392 VRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVAT 471
Cdd:TIGR02633 392 VKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSD 471
|
490 500
....*....|....*....|....
gi 1609612952 472 NIAVISDGKLSDAHPVEKMTLEKI 495
Cdd:TIGR02633 472 RVLVIGEGKLKGDFVNHALTQEQV 495
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-495 |
2.54e-85 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 272.26 E-value: 2.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIG 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSLDP-----KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRL 156
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVGSDV 236
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 237 ASVSRATGEALGAPQIEVMGLSvaprtpfAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPvynndaihlrgK 316
Cdd:PRK10762 243 EDQYPRLDKAPGEVRLKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-----------R 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 317 PVGRIGINGRRLM----------GAGFVPEERHGHAAVPGMSLSDNLLLARARsdrkaFLTGGFLRIVRGSVIKAAARRI 386
Cdd:PRK10762 305 TSGYVTLDGHEVVtrspqdglanGIVYISEDRKRDGLVLGMSVKENMSLTALR-----YFSRAGGSLKHADEQQAVSDFI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 387 sETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEI 466
Cdd:PRK10762 380 -RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEV 458
|
490 500
....*....|....*....|....*....
gi 1609612952 467 FEVATNIAVISDGKLSDAHPVEKMTLEKI 495
Cdd:PRK10762 459 LGMSDRILVMHEGRISGEFTREQATQEKL 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-495 |
3.12e-84 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 269.29 E-value: 3.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 9 LTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIGMVFQHFS 88
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 89 LFEALTVAENIALSLDPK----ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTS 164
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTkgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 165 VLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVGSdvaSVSRATG 244
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGR---SLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 245 EALGAPQ---IEVMGLSvAPRTPfavALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGeypvynndaihLRGKPVGRI 321
Cdd:PRK10982 241 DKENKPGeviLEVRNLT-SLRQP---SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG-----------IREKSAGTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 322 GINGRRL--------MGAGF--VPEERHGHAAVPGMSLSDNLLLARARSDRKAFltgGFLRIVRgsvIKAAARRISETMD 391
Cdd:PRK10982 306 TLHGKKInnhnaneaINHGFalVTEERRSTGIYAYLDIGFNSLISNIRNYKNKV---GLLDNSR---MKSDTQWVIDSMR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 392 VRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVAT 471
Cdd:PRK10982 380 VKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITD 459
|
490 500
....*....|....*....|....
gi 1609612952 472 NIAVISDGKLSDAHPVEKMTLEKI 495
Cdd:PRK10982 460 RILVMSNGLVAGIVDTKTTTQNEI 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
4.32e-83 |
|
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: 254.66 E-value: 4.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIGMV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQhfslfealtvaenialsldpkislkeiagqaeklsrayglpldpnahvadLSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:cd03216 81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 164 SVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTG 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-499 |
4.81e-79 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 255.87 E-value: 4.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLaPT---EGDIIWQGQPVSVGSPSEARRLG 79
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLDPK----ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPR 155
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAkrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRE--TPASLARMMVG 233
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADevTEDRIIRGMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 234 SDVASVSRATGEALGAPQIEVMGLSV-APRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELfdALS---GEYPVYNND 309
Cdd:NF040905 240 RDLEDRYPERTPKIGEVVFEVKNWTVyHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMSvfgRSYGRNISG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 310 AIHLRGKPVgRIGiNGRRLMGAG--FVPEERHGHAAVPGMSLSDNLLLARARsdrkafltggflRIVRGSVIK-----AA 382
Cdd:NF040905 318 TVFKDGKEV-DVS-TVSDAIDAGlaYVTEDRKGYGLNLIDDIKRNITLANLG------------KVSRRGVIDeneeiKV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 383 ARRISETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQD 462
Cdd:NF040905 384 AEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSE 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 1609612952 463 LDEIFEVATNIAVISDGKLSDAHPVEKMTLEKIGLLM 499
Cdd:NF040905 464 LPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-213 |
8.02e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 207.61 E-value: 8.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARRLgIGMV 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIAL--SLDPkISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFfaRLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-213 |
1.17e-60 |
|
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: 199.20 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIGMV 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENI-----------ALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQ 152
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 153 NPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
4.04e-59 |
|
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: 193.00 E-value: 4.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARRLgIGMV 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLdpkislkeiagqaeklsrayglpldpnahvadlsvGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:cd03230 79 PEEPSLYENLTVRENLKLSG-----------------------------------GMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1609612952 164 SVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-213 |
1.64e-58 |
|
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: 194.49 E-value: 1.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLD----------------PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRI 144
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAAHarlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 145 EIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-481 |
6.84e-57 |
|
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: 197.82 E-value: 6.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF--GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPT---EGDIIWQGQPVsVGSPSEAR 76
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RLGIGMVFQHF-SLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNP 154
Cdd:COG1123 82 GRRIGMVFQDPmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRR--ETPASLARmM 231
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEilAAPQALAA-V 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 232 VGSDVASVSRATGEALGAPQIEVMGLSV---APRTPFAVALKSISMTVRAGEVLAIAGvaGNGQGE---------LFDAL 299
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPLLEVRNLSKrypVRGKGGVRAVDDVSLTLRRGETLGLVG--ESGSGKstlarlllgLLRPT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 300 SGEypvynndaIHLRGKPVGRIGINGRRLMG--AGFV---PEerhgHAAVPGMSLSDnlLLARArsdrkafltggfLRIV 374
Cdd:COG1123 319 SGS--------ILFDGKDLTKLSRRSLRELRrrVQMVfqdPY----SSLNPRMTVGD--IIAEP------------LRLH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 375 RGSVIKAAARRISETMDV---RKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAK 451
Cdd:COG1123 373 GLLSRAERRERVAELLERvglPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQR 452
|
490 500 510
....*....|....*....|....*....|.
gi 1609612952 452 A-GSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:COG1123 453 ElGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-213 |
5.17e-55 |
|
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: 184.68 E-value: 5.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARRLgIGM 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQ-IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIA-LSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:COG4555 79 LPDERGLYDRLTVRENIRyFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
248-481 |
6.75e-55 |
|
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: 182.25 E-value: 6.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 248 GAPQIEVMGLSVAPRtpfavaLKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDaIHLRGKPVGRIGINGRR 327
Cdd:cd03215 1 GEPVLEVRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGE-ITLDGKPVTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 328 LMGAGFVPEERHGHAAVPGMSLSDNLLLARarsdrkafltggflrivrgsvikaaarrisetmdvrksgadplagSLSGG 407
Cdd:cd03215 74 RAGIAYVPEDRKREGLVLDLSVAENIALSS---------------------------------------------LLSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 408 NLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-213 |
1.98e-50 |
|
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: 172.38 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR-- 76
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RLGIGMVFQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPR 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-213 |
1.83e-49 |
|
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: 169.44 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFS--LFEAlTV 95
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQNPDdqLFAP-TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 96 AENIALSLDP-KISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:COG1122 94 EEDVAFGPENlGLPREEIRERVEEALELVGL-----EHLADrppheLSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1609612952 170 EADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1122 169 GRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-213 |
2.72e-49 |
|
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: 168.47 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRlgIGMV 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRN--IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLDP-KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 163 TSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03259 158 LSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-212 |
5.31e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.95 E-value: 5.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSL-FEALTVAEN 98
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQNPDDqFFGPTVEEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLDP-KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFET 177
Cdd:cd03225 97 VAFGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1609612952 178 LEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:cd03225 177 LKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-213 |
2.17e-47 |
|
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: 163.76 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEAR-RLGIGM 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPHERaRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSLdpkiSLKEIAGQAEKLSRAYGL-P-LDPNAH--VADLSVGERQRIEIVRALLQNPRLII 158
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGA----YARRRAKRKARLERVYELfPrLKERRKqlAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-213 |
2.87e-47 |
|
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: 164.00 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRL--G 79
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLD--PKISLKEIAGQA-EKLSRAyGLPldpnaHVAD-----LSVGERQRIEIVRALL 151
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLRehTDLSEAEIRELVlEKLELV-GLP-----GAADkmpseLSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 152 QNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
4.82e-46 |
|
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: 158.89 E-value: 4.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPV-SVGSPSEARRLGIGM 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSldpkislkeiagqaeklsrayglpldpnahvadLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
5.62e-46 |
|
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: 159.96 E-value: 5.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE---AR 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RLGIGMVFQHFSLFEALTVAENIALSLDP-KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPR 155
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLaGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRlEEVQRICDRATVLRHGKV 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-214 |
7.33e-46 |
|
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: 160.15 E-value: 7.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEAR-RLG 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-GLPPHRIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLdpkISLKEIAGQAEKLSRAYGL-P-LDP--NAHVADLSVGERQRIEIVRALLQNPR 155
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGA---YARRDRAEVRADLERVYELfPrLKErrRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-215 |
9.41e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.82 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEA-- 75
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 76 -RRLGIGMVFQHFSLFEALTVAENIALSLDP-KISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVR 148
Cdd:COG1136 83 lRRRHIGFVFQFFNLLPELTALENVALPLLLaGVSRKERRERARELLERVGL-----GDRLDhrpsqLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 149 ALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRlEEVQRICDRATVLRHGKVTG 215
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-226 |
1.76e-45 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 159.20 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLG--IG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSL-----DPKISLKEIAgqAEKLSRAyGLPLDPNAHVADLSVGERQRIEIVRALLQNPRL 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrehtrLSEEEIREIV--LEKLEAV-GLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVtGACDPRRETPAS 226
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI-VAEGTPEELRAS 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-213 |
4.37e-45 |
|
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: 158.05 E-value: 4.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRL 78
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 G--IGMVFQH--FSLFEALTVAENIAlslDPKISLKEIAGQAEKLSRAY----GLPLDP---NAHVADLSVGERQRIEIV 147
Cdd:cd03257 81 RkeIQMVFQDpmSSLNPRMTIGEQIA---EPLRIHGKLSKKEARKEAVLlllvGVGLPEevlNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 148 RALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-213 |
6.37e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.42 E-value: 6.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARrlGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDP-KISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNP 154
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMrGVPKAEIRARVAELLELVGL-----EGLADryphqLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 155 RLIILDEPTSVLTPQEADKL-FETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
2.49e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.36 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMV 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEAlTVAENIALSLdpkiSLKEIAGQAEKLSR---AYGLPLDP-NAHVADLSVGERQRIEIVRALLQNPRLIIL 159
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPF----QLRERKFDRERALElleRLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 160 DEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-213 |
3.48e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.16 E-value: 3.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlgIGMV 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERR--VGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRLI 157
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRvRPPSKAEIRARVEELLELVQL-----EGLADrypsqLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 158 ILDEPTSVLtpqeaD-KLFETLEK-----LKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1118 156 LLDEPFGAL-----DaKVRKELRRwlrrlHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-212 |
3.90e-44 |
|
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: 153.17 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 5 SVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVF 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 85 QhfslfealtvaenialsldpkislkeiagqaeklsrayglpldpnahvadLSVGERQRIEIVRALLQNPRLIILDEPTS 164
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 165 VLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-213 |
6.31e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 158.32 E-value: 6.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR--R 77
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 78 LGIGMVFQHFSLFEALTVAENIALSLdpkislkEIAG--QAEKLSRAYGLpLD-------PNAHVADLSVGERQRIEIVR 148
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPL-------EIAGvpKAEIRKRVAEL-LElvglsdkADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 149 ALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-164 |
1.54e-43 |
|
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: 151.26 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRLGIGMVFQHFSLFEALTVAENI 99
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTS 164
Cdd:pfam00005 81 RLGLLLKgLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
2.85e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 155.27 E-value: 2.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgSPSEARRLGI--- 80
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 --GmvfqhfsLFEALTVAENIA----LsldpK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQN 153
Cdd:COG4152 79 erG-------LYPKMKVGEQLVylarL----KgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-212 |
1.42e-42 |
|
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: 149.46 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLFSG-TIRENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 alsldpkislkeiagqaeklsrayglpldpnahvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLE 179
Cdd:cd03228 97 ------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|...
gi 1609612952 180 KLkAEGRSVLYISHRLEEVQRiCDRATVLRHGK 212
Cdd:cd03228 141 AL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
1.91e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.78 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSear 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 rlgIGMVFQHFSLFEALTVAENIALSLDPK-ISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRAL 150
Cdd:COG1116 82 ---RGVVFQEPALLPWLTVLDNVALGLELRgVPKAERRERARELLELVGL-----AGFEDayphqLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 151 LQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHG 211
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-213 |
1.20e-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: 148.20 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvgspsEARRLGIGMV 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-214 |
1.45e-41 |
|
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: 149.18 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFG----NFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRl 78
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIGMVFQHF--SLFEALTVAENIALSLdpKI-SLKEIAGQAEKLSRAYGLP---LDPNAHvaDLSVGERQRIEIVRALLQ 152
Cdd:COG1124 80 RVQMVFQDPyaSLHPRHTVDRILAEPL--RIhGLPDREERIAELLEQVGLPpsfLDRYPH--QLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 153 NPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-213 |
1.48e-41 |
|
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: 158.46 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSG-TIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSlDPKISLKEI---AGQA------EKLSRAYGLPLDPNAhvADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:COG2274 570 TLG-DPDATDEEIieaARLAglhdfiEALPMGYDTVVGEGG--SNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 171 ADKLFETLEKLKAeGRSVLYISHRLEEVqRICDRATVLRHGKV 213
Cdd:COG2274 647 EAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
1.97e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgspsEARRLGI 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEA--LTVAENIALSLDPKISLKEIAGQAEK------LSRAyGLpldpnAHVAD-----LSVGERQRIEIV 147
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADReavdeaLERV-GL-----EDLADrpigeLSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 148 RALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVtgACDPRRE--TPA 225
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEvlTPE 229
|
....
gi 1609612952 226 SLAR 229
Cdd:COG1121 230 NLSR 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
2.89e-41 |
|
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: 147.29 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR-RLGIGM 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSldPKISLKEIAGQAEKLSRAY----GLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERALELlekvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-213 |
3.24e-41 |
|
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: 147.27 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN--FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpvSVGSPSEARRLGIG 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILD 160
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 161 EPTSVLTPQEADKLFETLEKLKaEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-218 |
3.35e-41 |
|
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: 147.23 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSearrlg 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLElQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVL--RHGKVTGACD 218
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
4.81e-41 |
|
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: 146.59 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpvSVGSPSEARRLgIGMV 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENI-ALSLDPKISLKEIagqaEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03268 78 IEAPGFYPNLTARENLrLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-213 |
9.60e-41 |
|
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: 145.98 E-value: 9.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 6 VRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARRlGIGMVFQ 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRR-RIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 HFSLFEALTVAENIALSLD----PKISLKEiagQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARlygvPGAERRE---RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-229 |
1.98e-40 |
|
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: 146.34 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE-ARRlgIG 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSLDPKISL--------KEIAGQAEKLSRAYGLpldpnAH--VADLSVGERQRIEIVRALL 151
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYPHLGLfgrpsaedREAVEEALERTGLEHL-----ADrpVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 152 QNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRE--TPASLA 228
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIV-AQGPPEEvlTPELLE 232
|
.
gi 1609612952 229 R 229
Cdd:COG1120 233 E 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-214 |
2.01e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.20 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 14 GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRL--GIGMVFQHFSLFE 91
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 ALTVAENIALSLdpKI---SLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:COG2884 93 DRTVYENVALPL--RVtgkSRKEIRRRVREVLDLVGL-----SDKAKalpheLSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 164 SVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:COG2884 166 GNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-229 |
4.07e-40 |
|
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: 145.02 E-value: 4.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN-FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR--RLGI 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENI---ALSLDPKI-------SLKEIAGQAEKLSRAyGLPLDPNAHVADLSVGERQRIEIVRAL 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRSTWrslfglfPKEEKQRALAALERV-GLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 151 LQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLAR 229
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
5.92e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.91 E-value: 5.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARrlGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKDR--NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAygLPLDP--NAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKlRKVPKAEIDRRVREAAEL--LGLEDllDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-213 |
1.18e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 143.60 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPS-EARRLGIG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSldPKISLKEIAGQAEKLSRAY----GLPLDPNAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLA--PIKVKKMSKAEAEERAMELlervGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-213 |
2.89e-39 |
|
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: 142.32 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL-----APTEGDIIWQGQPV-SVGSPSEARR 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 78 LGIGMVFQHFSLFEAlTVAENIALSL-----DPKISLKEIAGQAekLSRAyGLP--LDPNAHVADLSVGERQRIEIVRAL 150
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLrlhgiKLKEELDERVEEA--LRKA-ALWdeVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 151 LQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEgRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-213 |
3.58e-39 |
|
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: 142.30 E-value: 3.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIGMV 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRLI 157
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEiRGLSKKEREEKLEELLEEFHI-----THLRKskassLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-213 |
4.53e-39 |
|
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: 144.43 E-value: 4.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAP---TEGDIIWQGQPVSVGSPSEA 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 76 RRL---GIGMVFQhfslfEALTvaenialSLDP----------------KISLKEIAGQAEKLSRAYGLPlDPNAHVAD- 135
Cdd:COG0444 81 RKIrgrEIQMIFQ-----DPMT-------SLNPvmtvgdqiaeplrihgGLSKAEARERAIELLERVGLP-DPERRLDRy 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 136 ---LSVGERQRIEIVRALLQNPRLIILDEPTSVL--TPQeADKLfETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLR 209
Cdd:COG0444 148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALdvTIQ-AQIL-NLLKDLQRElGLAILFITHDLGVVAEIADRVAVMY 225
|
....
gi 1609612952 210 HGKV 213
Cdd:COG0444 226 AGRI 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-213 |
6.06e-39 |
|
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: 141.35 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARRl 78
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIGMVFQHFSLFEALTVAENIAL-----SLDPKislkEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQN 153
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYfaglyGLKGD----ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-226 |
1.13e-38 |
|
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: 141.32 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 6 VRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPseaRRLGIGMVFQ 85
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 HFSLFEALTVAENIALSLDPK-----ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILD 160
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKprserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 161 EPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV--TGACDPRRETPAS 226
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIeqVGTPDEVYDHPAS 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-215 |
1.14e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.77 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLFSG-TIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSlDPKISLKEIAgQAEKLSRAY----GLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:COG1132 435 RYG-RPDATDEEVE-EAAKAAQAHefieALPDGYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1609612952 172 DKLFETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKVTG 215
Cdd:COG1132 513 ALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVE 554
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-213 |
3.10e-38 |
|
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: 140.86 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN------------------------FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGD 59
Cdd:cd03294 1 IKIKGLYKIFGKnpqkafkllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 60 IIWQGQPVSVGSPSEARRL---GIGMVFQHFSLFEALTVAENIALSLdpkislkEIAGQ--AEKLSRA------YGLPLD 128
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPHRTVLENVAFGL-------EVQGVprAEREERAaealelVGLEGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 129 PNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATV 207
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAI 233
|
....*.
gi 1609612952 208 LRHGKV 213
Cdd:cd03294 234 MKDGRL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-229 |
5.23e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 139.12 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACngIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPseARRlGIGMV 83
Cdd:COG3840 2 LRLDDLTYRYGDFPLR--FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AER-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLDPKISL--------KEIAGQ---AEKLSRaygLPldpnahvADLSVGERQRIEIVRALLQ 152
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLKLtaeqraqvEQALERvglAGLLDR---LP-------GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 153 NPRLIILDEPTSVLTP---QEADKLFETLekLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV--TGACDP--RRETPA 225
Cdd:COG3840 147 KRPILLLDEPFSALDPalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAARIADRVLLVADGRIaaDGPTAAllDGEPPP 224
|
....
gi 1609612952 226 SLAR 229
Cdd:COG3840 225 ALAA 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-214 |
6.75e-38 |
|
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: 137.77 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgsPSEARRLGIGMVFQH--FSLFEAlTVAE 97
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALSLDPkisLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFET 177
Cdd:cd03226 92 ELLLGLKE---LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1609612952 178 LEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:cd03226 169 IRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-213 |
9.49e-38 |
|
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: 138.52 E-value: 9.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARrlGIGMV 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKR--PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-224 |
1.23e-37 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 138.97 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEA-RRLGI 80
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQiARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDPKISLKEIAG----------QAEKLSRA------YGLPLDPNAHVADLSVGERQRI 144
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGllktpafrraESEALDRAatwlerVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 145 EIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGK--VTGACDPRR 221
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTplANGTPEEIR 242
|
...
gi 1609612952 222 ETP 224
Cdd:PRK11300 243 NNP 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-213 |
1.49e-37 |
|
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: 138.20 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN-FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGM 82
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSldPKIsLKEiaGQAEKLSRAYGL----PLDPnAHVAD-----LSVGERQRIEIVRALLQN 153
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALV--PKL-LKW--PKEKIRERADELlalvGLDP-AEFADrypheLSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-213 |
4.17e-37 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 137.02 E-value: 4.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVgSPSEAR-RLGIGM 82
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH-LPMHERaRLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENI--ALSLDPKISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPR 155
Cdd:TIGR04406 81 LPQEASIFRKLTVEENImaVLEIRKDLDRAEREERLEALLEEFQI-----SHLRDnkamsLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKV 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-213 |
5.34e-37 |
|
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: 135.89 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIaRGEIHALLGENGAGKSTLVKMLFGVLAPTEGDI-----IWQGQPVSVGSPSEARRlgIGMVFQHFSLFEALTVA 96
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLFDSRKKINLPPQQRK--IGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSLdPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFE 176
Cdd:cd03297 94 ENLAFGL-KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1609612952 177 TLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-212 |
7.24e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 139.20 E-value: 7.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 9 LTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgsPSEAR--RLGIGMVFQH 86
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARlaRARIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 87 FSLFEALTVAEN-IALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSV 165
Cdd:PRK13536 123 DNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1609612952 166 LTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-213 |
7.43e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 136.31 E-value: 7.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEAR-RLG 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKRaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLDP-KISLKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQN 153
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELrKLSKKEREERLEELLEEFGI-----THLRKskaysLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 154 PRLIILDEPTSVLTP---QEADKLfetLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1137 155 PKFILLDEPFAGVDPiavADIQKI---IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-220 |
8.38e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 135.93 E-value: 8.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNgIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARrlGIGMV 83
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKR--DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRkVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-216 |
9.44e-37 |
|
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: 142.97 E-value: 9.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 17 AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVA 96
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAWVPQNPYLFAG-TIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSlDPKISLKEIAgQAEKLSRAY----GLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTP 168
Cdd:COG4988 429 ENLRLG-RPDASDEELE-AALEAAGLDefvaALPDGLDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 169 QEADKLFETLEKLkAEGRSVLYISHRLEEVqRICDRATVLRHGKVTGA 216
Cdd:COG4988 507 ETEAEILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVEQ 552
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-213 |
1.01e-36 |
|
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: 134.97 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRkltklFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgspsEARRLGIGMV 83
Cdd:cd03235 5 LTVS-----YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSL---FeALTVAENIALSLDPKISLKEIAGQAEK------LSRAyGLpldpnAHVAD-----LSVGERQRIEIVRA 149
Cdd:cd03235 74 PQRRSIdrdF-PISVRDVVLMGLYGHKGLFRRLSKADKakvdeaLERV-GL-----SELADrqigeLSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 150 LLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-213 |
1.54e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.40 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 7 RKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR--RLGI 80
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkaRRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLdpkislkEIAGQAEKLSRAYGLPLDP--------NAHVADLSVGERQRIEIVRALLQ 152
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPL-------ELAGTPKAEIKARVTELLElvglsdkaDRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 153 NPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-213 |
6.95e-36 |
|
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: 132.92 E-value: 6.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 7 RKLTKLFGN-FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVS--VGSPSEARRLGIGMV 83
Cdd:cd03292 4 INVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEvTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-213 |
1.36e-35 |
|
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: 131.99 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEArrlGIGMV 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLDPKISLK-EIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKdEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-214 |
3.77e-35 |
|
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: 129.48 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 5 SVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVF 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 85 QhfslfeALTVAEnialsldpkislkeIAGQAEKlsrayglpldpnaHVADLSVGERQRIEIVRALLQNPRLIILDEPTS 164
Cdd:cd03214 80 Q------ALELLG--------------LAHLADR-------------PFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 165 VLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:cd03214 127 HLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-214 |
6.04e-35 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 130.55 E-value: 6.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLF--GNFA--ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEA--- 75
Cdd:TIGR02211 1 LLKCENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 76 RRLGIGMVFQHFSLFEALTVAENIAL-SLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNP 154
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMpLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRIcDRATVLRHGKVT 214
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-201 |
7.30e-35 |
|
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: 129.52 E-value: 7.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIg 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 mVFQHFSLFEALTVAENIALSLdpkiSLKEIAGQAEKLSRAY-GLPLDPNAH--VADLSVGERQRIEIVRALLQNPRLII 158
Cdd:COG4133 80 -LGHADGLKPELTVRENLRFWA----ALYGLRADREAIDEALeAVGLAGLADlpVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISH---RLEEVQRI 201
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-213 |
8.44e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.93 E-value: 8.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF----GNFA-------ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVG 70
Cdd:COG4608 6 PLLEVRDLKKHFpvrgGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPSEARRL--GIGMVFQ--HFSLFEALTVAENIALSLDpkisLKEIAGQAEKLSRAY------GLP---LDPNAHvaDLS 137
Cdd:COG4608 86 SGRELRPLrrRMQMVFQdpYASLNPRMTVGDIIAEPLR----IHGLASKAERRERVAellelvGLRpehADRYPH--EFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 138 VGERQRIEIVRALLQNPRLIILDEPTSVLtpqeaDK--------LfetLEKLKAE-GRSVLYISHRLEEVQRICDRATVL 208
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSAL-----DVsiqaqvlnL---LEDLQDElGLTYLFISHDLSVVRHISDRVAVM 231
|
....*
gi 1609612952 209 RHGKV 213
Cdd:COG4608 232 YLGKI 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-490 |
6.61e-34 |
|
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: 134.54 E-value: 6.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGV--LAPTEGDII----------WQGQPVSVGS 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 72 P------------------SEA------RRLGIgMVFQHFSLFEALTVAENIALSL-DPKISLKEIAGQAEKLSRAYGLP 126
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlSDKlrrrirKRIAI-MLQRTFALYGDDTVLDNVLEALeEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 127 lDPNAHVA-DLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDR 204
Cdd:TIGR03269 160 -HRITHIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 205 ATVLRHGKVTGACDPRRetpaSLARMMVGsdVASVSRATGEALGAPQIEVMGLS---VAPRTPFAVALKSISMTVRAGEV 281
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDE----VVAVFMEG--VSEVEKECEVEVGEPIIKVRNVSkryISVDRGVVKAVDNVSLEVKEGEI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 282 LAIAGVAGNGQGELFDAL-------SGEYPV-YNNDAIHLRGK-PVGRiginGRRLMGAGFVPEErhgHAAVPGMSLSDN 352
Cdd:TIGR03269 313 FGIVGTSGAGKTTLSKIIagvleptSGEVNVrVGDEWVDMTKPgPDGR----GRAKRYIGILHQE---YDLYPHRTVLDN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 353 LL------LARARSDRKAFLTggfLRIVRGSVIKAaarrisetmdvrKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLV 426
Cdd:TIGR03269 386 LTeaigleLPDELARMKAVIT---LKMVGFDEEKA------------EEILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 427 VNQPTWGVD----AGAASRIRQALVDLakaGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKM 490
Cdd:TIGR03269 451 LDEPTGTMDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-229 |
7.63e-34 |
|
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: 134.89 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 17 AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVA 96
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR-IAVVPQRPHLFDT-TLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSlDPKIS---LKEIAGQAEKLSRAYGLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:COG4987 427 ENLRLA-RPDATdeeLWAALERVGLGDWLAALPDGLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAA 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 170 EADKLFETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKVTgacdpRRETPASLAR 229
Cdd:COG4987 506 TEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDGRIV-----EQGTHEELLA 558
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-226 |
8.45e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.50 E-value: 8.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEArrlGI 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR---PI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSL-DPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIIL 159
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLkQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 160 DEPTSVLTPQEADKL-FETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRR--ETPAS 226
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEiyEHPTT 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-239 |
2.14e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.77 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgsPSEAR--RLG 79
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARhaRQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENI-ALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGK--VTGAcdprretPASLARMMVGSDV 236
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRkiAEGA-------PHALIESEIGCDV 234
|
...
gi 1609612952 237 ASV 239
Cdd:PRK13537 235 IEI 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-243 |
3.73e-33 |
|
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: 129.07 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDI-----IWQ--GQPVSVgsPSEARRlgIGMVFQHFSLFEALT 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggeVLQdsARGIFL--PPHRRR--IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 95 VAENI------ALSLDPKISLKEIA---GQAEKLSRayglpldpnaHVADLSVGERQRIEIVRALLQNPRLIILDEPTSV 165
Cdd:COG4148 94 VRGNLlygrkrAPRAERRISFDEVVellGIGHLLDR----------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 166 LTPQEADKLFETLEKLKAEGR-SVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRETPAS--LARMMVGSDVASVSRA 242
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVV-ASGPLAEVLSRpdLLPLAGGEEAGSVLEA 242
|
.
gi 1609612952 243 T 243
Cdd:COG4148 243 T 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-218 |
6.17e-33 |
|
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: 126.46 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLF---------GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPS 73
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 74 EARRL--GIGMVFQH-FSLFEA-LTVAENIALSLDPKISLKEIAGQAE--KLSRAYGLPLD-PNAHVADLSVGERQRIEI 146
Cdd:TIGR02769 82 QRRAFrrDVQLVFQDsPSAVNPrMTVRQIIGEPLRHLTSLDESEQKARiaELLDMVGLRSEdADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 147 VRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACD 218
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
1.06e-32 |
|
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: 122.93 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTklfgNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIG 81
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MV---FQHFSLFEALTVAENIALSldpkislkeiagqaeklsrayglpldpnahvADLSVGERQRIEIVRALLQNPRLII 158
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIALS-------------------------------SLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 159 LDEPT---SVLTPQEadkLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03215 128 LDEPTrgvDVGAKAE---IYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-291 |
2.45e-32 |
|
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: 129.80 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKS----TLVKMLFGVLAPTEGDIIWQGQPVSVGSP 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SEARRL---GIGMVFQH--FSLFEALTVAENIA--LSLDPKISLKEIAGQAEKLSRAYGLPlDPNAHVAD----LSVGER 141
Cdd:COG4172 84 RELRRIrgnRIAMIFQEpmTSLNPLHTIGKQIAevLRLHRGLSGAAARARALELLERVGIP-DPERRLDAyphqLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 142 QRIEIVRALLQNPRLIILDEPTSVL--TPQeADKLfETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV--TGA 216
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALdvTVQ-AQIL-DLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIveQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 217 CD-----PRRE-TPASLArmmvgsdvasvSRATGEALGAPQ-----IEVMGLSVA--------PRTPFAV-ALKSISMTV 276
Cdd:COG4172 241 TAelfaaPQHPyTRKLLA-----------AEPRGDPRPVPPdapplLEARDLKVWfpikrglfRRTVGHVkAVDGVSLTL 309
|
330
....*....|....*
gi 1609612952 277 RAGEVLAIAGVAGNG 291
Cdd:COG4172 310 RRGETLGLVGESGSG 324
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-213 |
3.52e-32 |
|
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: 123.10 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENIA 100
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQDTFLFSG-TIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LS-LDPKISLKEIAGQA-------EKLSRAYGLPLDPNAHvaDLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEAD 172
Cdd:cd03254 99 LGrPNATDEEVIEAAKEagahdfiMKLPNGYDTVLGENGG--NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1609612952 173 KLFETLEKLKaEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03254 177 LIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-214 |
8.34e-32 |
|
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: 121.53 E-value: 8.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGeIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRLgIGMV 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIA-LSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:cd03264 78 PQEFGVYPNFTVREFLDyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 163 TSVLTPQEADKLFETLEKLkAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:cd03264 158 TAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-227 |
8.84e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.83 E-value: 8.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRlgI 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRH--V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIIL 159
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRmQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 160 DEPTSVLtpqeaD-KLFETLE-KLKAEGRSV----LYISHRLEEVQRICDRATVLRHGKVTGACDPRR--ETPASL 227
Cdd:PRK09452 169 DESLSAL-----DyKLRKQMQnELKALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREiyEEPKNL 239
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
4-216 |
1.12e-31 |
|
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: 125.22 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRkLTKLFGNFaaCNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDI-----IWQGQPVSVGSPSEARRL 78
Cdd:TIGR02142 1 LSAR-FSKRLGDF--SLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrTLFDSRKGIFLPPEKRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIgmVFQHFSLFEALTVAENIALSLDpKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:TIGR02142 78 GY--VFQEARLFPHLSVRGNLRYGMK-RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGA 216
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-213 |
1.43e-31 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 121.71 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLA--PTEGDIIWQGQPVSVGSPSEARRLGIGMVFQHFSLFEALTVAE 97
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 --NIALS--LDPKISLKEIAGQAEKLSRAYGLP---LDPNAHVaDLSVGERQRIEIVRALLQNPRLIILDEPTSVLtpqe 170
Cdd:COG0396 97 flRTALNarRGEELSAREFLKLLKEKMKELGLDedfLDRYVNE-GFSGGEKKRNEILQMLLLEPKLAILDETDSGL---- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 171 aD-----KLFETLEKLKAEGRSVLYISHRleevQRI-----CDRATVLRHGKV 213
Cdd:COG0396 172 -DidalrIVAEGVNKLRSPDRGILIITHY----QRIldyikPDFVHVLVDGRI 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-213 |
5.28e-31 |
|
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: 119.52 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 23 DLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARrlgIGMVFQHFSLFEALTVAENIALS 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP---VSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 103 LDPKISLKEIAGQA-EKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKL 181
Cdd:cd03298 95 LSPGLKLTAEDRQAiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 1609612952 182 KAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:cd03298 175 HAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-216 |
7.68e-31 |
|
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: 120.19 E-value: 7.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEG-DIIWQGQPVSVGSPSEARRLgIGMV---FQHFslFEALTV 95
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR-IGLVspaLQLR--FPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 96 AENIALS-------LDPKISLKEIAgQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:COG1119 97 VLDVVLSgffdsigLYREPTDEQRE-RARELLELLGL-----AHLADrpfgtLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 164 SVLTPQEADKLFETLEKLKAEG-RSVLYISHRLEEVQRICDRATVLRHGKVTGA 216
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-261 |
1.03e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.50 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 8 KLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSpseARRLGIGMVFQHF 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH---ARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 88 SLFEALTVAENIA--LSLDP---KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:PRK10851 84 ALFRHMTVFDNIAfgLTVLPrreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGR--SVlYISHRLEEVQRICDRATVLRHGKVTGACDPRR--ETPASlarMMVGSDVAS 238
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELKftSV-FVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQvwREPAT---RFVLEFMGE 239
|
250 260
....*....|....*....|....*..
gi 1609612952 239 VSRATGEALGApQIEVMG----LSVAP 261
Cdd:PRK10851 240 VNRLQGTIRGG-QFHVGAhrwpLGYTP 265
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-219 |
1.12e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 7 RKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR-RLGIGMVFQ 85
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 HFSLFEALTVAENIALSldP----KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:PRK09493 85 QFYLFPHLTALENVMFG--PlrvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-228 |
1.57e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.79 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTK------LFGNFAA---CNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGS 71
Cdd:PRK10419 1 MTLLNVSGLSHhyahggLSGKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 72 PSEAR--RLGIGMVFQH-FSLFEA-LTVAENIALSLDPKISLKEIAGQA--EKLSRAYGLPldpnAHVAD-----LSVGE 140
Cdd:PRK10419 81 RAQRKafRRDIQMVFQDsISAVNPrKTVREIIREPLRHLLSLDKAERLAraSEMLRAVDLD----DSVLDkrppqLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 141 RQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV-----T 214
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIvetqpV 236
|
250
....*....|....
gi 1609612952 215 GACDpRRETPASLA 228
Cdd:PRK10419 237 GDKL-TFSSPAGRV 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-213 |
1.65e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 119.08 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDI------IWQGQPVSvGSPSE 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLS-QQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 75 ARRL--GIGMVFQHFSLFEALTVAENIALSldPKISLKEIAGQAEKLSRAY----GLPLDPNAHVADLSVGERQRIEIVR 148
Cdd:PRK11264 80 IRQLrqHVGFVFQNFNLFPHRTVLENIIEG--PVIVKGEPKEEATARARELlakvGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 149 ALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-213 |
1.67e-30 |
|
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: 118.80 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSlDPKISLKEIAgQAEKLSRAY----GLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:cd03249 98 RYG-KPDATDEEVE-EAAKKANIHdfimSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1609612952 172 DKLFETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03249 176 KLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-213 |
2.48e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 23 DLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPseARRlGIGMVFQHFSLFEALTVAENIALS 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP--SRR-PVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 103 LDP--------KISLKEIAGQ---AEKLSRaygLPldpnahvADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PRK10771 96 LNPglklnaaqREKLHAIARQmgiEDLLAR---LP-------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 172 DKLFETLEKLKAEGR-SVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK10771 166 QEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-229 |
3.04e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.68 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE-ARRLGIgmVFQHFSLFEALTVAEN 98
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAV--LPQHSSLAFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLDPKISLK----EIAGQAekLSRAyGLpldpnAHVAD-----LSVGERQRIEIVRALLQ-------NPRLIILDEP 162
Cdd:COG4559 96 VALGRAPHGSSAaqdrQIVREA--LALV-GL-----AHLAGrsyqtLSGGEQQRVQLARVLAQlwepvdgGPRWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRE--TPASLAR 229
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV-AQGTPEEvlTDELLER 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-218 |
4.04e-30 |
|
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: 123.64 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF-----------GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGvLAPTEGDIIWQGQPVSVG 70
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPSEARRL--GIGMVFQ--HFSLFEALTVAENIA---LSLDPKISLKEIAGQAEKLSRAYGLplDPNA-----HvaDLSV 138
Cdd:COG4172 353 SRRALRPLrrRMQVVFQdpFGSLSPRMTVGQIIAeglRVHGPGLSAAERRARVAEALEEVGL--DPAArhrypH--EFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 139 GERQRIEIVRALLQNPRLIILDEPTSVL--TPQeADKLfETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV-- 213
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALdvSVQ-AQIL-DLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVve 506
|
....*
gi 1609612952 214 TGACD 218
Cdd:COG4172 507 QGPTE 511
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-213 |
4.04e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 116.88 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 23 DLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARrlgIGMVFQHFSLFEALTVAENIALS 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP---VSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 103 LDPkiSLKEIAGQAEKL---SRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLE 179
Cdd:TIGR01277 95 LHP--GLKLNAEQQEKVvdaAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1609612952 180 KLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:TIGR01277 173 QLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-214 |
4.91e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.22 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF--GNFAA--CNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPV---SVGSPSE 74
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 75 ARRLGIGMVFQHFSLFEALTVAENIALSL-DPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQN 153
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLlIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRIcDRATVLRHGKVT 214
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-229 |
1.07e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 123.70 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 7 RKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlgIGMVFQH 86
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR--VGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 87 FSLFEALTVAENIAL-----SLDPkislKEIAGQAEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRL 156
Cdd:NF033858 348 FSLYGELTVRQNLELharlfHLPA----AEIAARVAEMLERFDL-----ADVADalpdsLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYIS-HRLEEVQRiCDRATVLRHGKVTgACDprreTPASLAR 229
Cdd:NF033858 419 LILDEPTSGVDPVARDMFWRLLIELSREDGVTIFIStHFMNEAER-CDRISLMHAGRVL-ASD----TPAALVA 486
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-219 |
1.14e-29 |
|
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: 122.22 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF-----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIwqgqpVSVGSP---- 72
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN-----VRVGDEwvdm 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SEARRLG-------IGMVFQHFSLFEALTVAENI--ALSLD-PK--------ISLKeIAGQAEKLSRAYgLPLDPNahva 134
Cdd:TIGR03269 353 TKPGPDGrgrakryIGILHQEYDLYPHRTVLDNLteAIGLElPDelarmkavITLK-MVGFDEEKAEEI-LDKYPD---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 135 DLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*.
gi 1609612952 214 TGACDP 219
Cdd:TIGR03269 507 VKIGDP 512
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-214 |
2.07e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.04 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFA--ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLg 79
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQH-FSLFEALTVAENIALSLD----PKISLKEIAGQAEKLSRAYGLPLDPNAHvadLSVGERQRIEIVRALLQNP 154
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLEnigvPREEMVERVDQALRQVGMEDFLNREPHR---LSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAEGR-SVLYISHRLEEVQRiCDRATVLRHGKVT 214
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-213 |
4.10e-29 |
|
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: 114.64 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 17 AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVA 96
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSlDPKISLKEIAgQAEKLSRAY----GLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTP 168
Cdd:cd03251 94 ENIAYG-RPGATREEVE-EAARAANAHefimELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 169 QEADKLFETLEKLkAEGRSVLYISHRLEEVQRIcDRATVLRHGKV 213
Cdd:cd03251 172 ESERLVQAALERL-MKNRTTFVIAHRLSTIENA-DRIVVLEDGKI 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
4.80e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQH-FSLFEALTVA 96
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK-KIGIIFQNpDNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSLDPK-ISLKEIAGQAEKLSRAYGLP--LDPNAHvaDLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:PRK13632 103 DDIAFGLENKkVPPKKMKDIIDDLAKKVGMEdyLDKEPQ--NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1609612952 174 LFETLEKLKAEG-RSVLYISHRLEEVQrICDRATVLRHGKVTGACDP 219
Cdd:PRK13632 181 IKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-213 |
4.93e-29 |
|
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: 114.51 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAlTVAENIAL 101
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-QVGVVLQENVLFNR-SIRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SlDPKISLKEIAgQAEKLSRAYG----LPLDPNAHV----ADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:cd03252 99 A-DPGMSMERVI-EAAKLAGAHDfiseLPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1609612952 174 LFETLEKLKAeGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03252 177 IMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-229 |
7.63e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE-ARRLgi 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDPkisLKEIAGQAEKLSRAY----GLpldpnAHVAD-----LSVGERQRIEIVRALL 151
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMGRAP---HGLSRAEDDALVAAAlaqvDL-----AHLAGrdypqLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 152 Q------NPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRE-- 222
Cdd:PRK13548 151 QlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV-ADGTPAEvl 229
|
....*..
gi 1609612952 223 TPASLAR 229
Cdd:PRK13548 230 TPETLRR 236
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-213 |
3.09e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 115.97 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGN------------------------FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPT 56
Cdd:COG4175 1 MPKIEVRNLYKIFGKrperalklldqgkskdeilektgqTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 57 EGDIIWQGQPVSVGSPSEARRL---GIGMVFQHFSLFEALTVAENIALSLdpkislkEIAG--QAEKLSRAY------GL 125
Cdd:COG4175 81 AGEVLIDGEDITKLSKKELRELrrkKMSMVFQHFALLPHRTVLENVAFGL-------EIQGvpKAERRERARealelvGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 126 PLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTP------QeaDKLFETLEKLKaegRSVLYISHRLEEVQ 199
Cdd:COG4175 154 AGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirremQ--DELLELQAKLK---KTIVFITHDLDEAL 228
|
250
....*....|....
gi 1609612952 200 RICDRATVLRHGKV 213
Cdd:COG4175 229 RLGDRIAIMKDGRI 242
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-229 |
4.98e-28 |
|
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: 117.54 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDPKislKEIAGQAEKLSRA----------YGLPLDPNAHVadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:COG4618 427 ARFGDAD---PEKVVAAAKLAGVhemilrlpdgYDTRIGEGGAR--LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 170 EADKLFETLEKLKAEGRSVLYISHRLeEVQRICDRATVLRHGKVTgACDPRRETPASLAR 229
Cdd:COG4618 502 GEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQ-AFGPRDEVLARLAR 559
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
5.73e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFA----ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvgSPSeAR 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPG-AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RlgiGMVFQHFSLFEALTVAENIALSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPR 155
Cdd:COG4525 78 R---GVVFQKDALLPWLNVLDNVAFGLRlRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEE 197
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEE 197
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-220 |
8.37e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.52 E-value: 8.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQH-FSLFEALTVAEN 98
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFET 177
Cdd:PRK13650 103 VAFGLENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1609612952 178 LEKLKAE-GRSVLYISHRLEEVQrICDRATVLRHGKVTGACDPR 220
Cdd:PRK13650 183 IKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPR 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-213 |
8.45e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 113.26 E-value: 8.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIiwqgqpvSVG--SPSE-----ARRlgIGMVF-QHFSL 89
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-------RVLgyVPFKrrkefARR--IGVVFgQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 90 FEALTVAENIAL-----SLDPKI------SLKEIAGQAEKLSRAyglpldpnahVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:COG4586 108 WWDLPAIDSFRLlkaiyRIPDAEykkrldELVELLDLGELLDTP----------VRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 159 LDEPT---SVLTpQEadKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG4586 178 LDEPTiglDVVS-KE--AIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-213 |
9.78e-28 |
|
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: 109.23 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 alsldpkislkeiagqaeklsrayglpldpnahvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLE 179
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....
gi 1609612952 180 KLKAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03246 141 ALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-208 |
1.30e-27 |
|
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: 116.23 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLF-GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGM 82
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEAlTVAENIALSlDPKISLKEIAGQAEK---------LSRAYGLPLDPNAhvADLSVGERQRIEIVRALLQN 153
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLA-RPDASDAEIREALERagldefvaaLPQGLDTPIGEGG--AGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKLkAEGRSVLYISHRLEEVQRiCDRATVL 208
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
1.49e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 110.74 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLdpkiSLKEIAGQAEKLSRAYGlpLDPNAH------VADLSVGERQRIEIVRALLQNP 154
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGG----FFAERDQFQERIKWVYE--LFPRLHerriqrAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-213 |
2.86e-27 |
|
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: 108.77 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLA--PTEGDIIWQGQPVSVGSPSEARRLGIG 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIAlSLDpkislkeiagqaeklsraYGlpldpnahvadLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLR-YVN------------------EG-----------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAEGRSVLYISHRleevQRIC-----DRATVLRHGKV 213
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHY----QRLLdyikpDRVHVLYDGRI 183
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-277 |
5.78e-27 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 111.05 E-value: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 34 LLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVgSPSEARrlGIGMVFQHFSLFEALTVAENIALSLD-PKISLKEI 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN-VPPHLR--HINMVFQSYALFPHMTVEENVAFGLKmRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 113 AGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYI 191
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 192 SHRLEEVQRICDRATVLRHGKVTGACDPRR--ETPASL--ARMMVGSDVASV--------SRATGEALGAPQIEVMGLSV 259
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEiyEEPANLfvARFIGEINVFEAtvierkseQVVLAGVEGRRCDIYTDVPV 237
|
250
....*....|....*...
gi 1609612952 260 APRTPFAVALKSISMTVR 277
Cdd:TIGR01187 238 EKDQPLHVVLRPEKIVIE 255
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-213 |
5.99e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.72 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLA---PTEGDIIWQGQPVS----VGSPSEA 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQregrLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 76 RRLGIGMVFQHFSLFEALTVAENI---ALSLDP---------KISLKEIAGQAekLSRAyGLPLDPNAHVADLSVGERQR 143
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVligALGSTPfwrtcfswfTREQKQRALQA--LTRV-GMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 144 IEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-213 |
7.39e-27 |
|
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: 108.06 E-value: 7.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 17 AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAlTVA 96
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSlDPKISLKEIAGQAEKLSRAYGLPLDPNA-------HVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:cd03245 96 DNITLG-APLADDERILRAAELAGVTDFVNKHPNGldlqigeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1609612952 170 EADKLFETLEKLkAEGRSVLYISHRLEEVQrICDRATVLRHGKV 213
Cdd:cd03245 175 SEERLKERLRQL-LGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-219 |
8.61e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.44 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENI--ALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-214 |
1.35e-26 |
|
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: 107.62 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 14 GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVgspsearrLGIGMVFQhfslfEAL 93
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 94 TVAENIALSL--------DPKISLKEIAGQAEkLSRAYGLPldpnahVADLSVGERQRIEIVRALLQNPRLIILDEPTSV 165
Cdd:cd03220 100 TGRENIYLNGrllglsrkEIDEKIDEIIEFSE-LGDFIDLP------VKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1609612952 166 LTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-463 |
1.38e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKS-TLVKMLFGVLAP----TEGDIIWQGQPVSVGS 71
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 72 PSEARRL---GIGMVFQH--FSLFEALTVAENIALSLDPKISLKEIAGQAEKLS-------RAYGLPLDPNAHvaDLSVG 139
Cdd:PRK15134 83 EQTLRGVrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNcldrvgiRQAAKRLTDYPH--QLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 140 ERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV--TGA 216
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCveQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 217 CDPRRETPA-SLARMMVGSDvasvsrATGEALGAPQ-----IEVMGLSVA---------PRTPFAVALKSISMTVRAGEV 281
Cdd:PRK15134 241 AATLFSAPThPYTQKLLNSE------PSGDPVPLPEpasplLDVEQLQVAfpirkgilkRTVDHNVVVKNISFTLRPGET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 282 LAIAGVAGNGQGELFDAL------SGEypvynndaIHLRGKPVGRIginGRRLMgagfVPeERHGHAAV---PGMSLSdn 352
Cdd:PRK15134 315 LGLVGESGSGKSTTGLALlrlinsQGE--------IWFDGQPLHNL---NRRQL----LP-VRHRIQVVfqdPNSSLN-- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 353 lllarARSDRKAFLTGGfLRiVRGSVIKAAAR--RISETMdvRKSGADPLA-----GSLSGGNLQKFIVGRELDRQPAVL 425
Cdd:PRK15134 377 -----PRLNVLQIIEEG-LR-VHQPTLSAAQReqQVIAVM--EEVGLDPETrhrypAEFSGGQRQRIAIARALILKPSLI 447
|
490 500 510
....*....|....*....|....*....|....*....
gi 1609612952 426 VVNQPTWGVDAGAASRIRQALVDL-AKAGSAVIVISQDL 463
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDL 486
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-220 |
1.90e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPS--EARRlGIGMVFQH--FSLFeAL 93
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRK-TVGIVFQNpdDQLF-AP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 94 TVAENIALS-LDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEAD 172
Cdd:PRK13639 95 TVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 173 KLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-214 |
3.23e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE-ARRLgiGM 82
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRL--AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSLDPKISL--------KEIAGQAEKLSRAYGLpldPNAHVADLSVGERQRIEIVRALLQNP 154
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLwgrlsaedNARVNQAMEQTRINHL---ADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
22-213 |
5.59e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 112.14 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAlTVAENIAL 101
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR-QMGVVLQENVLFSR-SIRDNIAL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SlDPKISLKEIAGQA---------EKLSRAYGLPLDpnAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEAD 172
Cdd:TIGR01846 554 C-NPGAPFEHVIHAAklagahdfiSELPQGYNTEVG--EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1609612952 173 KLFETLEKLKAeGRSVLYISHRLEEVqRICDRATVLRHGKV 213
Cdd:TIGR01846 631 LIMRNMREICR-GRTVIIIAHRLSTV-RACDRIIVLEKGQI 669
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-208 |
5.67e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 108.26 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR--RLGIGMVFQH--FSLFEAL 93
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 94 TVAENIALSLD---PKISLKEIAGQAEKLSRAYGL-PLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:PRK15079 116 TIGEIIAEPLRtyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1609612952 170 EADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVL 208
Cdd:PRK15079 196 IQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-204 |
6.45e-26 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 105.59 E-value: 6.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF-----GN--FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDII--WQGQPVSVGSP 72
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SE-----ARRLGIGMVFQHFSLF---EAL-TVAEN-IALSLDPKISLKEiagqAEKLSRAYGLP-----LDPnahvADLS 137
Cdd:COG4778 83 SPreilaLRRRTIGYVSQFLRVIprvSALdVVAEPlLERGVDREEARAR----ARELLARLNLPerlwdLPP----ATFS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 138 VGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDR 204
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-213 |
7.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR-RLGIGMVFQH--FSLFEAlT 94
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlRESVGMVFQDpdNQLFSA-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 95 VAENIAL-SLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:PRK13636 100 VYQDVSFgAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1609612952 174 LFETL-EKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK13636 180 IMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-214 |
8.37e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.49 E-value: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDiiwqgqpVSVGS--PSEARR---LGIGMVF-QHFSLFE 91
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE-------VRVAGlvPWKRRKkflRRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 ALTVAENIAL-----SLDPKISLKEIAGQAEKLSRAYGLpldpNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVL 166
Cdd:cd03267 109 DLPVIDSFYLlaaiyDLPPARFKKRLDELSELLDLEELL----DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1609612952 167 TPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:cd03267 185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-213 |
1.04e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQG-----QPVSVgspSEARRlGIGMVFQH--FSLF 90
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKL---SDIRK-KVGLVFQYpeYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 91 EAlTVAENIALSldPK---ISLKEIAGQAEKLSRAYGLPLDPNAHVA--DLSVGERQRIEIVRALLQNPRLIILDEPTSV 165
Cdd:PRK13637 98 EE-TIEKDIAFG--PInlgLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1609612952 166 LTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-213 |
1.10e-25 |
|
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: 105.39 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAlTVAENI 99
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR-AIGVVPQDTVLFND-TIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSlDPKISLKEI---AGQAEKLSRAYGLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEAD 172
Cdd:cd03253 96 RYG-RPDATDEEVieaAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1609612952 173 KLFETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03253 175 EIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-250 |
1.12e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.97 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 24 LDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQG---QPVSVGSPSEARRLGIGMVFQHFSLFEALTVAENIA 100
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLD-PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLE 179
Cdd:PRK10070 129 FGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 180 KLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV--TGACDPRRETPAS--LARMMVGSDVASVSRATGEALGAP 250
Cdd:PRK10070 209 KLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVvqVGTPDEILNNPANdyVRTFFRGVDISQVFSAKDIARRTP 284
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-204 |
2.29e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKML--FGVLAP---TEGDIIWQGQpvSVGSPS--- 73
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGH--NIYSPRtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 74 -EARRlGIGMVFQHFSLFeALTVAENIALSLDPK-ISLKEIAGQA-EKLSRAYGLPLDPNAHVAD----LSVGERQRIEI 146
Cdd:PRK14239 82 vDLRK-EIGMVFQQPNPF-PMSIYENVVYGLRLKgIKDKQVLDEAvEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 147 VRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKaEGRSVLYISHRLEEVQRICDR 204
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK-DDYTMLLVTRSMQQASRISDR 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-213 |
2.76e-25 |
|
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: 109.42 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFG--NFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGI 80
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR-QV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEAlTVAENIALSLDPKISLKEI---AGQAEKLSRAYGLPLDPNAHVAD----LSVGERQRIEIVRALLQN 153
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAEIeraLAAAYAQDFVDKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKLKaEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-213 |
3.75e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.65 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEArrlGI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLD-PKISLKEIAGQ----AEKLSRAYGLPLDPNAhvadLSVGERQRIEIVRALLQNPR 155
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKlAGAKKEEINQRvnqvAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 156 LIILDEPTSVLTPQ-------EADKLFETLeklkaeGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11000 154 VFLLDEPLSNLDAAlrvqmriEISRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-219 |
5.32e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.90 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR------- 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 -----RLGIGMVFQHFSLFEALTVAENIALSLDPKISLKEIAGQAEKLSRAYGLPLDPNA---HVADLSVGERQRIEIVR 148
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqgkYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 149 ALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-283 |
6.74e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.46 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVAD-----LSVGERQRIEIVRALLQNPR 155
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADrpvtsLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 156 LIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRE-TPASL-----AR 229
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVlTADTLraafdAR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 230 MMVGSDVASVS--------RATGEALGAPQIEVMGlSVAPRTPFAVALKSISMTVRAGEVLA 283
Cdd:PRK09536 240 TAVGTDPATGAptvtplpdPDRTEAAADTRVHVVG-GGQPAARAVSRLVAAGASVSVGPVPE 300
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-193 |
8.39e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 103.34 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGS-------PSE 74
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 75 AR-----RLGIGMVFQHFSLFEALTVAENIALSldP----KISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIE 145
Cdd:COG4598 87 RRqlqriRTRLGMVFQSFNLWSHMTVLENVIEA--PvhvlGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 146 IVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISH 193
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-213 |
1.37e-24 |
|
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: 101.78 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFeALTVAENIA 100
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLF-ARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLD--PKISLKEIAGQAEKLSRAYGLPLDPNAHV----ADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTpQEADKL 174
Cdd:cd03248 110 YGLQscSFECVKEAAQKAHAHSFISELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD-AESEQQ 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1609612952 175 FETLEKLKAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-219 |
2.47e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.39 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE-ARRLGIGMVFQ--HFSLFEAlTVAE 97
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVATVFQdpEQQIFYT-DIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALSL-DPKISLKEIA---GQAEKLSRAYGLPLDPnahVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:PRK13638 98 DIAFSLrNLGVPEAEITrrvDEALTLVDAQHFRHQP---IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1609612952 174 LFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
3.50e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGN-----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRL 78
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIGMVFQHFSL--FEALTVAENIAL--------SLDPKISLKEIAGQAEKLSRAyGLPLD--PNAHVADLSVGERQRIEI 146
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLALayrrgkrrGLRRGLTKKRRELFRELLATL-GLGLEnrLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 147 VRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGR-SVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-213 |
3.87e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 6 VRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGqpvSVGSPsearrLGIGMVFQ 85
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSAL-----LELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 HfslfeALTVAENIALS----------LDPKIslKEIAGQAEkLSRAYGLPldpnahVADLSVGERqrieiVR-----AL 150
Cdd:COG1134 101 P-----ELTGRENIYLNgrllglsrkeIDEKF--DEIVEFAE-LGDFIDQP------VKTYSSGMR-----ARlafavAT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 151 LQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-199 |
4.38e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAP---TEGDIIWQGQPVSvGSPSEARRlgIGMVFQHFSLFEALTVAE 97
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT-ALPAEQRR--IGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALSLDPKISLKEIAGQAEK-LSRAyGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFE 176
Cdd:COG4136 96 NLAFALPPTIGRAQRRARVEQaLEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|....
gi 1609612952 177 -TLEKLKAEGRSVLYISHRLEEVQ 199
Cdd:COG4136 175 fVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-213 |
4.93e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQH-FSLFEALTVAEN 98
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK-HIGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLD----PKISLKEIAGQA----EKLSRAyglPLDPNAhvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:PRK13648 105 VAFGLEnhavPYDEMHRRVSEAlkqvDMLERA---DYEPNA----LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1609612952 171 ADKLFETLEKLKAEGR-SVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-213 |
5.16e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFeALTVAENIA 100
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR-QVALVGQEPVLF-SGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLD--PKISLKEIAGQAEKLSRAYGLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKL 174
Cdd:TIGR00958 577 YGLTdtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190
....*....|....*....|....*....|....*....
gi 1609612952 175 FETlekLKAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-213 |
6.67e-24 |
|
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: 99.88 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENi 99
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-ISIIPQDPVLFSG-TIRSN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 alsLDP--------------KISLKE-IAGQAEKLsrayglpldpNAHVAD----LSVGERQRIEIVRALLQNPRLIILD 160
Cdd:cd03244 98 ---LDPfgeysdeelwqaleRVGLKEfVESLPGGL----------DTVVEEggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 161 EPTSVLTPQEADKLFETL-EKLKaeGRSVLYISHRLEEVqrI-CDRATVLRHGKV 213
Cdd:cd03244 165 EATASVDPETDALIQKTIrEAFK--DCTVLTIAHRLDTI--IdSDRILVLDKGRV 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-214 |
7.27e-24 |
|
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: 98.54 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvgSPSEARRLGIGMVFQHFSLFEAlTVAENIa 100
Cdd:cd03247 20 NLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLISVLNQRPYLFDT-TLRNNL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 lsldpkislkeiagqaeklsrayGLPLdpnahvadlSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEK 180
Cdd:cd03247 96 -----------------------GRRF---------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE 143
|
170 180 190
....*....|....*....|....*....|....
gi 1609612952 181 LkAEGRSVLYISHRLEEVQRIcDRATVLRHGKVT 214
Cdd:cd03247 144 V-LKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-266 |
8.86e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 101.91 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAP----TEGDIIWQGQPVSVGSP 72
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SEARRL---GIGMVFQH--FSLFEALTVAENIALSLdPKISLKEIAGQAEKLSRAYGLPL-------DP----NAHVADL 136
Cdd:COG4170 81 RERRKIigrEIAMIFQEpsSCLDPSAKIGDQLIEAI-PSWTFKGKWWQRFKWRKKRAIELlhrvgikDHkdimNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 137 SVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKV-- 213
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTve 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 214 TGACDPRRETP-----ASLARMM--VGSDVASVSRATGEALGAPQIEVM--GLSVAPRTPFA 266
Cdd:COG4170 240 SGPTEQILKSPhhpytKALLRSMpdFRQPLPHKSRLNTLPGSIPPLQHLpiGCRLGPRCPYA 301
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-220 |
1.24e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQH--FSLFeALTV 95
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQDpdDQVF-SSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 96 AENIA-----LSLDPKiSLKEIAGQAEKLSRAYGLPLDPNAHvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:PRK13647 98 WDDVAfgpvnMGLDKD-EVERRVEEALKAVRMWDFRDKPPYH---LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1609612952 171 ADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-220 |
1.81e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.24 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 16 FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIiwQGQPVSVGSPSEAR-----RLGIGMVFQ--HFS 88
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV--TVDDITITHKTKDKyirpvRKRIGMVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 89 LFEAlTVAENIALSldPK---ISLKEIAGQAEKLSRAYGLPLDPNAHVA-DLSVGERQRIEIVRALLQNPRLIILDEPTS 164
Cdd:PRK13646 98 LFED-TVEREIIFG--PKnfkMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 165 VLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-213 |
1.83e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQ---GQPVSVGSPSEARR 77
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrdGQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 78 lgigmvfQHFSLFEALTVAENIALSLDPKISlkeiAGQ--AEKL----SRAYG------------LPLDPnAHVADL--- 136
Cdd:PRK11701 84 -------RRLLRTEWGFVHQHPRDGLRMQVS----AGGniGERLmavgARHYGdiratagdwlerVEIDA-ARIDDLptt 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 137 -SVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11701 152 fSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-219 |
2.69e-23 |
|
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: 104.71 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFA--ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvgSPSEARRL 78
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIGMVFQHFSLFEALTVAENIALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKLKAeGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-229 |
3.40e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 98.37 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGvLAPTEGDIIWQGQPVSVGSPSEARRLGiGMVFQHFSLFEALTVAENIA 100
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHR-AYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQ-----NP--RLIILDEPTSVL-TPQEA- 171
Cdd:COG4138 92 LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSLdVAQQAa 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 172 -DKLfetLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRE--TPASLAR 229
Cdd:COG4138 172 lDRL---LRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV-ASGETAEvmTPENLSE 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-213 |
4.54e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.04 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF----GNFA------ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVG 70
Cdd:PRK11308 3 QPLLQAIDLKKHYpvkrGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPSE--ARRLGIGMVFQ--HFSLFEALTVAENIA--LSLDPKISLKEIAGQAEKLSRAYGLP---LDPNAHVadLSVGER 141
Cdd:PRK11308 83 DPEAqkLLRQKIQIVFQnpYGSLNPRKKVGQILEepLLINTSLSAAERREKALAMMAKVGLRpehYDRYPHM--FSGGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 142 QRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-225 |
8.33e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 8.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF-----------GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLApTEGDIIWQGQPVSVG 70
Cdd:PRK15134 274 PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPSE--ARRLGIGMVFQ--HFSLFEALTVAENIALSLD---PKISLKEIAGQAEKLSRAYGLplDPNA---HVADLSVGE 140
Cdd:PRK15134 353 NRRQllPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhqPTLSAAQREQQVIAVMEEVGL--DPETrhrYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 141 RQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGR-SVLYISHRLEEVQRICDRATVLRHGKVT--GAC 217
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVeqGDC 510
|
....*...
gi 1609612952 218 DPRRETPA 225
Cdd:PRK15134 511 ERVFAAPQ 518
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
8.59e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGN-----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDI----IWQGQPVSVGSPS 73
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 74 ------------EARRLgIGMVFQ--HFSLFEAlTVAENIalSLDPkISLKEIAGQAEKLSRAY----GLP---LDPNAH 132
Cdd:PRK13631 101 tnpyskkiknfkELRRR-VSMVFQfpEYQLFKD-TIEKDI--MFGP-VALGVKKSEAKKLAKFYlnkmGLDdsyLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 133 vaDLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:PRK13631 176 --GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
....*..
gi 1609612952 213 VTGACDP 219
Cdd:PRK13631 254 ILKTGTP 260
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-213 |
9.53e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.85 E-value: 9.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLaPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENIAL 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SlDPKISLKEI------AGQAEKLSR-AYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKL 174
Cdd:PRK11174 446 G-NPDASDEQLqqalenAWVSEFLPLlPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190
....*....|....*....|....*....|....*....
gi 1609612952 175 FETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:PRK11174 525 MQALNAA-SRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-206 |
1.08e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIiwqgqpvsvgspSEARRLGIGMVFQHFSLFEAL--TVAEN 98
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPDSLplTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLDPKISLKEIAGQAEKLS-----RAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:NF040873 78 VAMGRWARRGLWRRLTRDDRAAvddalERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|...
gi 1609612952 174 LFETLEKLKAEGRSVLYISHRLEEVQRICDRAT 206
Cdd:NF040873 158 IIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-195 |
1.13e-22 |
|
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: 101.28 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 14 GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAl 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 94 TVAENIALSlDPKISLKEIAGQAEKL-------SRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVL 166
Cdd:TIGR02868 424 TVRENLRLA-RPDATDEELWAALERVgladwlrALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180 190
....*....|....*....|....*....|
gi 1609612952 167 TPQEADKLFETLekLKA-EGRSVLYISHRL 195
Cdd:TIGR02868 503 DAETADELLEDL--LAAlSGRTVVLITHHL 530
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-213 |
1.32e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGqpVSVGSPS---EARRLgIGMVFQH-FSLFEAL 93
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSklqGIRKL-VGIVFQNpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 94 TVAENIA-----LSLDPKislkEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTP 168
Cdd:PRK13644 94 TVEEDLAfgpenLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 169 QEADKLFETLEKLKAEGRSVLYISHRLEEVQrICDRATVLRHGKV 213
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKI 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
1.54e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF-GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLg 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQH-----FSlfeaLTVAENIA-----LSLDPkislKEIAGQAEKLSRAYGLP--LDPNAHvaDLSVGERQRIEIV 147
Cdd:PRK13652 80 VGLVFQNpddqiFS----PTVEQDIAfgpinLGLDE----ETVAHRVSSALHMLGLEelRDRVPH--HLSGGEKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 148 RALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTG 215
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-213 |
1.89e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 6 VRKLTKLFGN-----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIW-------QGQPVS----- 68
Cdd:PRK13651 5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEkekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 69 ---VGSPSEARRLG--------IGMVFQ--HFSLFEAlTVAENIALSldpKISLKEIAGQAEKLSRAY----GLPLD--- 128
Cdd:PRK13651 85 eklVIQKTRFKKIKkikeirrrVGVVFQfaEYQLFEQ-TIEKDIIFG---PVSMGVSKEEAKKRAAKYielvGLDESylq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 129 --PnahvADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRAT 206
Cdd:PRK13651 161 rsP----FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
....*..
gi 1609612952 207 VLRHGKV 213
Cdd:PRK13651 237 FFKDGKI 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-213 |
1.93e-22 |
|
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: 100.66 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAlTVAENI 99
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA-AIGIVPQDTVLFND-TIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSlDPKISLKEIAgQAEKLsrayglpldpnAHVAD-------------------LSVGERQRIEIVRALLQNPRLIILD 160
Cdd:COG5265 453 AYG-RPDASEEEVE-AAARA-----------AQIHDfieslpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 161 EPTSVL-TPQEADKLfETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:COG5265 520 EATSALdSRTERAIQ-AALREV-ARGRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-214 |
3.05e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWqGQPVSVGspsearrlgig 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIG----------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 mVF-QHFSLF-EALTVAENIAlSLDPKISLKEIAGQAEKL--SRAyglplDPNAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:COG0488 382 -YFdQHQEELdPDKTVLDELR-DGAPGGTEQEVRGYLGRFlfSGD-----DAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 158 ILDEPTSVLTPqeadklfETLEKLKA-----EGrSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:COG0488 455 LLDEPTNHLDI-------ETLEALEEalddfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-213 |
4.93e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.77 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKMLFGVLAP--TEGDIIWQGQPVsvgSPSEARRLgIGMVFQHFSLFEALTVAENIALSldpk 106
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL---DKRSFRKI-IGYVPQDDILHPTLTVRETLMFA---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 107 islkeiagqaeklsrayglpldpnAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGR 186
Cdd:cd03213 107 ------------------------AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR 162
|
170 180
....*....|....*....|....*...
gi 1609612952 187 SVLYISHRL-EEVQRICDRATVLRHGKV 213
Cdd:cd03213 163 TIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-276 |
5.16e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgSPSEARRLGIGMV 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLD----PKISLKEIAGQAEKLSRAYGLpldPNAHVADLSVGERQRIEIVRALLQNPRLIIL 159
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKmlgvPKEERKQRVKEALELVDLAGF---EDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 160 DEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVT--GACDPRRETPAS--LARMMvGS 234
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMqiGSPQELYRQPASrfMASFM-GD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1609612952 235 dvASVSRATgeaLGAPQIEVMGLSVAPRTPFAVALKSISMTV 276
Cdd:PRK11432 240 --ANIFPAT---LSGDYVDIYGYRLPRPAAFAFNLPDGECTV 276
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-204 |
7.97e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.72 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVK----MLfgVLAP---TEGDIIWQGQPVSVGS--P 72
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrMN--DLIPgarVEGEILLDGEDIYDPDvdV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SEARRLgIGMVFQHFSLFeALTVAENIALSldPKI----SLKEIAGQAEKLSRAYGLP------LDPNAhvADLSVGERQ 142
Cdd:COG1117 88 VELRRR-VGMVFQKPNPF-PKSIYDNVAYG--LRLhgikSKSELDEIVEESLRKAALWdevkdrLKKSA--LGLSGGQQQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 143 RIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEgRSVLYISHRLEEVQRICDR 204
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDY 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-211 |
8.81e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.01 E-value: 8.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPsEARRLGIG 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFeALTVAENIAL-------SLDPKISLKEIAgqaeklsrAYGLPLDP-NAHVADLSVGERQRIEIVRALLQN 153
Cdd:PRK10247 85 YCAQTPTLF-GDTVYDNLIFpwqirnqQPDPAIFLDDLE--------RFALPDTIlTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 154 PRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHG 211
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-228 |
1.31e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLsVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgspSEARRlGIG 81
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEARE-DTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIALSLdpKISLKEIAGQAeklSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGL--KGQWRDAALQA---LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 162 P---TSVLTPQEADKLFETLekLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVtgACD-------PRRETPASLA 228
Cdd:PRK11247 160 PlgaLDALTRIEMQDLIESL--WQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI--GLDltvdlprPRRRGSARLA 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-197 |
1.32e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.00 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvgSPSEARrlgiGM 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSLD----PKISLKEIAGQAEKLsraYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQlagvEKMQRLEIAHQMLKK---VGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEE 197
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEE 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-213 |
1.40e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL-----APTEGDIIWQGQPVSVG--SPSEAR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPdvDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RlGIGMVFQHFSLFEALTVAENIALSL------DPKISLKEIAGQAEKLSRAYGLPLDP-NAHVADLSVGERQRIEIVRA 149
Cdd:PRK14267 85 R-EVGMVFQYPNPFPHLTIYDNVAIGVklnglvKSKKELDERVEWALKKAALWDEVKDRlNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 150 LLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLyISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVL-VTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-246 |
1.71e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.72 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFeALTVAENIALSlDPKIS 108
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR-NIAVVFQDAGLF-NRSIEDNIRVG-RPDAT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 109 LKEIAGQAEK-------LSRAYGLpldpNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFET 177
Cdd:PRK13657 438 DEEMRAAAERaqahdfiERKPDGY----DTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 178 LEKLKaEGRSVLYISHRLEEVqRICDRATVLRHGKV--TGACD---PRRETPASLAR---MMVGSDVASVSRATGEA 246
Cdd:PRK13657 514 LDELM-KGRTTFIIAHRLSTV-RNADRILVFDNGRVveSGSFDelvARGGRFAALLRaqgMLQEDERRKQPAAEGAN 588
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-201 |
1.71e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 97.80 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPseaRRLG--IGMVFQHFSLFEAlTVAE 97
Cdd:TIGR01842 335 RGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR---ETFGkhIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALSLDPKISLKEIAgqAEKLSRAYGLPLD-PNAHVAD-------LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:TIGR01842 411 NIARFGENADPEKIIE--AAKLAGVHELILRlPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190
....*....|....*....|....*....|....*
gi 1609612952 170 EADKLFETLEKLKAEGRSVLYISHR---LEEVQRI 201
Cdd:TIGR01842 489 GEQALANAIKALKARGITVVVITHRpslLGCVDKI 523
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-213 |
1.72e-21 |
|
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: 98.27 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENIAL 101
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INYLPQEPYIFSG-SILENLLL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SLDPKIS---------LKEIAGQAEKLSRAYGLPLdpNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEAD 172
Cdd:TIGR01193 571 GAKENVSqdeiwaaceIAEIKDDIENMPLGYQTEL--SEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1609612952 173 KLFETLEKLKAegRSVLYISHRLEEVQRIcDRATVLRHGKV 213
Cdd:TIGR01193 649 KIVNNLLNLQD--KTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-213 |
1.79e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.82 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL-----APTEGDIIWQGQPVSVGSPSEA 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 76 RRLgIGMVFQHFSLFEALTVAENIALSL------DPKISLKEIAGQA-EKLSRAYGLPLDPNAHVADLSVGERQRIEIVR 148
Cdd:PRK14247 81 RRR-VQMVFQIPNPIPNLSIFENVALGLklnrlvKSKKELQERVRWAlEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 149 ALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEgRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-210 |
4.44e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.48 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpvsvgspsearrLGI 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDPKISLKEIAGQAEKLSRAYGLpldpNAHVADLSVGERQRIEIVRALLQNPRLIILD 160
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLI----DAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 161 EPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRH 210
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-215 |
5.45e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 92.40 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLA--PTEGDIIWQGQPVSVGSPSEARRLG 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQH------FSLFEALTVAENIAL------SLDPkISLKEIAgqAEKLSRaygLPLDP---NAHVAD-LSVGERQR 143
Cdd:CHL00131 86 IFLAFQYpieipgVSNADFLRLAYNSKRkfqglpELDP-LEFLEII--NEKLKL---VGMDPsflSRNVNEgFSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 144 IEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHrleeVQR-----ICDRATVLRHGKV--TG 215
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH----YQRlldyiKPDYVHVMQNGKIikTG 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-213 |
5.47e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR-----RL 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKairelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 79 GIGMVFQHFSLFEALTVAENI------ALSLDPKISLKeiagQAEK-LSRaygLPLDPNAHV--ADLSVGERQRIEIVRA 149
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLieapcrVLGLSKDQALA----RAEKlLER---LRLKPYADRfpLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 150 LLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-220 |
1.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.07 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIGMVFQH-FSLFEALTVA 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIA-----LSLDPkislKEIAGQAEKLSRAYGLpLDPNAHVAD-LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:PRK13633 105 EDVAfgpenLGIPP----EEIRERVDESLKKVGM-YEYRRHAPHlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 171 ADKLFETLEKL-KAEGRSVLYISHRLEEVQRiCDRATVLRHGKVTGACDPR 220
Cdd:PRK13633 180 RREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPK 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-214 |
1.76e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 6 VRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQgqpvsvgspseaRRLGIGMVFQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 HFSLFEALTVAENI---------------ALSLDPKISLKEIAGQAEKLSR-----AY-------------GLP-LDPNA 131
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaelraleaeleELEAKLAEPDEDLERLAELQEEfealgGWeaearaeeilsglGFPeEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 132 HVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLtpqeaDklFET---LEK-LKAEGRSVLYISH-R--LEEV-QRICD 203
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHL-----D--LESiewLEEfLKNYPGTVLVVSHdRyfLDRVaTRILE 221
|
250
....*....|.
gi 1609612952 204 ratvLRHGKVT 214
Cdd:COG0488 222 ----LDRGKLT 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-214 |
3.34e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.86 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVS-----VGSPSEARRlgIGMVFQHFSLFEALTVA 96
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgICLPPEKRR--IGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSLDPKIslkeiAGQAEKLSRAYGL-PLdPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLF 175
Cdd:PRK11144 95 GNLRYGMAKSM-----VAQFDKIVALLGIePL-LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1609612952 176 ETLEKLKAEGR-SVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:PRK11144 169 PYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-220 |
3.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.63 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 17 AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGD---IIWQGQPVSVGSPSEARRlGIGMVFQH-FSLFEA 92
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE-KVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 93 LTVAENIALSLD----PKISLKEIAGQAekLSRAyGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTP 168
Cdd:PRK13640 100 ATVGDDVAFGLEnravPRPEMIKIVRDV--LADV-GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 169 QEADKLFETLEKLKAE-GRSVLYISHRLEEVQrICDRATVLRHGKVTGACDPR 220
Cdd:PRK13640 177 AGKEQILKLIRKLKKKnNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-216 |
3.84e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 13 FGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR--RLGIGMVFQHFSLF 90
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 91 EALTVAENIALSLDpkislkeIAGQA-EKLSRAYGLPLD-------PNAHVADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:PRK10908 92 MDRTVYDNVAIPLI-------IAGASgDDIRRRVSAALDkvglldkAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGA 216
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-229 |
7.74e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 26 IARGEIHALLGENGAGKSTLVKMLFGVLaPTEGDIIWQGQPVSVGSPSE-ARRLGIgMVFQHFSLFeALTVAENIALSLD 104
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElARHRAY-LSQQQTPPF-AMPVFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 105 PKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQ-----NP--RLIILDEPTSVL-TPQEA--DKL 174
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLdVAQQAalDRL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 175 fetLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRE--TPASLAR 229
Cdd:PRK03695 176 ---LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL-ASGRRDEvlTPENLAQ 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-220 |
8.81e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR---RLGIGMVFQhFS---LFEAlTV 95
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkklRKKVSLVFQ-FPeaqLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 96 AENIALSldPK---ISLKEIAGQAEKLSRAYGLPLDPNAHVA-DLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PRK13641 104 LKDVEFG--PKnfgFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1609612952 172 DKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-213 |
1.00e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.08 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLF----GNF-----AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPS 73
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 74 eARRLGIGMVFQHFSlfEALTVAENIALSLDPKISLK-EIAGQA------EKLSRAYGLPLDPNAHVADLSVGERQRIEI 146
Cdd:PRK15112 84 -YRSQRIRMIFQDPS--TSLNPRQRISQILDFPLRLNtDLEPEQrekqiiETLRQVGLLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 147 VRALLQNPRLIILDEPTSVLTPQEADKLFE-TLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINlMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-213 |
1.22e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.91 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MP---LLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSP- 72
Cdd:PRK10584 1 MPaenIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 --SEARRLGIGMVFQHFSLFEALTVAENIAL-SLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRA 149
Cdd:PRK10584 81 arAKLRAKHVGFVFQSFMLIPTLNALENVELpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 150 LLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-233 |
1.77e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 8 KLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVS-VGSPSEARRlgIGMVFQH 86
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVARR--IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 87 FSLFEALTVAENIALSLDPKISL-----KEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:PRK10253 90 ATTPGDITVQELVARGRYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRETPASLARMMVG 233
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-219 |
2.46e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.92 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPV-SVGSPSEARRlgIGMVFQHFSLFEALTVAENIALSLDPKI 107
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAFARK--VAYLPQQLPAAEGMTVRELVAIGRYPWH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 108 SLKEIAGQA--EKLSRAYGL-PLDPNAH--VADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLK 182
Cdd:PRK10575 115 GALGRFGAAdrEKVEEAISLvGLKPLAHrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLS 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 1609612952 183 AE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK10575 195 QErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-213 |
3.38e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAlTVAE 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN-QVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALSLDPKISLKEIAgQAEKLSRA--------YGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:PRK11176 436 NIAYARTEQYSREQIE-EAARMAYAmdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1609612952 170 EADKLFETLEKLKAEgRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:PRK11176 515 SERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-236 |
3.78e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.46 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQH-FSLFEALTVAEN 98
Cdd:PRK13642 24 NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-KIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFET 177
Cdd:PRK13642 103 VAFGMENQgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 178 LEKLKAEGR-SVLYISHRLEEVQRiCDRATVLRHGKVTGACDPRRETPASLARMMVGSDV 236
Cdd:PRK13642 183 IHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDV 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
267-481 |
5.37e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 85.89 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGvaGNGQGE--LFDALSGEYPVYNNDaIHLRGKPVGRIGINGRRLMGagFVPEErhgHAAV 344
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLG--PNGAGKttTIRMLLGLLRPTSGE-VRVLGEDVARDPAEVRRRIG--YVPQE---PALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 345 PGMSLSDNL-LLARARSdrkafltggflriVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQPA 423
Cdd:COG1131 86 PDLTVRENLrFFARLYG-------------LPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 424 VLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
5.92e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.00 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVG-SPSEARRL--GIGMVFQ---HfSLFEAlTV 95
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKLKPLrkKVGIVFQfpeH-QLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 96 AENIALSldPK---ISLKEIAGQAEKLSRAYGLPLDPNAHVA-DLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PRK13634 104 EKDICFG--PMnfgVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1609612952 172 DKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:PRK13634 182 KEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-203 |
1.17e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKML--FGVLAPT---EGDIIWQGQPVSVG--SPSEA 75
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPdvDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 76 RRLgIGMVFQHFSLFEAlTVAENIALSldPKI-------------SLKEIAGQAE---KLsRAYGLpldpnahvaDLSVG 139
Cdd:PRK14243 90 RRR-IGMVFQKPNPFPK-SIYDNIAYG--ARIngykgdmdelverSLRQAALWDEvkdKL-KQSGL---------SLSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 140 ERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKaEGRSVLYISHRLEEVQRICD 203
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-213 |
1.69e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 84.52 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 24 LDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGspsearRLGIGMVFQ--HFSLFEALTVAENIAL 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG------WRHIGYVPQrhEFAWDFPISVAHTVMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVAD-----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFE 176
Cdd:TIGR03771 75 GRTGHIGWLRRPCVADFAAVRDALRRVGLTELADrpvgeLSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1609612952 177 TLEKLKAEGRSVLYISHRLEEVQRICDRaTVLRHGKV 213
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRV 190
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-166 |
1.81e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF-GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEaRrlG 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-R--D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLdpKI---SLKEIAGQAEKLSRAYGLP--LD--PNAhvadLSVGERQRIEIVRALLQ 152
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGL--KIrgmPKAEIEERVAEAARILELEplLDrkPRE----LSGGQRQRVAMGRAIVR 151
|
170
....*....|....
gi 1609612952 153 NPRLIILDEPTSVL 166
Cdd:PRK11650 152 EPAVFLFDEPLSNL 165
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-213 |
2.09e-18 |
|
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: 84.24 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL---APTEGDIIWQGQPVSvgsPSEARRLgIGMVFQHFSLFEALTVA 96
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRK---PDQFQKC-VAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSldPKISLKEIAGQAEKLSRA--YGLPLDPNAHVAD-----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:cd03234 100 ETLTYT--AILRLPRKSSDAIRKKRVedVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 170 EADKLFETLEKLKAEGRSVLYISHR-LEEVQRICDRATVLRHGKV 213
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-211 |
2.39e-18 |
|
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: 88.92 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFA--ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsVGSPSEARRlGI 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQ-NM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEALTVAENIALSLDPK-ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIIL 159
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRgVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 160 DEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHG 211
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-212 |
2.47e-18 |
|
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: 81.73 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWqGQPVSVGspsearrlgigmv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVKIG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 fqhfslfealtvaenialsldpkislkeiagqaeklsrayglpldpnaHVADLSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:cd03221 67 ------------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1609612952 164 SVLTPQEADKLFETLEKLKaegRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:cd03221 99 NHLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-219 |
2.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIiwQGQPVSVGSPSEAR-----RLGIGMVFQ--HFSLFEAlT 94
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQKeikpvRKKVGVVFQfpESQLFEE-T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 95 VAENIALSldPK---ISLKEIAGQAEKLSRAYGLPLDP-NAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:PRK13643 102 VLKDVAFG--PQnfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1609612952 171 ADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-213 |
3.57e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPS---EARRlG 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRK-R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 80 IGMVFQHFSLFEALTVAENIALSLDPKISLKEIAGQAEKLSR--AYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKleAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-212 |
4.04e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.55 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAP---TEGDIIWQGQPVSVGSPS 73
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 74 EARRL---GIGMVFQH--FSLFEALTVAENIA--LSLDPKISLKEIAGQAEKLSRAYGLP-------LDPNahvaDLSVG 139
Cdd:PRK09473 90 ELNKLraeQISMIFQDpmTSLNPYMRVGEQLMevLMLHKGMSKAEAFEESVRMLDAVKMPearkrmkMYPH----EFSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 140 ERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-219 |
4.49e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 16 FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQ--PVSVGSPSEARRL--GIGMVFQ--HFSL 89
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLKKIKEVKRLrkEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 90 FEAlTVAENIALS-LDPKISLKEIAGQAEKLSRAYGLPLDPNAHVA-DLSVGERQRIEIVRALLQNPRLIILDEPTSVLT 167
Cdd:PRK13645 104 FQE-TIEKDIAFGpVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 168 PQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDP 219
Cdd:PRK13645 183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-213 |
4.62e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.19 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 14 GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVFQHFSLFEAl 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ-AISVVSQRVHLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 94 TVAENIALSlDPKIS---LKEIAGQA--EKL-SRAYGLpldpNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:PRK11160 429 TLRDNLLLA-APNASdeaLIEVLQQVglEKLlEDDKGL----NAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 164 SVLTPQEADKLFETLEKLkAEGRSVLYISHRL---EEVQRICdratVLRHGKV 213
Cdd:PRK11160 504 EGLDAETERQILELLAEH-AQNKTVLMITHRLtglEQFDRIC----VMDNGQI 551
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-220 |
1.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.26 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 17 AACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSE---ARRLGIGMVFQ--HFSLFE 91
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 AlTVAENIALSldPK---ISLKEiagqAEKLSRA----YGLPLDP-NAHVADLSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:PRK13649 101 E-TVLKDVAFG--PQnfgVSQEE----AEALAREklalVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 164 SVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTGACDPR 220
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-196 |
1.47e-17 |
|
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: 81.61 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 15 NFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR---RLGIGMVFQHFSLFE 91
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 AlTVAENI----------------ALSLDPKISLKEIAGQAEKLSRAyglpldpnahvADLSVGERQRIEIVRALLQNPR 155
Cdd:cd03290 93 A-TVEENItfgspfnkqrykavtdACSLQPDIDLLPFGDQTEIGERG-----------INLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 156 LIILDEPTSVLTPQEADKLFET--LEKLKAEGRSVLYISHRLE 196
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
268-480 |
1.64e-17 |
|
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: 81.33 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGvaGNGQGE--LFDALSGEYPVYNNdAIHLRGKPVGRIGINGRRLMGAGFVPEERhghAAVP 345
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLG--RNGAGKttLLKTIMGLLPPRSG-SIRFDGRDITGLPPHERARAGIGYVPEGR---RIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 346 GMSLSDNLLLARARSDRKAFltggflrivrgsviKAAARRISETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVL 425
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKR--------------KARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 426 VVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGK 480
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-193 |
2.96e-17 |
|
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: 80.10 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLG-IGm 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILyLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 vfqHFS-LFEALTVAENiaLSLDPKISLKEIAGQAEKLSRAyGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDE 161
Cdd:TIGR01189 80 ---HLPgLKPELSALEN--LHFWAAIHGGAQRTIEDALAAV-GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 1609612952 162 PTSVLTPQEADKLFETLEKLKAEGRSVLYISH 193
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-193 |
3.22e-17 |
|
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: 80.23 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARrlGIGMV 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEALTVAENIALSLDpkisLKEIAGQAEKLSRAyGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPT 163
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHA----DHSDEQVEEALARV-GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 1609612952 164 SVLTPQEADKLFETLEKLKAEGRSVLYISH 193
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-193 |
5.09e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.87 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEALTVAENIAl 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSAVFTDFHLFDQLLGPEGKP- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 sLDPKISLK--EIAGQAEKLSRAYGLPLDPNahvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQeADKLF--ET 177
Cdd:PRK10522 420 -ANPALVEKwlERLKMAHKLELEDGRISNLK-----LSKGQKKRLALLLALAEERDILLLDEWAADQDPH-FRREFyqVL 492
|
170
....*....|....*.
gi 1609612952 178 LEKLKAEGRSVLYISH 193
Cdd:PRK10522 493 LPLLQEMGKTIFAISH 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-215 |
5.63e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGI----------GMVFQHfslfe 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlcpedrkaeGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 alTVAENIALSLDPK-------ISLKEIAGQAEKLSRAYGLPlDPNAH--VADLSVGERQRIEIVRALLQNPRLIILDEP 162
Cdd:PRK11288 347 --SVADNINISARRHhlragclINNRWEAENADRFIRSLNIK-TPSREqlIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 163 TSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKVTG 215
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-266 |
5.98e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.77 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGV----LAPTEGDIIWQGQPVSVGSP 72
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SEARRL---GIGMVFQHFSlfEALTVAENIALSLDPKISLKEIAGQ-----------AEKLSRAYGLPlDPN----AHVA 134
Cdd:PRK15093 81 RERRKLvghNVSMIFQEPQ--SCLDPSERVGRQLMQNIPGWTYKGRwwqrfgwrkrrAIELLHRVGIK-DHKdamrSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 135 DLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 214 --TGACDPRRETP-----ASLARMM--VGSDVASVSRATGEALGAPQIE--VMGLSVAPRTPFA 266
Cdd:PRK15093 238 veTAPSKELVTTPhhpytQALIRAIpdFGSAMPHKSRLNTLPGAIPLLEhlPIGCRLGPRCPYA 301
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-203 |
6.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLfGVLAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 -------GMVFQHFSLFeALTVAENIALSLD-----PKISLKEIAGQAEKLSRAYGlPLDPNAHVA--DLSVGERQRIEI 146
Cdd:PRK14258 84 nrlrrqvSMVHPKPNLF-PMSVYDNVAYGVKivgwrPKLEIDDIVESALKDADLWD-EIKHKIHKSalDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 147 VRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGR-SVLYISHRLEEVQRICD 203
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
267-481 |
8.29e-17 |
|
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: 79.79 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVynnDA--IHLRGKPVGRIGINGRRLMGAG--F-VPEErhgh 341
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP---TSgsVLFDGEDITGLPPHEIARLGIGrtFqIPRL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 342 aaVPGMSLSDNLLLARARSDRKAFLTGGFLRivRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQ 421
Cdd:cd03219 87 --FPELTVLENVMVAAQARTGSGLLLARARR--EEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 422 PAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-244 |
1.16e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEA---RRLGIGMVFQHFSLFEALTVAE 97
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlRREHFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALsldPKISLKeiAGQAEKLSRA------YGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PRK10535 106 NVEV---PAVYAG--LERKQRLLRAqellqrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 172 DKLFETLEKLKAEGRSVLYISHRlEEVQRICDRATVLRHGKVTgacdprRETPASLARMMVGSDVASVSRATG 244
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV------RNPPAQEKVNVAGGTEPVVNTASG 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-213 |
1.19e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSP-----SEARR 77
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqidAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 78 LGIGMVFQHFSLFEALTVAENIALSLDPK--ISLKEIAGQAEKLSRAYGLPLDP----NAHVADLSVGERQRIEIVRALL 151
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHgiKEKREIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 152 QNPRLIILDEPTSVLTPQEADKLFETLEKLKAEgRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-221 |
3.86e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLF----GNFA-------ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVG 70
Cdd:PRK10261 312 PILQVRNLVTRFplrsGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPS--EARRLGIGMVFQ--HFSLFEALTVAENIALSLDPKISLKEIAGQ---AEKLSRAYGLPLDPNAHVADLSVGERQR 143
Cdd:PRK10261 392 SPGklQALRRDIQFIFQdpYASLDPRQTVGDSIMEPLRVHGLLPGKAAAarvAWLLERVGLLPEHAWRYPHEFSGGQRQR 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 144 IEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRR 221
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV-EIGPRR 549
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
268-501 |
1.26e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.20 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVynndaihlrGKPVGRIGINGRRLMGAGFVPEERHG----H-- 341
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH---------GTYEGEIIFEGEELQASNIRDTERAGiaiiHqe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 342 -AAVPGMSLSDNLLLARarsdrkafltggflRIVRGSVIKAAA--RRISETMDVRKSGADPLA--GSLSGGNLQKFIVGR 416
Cdd:PRK13549 91 lALVKELSVLENIFLGN--------------EITPGGIMDYDAmyLRAQKLLAQLKLDINPATpvGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 417 ELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKMTLEKIG 496
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDII 236
|
....*
gi 1609612952 497 LLMGG 501
Cdd:PRK13549 237 TMMVG 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-178 |
1.98e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEA-RRLGi 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAcHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 gmvfqHFS-LFEALTVAENIALsldpkisLKEIAGQAEKLSRA--YGLPLDPNAHV--ADLSVGERQRIEIVRALLQNPR 155
Cdd:PRK13539 80 -----HRNaMKPALTVAENLEF-------WAAFLGGEELDIAAalEAVGLAPLAHLpfGYLSAGQKRRVALARLLVSNRP 147
|
170 180
....*....|....*....|...
gi 1609612952 156 LIILDEPTSVLTPqEADKLFETL 178
Cdd:PRK13539 148 IWILDEPTAALDA-AAVALFAEL 169
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-213 |
2.18e-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: 74.76 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRLGIGMVFQHFSLFEAltvaeNIA 100
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQDPTLFSG-----TIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDP--KISLKEIAGqAEKLSRAyGLpldpnahvaDLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETL 178
Cdd:cd03369 100 SNLDPfdEYSDEEIYG-ALRVSEG-GL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1609612952 179 EKLKAeGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03369 169 REEFT-NSTILTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
267-481 |
4.14e-15 |
|
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: 73.20 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGvaGNGQGE--LFDALSGeypVYNNDA--IHLRGKPVGRIGINGRRLMGagFVPEERhghA 342
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLG--PNGAGKttLIKIILG---LLKPDSgeIKVLGKDIKKEPEEVKRRIG--YLPEEP---S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 343 AVPGMSLSDNLllararsdrkafltggflrivrgsvikaaarrisetmdvrksgadplagSLSGGNLQKFIVGRELDRQP 422
Cdd:cd03230 84 LYENLTVRENL-------------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 423 AVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-193 |
8.25e-15 |
|
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: 76.76 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEALTVAENIA- 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL-FSAVFSDFHLFDRLLGLDGEAd 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 ----------LSLDPKISLKEiagqaEKLSRayglpldpnahvADLSVGERQRIEIVRALLQNPRLIILDEPTsvltpqe 170
Cdd:COG4615 430 pararellerLELDHKVSVED-----GRFST------------TDLSQGQRKRLALLVALLEDRPILVFDEWA------- 485
|
170 180 190
....*....|....*....|....*....|.
gi 1609612952 171 AD------KLF--ETLEKLKAEGRSVLYISH 193
Cdd:COG4615 486 ADqdpefrRVFytELLPELKARGKTVIAISH 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
268-501 |
1.31e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.02 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDA-IHLRGKPVGRIGINGRRLMGAGFVPEERhghAAVPG 346
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGeIYWSGSPLKASNIRDTERAGIVIIHQEL---TLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 MSLSDNLLLARARSdrkafLTGGFLRIvrgsviKAAARRISETMDVRKSGADPLA---GSLSGGNLQKFIVGRELDRQPA 423
Cdd:TIGR02633 93 LSVAENIFLGNEIT-----LPGGRMAY------NAMYLRAKNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 424 VLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKMTLEKIGLLMGG 501
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-194 |
1.33e-14 |
|
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: 71.42 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGvlaptegdiIWqgqPVSVGSpsearrlgIGMVFQHFSLFealtvaeniaL 101
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAG---------LW---PWGSGR--------IGMPEGEDLLF----------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SLDPKI---SLKEIAgqaeklsrAYglPLDPNahvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETL 178
Cdd:cd03223 70 PQRPYLplgTLREQL--------IY--PWDDV-----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*.
gi 1609612952 179 EKLKAegrSVLYISHR 194
Cdd:cd03223 135 KELGI---TVISVGHR 147
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-212 |
1.47e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPT--EGDIIWQGqpvsvGSPSEARRLGIGMVFQHFSLFEALTVAE 97
Cdd:PLN03211 85 NGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANN-----RKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIA----LSLDPKISLKEIAGQAEKLSRAYGLP-----LDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTP 168
Cdd:PLN03211 160 TLVfcslLRLPKSLTKQEKILVAESVISELGLTkcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 169 QEADKLFETLEKLKAEGRSVLYISHR-LEEVQRICDRATVLRHGK 212
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-213 |
1.87e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.77 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAG--KSTLVKMLFGvlaPTEGDIIWQGQPVSVGSPSEARRLGIG 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHfSLFEALTVAEN---IALSLDpkISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLII 158
Cdd:NF000106 91 RPVR*-GRRESFSGRENlymIGR*LD--LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 159 LDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
3.18e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.82 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEG-----DIIWQGQPVSVGSPSEAR 76
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RLGIGMVFQHFSLFeALTVAENI-----ALSLDPKislKEIAGQAEKLSRAYGLPLDPNAHVAD----LSVGERQRIEIV 147
Cdd:PRK14271 100 RRRVGMLFQRPNPF-PMSIMDNVlagvrAHKLVPR---KEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 148 RALLQNPRLIILDEPTSVLTPQEADKLFETLEKLkAEGRSVLYISHRLEEVQRICDRATVLRHGKVT--GACDPRRETP- 224
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVeeGPTEQLFSSPk 254
|
250 260
....*....|....*....|.
gi 1609612952 225 -ASLARMMVG--SDVASVSRA 242
Cdd:PRK14271 255 hAETARYVAGlsGDVKDAKRG 275
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
249-501 |
4.35e-14 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 249 APQIEVMGLSVA-PRTPfavALKSISMTVRAGEVLAIAGVagNGQGE--LFDALSGEYPVYNNDaIHLRGKPVGRiginG 325
Cdd:COG1121 4 MPAIELENLTVSyGGRP---VLEDVSLTIPPGEFVAIVGP--NGAGKstLLKAILGLLPPTSGT-VRLFGKPPRR----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 326 RRLMGagFVPEERHGHAAVPgMSLSDNLLLARARSdrkafltGGFLRIVRgsviKAAARRISETMDvrKSGADPLA---- 401
Cdd:COG1121 74 RRRIG--YVPQRAEVDWDFP-ITVRDVVLMGRYGR-------RGLFRRPS----RADREAVDEALE--RVGLEDLAdrpi 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 402 GSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
250 260
....*....|....*....|
gi 1609612952 482 SDAHPVEKMTLEKIGLLMGG 501
Cdd:COG1121 218 AHGPPEEVLTPENLSRAYGG 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-486 |
4.46e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLF----GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQG--------QPVSVG 70
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPSEA-----RRLGIGMVFQH--FSLFEALTVAENIALSldpkISLKEIAGQAEKLSRAYGLpLD----PNAHVA----- 134
Cdd:PRK10261 92 EQSAAqmrhvRGADMAMIFQEpmTSLNPVFTVGEQIAES----IRLHQGASREEAMVEAKRM-LDqvriPEAQTIlsryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 135 -DLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGK 212
Cdd:PRK10261 167 hQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 213 V--TGACDPRRETP---------ASLARM--MVGSD------VASVSRATGE---------ALGAPQIEVMGLsvAPRTP 264
Cdd:PRK10261 247 AveTGSVEQIFHAPqhpytrallAAVPQLgaMKGLDyprrfpLISLEHPAKQeppieqdtvVDGEPILQVRNL--VTRFP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 265 F-----------AVALKSISMTVRAGEVLAIAGVAGNGQGELFDALsgeypvynndaIHLRGKPVGRIGINGRRLmgagf 333
Cdd:PRK10261 325 LrsgllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL-----------LRLVESQGGEIIFNGQRI----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 334 vpeerhghaavpgMSLSDNLLLARARSDRKAF----------LTGGF-----LRIVRGSVIKAAARRIS---ETMDVRKS 395
Cdd:PRK10261 389 -------------DTLSPGKLQALRRDIQFIFqdpyasldprQTVGDsimepLRVHGLLPGKAAAARVAwllERVGLLPE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 396 GADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIA 474
Cdd:PRK10261 456 HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVA 535
|
570
....*....|..
gi 1609612952 475 VISDGKLSDAHP 486
Cdd:PRK10261 536 VMYLGQIVEIGP 547
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-166 |
7.90e-14 |
|
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: 71.29 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 25 DIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVgSPsearrlgigmvfQHFSLFEALTVAENIALSLD 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KP------------QYIKADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 105 PKISLK----EIAG--QAEKLsrayglpLDPNahVADLSVGERQRIEIVRALLQNPRLIILDEPTSVL 166
Cdd:cd03237 88 DFYTHPyfktEIAKplQIEQI-------LDRE--VPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-189 |
1.07e-13 |
|
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: 69.58 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFG--VLAPTEGDIIWQGQPVsvgsPSEARRlGIGMVFQHFSLFEALTVAE 97
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPL----DKNFQR-STGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALSldpkislkeiagqaeklsrayglpldpnAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFET 177
Cdd:cd03232 99 ALRFS----------------------------ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRF 150
|
170
....*....|..
gi 1609612952 178 LEKLKAEGRSVL 189
Cdd:cd03232 151 LKKLADSGQAIL 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-162 |
1.08e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLT------KLFgnfaacNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR 76
Cdd:PRK13538 1 MLEARNLAcerderILF------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 RL-------GIGmvfqhfslfEALTVAEN--IALSLDPKISlKEIAGQAekLSRAyGLPLDPNAHVADLSVGERQRIEIV 147
Cdd:PRK13538 75 DLlylghqpGIK---------TELTALENlrFYQRLHGPGD-DEALWEA--LAQV-GLAGFEDVPVRQLSAGQQRRVALA 141
|
170
....*....|....*
gi 1609612952 148 RALLQNPRLIILDEP 162
Cdd:PRK13538 142 RLWLTRAPLWILDEP 156
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-229 |
1.26e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL--------APTEGDIIWQGQPVSVGSPSEARRLGIGMVFQHFSLFe 91
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 ALTVAENIALSLDP--------KISLKEIAGQAekLSRAYGLPLDpNAHVADLSVGERQRIEIVRALLQ---------NP 154
Cdd:PRK13547 97 AFSAREIVLLGRYPharragalTHRDGEIAWQA--LALAGATALV-GRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 155 RLIILDEPTSVLTPQEADKLFETLEKLKAEGR-SVLYISHRLEEVQRICDRATVLRHGKVTGACDPRRE-TPASLAR 229
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVlTPAHIAR 250
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-213 |
1.33e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDI-ARGEIhALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRlGIGMVfQHFSLFEALTVAENIA 100
Cdd:PRK10790 360 INLSVpSRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAMV-QQDPVVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDpkISLKEIAGQAEKLSRA---YGLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:PRK10790 437 LGRD--ISEEQVWQALETVQLAelaRSLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1609612952 174 LFETLEKLKaEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:PRK10790 515 IQQALAAVR-EHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-213 |
3.39e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.05 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEAR-RLGIgmVFQHFSLFEAlTVA 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRsRLAV--VSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIALSlDPKISLKEIAgQAEKLSRAYG----LPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTP 168
Cdd:PRK10789 407 NNIALG-RPDATQQEIE-HVARLASVHDdilrLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 169 QEADKLFETLEKLkAEGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:PRK10789 485 RTEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHI 527
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-229 |
5.46e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.96 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 5 SVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSE--ARRLGIgm 82
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRelAKRLAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQ--HFSLfeALTVAENIA----------LSLDPKislkeiagqaEKLSRAYG-LPLDP--NAHVADLSVGERQRIEIV 147
Cdd:COG4604 80 LRQenHINS--RLTVRELVAfgrfpyskgrLTAEDR----------EIIDEAIAyLDLEDlaDRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 148 RALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTgACDPRRE--TP 224
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVV-AQGTPEEiiTP 226
|
....*
gi 1609612952 225 ASLAR 229
Cdd:COG4604 227 EVLSD 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-213 |
6.44e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.07 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 18 ACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpvsvgspseARRLGIGMvfqhfSLFEALTVAE 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAISS-----GLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 98 NIALS-LDPKISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFE 176
Cdd:PRK13545 105 NIELKgLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1609612952 177 TLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-212 |
6.81e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 67.49 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGqpvsvgspsearrlGIGMVFQHFSLFEAlTVAENI 99
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ----------------ALSLDPKISLkeiagqaeklsraygLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIIL 159
Cdd:cd03250 87 lfgkpfdeeryekvikACALEPDLEI---------------LPDGDLTEIGEkginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 160 DEPTSVLTPQEADKLFET-LEKLKAEGRSVLYISHRLEEVQRiCDRATVLRHGK 212
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
249-488 |
1.01e-12 |
|
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: 70.32 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 249 APQIEVMGLSVAPRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVynndaihlRGKPVGRIGINGRRL 328
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH--------GGRISGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 329 MGAGfvPEERHGHAAVPGMSLSDNLLLARARsDRKAFltGGFLRIVRGSVIKAAARRISETMDVRKSGADPLAgSLSGGN 408
Cdd:COG1123 74 LELS--EALRGRRIGMVFQDPMTQLNPVTVG-DQIAE--ALENLGLSRAEARARVLELLEAVGLERRLDRYPH-QLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 409 LQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPV 487
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
.
gi 1609612952 488 E 488
Cdd:COG1123 228 E 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
269-481 |
1.56e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 66.91 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEypvynndaIHLRGKPVGRIGINGRRLMGA------GFVPEErhgHA 342
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--------VEGGGTTSGQILFNGQPRKPDqfqkcvAYVRQD---DI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 343 AVPGMSLSDNLLlararsdrkafltggFLRIVRGSVIKAAARRISETMDVR------KSGADPLAGSLSGGNLQKFIVGR 416
Cdd:cd03234 92 LLPGLTVRETLT---------------YTAILRLPRKSSDAIRKKRVEDVLlrdlalTRIGGNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 417 ELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIV-ISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-213 |
1.96e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.53 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 16 FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpVSVGSpsearrLGIGMVFQhfslfeaLTV 95
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIA------ISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 96 AENI-----ALSLDPKiSLKEIAGQAEKLSRAYGLPLDPnahVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:PRK13546 103 IENIefkmlCMGFKRK-EIKAMTPKIIEFSELGEFIYQP---VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 171 ADKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-223 |
3.02e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 26 IARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvgspSEARRLGIGMVFQHFSLFEALTV-AENIALS-- 102
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQSEEVDWSFPVlVEDVVMMgr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 103 -------LDPKISLKEIAGQAekLSRAYGLPLDpNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLF 175
Cdd:PRK15056 106 yghmgwlRRAKKRDRQIVTAA--LARVDMVEFR-HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 176 ETLEKLKAEGRSVLYISHRLEEVQRICDRaTVLRHGKVTgACDPRRET 223
Cdd:PRK15056 183 SLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVL-ASGPTETT 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-194 |
4.50e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgiGMVFQHFSLFEALTVAENI 99
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDPKISLKEIagqaEKLSRAYGLpldpnAHVAD-----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKL 174
Cdd:PRK13540 96 LYDIHFSPGAVGI----TELCRLFSL-----EHLIDypcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|
gi 1609612952 175 FETLEKLKAEGRSVLYISHR 194
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQ 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-213 |
5.09e-12 |
|
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: 68.82 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVS-VGSpsEARRLGIGMVFQHFSLFEAltvaeNIA 100
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkIGL--HDLRFKITIIPQDPVLFSG-----SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDP--KISLKEIAGQAEkLSRAYG----LPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTpQE 170
Cdd:TIGR00957 1378 MNLDPfsQYSDEEVWWALE-LAHLKTfvsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD-LE 1455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 171 ADKLFETLEKLKAEGRSVLYISHRLEEVQRICdRATVLRHGKV 213
Cdd:TIGR00957 1456 TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-220 |
7.77e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAacngidLDIARGEIHA-----LLGENGAGKSTLVKMLFGVLAPTEGDIIWQgqpvsvgspsear 76
Cdd:PRK13409 339 TLVEYPDLTKKLGDFS------LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 77 rLGIGMVFQHFSLFEALTVAE---NIALSLDPKISLKEIAG--QAEKLsrayglpLDPNahVADLSVGERQRIEIVRALL 151
Cdd:PRK13409 400 -LKISYKPQYIKPDYDGTVEDllrSITDDLGSSYYKSEIIKplQLERL-------LDKN--VKDLSGGELQRVAIAACLS 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 152 QNPRLIILDEPTSVLTPQEADKLFETLEKLkAEGR--SVLYISHRLEEVQRICDRATVL-----RHGKVTGACDPR 220
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQRLAVAKAIRRI-AEEReaTALVVDHDIYMIDYISDRLMVFegepgKHGHASGPMDMR 544
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-194 |
7.99e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEihALL--GENGAGKSTLVKMLFGvlaptegdiIW---QGQpvsVGSPSEAR--------RLGIGmvfqh 86
Cdd:COG4178 380 EDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAG---------LWpygSGR---IARPAGARvlflpqrpYLPLG----- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 87 fSLFEALTVAenialSLDPKISLKEIAgqaEKLSRAyGLP-----LDPNAHVAD-LSVGERQRIEIVRALLQNPRLIILD 160
Cdd:COG4178 441 -TLREALLYP-----ATAEAFSDAELR---EALEAV-GLGhlaerLDEEADWDQvLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|....
gi 1609612952 161 EPTSVLTPQEADKLFETLEKLKAEGrSVLYISHR 194
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGT-TVISVGHR 543
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-214 |
8.23e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKML-----FGVLapTEGDIIWQGQPVSvgsPSEARRlgIGMVFQHFSLFEALTVAENI---- 99
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLD---SSFQRS--IGYVQQQDLHLPTSTVRESLrfsa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHVA----DLSVGERQRIEIVRALLQNPRLII-LDEPTSVLTPQEADKL 174
Cdd:TIGR00956 862 YLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 175 FETLEKLKAEGRSVLYISHR-----LEEVqricDRATVLRHGKVT 214
Cdd:TIGR00956 942 CKLMRKLADHGQAILCTIHQpsailFEEF----DRLLLLQKGGQT 982
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-231 |
1.19e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENI 99
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 alslDPkISLKEIAGQAEKLSRAY------GLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQ 169
Cdd:PLN03232 1331 ----DP-FSEHNDADLWEALERAHikdvidRNPFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 170 eADKLFETLEKLKAEGRSVLYISHRLEEVQRiCDRATVLRHGKVTGACDPR----RETPAsLARMM 231
Cdd:PLN03232 1406 -TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQellsRDTSA-FFRMV 1468
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
1.22e-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: 66.88 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWqGQPVSVGSPSEARrlgigmv 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSR------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 fqhfslfEAL----TVAENIALSLDpKISLkeiaGQAEKLSRAY-------GlpLDPNAHVADLSVGERQRIEIVRALLQ 152
Cdd:TIGR03719 395 -------DALdpnkTVWEEISGGLD-IIKL----GKREIPSRAYvgrfnfkG--SDQQKKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 153 NPRLIILDEPTSVLTpqeadklFETL----EKLKAEGRSVLYISH 193
Cdd:TIGR03719 461 GGNVLLLDEPTNDLD-------VETLraleEALLNFAGCAVVISH 498
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-196 |
1.69e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGspsearrlgigmvfqhfslfEALTVAENI 99
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG--------------------REASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDPKISLKEIAgqAEKLSRAYgLPLDPNAHvadLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLE 179
Cdd:COG2401 107 GRKGDFKDAVELLN--AVGLSDAV-LWLRRFKE---LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*...
gi 1609612952 180 KL-KAEGRSVLYISHRLE 196
Cdd:COG2401 181 KLaRRAGITLVVATHHYD 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-435 |
1.87e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 23 DLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQH-----FSLFE---ALT 94
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL-VSDEWQRnntdmLSPGEddtGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 95 VAENIALSLDPKISLKEIAGQ---AEKLSRAYglpldpnahvADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PRK10938 102 TAEIIQDEVKDPARCEQLAQQfgiTALLDRRF----------KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 172 DKLFETLEKLKAEGRSVLYISHRLEEVQRICDRATVL--RHGKVTGacdprrETPASLARMMVgSDVASVSRATGEALGA 249
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLadCTLAETG------EREEILQQALV-AQLAHSEQLEGVQLPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 250 PQIEVMGLSVAPRTPFAV------------ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPV-YNNDaIHLRGK 316
Cdd:PRK10938 245 PDEPSARHALPANEPRIVlnngvvsyndrpILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgYSND-LTLFGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 317 pvgrigingRRLMGA---------GFVPEERH----GHAAVPGMSLS---DNLLLARARSDRKAFLTGGFLRIVrgsvik 380
Cdd:PRK10938 324 ---------RRGSGEtiwdikkhiGYVSSSLHldyrVSTSVRNVILSgffDSIGIYQAVSDRQQKLAQQWLDIL------ 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 381 aaarRISETMdvrksgADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVD 435
Cdd:PRK10938 389 ----GIDKRT------ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-214 |
1.98e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 23 DLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQgQPVSVgspseAR------RLGIGMVFQHfslfealtVA 96
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIV-----ARlqqdppRNVEGTVYDF--------VA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ENIA---------------LSLDPKIS-LKEIAGQAEKLSRAYG-------------LPLDPNAHVADLSVGERQRIEIV 147
Cdd:PRK11147 89 EGIEeqaeylkryhdishlVETDPSEKnLNELAKLQEQLDHHNLwqlenrinevlaqLGLDPDAALSSLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 148 RALLQNPRLIILDEPTSVLtpqEADKLfETLEK-LKAEGRSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHL---DIETI-EWLEGfLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-220 |
2.79e-11 |
|
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: 65.96 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAacngidLDIARGEIH-----ALLGENGAGKSTLVKMLFGVLAPTEGDIIWQ------GQPVSVG 70
Cdd:COG1245 340 TLVEYPDLTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 71 SPSEARRLgigmvfqhfsLFEALTVAenialsLDPKISLKEIAG--QAEKLsrayglpLDPNahVADLSVGERQRIEIVR 148
Cdd:COG1245 414 YDGTVEEF----------LRSANTDD------FGSSYYKTEIIKplGLEKL-------LDKN--VKDLSGGELQRVAIAA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 149 ALLQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVL-----RHGKVTGACDPR 220
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMVFegepgVHGHASGPMDMR 546
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
267-476 |
2.94e-11 |
|
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: 62.94 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNdAIHLRGKPVGRiginGRRLMGagFVPEERHGHAAVPg 346
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSG-SIRVFGKPLEK----ERKRIG--YVPQRRSIDRDFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 MSLSDNLLLARARSdrkafltGGFLRIVRGSViKAAARRISETMDVRKSGADPLaGSLSGGNLQKFIVGRELDRQPAVLV 426
Cdd:cd03235 85 ISVRDVVLMGLYGH-------KGLFRRLSKAD-KAKVDEALERVGLSELADRQI-GELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1609612952 427 VNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVI 476
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-199 |
3.48e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLGIGMVFQHFSLFEAlTVAENIAL 101
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SLdpkISLKEIAGQAEKLS----------------------------------------RAYGLPLDPN----------- 130
Cdd:PTZ00265 483 SL---YSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsneliemrKNYQTIKDSEvvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 131 ---------------AHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKA-EGRSVLYISHR 194
Cdd:PTZ00265 560 dfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHR 639
|
....*
gi 1609612952 195 LEEVQ 199
Cdd:PTZ00265 640 LSTIR 644
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-214 |
4.07e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWqgqpvsvgspSEARRLGIgMV 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANIGY-YA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 84 FQHFSLFEA-LTVAENIALSLDPkislkeiaGQAEKLSRAY-GLPL----DPNAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:PRK15064 389 QDHAYDFENdLTLFDWMSQWRQE--------GDDEQAVRGTlGRLLfsqdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKLKAegrSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:PRK15064 461 VMDEPTNHMDMESIESLNMALEKYEG---TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
267-480 |
4.65e-11 |
|
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: 61.11 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVagNGQG--ELFDALSGEYPVYNndaihlrgkpvGRIGINGRRLmGAGFVPEERHGHAAV 344
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGP--NGSGksTLLRAIAGLLKPTS-----------GEILIDGKDI-AKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 345 PGmslsdnlllararsdrkafltggflrivrgsvikaaarrisetmdvrksgadplagsLSGGNLQKFIVGRELDRQPAV 424
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 425 LVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGK 480
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-203 |
5.15e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.89 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 3 LLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGV--LAPTEGDIIWQGQPVSVGSPSEARRLGI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQ----------HFSLFEALTVAE-----------NIALSLDPKISLKEIagQAEKLSRAYGLpldpnahvaDLSVG 139
Cdd:PRK09580 81 FMAFQypveipgvsnQFFLQTALNAVRsyrgqepldrfDFQDLMEEKIALLKM--PEDLLTRSVNV---------GFSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 140 ERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHrleeVQRICD 203
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH----YQRILD 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
268-486 |
5.40e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEY-PvyNNDAIHLRGKPVgRIGiNGRRLMGAG--FVPEERHghaAV 344
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYqP--DAGSILIDGQEM-RFA-STTAALAAGvaIIYQELH---LV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 345 PGMSLSDNLLLARARSdrkaflTGGFlriVRGSVIKAAARRISETMDVRKSGADPLaGSLSGGNLQKFIVGRELDRQPAV 424
Cdd:PRK11288 92 PEMTVAENLYLGQLPH------KGGI---VNRRLLNYEAREQLEHLGVDIDPDTPL-KYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 425 LVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHP 486
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFD 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-166 |
5.73e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIiwqgqpvsvgspSEARRLGIG 81
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------------GLAKGIKLG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHfsLFEALTVAENiALSLDPKISLKEIAGQAEKLSRAYGLPLDPNAHV-ADLSVGERQRIEIVRALLQNPRLIILD 160
Cdd:PRK10636 379 YFAQH--QLEFLRADES-PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
....*.
gi 1609612952 161 EPTSVL 166
Cdd:PRK10636 456 EPTNHL 461
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-200 |
7.32e-11 |
|
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: 61.18 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKmlfgvlaptegDIIW-QGQPVSVGSPSearrlgigmvfqhfslfealTVAEN 98
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYaSGKARLISFLP--------------------KFSRN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 IALSLDpkiSLKEIAgqaeKLSRAYgLPLDPNAhvADLSVGERQRIEIVRALLQNPR--LIILDEPTSVLTPQEADKLFE 176
Cdd:cd03238 61 KLIFID---QLQFLI----DVGLGY-LTLGQKL--STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180
....*....|....*....|....
gi 1609612952 177 TLEKLKAEGRSVLYISHRLEEVQR 200
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
267-481 |
8.90e-11 |
|
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: 61.50 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNndaihlrgkpvGRIGINGRRLMGAGfvPEER------HG 340
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS-----------GRIYIGGRDVTDLP--PKDRdiamvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 341 HAAVPGMSLSDNLllararsdrkAFltGGFLRIVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDR 420
Cdd:cd03301 81 YALYPHMTVYDNI----------AF--GLKLRKVPKDEIDERVREVAELLQIEHL-LDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 421 QPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
261-481 |
1.03e-10 |
|
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: 61.72 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 261 PRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDAIhLRGKPVGRIgingrrlmgagfvpEERHG 340
Cdd:cd03248 22 PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL-LDGKPISQY--------------EHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 341 HAAVPGMSlSDNLLLARARSDRKAFLTGG--FLRIVRGSVIKAAARRISETMDVRKSGADPLAGSLSGGNLQKFIVGREL 418
Cdd:cd03248 87 HSKVSLVG-QEPVLFARSLQDNIAYGLQScsFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 419 DRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSaVIVISQDLDEIfEVATNIAVISDGKL 481
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRT-VLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-232 |
1.14e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAP----TEGDIIWQGQPVsvgSPSEARRLGIGMVFQH-FSLFEAL-T 94
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV---APCALRGRKIATIMQNpRSAFNPLhT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 95 VAENIALSLDPKISLKEIAGQAEKLsRAYGLPLDP---NAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PRK10418 98 MHTHARETCLALGKPADDATLTAAL-EAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 172 DKLFETLEKLKAE-GRSVLYISHRLEEVQRICDRATVLRHGKVTGACD-------PRRETpaslARMMV 232
Cdd:PRK10418 177 ARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDvetlfnaPKHAV----TRSLV 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
267-468 |
1.47e-10 |
|
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: 60.88 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDAL-------SGEYPVYNNDAIHLRGKPVGRIgingRRLMGagfvpeerh 339
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIykeelptSGTIRVNGQDVSDLRGRAIPYL----RRKIG--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 340 ghaavpgMSLSDNLLLararSDRKAFLTGGFLRIVRGSVIKAAARRISETMDV--RKSGADPLAGSLSGGNLQKFIVGRE 417
Cdd:cd03292 82 -------VVFQDFRLL----PDRNVYENVAFALEVTGVPPREIRKRVPAALELvgLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 418 LDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDlDEIFE 468
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA-KELVD 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-213 |
1.53e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.45 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 1 MPLLSVRKLTKLFGN----FAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVL----APTEGDIIWQGQPVSVGSP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 73 SEARRL---GIGMVFQH------------FSLFEALTVAE--NIALSLDPKISLKEIAGQAEKLSRayglpLDPNAHvaD 135
Cdd:PRK11022 81 KERRNLvgaEVAMIFQDpmtslnpcytvgFQIMEAIKVHQggNKKTRRQRAIDLLNQVGIPDPASR-----LDVYPH--Q 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 136 LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKL-KAEGRSVLYISHRLEEVQRICDRATVLRHGKV 213
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
266-480 |
1.68e-10 |
|
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: 59.89 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 266 AVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSG-EYPVYNNdaIHLRGKPVGRIGINGRRLMGA-GFVPEErhgHAA 343
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGS--ILIDGEDLTDLEDELPPLRRRiGMVFQD---FAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 344 VPGMSLSDNLLLArarsdrkafltggflrivrgsvikaaarrisetmdvrksgadplagsLSGGNLQKFIVGRELDRQPA 423
Cdd:cd03229 88 FPHLTVLENIALG-----------------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 424 VLVVNQPTWGVDAGAASRIRQALVDL-AKAGSAVIVISQDLDEIFEVATNIAVISDGK 480
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-220 |
2.05e-10 |
|
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: 59.89 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 25 DIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVgspsearrlgigmvfqhfslfealtvaenialsld 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY----------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 105 pkislkeiagqaeklsrayglpldpNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLKAE 184
Cdd:cd03222 66 -------------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 1609612952 185 G-RSVLYISHRLEEVQRICDRATVL--RHGKVTGACDPR 220
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIHVFegEPGVYGIASQPK 159
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
269-480 |
2.31e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYP--VYNNDAIHLRGKPVGRIGIngrRLMGAgFVPEErhgHAAVPG 346
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgVKGSGSVLLNGMPIDAKEM---RAISA-YVQQD---DLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 MSLSDNLLL-ARARSDRKAFLTGGFLR----IVRGSVIKAAARRIsetmdvrksGADPLAGSLSGGNLQKFIVGRELDRQ 421
Cdd:TIGR00955 114 LTVREHLMFqAHLRMPRRVTKKEKRERvdevLQALGLRKCANTRI---------GVPGRVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 422 PAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIV-ISQDLDEIFEVATNIAVISDGK 480
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGR 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
267-481 |
3.50e-10 |
|
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: 60.08 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDAiHLRGKPVGRIGINGRRLMGagFVPEERhghAAVPG 346
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA-TVAGHDVVREPREVRRRIG--IVFQDL---SVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 MSLSDNLLLararsdrKAFLTGgflriVRGSVikaAARRISETMDVRKSG--ADPLAGSLSGGNLQKFIVGRELDRQPAV 424
Cdd:cd03265 88 LTGWENLYI-------HARLYG-----VPGAE---RRERIDELLDFVGLLeaADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 425 LVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-246 |
4.26e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAltvaeNIA 100
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-LGIIPQAPVLFSG-----TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDPkISLKEIAGQAEKLSRAY------GLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTS---VLT 167
Cdd:PLN03130 1331 FNLDP-FNEHNDADLWESLERAHlkdvirRNSLGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAavdVRT 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 168 pqeaDKLFEtlEKLKAEGRS--VLYISHRLEEVqrI-CDRATVLRHGKVTgacdpRRETPASLArMMVGSDVASVSRATG 244
Cdd:PLN03130 1410 ----DALIQ--KTIREEFKSctMLIIAHRLNTI--IdCDRILVLDAGRVV-----EFDTPENLL-SNEGSAFSKMVQSTG 1475
|
..
gi 1609612952 245 EA 246
Cdd:PLN03130 1476 AA 1477
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-166 |
4.30e-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: 61.87 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 34 LLGENGAGKSTLVKMLFGVLAPTEGDIIwqgqpvsvgsPSEARRlgIGMVFQHFSLFEALTVAENIALSLDPKISL---- 109
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEAR----------PQPGIK--VGYLPQEPQLDPTKTVRENVEEGVAEIKDAldrf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 110 ---------------KEIAGQAE---------------KLSRAY-GLPLDPN-AHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:TIGR03719 104 neisakyaepdadfdKLAAEQAElqeiidaadawdldsQLEIAMdALRCPPWdADVTKLSGGERRRVALCRLLLSKPDML 183
|
....*....
gi 1609612952 158 ILDEPTSVL 166
Cdd:TIGR03719 184 LLDEPTNHL 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-193 |
4.33e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKMLFGVLAP---TEGDIIWQGQPVSvgspSEARRLGIGMVFQHFSLFEALTVAEniALSLDP 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPTLTVRE--HLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 106 KISLKEIAGQAEKLSRA----YGLPLDPNAH--------VADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:TIGR00955 125 HLRMPRRVTKKEKRERVdevlQALGLRKCANtrigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180
....*....|....*....|
gi 1609612952 174 LFETLEKLKAEGRSVLYISH 193
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIH 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
268-479 |
5.04e-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: 62.34 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDAIhlrgkpvgrigINGRRLMGAgfVPEERHGHAAVPGM 347
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT-----------VAGKSILTN--ISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 348 SLSDNLLLARARSDRKAFLTGgflriVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQPAVLVV 427
Cdd:TIGR01257 2021 DAIDDLLTGREHLYLYARLRG-----VPAEEIEKVANWSIQSLGLSLY-ADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 428 NQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDG 479
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
267-481 |
5.20e-10 |
|
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: 59.30 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGeypVYNNDAihlrgkpvGRIGINGRRLMGAGFVPEERHGhaavpg 346
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG---LLEPDA--------GFATVDGFDVVKEPAEARRRLG------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 mSLSDNLLLARARSDRKAFLTGGFLRIVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQPAVLV 426
Cdd:cd03266 82 -FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 427 VNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
267-481 |
1.30e-09 |
|
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: 58.27 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQ-------GELFDALSGEYPVYNNDAIHLRGKpvGRIGINGRRLmgaGFVPEErh 339
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKstllnilGGLDRPTSGEVRVDGTDISKLSEK--ELAAFRRRHI---GFVFQS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 340 gHAAVPGMSLSDNLLLArarsdrkAFLTGgflriVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELD 419
Cdd:cd03255 91 -FNLLPDLTALENVELP-------LLLAG-----VPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 420 RQPAVLVVNQPTWGVDAGAASRIRQALVDLAK-AGSAVIVISQDlDEIFEVATNIAVISDGKL 481
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-163 |
1.89e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 6 VRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIwQGQPVSVGSPSEARrlgigmvfq 85
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVKLAYVDQSR--------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 hfslfEAL----TVAENIALSLDpKISLkeiaGQAEKLSRAY-------GlpLDPNAHVADLSVGERQRIEIVRALLQNP 154
Cdd:PRK11819 397 -----DALdpnkTVWEEISGGLD-IIKV----GNREIPSRAYvgrfnfkG--GDQQKKVGVLSGGERNRLHLAKTLKQGG 464
|
....*....
gi 1609612952 155 RLIILDEPT 163
Cdd:PRK11819 465 NVLLLDEPT 473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-193 |
2.05e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 26 IARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDiiwqgqpVSVGSpsearRLGIGMVFQHfslFEAL----TVAENIAl 101
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-------IHCGT-----KLEVAYFDQH---RAELdpekTVMDNLA- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 slDPKISLkEIAGQAEK-LS----------RAyglpLDPnahVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTpqe 170
Cdd:PRK11147 406 --EGKQEV-MVNGRPRHvLGylqdflfhpkRA----MTP---VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD--- 472
|
170 180
....*....|....*....|....*...
gi 1609612952 171 adklFETLEKLKA-----EGrSVLYISH 193
Cdd:PRK11147 473 ----VETLELLEElldsyQG-TVLLVSH 495
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-163 |
2.43e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 34 LLGENGAGKSTLVKMLFGVLAPTEGDIIWQ-GqpvsvgspsearrLGIGMVFQHFSLFEALTVAENIALSLDPKISLKE- 111
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPApG-------------IKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 112 ------------------IAGQAE---------------KLSRA---YGLPlDPNAHVADLSVGERQRIEIVRALLQNPR 155
Cdd:PRK11819 105 fneiyaayaepdadfdalAAEQGElqeiidaadawdldsQLEIAmdaLRCP-PWDAKVTKLSGGERRRVALCRLLLEKPD 183
|
....*...
gi 1609612952 156 LIILDEPT 163
Cdd:PRK11819 184 MLLLDEPT 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
252-481 |
2.60e-09 |
|
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: 57.20 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 252 IEVMGLSVapRTPFAVALKSISMTVRAGeVLAIAGVAGNGQGELFDALSGEYPVyNNDAIHLRGKPVGRIGINGRRLMGa 331
Cdd:cd03264 1 LQLENLTK--RYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP-SSGTIRIDGQDVLKQPQKLRRRIG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 332 gFVPEERHGHaavPGMSLSDNLllararsDRKAFLTGgflriVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQK 411
Cdd:cd03264 76 -YLPQEFGVY---PNFTVREFL-------DYIAWLKG-----IPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 412 FIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAkAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
268-481 |
8.66e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEyPVYNNDAIHLRGKPVgrIGINGRRLM--GAGFVPEERHGHAAvp 345
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDI--TDWQTAKIMreAVAIVPEGRRVFSR-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 346 gMSLSDNLLLARARSDRKAFLTggflRIVRgsvIKAAARRISETMDVRksgadplAGSLSGGNLQKFIVGRELDRQPAVL 425
Cdd:PRK11614 95 -MTVEENLAMGGFFAERDQFQE----RIKW---VYELFPRLHERRIQR-------AGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 426 VVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-211 |
1.16e-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: 56.40 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpVSVGSpsearrlgigmvfqHFSLFEALTVAENI-- 99
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS--------------QFSWIMPGTIKENIif 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDPKISLKEI-AGQAEK-LSRaygLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:cd03291 121 GVSYDEYRYKSVVkACQLEEdITK---FPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190
....*....|....*....|....*....|....*....
gi 1609612952 174 LFET-LEKLKAEGRSVLyISHRLEEVqRICDRATVLRHG 211
Cdd:cd03291 198 IFEScVCKLMANKTRIL-VTSKMEHL-KKADKILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-211 |
1.48e-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: 57.61 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQpVSVGSpsearrlgigmvfqHFSLFEALTVAENI-- 99
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP--------------QTSWIMPGTIKDNIif 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 ALSLDP--KISLKEIAGQAEKLSRaygLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:TIGR01271 510 GLSYDEyrYTSVIKACQLEEDIAL---FPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*....
gi 1609612952 174 LFET-LEKLKAEGRSVLYIShRLEEVQRiCDRATVLRHG 211
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTS-KLEHLKK-ADKILLLHEG 623
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-195 |
1.50e-08 |
|
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: 57.10 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 28 RGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIiwqGQPVSvgspsearrlgIGMVFQHFS------LFEAL-----TVA 96
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPS-----------WDEVLKRFRgtelqdYFKKLangeiKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ------ENIALSLDPKIS-----------LKEIAgqaEKLSrayglpLDP--NAHVADLSVGERQRIEIVRALLQNPRLI 157
Cdd:COG1245 164 hkpqyvDLIPKVFKGTVRellekvdergkLDELA---EKLG------LENilDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 1609612952 158 ILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRL 195
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
269-480 |
1.69e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEypvynndaIHLRGKpVGRIGINGRR-----LMGAGFVPEerhghaa 343
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR--------IQGNNF-TGTILANNRKptkqiLKRTGFVTQ------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 344 vpgmslsDNLLLARArSDRKAFLTGGFLRI----VRGSVIKAAARRISEtMDVRKSGADPLAGS----LSGGNLQKFIVG 415
Cdd:PLN03211 148 -------DDILYPHL-TVRETLVFCSLLRLpkslTKQEKILVAESVISE-LGLTKCENTIIGNSfirgISGGERKRVSIA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 416 RELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIV-ISQDLDEIFEVATNIAVISDGK 480
Cdd:PLN03211 219 HEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
268-501 |
1.79e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGeypVYNNDA--IHLRGKPVGRIGINGRRLMGAGFVPEERHghaAVP 345
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG---IYTRDAgsILYLGKEVTFNGPKSSQEAGIGIIHQELN---LIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 346 GMSLSDNLLLARArsdrkafLTGGFLRIvRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQPAVL 425
Cdd:PRK10762 93 QLTIAENIFLGRE-------FVNRFGRI-DWKKMYAEADKLLARLNLRFS-SDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 426 VVNQPTWGV-DAGAASRIRqALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKMTLEKIGLLMGG 501
Cdd:PRK10762 164 IMDEPTDALtDTETESLFR-VIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVG 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
252-481 |
3.06e-08 |
|
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: 53.20 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 252 IEVMGLSVapRTPFAVALKSISMTVRAGEVLAIAGvaGNGQGE--LFDALSGEYPVynnDAihlrgkpvGRIGINGRRLM 329
Cdd:cd03216 1 LELRGITK--RFGGVKALDGVSLSVRRGEVHALLG--ENGAGKstLMKILSGLYKP---DS--------GEILVDGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 330 GAGFVPEERHGHAAVPGMSLSDNLLLARARSdrkafltggflrivrgsvikaaarrisetmdvrksgadplagslsggnl 409
Cdd:cd03216 66 FASPRDARRAGIAMVYQLSVGERQMVEIARA------------------------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 410 qkfivgreLDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03216 97 --------LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-213 |
3.31e-08 |
|
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: 54.86 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLF--GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLApTEGDIIWQGqpVSVGS-PSEARRLGI 80
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG--VSWNSvPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEAltvaeNIALSLDP--KISLKEIAGQAEKL---SRAYGLPLDPNAHVAD----LSVGERQRIEIVRALL 151
Cdd:cd03289 80 GVIPQKVFIFSG-----TFRKNLDPygKWSDEEIWKVAEEVglkSVIEQFPGQLDFVLVDggcvLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 152 QNPRLIILDEPTSVLTPQEADKLFETLEKLKAeGRSVLYISHRLEEVQRiCDRATVLRHGKV 213
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
117-216 |
4.66e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 117 EKLSRAYGLPLDPnaHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTpQEADKLFE-TLEKLKAEG-RSVLYISHR 194
Cdd:PTZ00265 1342 ESLPNKYDTNVGP--YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEkTIVDIKDKAdKTIITIAHR 1418
|
90 100
....*....|....*....|..
gi 1609612952 195 LEEVQRiCDRATVLRHGKVTGA 216
Cdd:PTZ00265 1419 IASIKR-SDKIVVFNNPDRTGS 1439
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
252-490 |
4.84e-08 |
|
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: 53.66 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 252 IEVMGLSVAPRTpfAVALKSISMTVRAGEVLAIAGVAGNGQ-------GELFDALSGEYPVYNNDAIHLRGKPVGRIgin 324
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKstllrliVGLLRPDSGEVLIDGEDISGLSEAELYRL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 325 gRRLMGAGFvpeerHGHAAVPGMSLSDNLllararsdrkAFLTGGFLRIVRGSVikaaARRISETMDV--RKSGADPLAG 402
Cdd:cd03261 76 -RRRMGMLF-----QSGALFDSLTVFENV----------AFPLREHTRLSEEEI----REIVLEKLEAvgLRGAEDLYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 403 SLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03261 136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
....*....
gi 1609612952 482 SDAHPVEKM 490
Cdd:cd03261 216 VAEGTPEEL 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-204 |
6.07e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.61 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 124 GLP-LDPNAHVADLSVGERQRIEIVRALlqNPRLI----ILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRlEEV 198
Cdd:PRK00635 464 GLPyLTPERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQM 540
|
....*.
gi 1609612952 199 QRICDR 204
Cdd:PRK00635 541 ISLADR 546
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-195 |
8.98e-08 |
|
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: 53.14 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKMLFGVLAPTEGDiiWQGQPVSVGSPSEARrlgiGMVFQHFslFEALtVAENIALSLDPK-- 106
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFR----GSELQNY--FTKL-LEGDVKVIVKPQyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 107 --------------ISLKEIAGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEAD 172
Cdd:cd03236 97 dlipkavkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 1609612952 173 KLFETLEKLKAEGRSVLYISHRL 195
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDL 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-232 |
1.11e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSPSEARRLgIGMVFQHFSLFEAlTVAENi 99
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDG-TVRQN- 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 alsLDPKISLK--------EIAGQAEKL-SRAYGLpldpNAHV----ADLSVGERQRIEIVRALLQ-NPRLIILDEPTSV 165
Cdd:PTZ00243 1404 ---VDPFLEASsaevwaalELVGLRERVaSESEGI----DSRVleggSNYSVGQRQLMCMARALLKkGSGFILMDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 166 LTPQeADKLFETLEKLKAEGRSVLYISHRLEEVQRiCDRATVLRHGKVTGACDPRR--ETPASLARMMV 232
Cdd:PTZ00243 1477 IDPA-LDRQIQATVMSAFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRElvMNRQSIFHSMV 1543
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-195 |
1.32e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 28 RGEIHALLGENGAGKSTLVKMLFGVLAPTEGDiiwqgqPVSVGSPSEarrlgigmVFQHFS------LFEAL-----TVA 96
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD------YEEEPSWDE--------VLKRFRgtelqnYFKKLyngeiKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 97 ------ENIALSLDPKIS--LKEI--AGQAEKLSRAYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVL 166
Cdd:PRK13409 164 hkpqyvDLIPKVFKGKVRelLKKVdeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*....
gi 1609612952 167 TPQEADKLFETLEKLkAEGRSVLYISHRL 195
Cdd:PRK13409 244 DIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
268-480 |
1.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYpvynndaihlrgKPV-GRIGINGRRLmgagfvpeerhGHAAVPG 346
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL------------KPSsGRILFDGKPI-----------DYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 MSLSDNLLLARARSDRKAFLTGGFLRIVRGSV-IKAAARRISETMD--VRKSGADPLAGS----LSGGNLQKFIVGRELD 419
Cdd:PRK13636 78 MKLRESVGMVFQDPDNQLFSASVYQDVSFGAVnLKLPEDEVRKRVDnaLKRTGIEHLKDKpthcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 420 RQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIAVISDGK 480
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
269-488 |
1.62e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELF---DAL----SGEYPVynnDAIHLRGKPVGRIGIngRRlmGAGFVPEERHgh 341
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLeeitSGDLIV---DGLKVNDPKVDERLI--RQ--EAGMVFQQFY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 342 aAVPGMSLSDNLllararsdrkAFltgGFLRiVRGSViKAAARRISETMdVRKSG----ADPLAGSLSGGNLQKFIVGRE 417
Cdd:PRK09493 88 -LFPHLTALENV----------MF---GPLR-VRGAS-KEEAEKQAREL-LAKVGlaerAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 418 LDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLS-DAHPVE 488
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAeDGDPQV 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-481 |
1.64e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.74 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYN-----NDAIHLRGKPVGRI-GINGRRLMGAGFVPEErhgha 342
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvDGKVLYFGKDIFQIdAIKLRKEVGMVFQQPN----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 343 AVPGMSLSDNL---LLARARSDRKAFltggflrivrGSVIKAAARRISETMDVRKSGADPlAGSLSGGNLQKFIVGRELD 419
Cdd:PRK14246 101 PFPHLSIYDNIaypLKSHGIKEKREI----------KKIVEECLRKVGLWKEVYDRLNSP-ASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 420 RQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAgSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
267-481 |
1.72e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.77 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 267 VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEY-PvyNNDAIHLRGKPV---GRIGINGRRLMGAGFvpeerhgha 342
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkP--TSGEVLIKGEPIkydKKSLLEVRKTVGIVF--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 343 avpgmSLSDNLLLARARSDRKAFltgGFLRIvrGSVIKAAARRISETMD-VRKSGADPLA-GSLSGGNLQKFIVGRELDR 420
Cdd:PRK13639 85 -----QNPDDQLFAPTVEEDVAF---GPLNL--GLSKEEVEKRVKEALKaVGMEGFENKPpHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 421 QPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
268-481 |
2.41e-07 |
|
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: 51.38 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSG-EYPvynnDAihlrgkpvGRIGINGRRLMGAGF-VPEERHGHAAV- 344
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEP----DS--------GTIIIDGLKLTDDKKnINELRQKVGMVf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 345 ------PGMSLSDNLLLArarsdrkafltggfLRIVRGsVIKAAARRISETMdVRKSG----ADPLAGSLSGGNLQKFIV 414
Cdd:cd03262 83 qqfnlfPHLTVLENITLA--------------PIKVKG-MSKAEAEERALEL-LEKVGladkADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 415 GRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-201 |
2.70e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEgdiiwqgqpvsvgSPSEARRLGIGMVFQHFSLFEAlTVAENIAL 101
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-------------TSSVVIRGSVAYVPQVSWIFNA-TVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SLDPKISLKEIAGQAEKLSraYGLPLDPNAHVADL-------SVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKL 174
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQ--HDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180 190
....*....|....*....|....*....|
gi 1609612952 175 FETLEKLKAEGRSVLYIS---HRLEEVQRI 201
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVTnqlHFLPLMDRI 809
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-196 |
4.49e-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: 52.99 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 4 LSVRKLTKLF--GNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGvLAPTEGDIIWQGqpVSVGSPS-EARRLGI 80
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDG--VSWNSVTlQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 81 GMVFQHFSLFEAlTVAENialsLDP--KISLKEIAGQAEKL---SRAYGLPLDPNAHVAD----LSVGERQRIEIVRALL 151
Cdd:TIGR01271 1295 GVIPQKVFIFSG-TFRKN----LDPyeQWSDEEIWKVAEEVglkSVIEQFPDKLDFVLVDggyvLSNGHKQLMCLARSIL 1369
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1609612952 152 QNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGrSVLYISHRLE 196
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEHRVE 1413
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
404-481 |
4.95e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.77 E-value: 4.95e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-204 |
5.53e-07 |
|
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: 50.72 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVkmlFGVLApTEGdiiwQGQPVSVGSPSEARRLGiGMVFQHFSLFEALTVAeniaL 101
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLA---FDTIY-AEG----QRRYVESLSAYARQFLG-QMDKPDVDSIEGLSPA----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 102 SLDPKI----------SLKEI----------AGQAEKLSRAYGLPLD---PNAHVADLSVGERQRIEIVRALLQNPR--L 156
Cdd:cd03270 81 AIDQKTtsrnprstvgTVTEIydylrllfarVGIRERLGFLVDVGLGyltLSRSAPTLSGGEAQRIRLATQIGSGLTgvL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRlEEVQRICDR 204
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADH 207
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
268-501 |
8.22e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGeypVYNNDA--IHLRGKPVGRIGINGRRLMGAGFVPEERHghaAVP 345
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG---IYQKDSgsILFQGKEIDFKSSKEALENGISMVHQELN---LVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 346 GMSLSDNLLLARarsdrkaFLTGGFLriVRGSVIKAAARRISETMDVRKSGADPLAgSLSGGNLQKFIVGRELDRQPAVL 425
Cdd:PRK10982 87 QRSVMDNMWLGR-------YPTKGMF--VDQDKMYRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 426 VVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKMTLEKIGLLMGG 501
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
404-481 |
1.09e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.21 E-value: 1.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-203 |
1.12e-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: 49.92 E-value: 1.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609612952 136 LSVGERQRIEIVRALLQ---NPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLeEVQRICD 203
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCAD 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
247-512 |
1.29e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.88 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 247 LGAPQIEVMGLSVAPRTPFAvALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDaIHLRGKPVGRiginGR 326
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK-ISILGQPTRQ----AL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 327 RLMGAGFVPEERHGHAAVPGMsLSDNLLLARarsdrkaFLTGGFLRIVRG---SVIKAAARRIsETMDVRKSGAdplaGS 403
Cdd:PRK15056 76 QKNLVAYVPQSEEVDWSFPVL-VEDVVMMGR-------YGHMGWLRRAKKrdrQIVTAALARV-DMVEFRHRQI----GE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSD 483
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222
|
250 260 270
....*....|....*....|....*....|.
gi 1609612952 484 AHPVEKMTLEKIGLLMGGI--HTSHSGAAQH 512
Cdd:PRK15056 223 GPTETTFTAENLELAFSGVlrHVALNGSEES 253
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
251-481 |
1.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 251 QIEVMGLSVAPRTPFAV-ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYP-----------VYNNDAIHLRGKPV 318
Cdd:PRK13643 3 KFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQptegkvtvgdiVVSSTSKQKEIKPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 319 grigingRRLMGAGFvpeerhghaAVPGMSLSDNLLLARArsdrkAFLTGGFlRIVRGSVIKAAARRIsETMDVRKSGAD 398
Cdd:PRK13643 83 -------RKKVGVVF---------QFPESQLFEETVLKDV-----AFGPQNF-GIPKEKAEKIAAEKL-EMVGLADEFWE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 399 PLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISD 478
Cdd:PRK13643 140 KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEK 219
|
...
gi 1609612952 479 GKL 481
Cdd:PRK13643 220 GHI 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
269-481 |
1.72e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.12 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPvYNNDAIHLRGKPVGRIGINGRRLMGAGFVPEERhghAAVPGMS 348
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIIDDEDISLLPLHARARRGIGYLPQEA---SIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 349 LSDNLLlararsdrkafltgGFLRIVRGSVIKAAARRISETMD------VRksgaDPLAGSLSGGNLQKFIVGRELDRQP 422
Cdd:PRK10895 95 VYDNLM--------------AVLQIRDDLSAEQREDRANELMEefhiehLR----DSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 423 AVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
248-490 |
2.56e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.94 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 248 GAPQIEVMGLSVAprtpFA--VALKSISMTVRAGEVLAIAGVAGNGQ-------GELFDALSGEYpvYNNDAIhLRGKPV 318
Cdd:PRK14271 18 AAPAMAAVNLTLG----FAgkTVLDQVSMGFPARAVTSLMGPTGSGKttflrtlNRMNDKVSGYR--YSGDVL-LGGRSI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 319 --GRIGINGRRLMGAGFvpeERHGhaAVPgMSLSDNLLL---ARARSDRKAFLTGGFLRIVRGSVIKAAARRISETmdvr 393
Cdd:PRK14271 91 fnYRDVLEFRRRVGMLF---QRPN--PFP-MSIMDNVLAgvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDS---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 394 ksgadPLagSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSaVIVISQDLDEIFEVATNI 473
Cdd:PRK14271 161 -----PF--RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISDRA 232
|
250
....*....|....*..
gi 1609612952 474 AVISDGKLSDAHPVEKM 490
Cdd:PRK14271 233 ALFFDGRLVEEGPTEQL 249
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
83-295 |
2.72e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 83 VFQHFSLFEALTVAENIALSLDPkiSLKEIAgqaEKLSRAY--GLP-LDPNAHVADLSVGERQRIEIVRALlqNPRLI-- 157
Cdd:TIGR00630 438 IREAHEFFNQLTLTPEEKKIAEE--VLKEIR---ERLGFLIdvGLDyLSLSRAAGTLSGGEAQRIRLATQI--GSGLTgv 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 158 --ILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRlEEVQRICDRATVL-----RHGKVTGACDPRRE---TPASL 227
Cdd:TIGR00630 511 lyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYVIDIgpgagEHGGEVVASGTPEEilaNPDSL 589
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 228 armmvgsdvasvsraTGEAL-GAPQIEVMGLSVAPRTPFAVA-------LKSISMTVRAGEVLAIAGVAGNGQGEL 295
Cdd:TIGR00630 590 ---------------TGQYLsGRKKIEVPAERRPGNGKFLTLkgarennLKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
249-488 |
3.10e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 49.45 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 249 APQIEVMGLSVAprtpFA--VALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGeypVYNNDA--IHLRGKPVGRIGIN 324
Cdd:PRK09536 1 MPMIDVSDLSVE----FGdtTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING---TLTPTAgtVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 325 --GRRLmgagfvpeerhghAAVP-GMSLSDNLLLARARSDRKAFLTGGFLRIvrGSVIKAAARRISETMDVRKSGADPLA 401
Cdd:PRK09536 74 aaSRRV-------------ASVPqDTSLSFEFDVRQVVEMGRTPHRSRFDTW--TETDRAAVERAMERTGVAQFADRPVT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 402 gSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK09536 139 -SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
....*..
gi 1609612952 482 SDAHPVE 488
Cdd:PRK09536 218 RAAGPPA 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-228 |
3.36e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 136 LSVGERQRIEIVRALL---QNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLEEVqRICDRATVL---- 208
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELgpeg 888
|
90 100
....*....|....*....|....*.
gi 1609612952 209 --RHGKVTGACDPR----RETPASLA 228
Cdd:PRK00635 889 gnLGGYLLASCSPEelihLHTPTAKA 914
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
249-488 |
4.66e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 249 APQIEVMGLSVapRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEY-PvyNNDAIHLRGKPVGriGINGRR 327
Cdd:PRK11300 3 QPLLSVSGLMM--RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkP--TGGTILLRGQHIE--GLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 328 LMGAGFVPEERHGHaAVPGMSLSDNLLLARARSDRKAFLTG-----GFLRIVRGSVIKAAARRisETMDVRKSgADPLAG 402
Cdd:PRK11300 77 IARMGVVRTFQHVR-LFREMTVIENLLVAQHQQLKTGLFSGllktpAFRRAESEALDRAATWL--ERVGLLEH-ANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 403 SLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQDLDEIFEVATNIAVISDGK- 480
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTp 232
|
....*...
gi 1609612952 481 LSDAHPVE 488
Cdd:PRK11300 233 LANGTPEE 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
268-501 |
5.58e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVyNNDAIHLRGKPVGRIGINGRRLMGAGFVPEERhghAAVPGM 347
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYNKLDHKLAAQLGIGIIYQEL---SVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 348 SLSDNLLLARARSdRKAFltggFLRIVRGSVIKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQPAVLVV 427
Cdd:PRK09700 96 TVLENLYIGRHLT-KKVC----GVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 428 NQPTwgvdagaaSRIRQALVD--------LAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKMTLEKIGLLM 499
Cdd:PRK09700 170 DEPT--------SSLTNKEVDylflimnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
..
gi 1609612952 500 GG 501
Cdd:PRK09700 242 VG 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-201 |
5.90e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTE-GDIIWQGQpvsvgspsearrlgIGMVFQHFSLFEAlTVAENIA 100
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT--------------VAYVPQVSWIFNA-TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDPKISLKEIAGQAEKLSRayGLPLDPNAHVAD-------LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:PLN03130 701 FGSPFDPERYERAIDVTALQH--DLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
|
170 180 190
....*....|....*....|....*....|.
gi 1609612952 174 LFETLEKLKAEGRSVLYIS---HRLEEVQRI 201
Cdd:PLN03130 779 VFDKCIKDELRGKTRVLVTnqlHFLSQVDRI 809
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
252-481 |
6.28e-06 |
|
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: 46.44 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 252 IEVMGLSVAPRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVyNNDAIHLRGKPVGRIGINGRRLMgA 331
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP-TSGRVRLDGADISQWDPNELGDH-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 332 GFVPEerhghaavpgmslsDNLLLArarsdrkafltggflrivrGSVikaaARRIsetmdvrksgadplagsLSGGNLQK 411
Cdd:cd03246 79 GYLPQ--------------DDELFS-------------------GSI----AENI-----------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 412 FIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLdEIFEVATNIAVISDGKL 481
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
252-480 |
6.48e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 47.53 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 252 IEVMGLSVA-PRTPFAVALKSISMTVRAGEVLAIAGVAGNGQG-------ELFDALSGEypvynndaIHLRGKPVGRIGI 323
Cdd:cd03249 1 IEFKNVSFRyPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKStvvslleRFYDPTSGE--------ILLDGVDIRDLNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 324 NG-RRLMGagFVPEErhghaavP---GMSLSDNLLLARARSDRkafltggflrivrgSVIKAAARR------ISETMDvr 393
Cdd:cd03249 73 RWlRSQIG--LVSQE-------PvlfDGTIAENIRYGKPDATD--------------EEVEEAAKKanihdfIMSLPD-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 394 ksGADPLAG----SLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALvDLAKAGSAVIVISQDLDEIfEV 469
Cdd:cd03249 128 --GYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLSTI-RN 203
|
250
....*....|.
gi 1609612952 470 ATNIAVISDGK 480
Cdd:cd03249 204 ADLIAVLQNGQ 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
401-490 |
8.00e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 401 AGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIViSQDLDEIFEVATNIAVISDGK 480
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGK 225
|
90
....*....|
gi 1609612952 481 LSDAHPVEKM 490
Cdd:PRK14267 226 LIEVGPTRKV 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
269-490 |
1.14e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSG-EYP-----VYNNDAIHLRGKPVGRIGI---NGRRLMGAGFVPEERH 339
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlEKPsegsiVVNGQTINLVRDKDGQLKVadkNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 340 ----GHaavpgMSLSDNLLLARARsdrkafltggFLRIVRGSVIKAAARRISET-MDVRKSGADPLagSLSGGNLQKFIV 414
Cdd:PRK10619 101 fnlwSH-----MTVLENVMEAPIQ----------VLGLSKQEARERAVKYLAKVgIDERAQGKYPV--HLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 415 GRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKM 490
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
268-485 |
2.09e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSG-EYPvynndaihlrgkPVGRIGINGRRLmgagfvpeERHGHAAVP- 345
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERP------------SAGKIWFSGHDI--------TRLKNREVPf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 346 -----GMSLSDNLLLArarsDRKAFLTGGFLRIVRGSVIKAAARRISETMD----VRKSGADPLagSLSGGNLQKFIVGR 416
Cdd:PRK10908 77 lrrqiGMIFQDHHLLM----DRTVYDNVAIPLIIAGASGDDIRRRVSAALDkvglLDKAKNFPI--QLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 417 ELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAH 485
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-214 |
2.11e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDiARgeiHALLGENGAGKSTLVKMLFGVLAPTEGDIIwqgqpvsvgspsEARRLGIGMVFQHFslfealtvAENIA 100
Cdd:PLN03073 531 GIDLD-SR---IAMVGPNGIGKSTILKLISGELQPSSGTVF------------RSAKVRMAVFSQHH--------VDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 LSLDPKISL-KEIAGQAEKLSRAY--------GLPLDPnahVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEA 171
Cdd:PLN03073 587 LSSNPLLYMmRCFPGVPEQKLRAHlgsfgvtgNLALQP---MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1609612952 172 DKLFETLEKLKAegrSVLYISHRLEEVQRICDRATVLRHGKVT 214
Cdd:PLN03073 664 EALIQGLVLFQG---GVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
268-479 |
2.16e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.23 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 268 ALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPvYNNDAIHLRGKPVGriGINGRRlmgaGFVPEErhgHAAVPGM 347
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP-YQHGSITLDGKPVE--GPGAER----GVVFQN---EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 348 SLSDN----LLLARARSDRKAFLTGGFLRIVrgSVIKAAARRISEtmdvrksgadplagsLSGGNLQKFIVGRELDRQPA 423
Cdd:PRK11248 86 NVQDNvafgLQLAGVEKMQRLEIAHQMLKKV--GLEGAEKRYIWQ---------------LSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 424 VLVVNQPTWGVDAGAASRIRQALVDL-AKAGSAVIVISQDLDEIFEVATNIAVISDG 479
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-194 |
2.26e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 29 GEIHALLGENGAGKSTLVKMLFG--VLAPTEGDIIWQGQP--------VS-------VGSPSEARRLGigMVFQHFSLFE 91
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGFPkkqetfarISgyceqndIHSPQVTVRES--LIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 92 ALTVAENIALSLDPKISLKEIagqaEKLSRA-YGLPldpnaHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQE 170
Cdd:PLN03140 984 KEVSKEEKMMFVDEVMELVEL----DNLKDAiVGLP-----GVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180
....*....|....*....|....
gi 1609612952 171 ADKLFETLEKLKAEGRSVLYISHR 194
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
272-493 |
2.33e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.34 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 272 ISMTVRAGEVLAIAGVAGNGQGELFDALSG-EYPvyNNDAIHLRGKPVGRIGINGRrlMGAGFVPEERHghaAVPGMSLS 350
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHP--DAGSISLCGEPVPSRARHAR--QRVGVVPQFDN---LDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 351 DNLLLararsdrkafltggFLRIVrGSVIKAAARRISETMDVRK--SGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVN 428
Cdd:PRK13537 99 ENLLV--------------FGRYF-GLSAAAARALVPPLLEFAKleNKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609612952 429 QPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDG-KLSDAHPVEKMTLE 493
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHALIESE 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
261-481 |
2.40e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.02 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 261 PRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYpVYNNDAIHLRGKPVGRIgiNGRRLmgagfvpeerHG 340
Cdd:TIGR00958 489 PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-QPTGGQVLLDGVPLVQY--DHHYL----------HR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 341 HAAVPGmslSDNLLLARARSDRKAF-LTGGFLRIVRGSVIKAAARR-ISETMDVRKSGADPLAGSLSGGNLQKFIVGREL 418
Cdd:TIGR00958 556 QVALVG---QEPVLFSGSVRENIAYgLTDTPDEEIMAAAKAANAHDfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 419 DRQPAVLVVNQPTWGVDAgaasRIRQALVDLAKAGS-AVIVISQDLDEIfEVATNIAVISDGKL 481
Cdd:TIGR00958 633 VRKPRVLILDEATSALDA----ECEQLLQESRSRASrTVLLIAHRLSTV-ERADQILVLKKGSV 691
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
250-495 |
2.87e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.80 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 250 PQIEVMGLSVAPRTpfAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALS------GEYPV-----YNNDAIHLRgkpv 318
Cdd:PRK14258 6 PAIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVegrveFFNQNIYER---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 319 gRIGINGRRLMGAGFVPEERhghaAVPgMSLSDNLLLARArsdrkafLTGGFLRIVRGSVIKAAARRiSETMDVRKSGAD 398
Cdd:PRK14258 80 -RVNLNRLRRQVSMVHPKPN----LFP-MSVYDNVAYGVK-------IVGWRPKLEIDDIVESALKD-ADLWDEIKHKIH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 399 PLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLA-KAGSAVIVISQDLDEIFEVATNIAVIS 477
Cdd:PRK14258 146 KSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
250
....*....|....*...
gi 1609612952 478 DGKLSDAHPVEKMTLEKI 495
Cdd:PRK14258 226 GNENRIGQLVEFGLTKKI 243
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-195 |
3.13e-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: 3.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 136 LSVGERQRIEIVRALLQ---NPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRL 195
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-458 |
3.19e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.67 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALsgeypvynNDAIHLRGKP--VGRIGINGRRLMGAGFVPEERHGHAA--- 343
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVF--------NRLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVfqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 344 ---VPGMSLSDNLLLArARSDRKAFLTGGFLRIVRGSVIKAaarrisETMDVRKSGADPLAGSLSGGNLQKFIVGRELDR 420
Cdd:PRK14247 91 pnpIPNLSIFENVALG-LKLNRLVKSKKELQERVRWALEKA------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1609612952 421 QPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIV 458
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLV 201
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-169 |
4.61e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 2 PLLSVRKLTKLFGNFAACNGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSVGSpseaRRLGIG 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 82 MVFQHFSLFEALTVAENIA-LSLDPKISLKEIAGQAEKLsraYGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILD 160
Cdd:PRK13543 86 YLGHLPGLKADLSTLENLHfLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
....*....
gi 1609612952 161 EPTSVLTPQ 169
Cdd:PRK13543 163 EPYANLDLE 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
250-495 |
5.02e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.15 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 250 PQIEVMGLSVapRTPFAVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNndaihlrgkpvGRIGINGRRLm 329
Cdd:PRK13548 1 AMLEARNLSV--RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS-----------GEVRLNGRPL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 330 gAGFVPEERHGHAAVpgMSLSDNLllararsdrkAFltgGFL--------RIVRGSVIKAAARRISETMdvRKSGADPLA 401
Cdd:PRK13548 67 -ADWSPAELARRRAV--LPQHSSL----------SF---PFTveevvamgRAPHGLSRAEDDALVAAAL--AQVDLAHLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 402 G----SLSGGNLQKFIVGREL------DRQPAVLVVNQPTwgvdagAASRIR--QALVDLAK-----AGSAVIVISQDLD 464
Cdd:PRK13548 129 GrdypQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPT------SALDLAhqHHVLRLARqlaheRGLAVIVVLHDLN 202
|
250 260 270
....*....|....*....|....*....|..
gi 1609612952 465 EIFEVATNIAVISDGKL-SDAHPVEKMTLEKI 495
Cdd:PRK13548 203 LAARYADRIVLLHQGRLvADGTPAEVLTPETL 234
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
136-194 |
5.72e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 5.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 136 LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLEKLkaeGRSVLYISHR 194
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSHR 638
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
399-466 |
7.19e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 7.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 399 PLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLA-KAGSAVIVISQDLDEI 466
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI 1422
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
251-488 |
9.65e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.92 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 251 QIEVMGLSVAPRTPFavaLKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPV---YNNDAIHLRGKPVGRIGINGRR 327
Cdd:PRK10418 4 QIELRNIALQAAQPL---VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVAPCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 328 LmgAGFVPEERHGHAAVPGM-SLSDNLLLARARSDRKAFLtggfLRIVRGsVIKAAARRIsetmdvrksgADPLAGSLSG 406
Cdd:PRK10418 81 I--ATIMQNPRSAFNPLHTMhTHARETCLALGKPADDATL----TAALEA-VGLENAARV----------LKLYPFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 407 GNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDL-AKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAH 485
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
...
gi 1609612952 486 PVE 488
Cdd:PRK10418 224 DVE 226
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-196 |
1.20e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 21 GIDLDIARGEIHALLGENGAGKSTLVKmlfgvlaptegDIIWqgqpvsvgspsearrlGIGMVFQHFSLFEALTVAENIA 100
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGL----------------ALGGAQSATRRRSGVKAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 101 L-SLDPKISLKEI-AGQAEKLSRAYGLPLdpnahvadlsvgerqrieivrALLQNPRLIILDEPTSVLTPQEADKLFETL 178
Cdd:cd03227 66 AvSAELIFTRLQLsGGEKELSALALILAL---------------------ASLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170
....*....|....*...
gi 1609612952 179 EKLKAEGRSVLYISHRLE 196
Cdd:cd03227 125 LEHLVKGAQVIVITHLPE 142
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-193 |
1.43e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 125 LPLDPNahVADLSVGERQRIEIVRALLQNPR---LIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISH 193
Cdd:PRK00635 1691 LPLGQN--LSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDH 1760
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
383-497 |
1.43e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.84 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 383 ARRISETM---DVRKSGADPLAgSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVI 459
Cdd:PRK13638 114 TRRVDEALtlvDAQHFRHQPIQ-CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS 192
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1609612952 460 SQDLDEIFEVATNIAVISDGK-LSDAHPVEKM----TLEKIGL 497
Cdd:PRK13638 193 SHDIDLIYEISDAVYVLRQGQiLTHGAPGEVFacteAMEQAGL 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
252-497 |
1.88e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.50 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 252 IEVMGLS--VAPRTPFA-VALKSISMTVRAGEVLAIAGVAGNGQGELFDalsgeypvynndaiHLRG--KPV-GRIGING 325
Cdd:PRK13637 3 IKIENLThiYMEGTPFEkKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQ--------------HLNGllKPTsGKIIIDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 326 -------------RRLMGAGF-VPE--------ERHGHAAVPGMSLSDNLLLARarsdrkafltggflrivrgsvIKAAA 383
Cdd:PRK13637 69 vditdkkvklsdiRKKVGLVFqYPEyqlfeetiEKDIAFGPINLGLSEEEIENR---------------------VKRAM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 384 RRISETMDVRKsgaDPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQD 462
Cdd:PRK13637 128 NIVGLDYEDYK---DKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHS 204
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1609612952 463 LDEIFEVATNIAVISDGKLS-DAHPVEKM----TLEKIGL 497
Cdd:PRK13637 205 MEDVAKLADRIIVMNKGKCElQGTPREVFkeveTLESIGL 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
404-481 |
1.91e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 1.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
266-481 |
1.99e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.07 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 266 AVALKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPvYNndaihlrgkpvGRIGINGRRLmgAGFVPEERHGHAA-- 343
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQ-----------GSLKINGIEL--RELDPESWRKHLSwv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 344 -----VPGMSLSDNLLLARARSDRKAfltggflrivrgsvIKAAARR--ISETMDVRKSGAD-PL---AGSLSGGNLQKF 412
Cdd:PRK11174 429 gqnpqLPHGTLRDNVLLGNPDASDEQ--------------LQQALENawVSEFLPLLPQGLDtPIgdqAAGLSVGQAQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 413 IVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDlAKAGSAVIVISQDLDEIFEVATnIAVISDGKL 481
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQ-IWVMQDGQI 561
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-210 |
2.03e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 28 RGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIwqgqpvsvgspsearrlgigmvfqhfslfealtvaenialSLDPKI 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------------------YIDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 108 SLKEIAGQAEKLSRayglpldpNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKLFETLE------KL 181
Cdd:smart00382 41 ILEEVLDQLLLIIV--------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLK 112
|
170 180
....*....|....*....|....*....
gi 1609612952 182 KAEGRSVLYISHRLEEVQRICDRATVLRH 210
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
269-463 |
2.26e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.88 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSGEYPVYNNDAIhLRGKPVGRIGINGR---RLMGAGFVPEERHghaAVP 345
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI-FNGQPMSKLSSAAKaelRNQKLGFIYQFHH---LLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 346 GMSLSDN----LLL---ARARSDRKAFltgGFLRIVrgSVIKAAARRISEtmdvrksgadplagsLSGGNLQKFIVGREL 418
Cdd:PRK11629 101 DFTALENvampLLIgkkKPAEINSRAL---EMLAAV--GLEHRANHRPSE---------------LSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1609612952 419 DRQPAVLVVNQPTWGVDAGAASRIRQALVDL-AKAGSAVIVISQDL 463
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-196 |
2.47e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 2.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 136 LSVGERQRIEIVRALL---QNPRLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISHRLE 196
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLD 890
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
269-487 |
4.31e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 42.37 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELFDALSG-EYPVYNNdaIHLRGKPVGRIgingrrlmgagfvpeERHGHAAVPG- 346
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQGN--VSWRGEPLAKL---------------NRAQRKAFRRd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 347 --MSLSDNLLLARARSDRKAFLtGGFLRIVRGSVIKAAARRISE---TMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQ 421
Cdd:PRK10419 91 iqMVFQDSISAVNPRKTVREII-REPLRHLLSLDKAERLARASEmlrAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 422 PAVLVVNQPTWGVDAGAASRIRQALVDL-AKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPV 487
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-197 |
4.48e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKM--------------LFGVLAPTeGDIIWqgqpvsvgspsEARRlGIGMVFQ 85
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLFGRRRGS-GETIW-----------DIKK-HIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 86 HFSL-FEALTVAENIALS--LDpKISL-KEIAGQAEKLSRAYGLPLDPNAHVAD-----LSVGERQRIEIVRALLQNPRL 156
Cdd:PRK10938 344 SLHLdYRVSTSVRNVILSgfFD-SIGIyQAVSDRQQKLAQQWLDILGIDKRTADapfhsLSWGQQRLALIVRALVKHPTL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1609612952 157 IILDEPTSVLTPQEADKLFETLEKLKAEGRS-VLYISHRLEE 197
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAED 464
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
404-483 |
4.95e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLA-KAGSAVIVISQDLDEIFEVATNIAVISDGKLS 482
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
.
gi 1609612952 483 D 483
Cdd:PRK13646 226 S 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-193 |
4.98e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 36 GENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVsvgspSEARRLGIGMVFQHFSLFEALTVAENIALsldpkisLKEIAGQ 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-----NNIAKPYCTYIGHNLGLKLEMTVFENLKF-------WSEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 116 AEKLSRA---YGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTpQEADKLFETLEKLKA-EGRSVLYI 191
Cdd:PRK13541 101 AETLYAAihyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKAnSGGIVLLS 179
|
..
gi 1609612952 192 SH 193
Cdd:PRK13541 180 SH 181
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-198 |
5.59e-04 |
|
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: 41.82 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 26 IARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDIIWQGQPVSvGSPSEARRLGIGMVFQHFSLFEAltvaeNIALSLDP 105
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-KLPLHTLRSRLSIILQDPILFSG-----SIRFNLDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 106 KISLK--------EIAgQAEKLSRAygLPLDPNAHVAD----LSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADK 173
Cdd:cd03288 118 ECKCTddrlwealEIA-QLKNMVKS--LPGGLDAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180
....*....|....*....|....*
gi 1609612952 174 LFETLEKLKAEgRSVLYISHRLEEV 198
Cdd:cd03288 195 LQKVVMTAFAD-RTVVTIAHRVSTI 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
365-508 |
7.33e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 365 FLTGGFLRIVRGSViKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQ 444
Cdd:NF000106 108 YMIGR*LDLSRKDA-RARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWD 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1609612952 445 ALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLSDAHPVEKMTlEKIGLLMGGIHTSHSG 508
Cdd:NF000106 186 EVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK-TKVGGRTLQIRPAHAA 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
269-462 |
1.20e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.53 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 269 LKSISMTVRAGEVLAIAGVAGNGQGELF-------DALSGEypvynndaIHLRGKPVGRIGINGRRLMGA---GFVPEEr 338
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLailagldDGSSGE--------VSLVGQPLHQMDEEARAKLRAkhvGFVFQS- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 339 hgHAAVPGMSLSDNL---LLARARSDRKAfltggflrivrgsviKAAARRISETMDVRKSgADPLAGSLSGGNLQKFIVG 415
Cdd:PRK10584 97 --FMLIPTLNALENVelpALLRGESSRQS---------------RNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1609612952 416 RELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKA-GSAVIVISQD 462
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
404-482 |
1.41e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKLS 482
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
281-489 |
1.42e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.01 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 281 VLAIAGVAGNGQGELFDALSGeypvynndaihLRGKPVGRIGINGRRL----MGAGFVPEERH------GHAAVPGMSLS 350
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISG-----------LTRPQKGRIVLNGRVLfdaeKGICLPPEKRRigyvfqDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 351 DNLLLARARSDRkafltGGFLRIVRGSVIKAAARRisetmdvrksgadpLAGSLSGGNLQKFIVGRELDRQPAVLVVNQP 430
Cdd:PRK11144 95 GNLRYGMAKSMV-----AQFDKIVALLGIEPLLDR--------------YPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609612952 431 TWGVDAgaaSRIRQALVDLAKAGSAV----IVISQDLDEIFEVATNIAVISDGKLSDAHPVEK 489
Cdd:PRK11144 156 LASLDL---PRKRELLPYLERLAREInipiLYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
8-60 |
1.76e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609612952 8 KLTKL----FGNFAACNgIDLDIARGeIHALLGENGAGKSTLVKMLFGVLAPTEGDI 60
Cdd:COG3950 2 RIKSLtienFRGFEDLE-IDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
404-463 |
1.81e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.10 E-value: 1.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAasriRQALVDL-----AKAGSAVIVISQDL 463
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG----QVALYDLidqlrRELDCAVLMVSHDL 181
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
404-490 |
2.02e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGS-AVIVISQDLDEIFEVATNIAVISDGKLS 482
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 1609612952 483 DAHPVEKM 490
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-292 |
3.13e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 22 IDLDIARGEIHALLGENGAGKSTLVKMLFGVLAPTEGDiIWqgqpvsvgspseARRlGIGMVFQHFSLFEAlTVAENI-- 99
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-VW------------AER-SIAYVPQQAWIMNA-TVRGNIlf 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 100 -----ALSLDPKISLKEIAGQAEKLSRayGLPLDPNAHVADLSVGERQRIEIVRALLQNPRLIILDEPTSVLTPQEADKL 174
Cdd:PTZ00243 744 fdeedAARLADAVRVSQLEADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 175 FETLEKLKAEGRSVLYISHRLEEVQRiCDRATVLRHGKVTGACDPRRETPASLARMMVGSDVASVSRATGEAlgapQIEV 254
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKENKDSKEGDA----DAEV 896
|
250 260 270
....*....|....*....|....*....|....*...
gi 1609612952 255 MGLSVAPRTPFAVALKSISMTVRAGEVLAIAGVAGNGQ 292
Cdd:PTZ00243 897 AEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGR 934
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
132-193 |
3.44e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 3.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609612952 132 HVADLSVGERQRIEIVRAL-----LQNP-----RLIILDEPTSVLTPQEADKLFETLEKLKAEGRSVLYISH 193
Cdd:cd03279 120 PVSTLSGGETFLASLSLALalsevLQNRggarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
385-482 |
3.90e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 385 RISETMDVRKSGADPLAGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLakAGSaVIVISQDLD 464
Cdd:PRK11147 138 RINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGS-IIFISHDRS 214
|
90
....*....|....*...
gi 1609612952 465 EIFEVATNIAVISDGKLS 482
Cdd:PRK11147 215 FIRNMATRIVDLDRGKLV 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
404-481 |
4.71e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 38.96 E-value: 4.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1609612952 404 LSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLAKAGSAVIVISQDLDEIFEVATNIAVISDGKL 481
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
401-493 |
4.72e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.99 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 401 AGSLSGGNLQKFIVGRELDRQPAVLVVNQPTWGVDAGAASRIRQALVDLaKAGSAVIVISQDLDEIFEVATNIAVISDGK 480
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGD 224
|
90
....*....|...
gi 1609612952 481 LSDAHPVEKMTLE 493
Cdd:PRK14239 225 LIEYNDTKQMFMN 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-166 |
5.74e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 34 LLGENGAGKSTLVKMLFGVLAPTEGDiiwqgqpVSVgSPSEarRLG--------------IGMVFQ-HFSLFEALTVAEN 98
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGN-------VSL-DPNE--RLGklrqdqfafeeftvLDTVIMgHTELWEVKQERDR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609612952 99 I-AL---SLDPKISLKEIAGQ--------AEklSRA------YGLPLD----PNAHVADlsvGERQRIEIVRALLQNPRL 156
Cdd:PRK15064 102 IyALpemSEEDGMKVADLEVKfaemdgytAE--ARAgelllgVGIPEEqhygLMSEVAP---GWKLRVLLAQALFSNPDI 176
|
170
....*....|
gi 1609612952 157 IILDEPTSVL 166
Cdd:PRK15064 177 LLLDEPTNNL 186
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-55 |
8.26e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 8.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1609612952 20 NGIDLDIARGEIHALLGENGAGKSTLVKMLFGVLAP 55
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| |
