|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-506 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 732.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKR 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR-SPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQSSGlFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLGREPRRGG-LIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVG 241
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 242 RDVVfNRRPPSetHHQDKPVRLAVKGLSREKppldahgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSG 321
Cdd:COG1129 239 RELE-DLFPKR--AAAPGEVVLEVEGLSVGG--------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 322 EFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRWRWfVNTRKEDDLIDAYRQALHIKMV 401
Cdd:COG1129 308 EIRLDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGL-LDRRRERALAEEYIKRLRIKTP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 402 NSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIIT 481
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILV 466
|
490 500
....*....|....*....|....*
gi 504513498 482 LSEGRISGEIHGDDATEEKLMTMMA 506
Cdd:COG1129 467 MREGRIVGELDREEATEEAIMAAAT 491
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-504 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 539.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLlESPVERQKR 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF-ASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQSSGlFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGQLPHKGG-IVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGS-GDVASTNVQEIIRLMV 240
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQAMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 241 GRDV--VFNRRPpsethHQDKPVRLAVKGLSrekppldahGIALK-DISFQVHAGEVLGIAGLVGAGRTEIARCLFGADG 317
Cdd:PRK11288 239 GREIgdIYGYRP-----RPLGEVRLRLDGLK---------GPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 318 FSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRWRWFVNTRKEDDLIDAYRQALH 397
Cdd:PRK11288 305 RTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 398 IKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISD 477
Cdd:PRK11288 385 IKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVAD 464
|
490 500
....*....|....*....|....*..
gi 504513498 478 RIITLSEGRISGEIHGDDATEEKLMTM 504
Cdd:PRK11288 465 RIVVMREGRIAGELAREQATERQALSL 491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-503 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 519.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTS--GDIWFGGQQLLLlESPVER 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQA-SNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRGIITIYQEFNLLPNMSVAENMFLGREPQSSGLfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARAL 158
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEITPGGI-MDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 159 TLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRL 238
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 239 MVGRDVvfNRRPPSETHHQDKPVrLAVKGLSREKPpLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGA-DG 317
Cdd:PRK13549 239 MVGREL--TALYPREPHTIGEVI-LEVRNLTAWDP-VNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 318 FSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRWRwFVNTRKEDDLIDAYRQALH 397
Cdd:PRK13549 315 RWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGS-RIDDAAELKTILESIQRLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 398 IKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISD 477
Cdd:PRK13549 394 VKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSD 473
|
490 500
....*....|....*....|....*.
gi 504513498 478 RIITLSEGRISGEIHGDDATEEKLMT 503
Cdd:PRK13549 474 RVLVMHEGKLKGDLINHNLTQEQVME 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-506 |
7.67e-178 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 509.57 E-value: 7.67e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLlESPVERQK 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI-RSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAENMFLGREPqSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTL 160
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLEP-TKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 161 NAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMV 240
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 241 GRDVVFNRRPPSethHQDKPVRLAVKGLSREKpplDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSS 320
Cdd:COG3845 239 GREVLLRVEKAP---AEPGEVVLEVENLSVRD---DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 321 GEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNL-SSLMRWRWFVNTRKE----DDLIDAYRqa 395
Cdd:COG3845 313 GSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYrRPPFSRGGFLDRKAIrafaEELIEEFD-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 396 lhIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAI 475
Cdd:COG3845 391 --VRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILAL 468
|
490 500 510
....*....|....*....|....*....|.
gi 504513498 476 SDRIITLSEGRISGEIHGDDATEEKLMTMMA 506
Cdd:COG3845 469 SDRIAVMYEGRIVGEVPAAEATREEIGLLMA 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-502 |
2.37e-170 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 490.29 E-value: 2.37e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLlESPVERQKR 81
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF-NGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVG 241
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 242 RDVVfNRRPPSETHHQDkpVRLAVKGLSrekppldahGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSG 321
Cdd:PRK10762 240 RKLE-DQYPRLDKAPGE--VRLKVDNLS---------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 322 EFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRWRWFVNTRKEDDLIDAYRQALHIKMV 401
Cdd:PRK10762 308 YVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 402 NSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIIT 481
Cdd:PRK10762 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILV 467
|
490 500
....*....|....*....|.
gi 504513498 482 LSEGRISGEIHGDDATEEKLM 502
Cdd:PRK10762 468 MHEGRISGEFTREQATQEKLM 488
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-505 |
1.28e-167 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 483.52 E-value: 1.28e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTS--GDIWFGGQqllllespvERQ--- 79
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE---------VCRfkd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 80 -----KRGIITIYQEFNLLPNMSVAENMFLGREPQSSGlFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEI 154
Cdd:NF040905 72 irdseALGIVIIHQELALIPYLSIAENIFLGNERAKRG-VIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 155 ARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQE 234
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADEVTE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 235 --IIRLMVGRDVVfNRRPPSETHHQDkpVRLAVKGLSREKPpLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCL 312
Cdd:NF040905 231 drIIRGMVGRDLE-DRYPERTPKIGE--VVFEVKNWTVYHP-LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 313 FGAD--GFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRwRWFVNTRKEDDLID 390
Cdd:NF040905 307 FGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSR-RGVIDENEEIKVAE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 391 AYRQALHIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLP 470
Cdd:NF040905 386 EYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELP 465
|
490 500 510
....*....|....*....|....*....|....*
gi 504513498 471 EIMAISDRIITLSEGRISGEIHGDDATEEKLMTMM 505
Cdd:NF040905 466 ELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-502 |
7.02e-158 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 458.86 E-value: 7.02e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLEsPVERQK 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAENMFLGREPQSSGL---FVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARA 157
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIGRHLTKKVCgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 158 LTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIR 237
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 238 LMVGRDVV--FNRRPPSETHHQDKPVrLAVKGLSREKPPldahgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGA 315
Cdd:PRK09700 240 LMVGRELQnrFNAMKENVSNLAHETV-FEVRNVTSRDRK------KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 316 DGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRWR--W-FVNTRKEDDLIDAY 392
Cdd:PRK09700 313 DKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKgaMgLFHEVDEQRTAENQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 393 RQALHIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEI 472
Cdd:PRK09700 393 RELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI 472
|
490 500 510
....*....|....*....|....*....|.
gi 504513498 473 MAISDRIITLSEGRISGEI-HGDDATEEKLM 502
Cdd:PRK09700 473 ITVCDRIAVFCEGRLTQILtNRDDMSEEEIM 503
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-502 |
1.85e-144 |
|
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: 424.24 E-value: 1.85e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTS--GDIWFGGQQLLLlESPVERQKRG 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKA-SNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQ-VARLSVAQQQMVEIARALTLN 161
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVG 241
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 242 RDV--VFNRRPpsethHQDKPVRLAVKGLSREKPpLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGA-DGF 318
Cdd:TIGR02633 240 REItsLYPHEP-----HEIGDVILEARNLTCWDV-INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 319 SSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLMRwRWFVNTRKEDDLIDAYRQALHI 398
Cdd:TIGR02633 314 FEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCF-KMRIDAAAELQIIGSAIQRLKV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 399 KMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDR 478
Cdd:TIGR02633 393 KTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDR 472
|
490 500
....*....|....*....|....
gi 504513498 479 IITLSEGRISGEIHGDDATEEKLM 502
Cdd:TIGR02633 473 VLVIGEGKLKGDFVNHALTQEQVL 496
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-506 |
2.13e-142 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 418.75 E-value: 2.13e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLlESPVERQKRGIITIY 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-KSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 QEFNLLPNMSVAENMFLGREPQSsGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVM 167
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTK-GMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 168 DEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVGRDVvfN 247
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSL--T 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 248 RRPPSEThHQDKPVRLAVKGLSREKPPldahgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDD 327
Cdd:PRK10982 237 QRFPDKE-NKPGEVILEVRNLTSLRQP------SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 328 APYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISLSNLSSLM-RWRWFVNTRKEDD---LIDAYRqalhIKMVNS 403
Cdd:PRK10982 310 KKINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKnKVGLLDNSRMKSDtqwVIDSMR----VKTPGH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 404 DQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLS 483
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
490 500
....*....|....*....|...
gi 504513498 484 EGRISGEIHGDDATEEKLMTMMA 506
Cdd:PRK10982 466 NGLVAGIVDTKTTTQNEILRLAS 488
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-504 |
6.03e-135 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 400.58 E-value: 6.03e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRGI 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENMFLG--REPQSSglfvdalavnREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGlpKRQASM----------QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLM-- 239
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 240 ------------VGRDVVFNRRppseTHHQDKPVrLAVKGLSREkppldahgiALKDISFQVHAGEVLGIAGLVGAGRTE 307
Cdd:PRK15439 239 aarekslsasqkLWLELPGNRR----QQAAGAPV-LTVEDLTGE---------GFRNISLEVRAGEILGLAGVVGAGRTE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 308 IARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVLGLSIRENISlsnlsSLMRWR--WFVNTRKE 385
Cdd:PRK15439 305 LAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC-----ALTHNRrgFWIKPARE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 386 DDLIDAYRQALHIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVI 465
Cdd:PRK15439 380 NAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI 459
|
490 500 510
....*....|....*....|....*....|....*....
gi 504513498 466 SSDLPEIMAISDRIITLSEGRISGEIHGDDATEEKLMTM 504
Cdd:PRK15439 460 SSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRL 498
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
260-487 |
8.22e-86 |
|
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: 262.37 E-value: 8.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 260 PVRLAVKGLSREKppldahgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHAL 339
Cdd:cd03215 2 EPVLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 340 SQGIALVPEDRKKEGAVLGLSIRENISLSNLsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrkLSGGNQQKVI 419
Cdd:cd03215 74 RAGIAYVPEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 420 LARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-224 |
2.50e-69 |
|
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: 219.22 E-value: 2.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRGIIT 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-SPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQefnllpnmsvaenmflgrepqssglfvdalavnreakavldylklniapttqvarLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 166 VMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGS 224
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-487 |
3.39e-63 |
|
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: 214.38 E-value: 3.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSG--VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQT---SGDIWFGGQQLLLLeSPVE 77
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL-SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 RQKRgIITIYQEFNLLPNMS-----VAENMFLGREPQSsglfvdalAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMV 152
Cdd:COG1123 81 RGRR-IGMVFQDPMTQLNPVtvgdqIAEALENLGLSRA--------EARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTn 231
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 232 VQEIIRLMVGRDVVFNRRPPSETHHQDKPVrLAVKGLSREKPPLDAHGI-ALKDISFQVHAGEVLGIAGLVGAGRTEIAR 310
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 311 CLFGADGFSSGEFVLDDAPYHPSTP--LHALSQGIALVPED-------RkkegavlgLSIREnislsnlsSLMRWRWFVN 381
Cdd:COG1123 310 LLLGLLRPTSGSILFDGKDLTKLSRrsLRELRRRVQMVFQDpysslnpR--------MTVGD--------IIAEPLRLHG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 382 TRKEDDLIDAYRQALhiKMVNSDQEVRK-----LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMA 456
Cdd:COG1123 374 LLSRAERRERVAELL--ERVGLPPDLADrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQ 451
|
490 500 510
....*....|....*....|....*....|..
gi 504513498 457 KR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1123 452 RElGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-220 |
2.31e-54 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 183.32 E-value: 2.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKR 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-PPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQSSGLFVDAL-----------AVNREAKAVLDYLKLNIAPTTQVARLSVAQQQ 150
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALlrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELK-GRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-220 |
2.33e-52 |
|
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: 177.63 E-value: 2.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRGIIT 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNRE------AKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALT 159
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREErearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 160 LNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-220 |
2.02e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.77 E-value: 2.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVE-RQKRGII 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED--VARDPAEvRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TiyQEFNLLPNMSVAENM-FLGRepqssgLF-VDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNA 162
Cdd:COG1131 79 P--QEPALYPDLTVRENLrFFAR------LYgLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 163 KLIVMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1131 151 ELLILDEPTSGL-DPEaRRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-228 |
7.14e-42 |
|
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: 149.75 E-value: 7.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRG 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREPQSsglfvDALAVNREAKAVLDY---LK--LNiapttQVA-RLSVAQQQMVEIAR 156
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-----DRAEVRADLERVYELfprLKerRR-----QRAgTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 157 ALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-228 |
8.44e-42 |
|
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: 149.12 E-value: 8.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRGIIT 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL-PPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSsglfvdalavNREAKAVLDYLkLNIAP------TTQVARLSVAQQQMVEIARALT 159
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARR----------RAKRKARLERV-YELFPrlkerrKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 160 LNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
3.39e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 151.40 E-value: 3.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQK 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAEN-MFlgrepqssGLFVDALAVNREAKAVLDYLKL-NIAP--TTQVARLSVAQQQMVEIAR 156
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENvAF--------GLRMRGVPKAEIRARVAELLELvGLEGlaDRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 157 ALTLNAKLIVMDEPSAALsDSEV-DSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG3842 149 ALAPEPRVLLLDEPLSAL-DAKLrEEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-220 |
4.17e-41 |
|
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: 145.79 E-value: 4.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIIT 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGrepqssglfvdalavnreakavldylklniapttqvarLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 166 VMDEPSAALsDSEV-DSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03229 123 LLDEPTSAL-DPITrREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-220 |
1.07e-40 |
|
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: 145.74 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPVERqkRGIIT 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPER--RNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRG----VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 166 VMDEPSAALsDSEV-DSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03259 153 LLDEPLSAL-DAKLrEELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-220 |
2.72e-40 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 143.31 E-value: 2.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQlllLESPVERQKRGIIT 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD---IKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMflgrepqssglfvdalavnreakavldylklniapttqvaRLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03230 78 LPEEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 166 VMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03230 118 ILDEPTSGL-DPEsRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-220 |
4.55e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.00 E-value: 4.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQkrgII 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ---IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TIYQEFNLLPNMSVAEN-MFLGRepqSSGLFVDALAvnREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAK 163
Cdd:COG4555 78 VLPDERGLYDRLTVRENiRYFAE---LYGLFDEELK--KRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 164 LIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-220 |
6.65e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.42 E-value: 6.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSF-SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLE-SPVERQKR 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQSS------GLFVDALAvnREAKAVLDylKLNIAP--TTQVARLSVAQQQMVE 153
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsllGLFPPEDR--ERALEALE--RVGLADkaYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 154 IARALTLNAKLIVMDEPSAAL----SDSEVDSLHRVVRElkgRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG3638 157 IARALVQEPKLILADEPVASLdpktARQVMDLLRRIARE---DGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-220 |
3.77e-37 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 136.47 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQK- 80
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL-SEKELAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 --RGIITIYQEFNLLPNMSVAEN----MFLGREPQSSglfvdalaVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEI 154
Cdd:cd03255 80 rrRHIGFVFQSFNLLPDLTALENvelpLLLAGVPKKE--------RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 155 ARALTLNAKLIVMDEPSAALsDSE-----VDSLHRVVRElkgRGVSVVYVTHRlHEVFQLCDRFTVFQDGR 220
Cdd:cd03255 152 ARALANDPKIILADEPTGNL-DSEtgkevMELLRELNKE---AGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-220 |
2.80e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSF----SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVE- 77
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL-SEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 ----RQKRGIitIYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKL-NIApTTQVARLSVAQQQMV 152
Cdd:COG1136 81 arlrRRHIGF--VFQFFNLLPELTALENVALPLLLAG----VSRKERRERARELLERVGLgDRL-DHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 153 EIARALTLNAKLIVMDEPSAALsDSE-----VDSLHRVVRELkgrGVSVVYVTHRlHEVFQLCDRFTVFQDGR 220
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNL-DSKtgeevLELLRELNREL---GTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-487 |
9.73e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 139.82 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKS----TLLKALAGAQPQTSGDIWFGGQQLLLL 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 73 ESPVERQKRG--IITIYQEfnllPnMS-----------VAENMFLGRepqssGLfvdalaVNREAKA-VLDYLKL-NI-A 136
Cdd:COG4172 82 SERELRRIRGnrIAMIFQE----P-MTslnplhtigkqIAEVLRLHR-----GL------SGAAARArALELLERvGIpD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 137 PTTQVAR----LSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEV-----DSLHRVVRELkgrGVSVVYVTHRLHEVF 207
Cdd:COG4172 146 PERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTAL-DVTVqaqilDLLKDLQREL---GMALLLITHDLGVVR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 208 QLCDRFTVFQDGRYTGSGDVAStnvqeiirlmvgrdvVFNR--------------RPPSETHHQDKPVRLAVKGLSREKP 273
Cdd:COG4172 222 RFADRVAVMRQGEIVEQGPTAE---------------LFAApqhpytrkllaaepRGDPRPVPPDAPPLLEARDLKVWFP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 274 -------PLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGfSSGEFVLDDapyhpsTPLHALSQGiALV 346
Cdd:COG4172 287 ikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDG------QDLDGLSRR-ALR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 347 PedrkkegavlglsIRENI---------SLSNlsslmrwRWFV--------------NTRKE-DDLIdayRQALhiKMVN 402
Cdd:COG4172 359 P-------------LRRRMqvvfqdpfgSLSP-------RMTVgqiiaeglrvhgpgLSAAErRARV---AEAL--EEVG 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 403 SDQEVR-----KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAIS 476
Cdd:COG4172 414 LDPAARhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALA 493
|
570
....*....|.
gi 504513498 477 DRIITLSEGRI 487
Cdd:COG4172 494 HRVMVMKDGKV 504
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-172 |
9.88e-36 |
|
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: 130.08 E-value: 9.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGiiTIYQEFNLLPNMSVAE 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIG--YVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 101 NMFLGREPQssglFVDALAVNREAKAVLDYLKLNIAPTT----QVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:pfam00005 79 NLRLGLLLK----GLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-246 |
1.56e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.91 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPVERQK 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-------PPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGI------ITIYQEFnllPnMSVAENMFLGREPQsSGLFVDALAVNRE-AKAVLDylKLNIAP--TTQVARLSVAQQQM 151
Cdd:COG1121 75 RRIgyvpqrAEVDWDF---P-ITVRDVVLMGRYGR-RGLFRRPSRADREaVDEALE--RVGLEDlaDRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 152 VEIARALTLNAKLIVMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTgSGDVAST 230
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGV-DAAtEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEV 225
|
250
....*....|....*.
gi 504513498 231 NVQEIIRLMVGRDVVF 246
Cdd:COG1121 226 LTPENLSRAYGGPVAL 241
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-206 |
4.77e-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: 130.29 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQkrgI 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENM-FLGRepqSSGLFVDALAVNreakAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNA 162
Cdd:COG4133 78 AYLGHADGLKPELTVRENLrFWAA---LYGLRADREAID----EALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEV 206
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-220 |
1.29e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 130.55 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVER-QKRGI 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-SRRELaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITiyQEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDylKLNIAP--TTQVARLSVAQQQMVEIARALTLN 161
Cdd:COG1120 80 VP--QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALE--RTGLEHlaDRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 162 AKLIVMDEPSAALsdsevDSLHRV-----VREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1120 156 PPLLLLDEPTSHL-----DLAHQLevlelLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-220 |
1.85e-34 |
|
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: 129.61 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSF-SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRG-I 83
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENMFLGREPQSS------GLFvdALAVNREAKAVLDylKLNIAP--TTQVARLSVAQQQMVEIA 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRStwrslfGLF--PKEEKQRALAALE--RVGLLDkaYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 156 RALTLNAKLIVMDEPSAALsdsEVDSLHRVVRELKG----RGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03256 157 RALMQQPKLILADEPVASL---DPASSRQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-220 |
6.66e-34 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 128.12 E-value: 6.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLllesPVERQKRGIIT 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT----NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKK----LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 166 VMDEPSAALSDS-------EVDSLHRVVrelkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03300 153 LLDEPLGALDLKlrkdmqlELKRLQKEL------GITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-220 |
2.57e-33 |
|
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: 126.08 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQK 80
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RG--IITIYQE----FNllPNMSVAENMflgREPQssgLFVDALAVNREAKAVLDYLKLNIAPTTQVAR-----LSVAQQ 149
Cdd:cd03257 80 RRkeIQMVFQDpmssLN--PRMTIGEQI---AEPL---RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 150 QMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELK-GRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
3.76e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.04 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEplLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQK 80
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAENMflgrepqSSGLF---VDALAVNREAKAVLDYLKLniapTTQVAR----LSVAQQQMVE 153
Cdd:COG3839 75 RNIAMVFQSYALYPHMTVYENI-------AFPLKlrkVPKAEIDRRVREAAELLGL----EDLLDRkpkqLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 154 IARALTLNAKLIVMDEPSAALsD--------SEVDSLHrvvRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNL-DaklrvemrAEIKRLH---RRL---GTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-220 |
3.85e-33 |
|
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: 123.51 E-value: 3.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIItiy 87
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 qefnllpnmsvaenmflgrePQssglfvdalavnreakavldylklniapttqvarLSVAQQQMVEIARALTLNAKLIVM 167
Cdd:cd00267 79 --------------------PQ----------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 168 DEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
4.73e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.36 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSF----SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPV 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-------PV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 77 ERQKRGIITIYQEFNLLPNMSVAENMFLGREpqssglFVDALAVNREAKAvLDYLKLniapttqV----------ARLSV 146
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPWLTVLDNVALGLE------LRGVPKAERRERA-RELLEL-------VglagfedaypHQLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 147 AQQQMVEIARALTLNAKLIVMDEPSAALsDSEV-DSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDR 212
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGAL-DALTrERLQDELLRLwQETGKTVLFVTHDVDEAVFLADR 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-220 |
8.09e-33 |
|
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: 124.12 E-value: 8.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 19 WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGII-----------TIY 87
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVfqnpddqffgpTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 QE--FNLlpnmsvaENMFLGREpqssglfvdalAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03225 95 EEvaFGL-------ENLGLPEE-----------EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 166 VMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-220 |
1.47e-32 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 124.37 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIITIY 87
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 QEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVM 167
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 168 DEPSAALsDSEV-DSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03296 161 DEPFGAL-DAKVrKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
2.52e-32 |
|
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: 129.64 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSF-----SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESP 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 VERQKRGII-TIYQE----FNllPNMSVAENMflgREPQSSGLFVDALAVNREAKAVLDYLKLniaPTTQVAR----LSV 146
Cdd:COG1123 336 SLRELRRRVqMVFQDpyssLN--PRMTVGDII---AEPLRLHGLLSRAERRERVAELLERVGL---PPDLADRypheLSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 147 AQQQMVEIARALTLNAKLIVMDEPSAALsDSEV-----DSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSAL-DVSVqaqilNLLRDLQREL---GLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-227 |
3.90e-32 |
|
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: 123.07 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLL-ESPVERQ 79
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 80 KRGIITIYQEFNLLPNMSVAEN----MFLGREPQSsglfvdalavNREAKaVLDYLKL-------NIAPttqvARLSVAQ 148
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENvalpLEIAGVPKA----------EIEER-VLELLELvgledkaDAYP----AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 149 QQMVEIARALTLNAKLIVMDEPSAAL----SDSEVDSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGS 224
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
...
gi 504513498 225 GDV 227
Cdd:cd03258 223 GTV 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-228 |
6.14e-32 |
|
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: 122.65 E-value: 6.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPV-ERQKRGII 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TIYQEFNLLPNMSVAENMFLGREpqssGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-220 |
9.53e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.26 E-value: 9.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPverQKRGIIT 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP---RERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAEN-MF-LGREPQSSglfvdalavnREAKA-VLDYLKL----NIA---PttqvARLSVAQQQMVEIA 155
Cdd:COG1118 80 VFQHYALFPHMTVAENiAFgLRVRPPSK----------AEIRArVEELLELvqleGLAdryP----SQLSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 156 RALTLNAKLIVMDEPSAALsDSEV-DSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1118 146 RALAVEPEVLLLDEPFGAL-DAKVrKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-241 |
1.30e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.45 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNL-AKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKR 81
Cdd:COG3845 255 EVVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL-SPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQE---FNLLPNMSVAENMFLGR---EPQSSGLFVDALAVNREAKAVLDylKLNI---APTTQVARLSVAQQQMV 152
Cdd:COG3845 334 GVAYIPEDrlgRGLVPDMSVAENLILGRyrrPPFSRGGFLDRKAIRAFAEELIE--EFDVrtpGPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNV 232
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
....*....
gi 504513498 233 QEIIRLMVG 241
Cdd:COG3845 492 EEIGLLMAG 500
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-226 |
1.49e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 125.33 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGI 83
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENMflgrepqSSGLFVDALAVNREAKAVLDYLKLniAPTTQVAR-----LSVAQQQMVEIARAL 158
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNI-------AFGLKQDKLPKAEIASRVNEMLGL--VHMQEFAKrkphqLSGGQRQRVALARSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 159 TLNAKLIVMDEPSAALSDSEVDSL-HRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-220 |
2.28e-31 |
|
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: 120.90 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGII-----------T 85
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVfqnpddqlfapT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEfnllpnmsVA---ENMFLGREpqssglfvdalAVNREAKAVLDYLKL-NIApTTQVARLSVAQQQMVEIARALTLN 161
Cdd:COG1122 93 VEED--------VAfgpENLGLPRE-----------EIRERVEEALELVGLeHLA-DRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-220 |
4.49e-31 |
|
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: 119.31 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIIT 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 iyQEFNLLPNMSVAENM-FLGrepQSSGLfvdalaVNREAKAVLDYL--KLNIAP--TTQVARLSVAQQQMVEIARALTL 160
Cdd:cd03269 77 --EERGLYPKMKVIDQLvYLA---QLKGL------KKEEARRRIDEWleRLELSEyaNKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 161 NAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-220 |
7.32e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 118.90 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIIT 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRK----VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 166 VMDEPSAAL-------SDSEVDSLHrvvRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03301 153 LMDEPLSNLdaklrvqMRAELKRLQ---QRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-220 |
7.37e-31 |
|
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: 118.79 E-value: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIIT 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGrepQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA---PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 166 VMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03262 158 LFDEPTSAL-DPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-216 |
1.10e-30 |
|
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: 118.73 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPVERQKR 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-------PVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQSsglfvdalAVNREAKA-VLDYLKL-------NIAPttqvARLSVAQQQMVE 153
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQG--------VPKAEARErAEELLELvglsgfeNAYP----HQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 154 IARALTLNAKLIVMDEPSAALsdsevDSLHR------VVRELKGRGVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSAL-----DALTReqlqeeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-212 |
1.18e-30 |
|
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: 118.40 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPVERQKRGIITIY 87
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-------PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 QEFNLLPNM--SVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513498 166 VMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDR 212
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-220 |
1.31e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.62 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 10 NLAKSFS-GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLL---ESPVERQKRGIit 85
Cdd:COG2884 6 NVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRIGV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAEN-MF----LGREPQssglfvdalAVNREAKAVLDYL----KLNIAPTTqvarLSVAQQQMVEIAR 156
Cdd:COG2884 84 VFQDFRLLPDRTVYENvALplrvTGKSRK---------EIRRRVREVLDLVglsdKAKALPHE----LSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 157 ALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-239 |
1.59e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 118.40 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRGIIT 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL-PPHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSsglfvdalavnREAKAVLDYLkLNIAPTTQVAR------LSVAQQQMVEIARALT 159
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALP-----------RRSRKIPDEI-YELFPVLKEMLgrrggdLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 160 LNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRL 238
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRY 227
|
.
gi 504513498 239 M 239
Cdd:TIGR03410 228 L 228
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-220 |
2.28e-30 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 121.30 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPverQKRGI 83
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL-PP---QKRDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENMFLGREPQSSGlfvdALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAK 163
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMG----RAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 164 LIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGV 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-220 |
4.15e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.78 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSF-SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQ-KRG 82
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGRE------PQSSGLFVDAlaVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIAR 156
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLgykptwRSLLGRFSEE--DKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 157 ALTLNAKLIVMDEPSAAL----SDSEVDSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLdpktSKQVMDYLKRINKED---GITVIINLHQVDLAKKYADRIVGLKAGE 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
281-487 |
4.30e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.47 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapYHPSTPLHALSQGIALVPEDrkkegAVL--G 358
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG--EDVARDPAEVRRRIGYVPQE-----PALypD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENISLsnLSSLMRWRWFVNTRKEDDLIDAYRqaLHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:COG1131 88 LTVRENLRF--FARLYGLPRKEARERIDELLELFG--LTDAA---DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 439 GIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-487 |
4.74e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 123.28 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFS--GV--WALSNAQLTVQRGEIHALLGENGAGKST-------LLKALAGAQPQtsGDIWFGGQQL 69
Cdd:PRK15134 1 MTQPLLAIENLSVAFRqqQTvrTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYPS--GDIRFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 70 LLLESPVERQKRG--IITIYQE----FNLLPNM--SVAENMFL----GREPQSSGLF--VDALAVNREAKAVLDYlklni 135
Cdd:PRK15134 79 LHASEQTLRGVRGnkIAMIFQEpmvsLNPLHTLekQLYEVLSLhrgmRREAARGEILncLDRVGIRQAAKRLTDY----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 136 aPttqvARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFT 214
Cdd:PRK15134 154 -P----HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 215 VFQDGRYtgsgdVASTNVQEII---------RLMvgrdvvfNRRPPSETH--HQDKPVRLAVKGLSREKP-------PLD 276
Cdd:PRK15134 229 VMQNGRC-----VEQNRAATLFsapthpytqKLL-------NSEPSGDPVplPEPASPLLDVEQLQVAFPirkgilkRTV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 277 AHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGfSSGEFVLDDAPYHPSTP--LHALSQGIALVPEDRKKeg 354
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRrqLLPVRHRIQVVFQDPNS-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 355 avlGLSIRENIsLSNLSSLMR--WRWFVNTRKEDDLIDAYRQalhikmVNSDQEVR-----KLSGGNQQKVILARCMALN 427
Cdd:PRK15134 374 ---SLNPRLNV-LQIIEEGLRvhQPTLSAAQREQQVIAVMEE------VGLDPETRhrypaEFSGGQRQRIAIARALILK 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-220 |
4.85e-30 |
|
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: 116.55 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQkrGIIT 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI--GALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNllPNMSVAENM-FLGREPQSSglfvdalavNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:cd03268 79 EAPGFY--PNLTARENLrLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-229 |
6.62e-30 |
|
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: 117.05 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFsGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPVErqKRGIIT 85
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPE--KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLK----LNIAPTTqvarLSVAQQQMVEIARALTLN 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRK----VDKKEIERKVLEIAEMLGidhlLNRKPET----LSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVAS 229
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-220 |
9.19e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.63 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGII 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TIYQEFNLLPNMSVAENMFLGrePqssglfVDALAVNR-EAKAV-LDYL-------KLNIAPttqvARLSVAQQQMVEIA 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLA--P------IKVKKMSKaEAEERaMELLervgladKADAYP----AQLSGGQQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 156 RALTLNAKLIVMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1126 149 RALAMEPKVMLFDEPTSAL-DPElVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-228 |
1.12e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.90 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQK----- 80
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRigylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 --RGiitiyqefnLLPNMSVAEN-MFLGRepqSSGLfvDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARA 157
Cdd:COG4152 78 eeRG---------LYPKMKVGEQlVYLAR---LKGL--SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 158 LTLNAKLIVMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:COG4152 144 LLHDPELLILDEPFSGL-DPVnVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-225 |
1.76e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 115.08 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 31 GEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqlLLLES------PVerQKRGIITIYQEFNLLPNMSVAENMFL 104
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT--VLFDSrkkinlPP--QQRKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 105 GREPQSSGlfVDALAVNreakAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHR 184
Cdd:cd03297 99 GLKRKRNR--EDRISVD----ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513498 185 VVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-225 |
3.10e-29 |
|
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: 113.30 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVER-QKRGIIti 86
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-SPKELaRKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 87 yqefnllpnmsvaenmflgrePQSSGLF-VDALAvNREakavldylklniapttqVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:cd03214 79 ---------------------PQALELLgLAHLA-DRP-----------------FNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 166 VMDEPSAALsD--SEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:cd03214 120 LLDEPTSHL-DiaHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
281-490 |
3.66e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.52 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEdrkkegavlgls 360
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 irenislsnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrkLSGGNQQKVILARCMALNPKVLIVDEPTRGI 440
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 441 DVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-241 |
4.00e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.12 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLaksfSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRG 82
Cdd:COG1129 254 EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR-SPRDAIRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IItiY-----QEFNLLPNMSVAENMFLGR-EPQSSGLFVDAlavNREAKAVLDYLK-LNI---APTTQVARLSVAQQQMV 152
Cdd:COG1129 329 IA--YvpedrKGEGLVLDLSIRENITLASlDRLSRGGLLDR---RRERALAEEYIKrLRIktpSPEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 153 EIARALTLNAKLIVMDEPSAAlsdseVD-----SLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDV 227
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRG-----IDvgakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
250
....*....|....
gi 504513498 228 ASTNVQEIIRLMVG 241
Cdd:COG1129 479 EEATEEAIMAAATG 492
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
279-487 |
6.66e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 112.11 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 279 GIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapYHPSTPLHALSQGIALVPEDRKKEGavlG 358
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--KDIKKEPEEVKRRIGYLPEEPSLYE---N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENIslsnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:cd03230 88 LTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 439 GIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-225 |
1.45e-28 |
|
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: 112.67 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGeIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVE-RQKRGII 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKlRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TiyQEFNLLPNMSVAEnmflgrepqssglFVDALAV-----NREAKA----VLDYLKLNIAPTTQVARLSVAQQQMVEIA 155
Cdd:cd03264 78 P--QEFGVYPNFTVRE-------------FLDYIAWlkgipSKEVKArvdeVLELVNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 156 RALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELkGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
278-486 |
3.12e-28 |
|
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: 110.03 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 278 HGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEdrkkegavl 357
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 glsirenislsnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrkLSGGNQQKVILARCMALNPKVLIVDEPT 437
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 438 RGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-220 |
4.36e-28 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 110.21 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLaksfSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRG 82
Cdd:cd03215 2 EPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR-SPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITI---YQEFNLLPNMSVAENMFLGRepqssglfvdalavnreakavldylklniapttqvaRLSVAQQQMVEIARALT 159
Cdd:cd03215 77 IAYVpedRKREGLVLDLSVAENIALSS------------------------------------LLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 160 LNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-220 |
4.69e-28 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.82 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQK--RGIIT 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGL-SEAELYRlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAEN-MFLGREpqsSGLFVDALaVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:cd03261 82 LFQSGALFDSLTVFENvAFPLRE---HTRLSEEE-IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-220 |
5.73e-28 |
|
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: 111.61 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL-SEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 rgiitiyqefnLLPNMSVaenMFlgrepQSSGLFvDALAV--N-----RE---------AKAVLDYLKLniapttqvARL 144
Cdd:COG1127 80 -----------LRRRIGM---LF-----QGGALF-DSLTVfeNvafplREhtdlseaeiRELVLEKLEL--------VGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 145 SVAQQQM-----------VEIARALTLNAKLIVMDEPSAAL---SDSEVDSLhrvVRELKGR-GVSVVYVTHRLHEVFQL 209
Cdd:COG1127 132 PGAADKMpselsggmrkrVALARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAI 208
|
250
....*....|.
gi 504513498 210 CDRFTVFQDGR 220
Cdd:COG1127 209 ADRVAVLADGK 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
277-486 |
5.79e-28 |
|
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: 109.97 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 277 AHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpstplhaLSQGIALVPEDRKKEGAV 356
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED---------LTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 L-------GLSIRENISLSnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrkLSGGNQQKVILARCMALNPK 429
Cdd:cd03229 82 FqdfalfpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 430 VLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
6.94e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.66 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQK 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAENMFLGREPQSSGlfvdalavNREAKA-VLDYLKL----NIAPtTQVARLSVAQQQMVEIA 155
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTP--------AAEITPrVMEALRMvqleEFAQ-RKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 156 RALTLNAKLIVMDEPSAALS-------DSEVDSLHrvvRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDyklrkqmQNELKALQ---RKL---GITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
263-487 |
8.06e-28 |
|
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: 111.06 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQG 342
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 --IALVPEDrkkegavlglsireniSLSNLSSLMR---------WRWFVNTRKEDDLIdayRQALHIKMVNSDQEVRK-- 409
Cdd:cd03257 82 keIQMVFQD----------------PMSSLNPRMTigeqiaeplRIHGKLSKKEARKE---AVLLLLVGVGLPEEVLNry 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 410 ---LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEG 485
Cdd:cd03257 143 pheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
..
gi 504513498 486 RI 487
Cdd:cd03257 223 KI 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-220 |
8.51e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 111.62 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLES-PVERQ 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 80 krGIITIYQEFNLLPNMSVAENMFLGREPQS-----SGLFVDALAVNREAKAV------LDYLKLNIAPTTQVARLSVAQ 148
Cdd:PRK11300 81 --GVVRTFQHVRLFREMTVIENLLVAQHQQLktglfSGLLKTPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 149 QQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
281-486 |
1.15e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 109.86 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALV---PEDRkkegaVL 357
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKVGLVfqnPDDQ-----FF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 GLSIRENI--SLSNLSslmrwrwfvntRKEDDLIDAYRQALhiKMVNS----DQEVRKLSGGNQQKVILARCMALNPKVL 431
Cdd:cd03225 90 GPTVEEEVafGLENLG-----------LPEEEIEERVEEAL--ELVGLeglrDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-220 |
3.00e-27 |
|
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: 107.47 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 14 SFS----GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQE 89
Cdd:cd03228 7 SFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVP--QD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 90 FNLLpNMSVAENMflgrepqssglfvdalavnreakavldylklniapttqvarLSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:cd03228 85 PFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 170 PSAAL-SDSEvDSLHRVVRELKgRGVSVVYVTHRLHEVfQLCDRFTVFQDGR 220
Cdd:cd03228 123 ATSALdPETE-ALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
263-487 |
3.52e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.75 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREkpplDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPlHALSQG 342
Cdd:COG4619 1 LELEGLSFR----VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP-PEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 IALVPEdrkkEGAVLGLSIRENislsnlssLMRWRWFVNTRKEDDLIDAYRQALHIKMVNSDQEVRKLSGGNQQKVILAR 422
Cdd:COG4619 76 VAYVPQ----EPALWGGTVRDN--------LPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 423 CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-225 |
6.79e-27 |
|
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: 108.22 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFS----GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGqqLLLLESPVErQK 80
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAE-AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAENMflgrepqssGLFVDALAVNR-EAKAVLDYL--KLNIAPT--TQVARLSVAQQQMVEIA 155
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENL---------EYFAGLYGLKGdELTARLEELadRLGMEELldRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 156 RALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-227 |
9.79e-27 |
|
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: 108.04 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG---AQPQ--TSGDIWFGGQQLLLLESPVERQK 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPnMSVAENMFLGrePQSSGL----FVDALAVNREAKAVL-DYLKLNIAPTtqvaRLSVAQQQMVEIA 155
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG--LRLHGIklkeELDERVEEALRKAALwDEVKDRLHAL----GLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 156 RALTLNAKLIVMDEPSAAL---SDSEVDSLhrvVRELKGRgVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDV 227
Cdd:cd03260 154 RALANEPEVLLLDEPTSALdpiSTAKIEEL---IAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-273 |
1.24e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.55 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQK--R 81
Cdd:COG1135 4 LENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAL-SERELRAarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMflgrepqssglfvdALA-----VNREAKA--VLDYLKLniapttqV----------ARL 144
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENV--------------ALPleiagVPKAEIRkrVAELLEL-------VglsdkadaypSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 145 SVAQQQMVEIARALTLNAKLIVMDEPSAALsDSE-----VDSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDG 219
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSAL-DPEttrsiLDLLKDINREL---GLTIVLITHEMDVVRRICDRVAVLENG 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 220 RYTGSGDVAS--TNVQ-EIIRLMVGRdvVFNRRPPSET-------HHQDKPVRLAVKGLSREKP 273
Cdd:COG1135 218 RIVEQGPVLDvfANPQsELTRRFLPT--VLNDELPEELlarlreaAGGGRLVRLTFVGESADEP 279
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
263-487 |
2.02e-26 |
|
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: 106.81 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQG 342
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG------TDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 iALVPEDRKKEGAVL-------GLSIRENISLSnlsslMRWRwfvnTRKEDDLIDAYRQAL-HIKMVNS-DQEVRKLSGG 413
Cdd:cd03255 75 -ELAAFRRRHIGFVFqsfnllpDLTALENVELP-----LLLA----GVPKKERRERAEELLeRVGLGDRlNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 414 NQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDlPEIMAISDRIITLSEGRI 487
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-220 |
2.24e-26 |
|
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: 107.39 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVW-ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLllESPVERQKRGII 84
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR--EQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TIYQEFNLLPNMSVAENMflgrepqssGLFVDALAVNREAKA--VLDYLKL-NIAPTTQVAR----LSVAQQQMVEIARA 157
Cdd:cd03295 79 YVIQQIGLFPHMTVEENI---------ALVPKLLKWPKEKIRerADELLALvGLDPAEFADRypheLSGGQQQRVGVARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 158 LTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
282-487 |
2.41e-26 |
|
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: 107.20 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDdapyhpSTPLHALSQgIALVPEDRK-----KEGAV 356
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID------GEDISGLSE-AELYRLRRRmgmlfQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 LG-LSIRENISLsnlssLMRwrwfVNTRKEDDLIDAyRQALHIKMVNSDQEVRK----LSGGNQQKVILARCMALNPKVL 431
Cdd:cd03261 89 FDsLTVFENVAF-----PLR----EHTRLSEEEIRE-IVLEKLEAVGLRGAEDLypaeLSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-220 |
2.60e-26 |
|
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: 107.20 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVW----ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERqk 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQE----FNllPNMSVAENMflgREP-QSSGLfvdaLAVNREAKAVLDYLKLNIA-----PttqvARLSVAQQQ 150
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDRIL---AEPlRIHGL----PDREERIAELLEQVGLPPSfldryP----HQLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALsDSEV-DSLHRVVRELKG-RGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSAL-DVSVqAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
280-482 |
4.52e-26 |
|
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: 105.69 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpstpLHALSQGIALVPE----DRKkega 355
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------LEKERKRIGYVPQrrsiDRD---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 356 vLGLSIRENISLSNLSslmRWRWFVNTRKEDDliDAYRQALhiKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVL 431
Cdd:cd03235 83 -FPISVRDVVLMGLYG---HKGLFRRLSKADK--AKVDEAL--ERVGlselADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITL 482
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-220 |
4.75e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFsGVWALsNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESpverQKRGIIT 85
Cdd:COG3840 2 LRLDDLTYRY-GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENMFLGREPqssglfvdALAVNREAKAVLDYL--KLNIA------PttqvARLSVAQQQMVEIARA 157
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRP--------GLKLTAEQRAQVEQAleRVGLAglldrlP----GQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 158 LTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-212 |
6.84e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 107.83 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQP---QTSGDIWFGGQQLLLLeSPVE 77
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKL-SEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 RQK---RGIITIYQE----FNllPNMSVAENMflgREPQSSGLFVDALAVNREAKAVLDYLKLNIAPttQVAR-----LS 145
Cdd:COG0444 80 LRKirgREIQMIFQDpmtsLN--PVMTVGDQI---AEPLRIHGGLSKAEARERAIELLERVGLPDPE--RRLDrypheLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 146 VAQQQMVEIARALTLNAKLIVMDEPSAALsDSEV-----DSLHRVVRElkgRGVSVVYVTHRLHEVFQLCDR 212
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTAL-DVTIqaqilNLLKDLQRE---LGLAILFITHDLGVVAEIADR 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-212 |
1.14e-25 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 104.23 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESpveRQKRGIIT-- 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNS---KKASKFRRek 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 ---IYQEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNiaptTQVARLSVAQQQMVEIARALTLNA 162
Cdd:TIGR03608 78 lgyLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLK----QKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLhEVFQLCDR 212
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADR 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-230 |
1.57e-25 |
|
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: 107.49 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 23 NAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqlLLLES------PVERqkRGIITIYQEFNLLPNM 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--VLQDSargiflPPHR--RRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENMFLGREPqssglfvdalAVNREAKAVLDYL--KLNIAP--TTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:COG4148 93 SVRGNLLYGRKR----------APRAERRISFDEVveLLGIGHllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 173 ALSD---SEV-DSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVAST 230
Cdd:COG4148 163 ALDLarkAEIlPYLERLRDEL---DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-219 |
1.91e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIITIY 87
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 QEFNLLPNMSVAENMflgrepqSSGLFV-------DALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTL 160
Cdd:PRK10851 81 QHYALFRHMTVFDNI-------AFGLTVlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 161 NAKLIVMDEPSAALsDSEV-DSLHRVVR----ELKgrgVSVVYVTHRLHEVFQLCDRFTVFQDG 219
Cdd:PRK10851 154 EPQILLLDEPFGAL-DAQVrKELRRWLRqlheELK---FTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
281-487 |
2.08e-25 |
|
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: 104.05 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALSQ-GIALVPEDRkkegAVLG- 358
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPHERARaGIGYVPEGR----RIFPe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENIslsnlssLMRWRWFVNTRKEDDLIDAY------RQALHikmvnsdQEVRKLSGGNQQKVILARCMALNPKVLI 432
Cdd:cd03224 90 LTVEENL-------LLGAYARRRAKRKARLERVYelfprlKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 433 VDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-220 |
4.00e-25 |
|
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: 103.22 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 10 NLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQlLLLESPVERQKRGIitIYQE 89
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD-VVREPREVRRRIGI--VFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 90 FNLLPNMSVAENMFL-GREPQSSGlfvdALAVNReAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:cd03265 82 LSVDDELTGWENLYIhARLYGVPG----AERRER-IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 169 EPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-487 |
4.36e-25 |
|
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: 108.35 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQ--PQTSGDIW----------------FGGQ 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 68 QLLLLESPVERQ----------------KRGIITIYQEFNLLPNMSVAENMF-----LGREPQSsglfvdalAVNREAKa 126
Cdd:TIGR03269 81 PCPVCGGTLEPEevdfwnlsdklrrrirKRIAIMLQRTFALYGDDTVLDNVLealeeIGYEGKE--------AVGRAVD- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 127 VLDYLKLNiAPTTQVAR-LSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLH 204
Cdd:TIGR03269 152 LIEMVQLS-HRITHIARdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 205 EVFQLCDRFTVFQDGRYTGSGDvASTNVQEIIRL--MVGRDVVFnrrppsethHQDKPVrLAVKGLSREKPPLDAHGI-A 281
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGT-PDEVVAVFMEGvsEVEKECEV---------EVGEPI-IKVRNVSKRYISVDRGVVkA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEF---VLDD---------------APYhpstpLHALSQGI 343
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEwvdmtkpgpdgrgraKRY-----IGILHQEY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 344 ALVPEDrkkegAVLGlSIRENISLsnlsslmrwrwfvntrkedDLID--AYRQALH-IKMVNSDQEVRK---------LS 411
Cdd:TIGR03269 375 DLYPHR-----TVLD-NLTEAIGL-------------------ELPDelARMKAVItLKMVGFDEEKAEeildkypdeLS 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 412 GGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEV-HQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-220 |
9.83e-25 |
|
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: 102.20 E-value: 9.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVW--ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVERQKRgi 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--IRTDRKAARQS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFN-LLPNMSVAENM-FLGRepqSSGLFVDalAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:cd03263 77 LGYCPQFDaLFDELTVREHLrFYAR---LKGLPKS--EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 162 AKLIVMDEPSAALSDSEVDSLHRVVRELKgRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
281-487 |
1.05e-24 |
|
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: 102.52 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQ-GIA-------LVPEdrkk 352
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-GLPPHEIARlGIGrtfqiprLFPE---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 353 egavlgLSIRENISLSNLSSLMRWRWFVNTRKEDDliDAYRQALHI-KMVN----SDQEVRKLSGGNQQKVILARCMALN 427
Cdd:cd03219 90 ------LTVLENVMVAAQARTGSGLLLARARREER--EARERAEELlERVGladlADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
282-487 |
1.25e-24 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 102.81 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEDRkkeGAVLGLSI 361
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRRELARRIAYVPQEP---PAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNLSSLMRWRWFvntRKEDDliDAYRQALhiKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPT 437
Cdd:COG1120 93 RELVALGRYPHLGLFGRP---SAEDR--EAVEEAL--ERTGlehlADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 438 RGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-226 |
1.60e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE--RQKRG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERliRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IitIYQEFNLLPNMSVAEN-MFLGREPQSSGlfvdALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:PRK09493 81 M--VFQQFYLFPHLTALENvMFGPLRVRGAS----KEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 162 AKLIVMDEPSAALsDSEV-DSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK09493 155 PKLMLFDEPTSAL-DPELrHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
281-487 |
1.62e-24 |
|
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: 101.64 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALV---PEDrkkegAVL 357
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN-LRELRRKVGLVfqnPDD-----QLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 GLSIRENI--SLSNLSslmrwrwfvntRKEDDLIDAYRQALhiKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVL 431
Cdd:COG1122 90 APTVEEDVafGPENLG-----------LPREEIRERVEEAL--ELVGlehlADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-220 |
1.76e-24 |
|
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: 102.72 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 13 KSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLL------LLEspVERQKRGIitI 86
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrkeLRE--LRRKKISM--V 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 87 YQEFNLLPNMSVAENMFLGREPQSSGlfvdalAVNREAKA--VLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVP------RAEREERAaeALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 165 IVMDEPSAALsDSEV-----DSLHRVVRELKgrgVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03294 182 LLMDEAFSAL-DPLIrremqDELLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-220 |
2.24e-24 |
|
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: 107.23 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 16 SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLpN 95
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVL--QDVFLF-S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 MSVAENMFLGREPQSSGLFVDALavnREAkAVLDYLK-----LNiaptTQV----ARLSVAQQQMVEIARALTLNAKLIV 166
Cdd:COG2274 563 GTIRENITLGDPDATDEEIIEAA---RLA-GLHDFIEalpmgYD----TVVgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 167 MDEPSAALsDSEvdSLHRVVRELK--GRGVSVVYVTHRLhEVFQLCDRFTVFQDGR 220
Cdd:COG2274 635 LDEATSAL-DAE--TEAIILENLRrlLKGRTVIIIAHRL-STIRLADRIIVLDKGR 686
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-201 |
2.71e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 10 NLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE------RQKRGI 83
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEkairllRQKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ItiYQEFNLLPNMSVAENMF------LGREPQssglfvdalAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARA 157
Cdd:COG4161 87 V--FQQYNLWPHLTVMENLIeapckvLGLSKE---------QAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513498 158 LTLNAKLIVMDEPSAALsDSEVDS-LHRVVRELKGRGVSVVYVTH 201
Cdd:COG4161 156 LMMEPQVLLFDEPTAAL-DPEITAqVVEIIRELSQTGITQVIVTH 199
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
282-487 |
2.73e-24 |
|
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: 99.43 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEdrkkegavlglsi 361
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-SLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 reNISLSNLSSLmrwrwfvntrkeddlidayrqalhikmvnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGID 441
Cdd:cd03214 81 --ALELLGLAHL-----------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513498 442 VGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03214 130 IAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
281-487 |
2.81e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 101.32 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQGIALVPEdRKKEGAVLGLS 360
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG------KPPRRARRRIGYVPQ-RAEVDWDFPIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLSSLMRWRWFvnTRKEDDLIDayrQALhiKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEP 436
Cdd:COG1121 94 VRDVVLMGRYGRRGLFRRP--SRADREAVD---EAL--ERVGledlADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 437 TRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-201 |
3.96e-24 |
|
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: 100.17 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLES---PVERQKRGIItiYQEFNLL 93
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraiPYLRRKIGVV--FQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 PNMSVAENMFL-----GREPQSsglfvdalaVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:cd03292 91 PDRNVYENVAFalevtGVPPRE---------IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 504513498 169 EPSAALsdsEVDSLHRVVRELKG---RGVSVVYVTH 201
Cdd:cd03292 162 EPTGNL---DPDTTWEIMNLLKKinkAGTTVVVATH 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-220 |
4.08e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.26 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITnlaKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGqqllllESPVER--QKRG 82
Cdd:PRK11432 9 LKNIT---KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG------EDVTHRsiQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNA 162
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLG----VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
7.32e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVERQK 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD--ITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQE-FNLLPNMSVAENMFLGrepqssGLFVDALAVNREAKAVLD-YLKLNIAPTTQVARLSVAQQQMVEIARAL 158
Cdd:PRK11614 79 REAVAIVPEgRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 159 TLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
281-487 |
7.46e-24 |
|
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: 105.69 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEDrkkeGAVLGLS 360
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIGVVLQD----VFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLsslmrwrwfvnTRKEDDLIDAyrqalhIKMVNSDQEVRK---------------LSGGNQQKVILARCMA 425
Cdd:COG2274 565 IRENITLGDP-----------DATDEEIIEA------ARLAGLHDFIEAlpmgydtvvgeggsnLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLpEIMAISDRIITLSEGRI 487
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
263-487 |
8.99e-24 |
|
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: 100.26 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPsTPLHALSQG 342
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-RRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 IALVPED-------RKKEGAVLGLSIRenislsnlssLMRwrwfvNTRKEDDLIDAYRQalhikmVNSDQEVR-----KL 410
Cdd:COG1124 81 VQMVFQDpyaslhpRHTVDRILAEPLR----------IHG-----LPDREERIAELLEQ------VGLPPSFLdryphQL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 411 SGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-254 |
9.32e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.19 E-value: 9.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVER-QKRGI 83
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW-SPWELaRRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITiyQEFNLLPNMSVAENMFLGREPQSSGlfvdALAVNREAKAVLDylklniapTTQVA--------RLSVAQQQMVEIA 155
Cdd:COG4559 80 LP--QHSSLAFPFTVEEVVALGRAPHGSS----AAQDRQIVREALA--------LVGLAhlagrsyqTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 156 RALT-------LNAKLIVMDEPSAALsdsevDSLH-----RVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTG 223
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSAL-----DLAHqhavlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
250 260 270
....*....|....*....|....*....|.
gi 504513498 224 SGDVASTNVQEIIRLMVGRDVVFNRRPPSET 254
Cdd:COG4559 221 QGTPEEVLTDELLERVYGADLRVLAHPEGGC 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
263-492 |
1.22e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALS-- 340
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG------QDISSLSer 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 --------------QGIALVPEdrkkegavlgLSIRENISLSNLSSLMRWRwfvntrkeddliDAYRQALHI-KMVN--- 402
Cdd:COG1136 79 elarlrrrhigfvfQFFNLLPE----------LTALENVALPLLLAGVSRK------------ERRERARELlERVGlgd 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 403 -SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDlPEIMAISDRII 480
Cdd:COG1136 137 rLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVI 215
|
250
....*....|..
gi 504513498 481 TLSEGRISGEIH 492
Cdd:COG1136 216 RLRDGRIVSDER 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-226 |
1.30e-23 |
|
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: 101.42 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 36 LLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLlespVERQKRGIITIYQEFNLLPNMSVAENMFLGREPQSsglfV 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRK----V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 116 DALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GV 194
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
|
170 180 190
....*....|....*....|....*....|..
gi 504513498 195 SVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-230 |
1.39e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 99.77 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSG-DIWFGGQQlLLLESPVE-RQK 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER-RGGEDVWElRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIIT--IYQEFNllPNMSVaENMFLgrepqsSGLF--------VDALAVNReAKAVLDYLKLNIAPTTQVARLSVAQQQ 150
Cdd:COG1119 80 IGLVSpaLQLRFP--RDETV-LDVVL------SGFFdsiglyrePTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVAS 229
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
.
gi 504513498 230 T 230
Cdd:COG1119 230 V 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
284-487 |
1.56e-23 |
|
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: 98.52 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 284 DISFQVhAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPStplhalSQGIALVPEDRK-----KEGAVL- 357
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDS------RKKINLPPQQRKiglvfQQYALFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 GLSIRENISLSnlssLMRWRWFVNTRKEDDLIDAyrqaLHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPT 437
Cdd:cd03297 89 HLNVRENLAFG----LKRKRNREDRISVDELLDL----LGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 438 RGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-228 |
1.92e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 103.68 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRgIITIYQEfNLLPNM 96
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-DPASWRRQ-IAWVPQN-PYLFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENMFLGREPQSSGLFVDAL-AVNreAKAVLDYLKLNIAptTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:COG4988 426 TIRENLRLGRPDASDEELEAALeAAG--LDEFVAALPDGLD--TPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 172 AAL-SDSEVDsLHRVVRELKgRGVSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSGDVA 228
Cdd:COG4988 502 AHLdAETEAE-ILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHE 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-225 |
2.17e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.81 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPV-ERQKRGI 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL--PLhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENMFLGREPQSsglfvDALAVNREAKAV-------LDYLKLNIAPTtqvarLSVAQQQMVEIAR 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRD-----DLSAEQREDRANelmeefhIEHLRDSMGQS-----LSGGERRRVEIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 157 ALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
263-501 |
2.66e-23 |
|
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: 98.41 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPpldAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYH--PSTPLHAL- 339
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 340 ------SQGIALVPEdrkkegavlgLSIRENISLSNLSSLMRWRWFVNTRKEDDLIDAyRQALhiKMVNSD----QEVRK 409
Cdd:cd03256 78 rqigmiFQQFNLIER----------LSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRA-LAAL--ERVGLLdkayQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
250
....*....|...
gi 504513498 489 GEIHGDDATEEKL 501
Cdd:cd03256 225 FDGPPAELTDEVL 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-288 |
2.87e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 100.65 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLL-ESPVERQKRG 82
Cdd:PRK11153 4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREpqssglfvdaLA-VNREA--KAVLDYLKL-------NIAPttqvARLSVAQQQMV 152
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLE----------LAgTPKAEikARVTELLELvglsdkaDRYP----AQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 153 EIARALTLNAKLIVMDEPSAAL----SDSEVDSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGRY--TGS-G 225
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALdpatTRSILELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLveQGTvS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 226 DVASTNVQEIIRLMVgrdvvfnrrppSETHHQDKPVRLavkgLSREKPPLDAHGIALKDISFQ 288
Cdd:PRK11153 227 EVFSHPKHPLTREFI-----------QSTLHLDLPEDY----LARLQAEPTTGSGPLLRLEFT 274
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-201 |
3.00e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE------RQKR 81
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDkairelRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIItiYQEFNLLPNMSVAENMFlgrEPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:PRK11124 85 GMV--FQQYNLWPHLTVQQNLI---EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504513498 162 AKLIVMDEPSAALsDSEVDS-LHRVVRELKGRGVSVVYVTH 201
Cdd:PRK11124 160 PQVLLFDEPTAAL-DPEITAqIVSIIRELAETGITQVIVTH 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
263-492 |
3.33e-23 |
|
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: 97.54 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpstpLHALSQG 342
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP------VTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 IALVPEDrkkeGAVLG-LSIRENISLSNLSSLMRWRwfvntrkeddliDAYRQALH-IKMVN-SDQEVR---KLSGGNQQ 416
Cdd:cd03293 75 RGYVFQQ----DALLPwLTVLDNVALGLELQGVPKA------------EARERAEElLELVGlSGFENAyphQLSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 417 KVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSE--GRISGEIH 492
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-220 |
6.31e-23 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 97.75 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKAL-----AGAQPQTSGDIWFGGQQLLLLESPVERQ 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 80 KRGIITIYQEFNLLPnMSVAENMFLGrePQSSGL----FVDALAVNREAKAVL-DYLK--LNIAPTtqvaRLSVAQQQMV 152
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYG--PRLHGIkdkkELDEIVEESLKKAALwDEVKdrLHDSAL----GLSGGQQQRL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRgVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGE 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
282-487 |
6.67e-23 |
|
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: 96.56 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHAlsqgIALVPEDRKKEgaVLGLSI 361
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQDVDYQ--LFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNlsslmrwrwfvntrkeDDLIDAYRQA--------LHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIV 433
Cdd:cd03226 90 REELLLGL----------------KELDAGNEQAetvlkdldLYALK---ERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 434 DEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-245 |
1.17e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQlLLLESPVERQK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP-VPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITiyQEFNLLPNMSVAENMFL-GRepqSSGLfvDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALT 159
Cdd:PRK13537 82 VGVVP--QFDNLDPDFTVRENLLVfGR---YFGL--SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 160 LNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRytgsgDVASTNVQEIIRLM 239
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR-----KIAEGAPHALIESE 229
|
....*.
gi 504513498 240 VGRDVV 245
Cdd:PRK13537 230 IGCDVI 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
276-487 |
1.22e-22 |
|
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: 96.53 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 276 DAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALVPEDrkkegA 355
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGVVPQD-----T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 356 VL-GLSIRENISLSNLSSlmrwrwfvntrKEDDLIDAYRQA-LHIKMVNS----DQEV--R--KLSGGNQQKVILARCMA 425
Cdd:cd03253 85 VLfNDTIGYNIRYGRPDA-----------TDEEVIEAAKAAqIHDKIMRFpdgyDTIVgeRglKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-225 |
1.64e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 95.64 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLEsPVERQkrgIITIYQEFNLLPNMSVAENMFLG 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-PADRP---VSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 106 REPQSSGLFVDALAVNREAKAV-LDYLKLNIAPTtqvarLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHR 184
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVgLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513498 185 VVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:cd03298 170 LVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-212 |
1.86e-22 |
|
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: 95.02 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIITI----YQEFnllpNM 96
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVMqdvdYQLF----TD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENMFLGREpqssglfvDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSD 176
Cdd:cd03226 88 SVREELLLGLK--------ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 504513498 177 SEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDR 212
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDR 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-222 |
2.92e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 95.27 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFS----GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESP- 75
Cdd:PRK11629 1 MNKILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 -VERQKRGIITIYQEFNLLPNMSVAENMFL-----GREPQSsglfvdalaVNREAKAVLDYLKLNIAPTTQVARLSVAQQ 149
Cdd:PRK11629 81 kAELRNQKLGFIYQFHHLLPDFTALENVAMplligKKKPAE---------INSRALEMLAAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 150 QMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLcDRFTVFQDGRYT 222
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-487 |
3.44e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.31 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGG-------QQLL 70
Cdd:PRK10261 9 ARDVLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 71 LLESPVERQKRG-----IITIYQE--FNLLPNMSVAENMF--------LGREpqssglfvDALAvnrEAKAVLDYLKLni 135
Cdd:PRK10261 89 ELSEQSAAQMRHvrgadMAMIFQEpmTSLNPVFTVGEQIAesirlhqgASRE--------EAMV---EAKRMLDQVRI-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 136 aPTTQVA------RLSVAQQQMVEIARALTLNAKLIVMDEPSAALS---DSEVDSLHRVVRELKGRGvsVVYVTHRLHEV 206
Cdd:PRK10261 156 -PEAQTIlsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHDMGVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 207 FQLCDRFTVFQDGRYTGSGDV-----------ASTNVQEIIRLMVGRDVVFNRRPP----------SETHHQDKPVR--- 262
Cdd:PRK10261 233 AEIADRVLVMYQGEAVETGSVeqifhapqhpyTRALLAAVPQLGAMKGLDYPRRFPlislehpakqEPPIEQDTVVDgep 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 -LAVKGLSREKP---------PLDAHgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYH- 331
Cdd:PRK10261 313 iLQVRNLVTRFPlrsgllnrvTREVH--AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDt 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 332 -PSTPLHALSQGIALVPEDRKKE---GAVLGLSIRENISLSNL----SSLMRWRWF---VNTRKEddliDAYRQAlhikm 400
Cdd:PRK10261 391 lSPGKLQALRRDIQFIFQDPYASldpRQTVGDSIMEPLRVHGLlpgkAAAARVAWLlerVGLLPE----HAWRYP----- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 401 vnsdqevRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRI 479
Cdd:PRK10261 462 -------HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRV 534
|
....*...
gi 504513498 480 ITLSEGRI 487
Cdd:PRK10261 535 AVMYLGQI 542
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-226 |
5.38e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFG----------GQQLLLLESPve 77
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLIRQL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 RQKRGIItiYQEFNLLPNMSVAENMFLG-----REPQSSglfvdalAVNReAKAVLDYLKLNIAPTTQVARLSVAQQQMV 152
Cdd:PRK11264 84 RQHVGFV--FQNFNLFPHRTVLENIIEGpvivkGEPKEE-------ATAR-ARELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-212 |
5.60e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.71 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPV-ERQKR 81
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL--PMhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFLGREPQssglFVDALAVNREAKAVLDYLKLniaptTQVAR-----LSVAQQQMVEIAR 156
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELR----KLSKKEREERLEELLEEFGI-----THLRKskaysLSGGERRRVEIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 157 ALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDR 212
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDR 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-227 |
7.41e-22 |
|
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: 93.36 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGaQPQ---TSGDIWFGGQQLLLLEsPVERQKRG 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevTEGEILFKGEDITDLP-PEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEfnllPnmsvaenmflgrePQSSGLfvdalavnreakAVLDYLK-LNiapttqvARLSVAQQQMVEIARALTLN 161
Cdd:cd03217 79 IFLAFQY----P-------------PEIPGV------------KNADFLRyVN-------EGFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 162 AKLIVMDEPSAALsdsEVDSLH---RVVRELKGRGVSVVYVTHRlHEVFQLC--DRFTVFQDGRYTGSGDV 227
Cdd:cd03217 123 PDLAILDEPDSGL---DIDALRlvaEVINKLREEGKSVLIITHY-QRLLDYIkpDRVHVLYDGRIVKSGDK 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
278-487 |
7.64e-22 |
|
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: 94.23 E-value: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 278 HGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHP----STPLHALSQGIALVPEdrkke 353
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphKRPVNTVFQNYALFPH----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 gavlgLSIRENISLSnlsslMRWRwfvntRKEDDLIDAyRQALHIKMVN-SDQEVRK---LSGGNQQKVILARCMALNPK 429
Cdd:cd03300 87 -----LTVFENIAFG-----LRLK-----KLPKAEIKE-RVAEALDLVQlEGYANRKpsqLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 430 VLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-220 |
1.02e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 93.65 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLL-ESP 75
Cdd:COG4181 4 SSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 ---VERQKRGIitIYQEFNLLPNMSVAENMFLGREpqssglfvdaLAVNREAKAV-LDYLK-------LNIAPttqvARL 144
Cdd:COG4181 84 rarLRARHVGF--VFQSFQLLPTLTALENVMLPLE----------LAGRRDARARaRALLErvglghrLDHYP----AQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 145 SVAQQQMVEIARALTLNAKLIVMDEPSAALsDSE-----VDSLHRVVRElkgRGVSVVYVTHRlHEVFQLCDRFTVFQDG 219
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNL-DAAtgeqiIDLLFELNRE---RGTTLVLVTHD-PALAARCDRVLRLRAG 222
|
.
gi 504513498 220 R 220
Cdd:COG4181 223 R 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
282-487 |
1.12e-21 |
|
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: 91.89 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHaLSQGIALVPEDRKkegaVLGLSI 361
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE-LGDHVGYLPQDDE----LFSGSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENIslsnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrkLSGGNQQKVILARCMALNPKVLIVDEPTRGID 441
Cdd:cd03246 93 AENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513498 442 VGTKSEVHQVLFDMAKRGVAVIVISSDlPEIMAISDRIITLSEGRI 487
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-245 |
1.16e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqlLLLESPVERQKR---- 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-------TVLGVPVPARARlara 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFL-GREPQSSglfvdalavNREAKAV----LDYLKLNIAPTTQVARLSVAQQQMVEIAR 156
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVfGRYFGMS---------TREIEAVipslLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 157 ALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRytgsgDVASTNVQEII 236
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR-----KIAEGRPHALI 260
|
....*....
gi 504513498 237 RLMVGRDVV 245
Cdd:PRK13536 261 DEHIGCQVI 269
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
281-486 |
1.29e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 91.68 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyHPSTPLHALSQGIALVPEDrkkegAVL-GL 359
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDLESLRKNIAYVPQD-----PFLfSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENIslsnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevrkLSGGNQQKVILARCMALNPKVLIVDEPTRG 439
Cdd:cd03228 91 TIRENI--------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513498 440 IDVGTKSEVHQVLFDMAKrGVAVIVISSDLpEIMAISDRIITLSEGR 486
Cdd:cd03228 127 LDPETEALILEALRALAK-GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
281-487 |
1.45e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.73 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTplhalSQGIALVPEDRkkegavlGLS 360
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYLPEER-------GLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENIsLSNLSSLMRWRwfvNTRKEDDL--IDAYRQALHIkMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:cd03269 83 PKMKV-IDQLVYLAQLK---GLKKEEARrrIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 439 GIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
281-495 |
1.59e-21 |
|
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: 93.51 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKkegaVLG-L 359
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRR----IFPsL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSnlsslMRWRWFVNTRKED-DLIDAYRQALHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:COG0410 94 TVEENLLLG-----AYARRDRAEVRADlERVYELFPRLKERR---RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 439 G-----IDvgtksEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGEIHGDD 495
Cdd:COG0410 166 GlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-220 |
2.13e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 10 NLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIITIYQE 89
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM----NDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 90 FNLLPNMSVAENMFLGrepqssglfvdaLAVNREAKAVLDYLKLNIAPTTQVAR--------LSVAQQQMVEIARALTLN 161
Cdd:PRK11000 84 YALYPHLSVAENMSFG------------LKLAGAKKEEINQRVNQVAEVLQLAHlldrkpkaLSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 162 AKLIVMDEP----SAALS---DSEVDSLHRVVrelkgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK11000 152 PSVFLLDEPlsnlDAALRvqmRIEISRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-241 |
2.55e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLaksfSGVwALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVERQKRGI 83
Cdd:PRK15439 267 PVLTVEDL----TGE-GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL-STAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ItiyqefnllpnmsvaenmFLGREPQSSGLFVDA--------LAVNREA--------KAVLD--YLKLNIA---PTTQVA 142
Cdd:PRK15439 341 V------------------YLPEDRQSSGLYLDAplawnvcaLTHNRRGfwikpareNAVLEryRRALNIKfnhAEQAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 143 RLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYT 222
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
250
....*....|....*....
gi 504513498 223 GSGDVASTNVQEIIRLMVG 241
Cdd:PRK15439 483 GALTGAAINVDTIMRLAFG 501
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
281-487 |
2.82e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 92.21 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAP-YHPSTPLHALSQGIALV-------PEdrkk 352
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKlTDDKKNINELRQKVGMVfqqfnlfPH---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 353 egavlgLSIRENISLSnlsslmrwrwFVNTRKEDDlIDAYRQALHI-KMV----NSDQEVRKLSGGNQQKVILARCMALN 427
Cdd:cd03262 91 ------LTVLENITLA----------PIKVKGMSK-AEAEERALELlEKVgladKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-224 |
3.73e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.15 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAqpqTSGDIwFGGQQLLLLESPVERQKR- 81
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDK-SAGSHIELLGRTVQREGRl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 ---------GIITIYQEFNLLPNMSVAENMFLGrEPQSSGLFVDAL-----AVNREAKAVLDYLKLNIAPTTQVARLSVA 147
Cdd:PRK09984 78 ardirksraNTGYIFQQFNLVNRLSVLENVLIG-ALGSTPFWRTCFswftrEQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 148 QQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR--YTGS 224
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHvfYDGS 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
281-487 |
3.94e-21 |
|
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: 91.81 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHA-----LSQGIALVPEdrkkega 355
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERrnigmVFQDYALFPH------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 356 vlgLSIRENISLSnlsslMRwrwfVNTRKEDDLIDAYRQALhiKMVN-SDQEVRK---LSGGNQQKVILARCMALNPKVL 431
Cdd:cd03259 87 ---LTVAENIAFG-----LK----LRGVPKAEIRARVRELL--ELVGlEGLLNRYpheLSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
6.28e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.30 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQ--QLLLLESPVER 78
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKR-------GIITIYQEFNLLPNMSVAEN-----MFLG-------REPQSSGLfvdalavnreAKAVLDYLKLNIAPTT 139
Cdd:PRK11701 82 ERRrllrtewGFVHQHPRDGLRMQVSAGGNigerlMAVGarhygdiRATAGDWL----------ERVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 140 qvarLSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEV-----DSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFT 214
Cdd:PRK11701 152 ----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGL-DVSVqarllDLLRGLVREL---GLAVVIVTHDLAVARLLAHRLL 223
|
250
....*....|.
gi 504513498 215 VFQDGRYTGSG 225
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-237 |
6.50e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLES-PVERQkrg 82
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSArAASRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREPQSSGLF----VDALAVNReakavldylKLNIAPTTQVA-----RLSVAQQQMVE 153
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDtwteTDRAAVER---------AMERTGVAQFAdrpvtSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 154 IARALTLNAKLIVMDEPSAALS-DSEVDSLhRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNV 232
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
....*
gi 504513498 233 QEIIR 237
Cdd:PRK09536 229 ADTLR 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
280-487 |
6.65e-21 |
|
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: 91.03 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapYHPSTPLHALSQGIALVPEDRkkeGAVLGL 359
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQSLGYCPQFD---ALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENIslsNLSSLMRWrwfVNTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRG 439
Cdd:cd03263 91 TVREHL---RFYARLKG---LPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513498 440 IDVGTKSEVHQVLFDMaKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03263 164 LDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-206 |
6.84e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 14 SFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLespVERQKRGIITiyqefnlL 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY---VPQRSEVPDS-------L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 PnMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAA 173
Cdd:NF040873 71 P-LTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 504513498 174 LSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEV 206
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-220 |
7.86e-21 |
|
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: 89.58 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 19 WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLEspvERQKRGII-TIYQEFNLLPNmS 97
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDHVgYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMflgrepqssglfvdalavnreakavldylklniapttqvarLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDS 177
Cdd:cd03246 92 IAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504513498 178 EVDSLHRVVRELKGRGVSVVYVTHRLhEVFQLCDRFTVFQDGR 220
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-212 |
9.85e-21 |
|
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: 95.43 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVW-ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERqkRG 82
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR--DQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNmSVAENMFLGREPQSSGLFVDALavnrEAKAVLDYLK-LNIAPTTQV----ARLSVAQQQMVEIARA 157
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLARPDASDAEIREAL----ERAGLDEFVAaLPQGLDTPIgeggAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 158 LTLNAKLIVMDEPSAAL-SDSEVDSLHRVVRELKGRgvSVVYVTHRLHeVFQLCDR 212
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLdAETEAEVLEALRALAQGR--TVLLVTHRLA-LAALADR 525
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-226 |
1.01e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.28 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAG--AQPQTSGDIWFGGQQLLLLeSPVERQKRGIITIYQ---EFnllPNMSVAE 100
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILEL-SPDERARAGIFLAFQypvEI---PGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 nmFL-------GREPQSSGLFVDalAVNREAKAV---LDYLK--LNiapttqvARLSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:COG0396 97 --FLrtalnarRGEELSAREFLK--LLKEKMKELgldEDFLDryVN-------EGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 169 EPsaalsDS--EVDSLHRV---VRELKGRGVSVVYVTH--RLHEVFQlCDRFTVFQDGRYTGSGD 226
Cdd:COG0396 166 ET-----DSglDIDALRIVaegVNKLRSPDRGILIITHyqRILDYIK-PDFVHVLVDGRIVKSGG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
266-487 |
1.11e-20 |
|
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: 90.79 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 266 KGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRT---EIARCLFGADGFSSGEFVLDDAPYHPstplHALSQG 342
Cdd:cd03234 7 WDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTtllDAISGRVEGGGTTSGQILFNGQPRKP----DQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 IALVPEDrkkEGAVLGLSIRENISLSNLSSLMRWRWFVNTRKEDDliDAYRQALHIKMVnSDQEVRKLSGGNQQKVILAR 422
Cdd:cd03234 83 VAYVRQD---DILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRI-GGNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 423 CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIV-ISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
260-492 |
1.33e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 91.30 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 260 PVRLAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpstpLHAL 339
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP------VTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 340 SQGIALVP-EDRkkegavlgL----SIRENISLSnlsslMRWRWfVNTRKEDDLIDAYrqalhIKMVN-SDQEVRK---L 410
Cdd:COG1116 79 GPDRGVVFqEPA--------LlpwlTVLDNVALG-----LELRG-VPKAERRERAREL-----LELVGlAGFEDAYphqL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 411 SGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSE--GRI 487
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
....*
gi 504513498 488 SGEIH 492
Cdd:COG1116 220 VEEID 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-219 |
1.33e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.60 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLllESPVERqkrgiITIYQEFNLLPNMSVAE 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT--EPGPDR-----MVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NMflgrepqssglfvdALAVNR--------EAKAV----LDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:TIGR01184 74 NI--------------ALAVDRvlpdlsksERRAIveehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 169 EPSAALSDSEVDSLH-RVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDG 219
Cdd:TIGR01184 140 EPFGALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
280-487 |
1.50e-20 |
|
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: 90.36 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEDRkkegAVLGL 359
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDT----FLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNlsslmrwrwfvNTRKEDDLIDAyrqalhIKMVNSDQEVRK---------------LSGGNQQKVILARCM 424
Cdd:cd03254 92 TIMENIRLGR-----------PNATDEEVIEA------AKEAGAHDFIMKlpngydtvlgenggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 425 ALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
1.65e-20 |
|
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: 94.83 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSG--VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQ 79
Cdd:COG4987 330 GGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 80 KRGIITiyQEFNLLpNMSVAENMFLGRePQSSglfvDAlavnrEAKAVLDylKLNIAPT---------TQV----ARLSV 146
Cdd:COG4987 410 RIAVVP--QRPHLF-DTTLRENLRLAR-PDAT----DE-----ELWAALE--RVGLGDWlaalpdgldTWLgeggRRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 147 AQQQMVEIARALTLNAKLIVMDEPSAAL-SDSEVDSLHRVVRELKGRgvSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSG 225
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLdAATEQALLADLLEALAGR--TVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
.
gi 504513498 226 D 226
Cdd:COG4987 552 T 552
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-201 |
2.27e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 90.63 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTE---PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESP-- 75
Cdd:COG4598 1 MTDtapPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 ---------VERQKRGIITIYQEFNLLPNMSVAENMF------LGREPQssglfvDALAvnrEAKAVLDylKLNIAPTTQ 140
Cdd:COG4598 81 elvpadrrqLQRIRTRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPKA------EAIE---RAEALLA--KVGLADKRD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 141 V--ARLSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSE-VDSLHRVVRELKGRGVSVVYVTH 201
Cdd:COG4598 150 AypAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL-DPElVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-205 |
2.34e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLlllESPveRQ 79
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV---TGP--GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 80 KRGIItiYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALT 159
Cdd:COG4525 77 DRGVV--FQKDALLPWLNVLDNVAFGLRLRG----VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 160 LNAKLIVMDEPSAALsdsevDSLHR------VVRELKGRGVSVVYVTHRLHE 205
Cdd:COG4525 151 ADPRFLLMDEPFGAL-----DALTReqmqelLLDVWQRTGKGVFLITHSVEE 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
281-487 |
2.72e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 94.05 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEDrkkeGAVLGLS 360
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAWVPQN----PYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLSSlmrwrwfvntrKEDDLIDAYRQA-LHiKMVNS-----DQEV----RKLSGGNQQKVILARCMALNPKV 430
Cdd:COG4988 427 IRENLRLGRPDA-----------SDEELEAALEAAgLD-EFVAAlpdglDTPLgeggRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 431 LIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLpEIMAISDRIITLSEGRI 487
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRI 549
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-225 |
3.10e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 14 SFS---GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL--LLLESpvERQKRGIITiyQ 88
Cdd:COG1132 346 SFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdLTLES--LRRQIGVVP--Q 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 89 EFNLLpNMSVAENMFLGREPQSSGLFVDALavnREAKA--VLDYL--KLNiaptTQV----ARLSVAQQQMVEIARALTL 160
Cdd:COG1132 422 DTFLF-SGTIRENIRYGRPDATDEEVEEAA---KAAQAheFIEALpdGYD----TVVgergVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 161 NAKLIVMDEPSAALsDSEVDSL--HRVVRELKGRgvSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSG 225
Cdd:COG1132 494 DPPILILDEATSAL-DTETEALiqEALERLMKGR--TTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
281-505 |
3.10e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGA--DGFSSGEFVLDDAPYHPSTPLHALSQGIA-------LVPEdrk 351
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAGIAiihqelaLVKE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 352 kegavlgLSIRENISLSNlsslmrwRWFVNTRKEDDLIDAYRQAL--HIKM-VNSDQEVRKLSGGNQQKVILARCMALNP 428
Cdd:PRK13549 97 -------LSVLENIFLGN-------EITPGGIMDYDAMYLRAQKLlaQLKLdINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 429 KVLIVDEPTRGIdvgTKSEVhQVLFDMAK----RGVAVIVISSDLPEIMAISDRIITLSEGRISGEIHGDDATEEKLMTM 504
Cdd:PRK13549 163 RLLILDEPTASL---TESET-AVLLDIIRdlkaHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
|
.
gi 504513498 505 M 505
Cdd:PRK13549 239 M 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-220 |
3.74e-20 |
|
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: 89.19 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGG---QQLllleSPVERqKRGIITIYQEFNLLpNM 96
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQL----DPADL-RRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENMFLGREPQSSGLFVDALavnrEAKAVLDYLKLNiaP---TTQVAR----LSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:cd03245 93 TLRDNITLGAPLADDERILRAA----ELAGVTDFVNKH--PnglDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 170 PSAALSD-SEVDSLHRVVRELKGRgvSVVYVTHRLhEVFQLCDRFTVFQDGR 220
Cdd:cd03245 167 PTSAMDMnSEERLKERLRQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGR 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-201 |
4.22e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.69 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQP---QTSGDIWFGGQQLLLLesPVERqkRG 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTAL--PAEQ--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREPqssglfvdalAVNREAK-----AVLDYLKLNIAPTTQVARLSVAQQQMVEIARA 157
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPP----------TIGRAQRrarveQALEEAGLAGFADRDPATLSGGQRARVALLRA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 158 LTLNAKLIVMDEPSAALsdsevDSLHR------VVRELKGRGVSVVYVTH 201
Cdd:COG4136 148 LLAEPRALLLDEPFSKL-----DAALRaqfrefVFEQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
263-490 |
4.41e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.07 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPplDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTplhalsqg 342
Cdd:PRK13635 6 IRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 ialVPEDRKKEGAV--------LGLSIRENI--SLSNlsslmrwrwfvNTRKEDDLIDAYRQALH-IKMVN-SDQEVRKL 410
Cdd:PRK13635 76 ---VWDVRRQVGMVfqnpdnqfVGATVQDDVafGLEN-----------IGVPREEMVERVDQALRqVGMEDfLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 411 SGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEImAISDRIITLSEGRISG 489
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEA-AQADRVIVMNKGEILE 220
|
.
gi 504513498 490 E 490
Cdd:PRK13635 221 E 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
282-487 |
4.57e-20 |
|
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: 89.32 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhpsTPLHALSQGIALVPEDRkkegaVL--GL 359
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVPQNY-----ALfpHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSnlsslMRWRwfVNTRKEDDlidayRQALHI-KMVNS----DQEVRKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:cd03299 87 TVYKNIAYG-----LKKR--KVDKKEIE-----RKVLEIaEMLGIdhllNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
282-487 |
5.02e-20 |
|
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: 89.27 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQG--IALvpedRKK------E 353
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG------QDITGLSEKelYEL----RRRigmlfqG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 GAVLG-LSIRENISLSnlsslMRwrwfVNTRKEDDLIDAyRQALHIKMVNSDQEVRK----LSGGNQQKVILARCMALNP 428
Cdd:COG1127 91 GALFDsLTVFENVAFP-----LR----EHTDLSEAEIRE-LVLEKLELVGLPGAADKmpseLSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-220 |
5.71e-20 |
|
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: 88.93 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 18 VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGqqllllESPVERQKRgiitiyqefnLLPNMS 97
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWKRRKK----------FLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VaenMFLGREPQSSGLFV-DALAVNR--------EAKAVLDYLK--LNIAPT--TQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:cd03267 98 V---VFGQKTQLWWDLPViDSFYLLAaiydlppaRFKKRLDELSelLDLEELldTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
281-487 |
7.54e-20 |
|
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: 88.39 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG----ADGF-SSGEFVLDDAP-YHPSTPLHALSQGIALV---Pedrk 351
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlIPGApDEGEVLLDGKDiYDLDVDVLELRRRVGMVfqkP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 352 kegAVLGLSIRENISLSNLSSLMRWRWFVNTRKEDDLIDAyrqALHiKMVNSDQEVRKLSGGNQQKVILARCMALNPKVL 431
Cdd:cd03260 91 ---NPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKA---ALW-DEVKDRLHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDMAKRgVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
281-487 |
8.57e-20 |
|
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: 87.93 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhPST-PLHALSQGIALVPEDrkkegAVL-- 357
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVD--ISKiGLHDLRSRISIIPQD-----PVLfs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 GlSIRENISLSNLSSlmrwrwfvntrkEDDLIDAYRQALHIKMVNS-----DQEV----RKLSGGNQQKVILARCMALNP 428
Cdd:cd03244 92 G-TIRSNLDPFGEYS------------DEELWQALERVGLKEFVESlpgglDTVVeeggENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLfDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
282-437 |
1.16e-19 |
|
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: 85.39 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyHPSTPLHALSQGIALVPEDrkkEGAVLGLSI 361
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD-LTDDERKSLRKEIGYVFQD---PQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 362 RENISLSNLSslmrwrWFVNTRKEDDLIDAYRQAL---HIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPT 437
Cdd:pfam00005 77 RENLRLGLLL------KGLSKREKDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-225 |
1.41e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSG-----DIWFGGQQLLLLESPVER 78
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRgIITIYQEFNLLPnMSVAENMFlgrepqsSGLFVDALAVNRE----AKAVLDYLKLNIAPTTQVA----RLSVAQQQ 150
Cdd:PRK14271 100 RRR-VGMLFQRPNPFP-MSIMDNVL-------AGVRAHKLVPRKEfrgvAQARLTEVGLWDAVKDRLSdspfRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRgVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-228 |
1.86e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 87.77 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG--AQPQTSGDIWFGGQQLLLLEsPVER 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE-PEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRGIITIYQ---EFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLKLNiapTTQVAR-----LSVAQQQ 150
Cdd:CHL00131 82 AHLGIFLAFQypiEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMD---PSFLSRnvnegFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALsdsEVDSLHRV---VRELKGRGVSVVYVTH--RLHEVFQlCDRFTVFQDGR--YTG 223
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGL---DIDALKIIaegINKLMTSENSIILITHyqRLLDYIK-PDYVHVMQNGKiiKTG 234
|
....*
gi 504513498 224 SGDVA 228
Cdd:CHL00131 235 DAELA 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-225 |
1.99e-19 |
|
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: 87.20 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLEspverqkrgii 84
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 tiyqeFN--LLPNMSVAEN-----MFLGREPQSSGLFVDALAVNREAKAVLDyLKLNIAPTTQVARLSVAqqqmveIARA 157
Cdd:cd03220 91 -----LGggFNPELTGRENiylngRLLGLSRKEIDEKIDEIIEFSELGDFID-LPVKTYSSGMKARLAFA------IATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 158 LtlNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:cd03220 159 L--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-220 |
2.23e-19 |
|
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: 87.10 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTePLLNITNLAKSFS-------GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWF--GGQQLLL 71
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 72 LESPvERQ-----KRGIITIYQEFNLLPNMS----VAENMF-LGREPQssglfvDALAvnrEAKAVLDYLKL-----NIA 136
Cdd:COG4778 80 AQAS-PREilalrRRTIGYVSQFLRVIPRVSaldvVAEPLLeRGVDRE------EARA---RARELLARLNLperlwDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 137 PTTqvarLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:COG4778 150 PAT----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
....
gi 504513498 217 QDGR 220
Cdd:COG4778 226 TPFS 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
265-490 |
2.54e-19 |
|
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: 86.87 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 265 VKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSqGIA 344
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG------TDLTLLS-GKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 345 LVPEdRKKEGAVL-------GLSIRENISLSnlssLMRWRWfvnTRKEddlidAYRQALH-IKMVN-SDQEVRK---LSG 412
Cdd:cd03258 77 LRKA-RRRIGMIFqhfnllsSRTVFENVALP----LEIAGV---PKAE-----IEERVLElLELVGlEDKADAYpaqLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 413 GNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-487 |
3.41e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWF-GGQQLLLLEspverqkrgiiti 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 87 yQEFNLLPNMSVAENMFLGREPQSS--------------------------GLF--VDALAVNREAKAVLDYLKLNIAP- 137
Cdd:COG0488 68 -QEPPLDDDLTVLDTVLDGDAELRAleaeleeleaklaepdedlerlaelqEEFeaLGGWEAEARAEEILSGLGFPEEDl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 138 TTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALsDseVDSLHRVVRELKGRGVSVVYVTH-R--LHEV----FQLc 210
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHL-D--LESIEWLEEFLKNYPGTVLVVSHdRyfLDRVatriLEL- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 211 DRFTVFqdgRYTGSGD--------------VASTNVQEIIRlmvgRDVVFNRRPPS---------------------ETH 255
Cdd:COG0488 223 DRGKLT---LYPGNYSayleqraerleqeaAAYAKQQKKIA----KEEEFIRRFRAkarkakqaqsrikaleklereEPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 256 HQDKPVRLAVKGLSRE-KPPLDAHGIA--------LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFV-- 324
Cdd:COG0488 296 RRDKTVEIRFPPPERLgKKVLELEGLSksygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlg 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 325 --------------LDDApyhpSTPLHALSQGialvpEDRKKEGAVLGLsirenislsnLSSLMrwrwFvntrKEDDLid 390
Cdd:COG0488 376 etvkigyfdqhqeeLDPD----KTVLDELRDG-----APGGTEQEVRGY----------LGRFL----F----SGDDA-- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 391 ayrqalhikmvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVL--FDmakrGvAVIVISSD 468
Cdd:COG0488 427 -------------FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALddFP----G-TVLLVSHD 488
|
570 580
....*....|....*....|.
gi 504513498 469 --LpeIMAISDRIITLSEGRI 487
Cdd:COG0488 489 ryF--LDRVATRILEFEDGGV 507
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-250 |
3.91e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPVER-QKRG 82
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW-SPAELaRRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITiyQEFNLLPNMSVAENMFLGREPQSSGlfvdalavNREAKAVLDyLKLNIAPTTQVA-----RLSVAQQQMVEIARA 157
Cdd:PRK13548 80 VLP--QHSSLSFPFTVEEVVAMGRAPHGLS--------RAEDDALVA-AALAQVDLAHLAgrdypQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 158 LT------LNAKLIVMDEPSAALsdsevDSLH-----RVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSAL-----DLAHqhhvlRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
250 260
....*....|....*....|....*
gi 504513498 226 DVASTNVQEIIRLMVGRDVVFNRRP 250
Cdd:PRK13548 224 TPAEVLTPETLRRVYGADVLVQPHP 248
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-220 |
4.12e-19 |
|
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: 90.58 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIITIY--QEFNLLPNmSV 98
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL----SQWDREELGRHIGYlpQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 99 AENmfLGREPQssglfVDALAVNREAKA--VLDY-LKLNIAPTTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:COG4618 423 AEN--IARFGD-----ADPEKVVAAAKLagVHEMiLRLPDGYDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 172 AALsDSE-VDSLHRVVRELKGRGVSVVYVTHRLHeVFQLCDRFTVFQDGR 220
Cdd:COG4618 496 SNL-DDEgEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGR 543
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
262-486 |
5.22e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 85.22 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 262 RLAVKGLS--REKPPLdahgiaLKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTP---- 335
Cdd:COG4133 2 MLEAENLScrRGERLL------FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdyrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 336 -LHALSQGIALVPEdrkkegavlgLSIRENISLsnlsslmrWRWFVNTRKEDDLIDAyrqalHIKMVN----SDQEVRKL 410
Cdd:COG4133 76 rLAYLGHADGLKPE----------LTVRENLRF--------WAALYGLRADREAIDE-----ALEAVGlaglADLPVRQL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 411 SGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDlpEIMAISDRIITLSEGR 486
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ--PLELAAARVLDLGDFK 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-201 |
5.23e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG-----AQPQTSGDIWFGGQQLLLLesPVERQK 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKM--DVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQEFNLLPNMSVAENMFLG----REPQSSGLFVDALAVNREAKAVLDYLKLNI-APTtqvARLSVAQQQMVEIA 155
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKELQERVRWALEKAQLWDEVKDRLdAPA---GKLSGGQQQRLCIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513498 156 RALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKgRGVSVVYVTH 201
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTH 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-223 |
6.21e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLE-SPVERQKRGIITIYQEFNLLPN 95
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 MSVAENMFLgrepqssGLFVDALA---VNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:PRK10908 94 RTVYDNVAI-------PLIIAGASgddIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 173 ALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTG 223
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-224 |
6.52e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.79 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQlLLLESPverQKRGIITIYQEFNLLPNMSVAENMFLG 105
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPP---SRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 106 REPqssglfvdALAVNREAKAVLDYLKLNIAPTTQVARL----SVAQQQMVEIARALTLNAKLIVMDEP-SA---ALSDS 177
Cdd:PRK10771 96 LNP--------GLKLNAAQREKLHAIARQMGIEDLLARLpgqlSGGQRQRVALARCLVREQPILLLDEPfSAldpALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 178 EVDSLHRVVRElkgRGVSVVYVTHRLHEVFQLCDRFTVFQDGR--YTGS 224
Cdd:PRK10771 168 MLTLVSQVCQE---RQLTLLMVSHSLEDAARIAPRSLVVADGRiaWDGP 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
280-487 |
9.74e-19 |
|
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: 86.16 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQGiALVPEDRKKEGAV--- 356
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDG------QDIAAMSRK-ELRELRRKKISMVfqs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 LGL----SIRENI----SLSNLSSLMRwrwfvntrkeddlidaYRQALH-IKMVN----SDQEVRKLSGGNQQKVILARC 423
Cdd:cd03294 111 FALlphrTVLENVafglEVQGVPRAER----------------EERAAEaLELVGlegwEHKYPDELSGGMQQRVGLARA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 424 MALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03294 175 LAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
261-487 |
9.83e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 85.46 E-value: 9.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 261 VRLAVKGLSREKPpldahgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEF-VLDdapyhpstplhal 339
Cdd:cd03267 23 LKSLFKRKYREVE-------ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAG------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 340 sqgiaLVPEDRKKE-----GAVLG--------LSIRENISLsnLSSLMRWRWFVNTRKEDDLIDAyrqaLHIKMVnSDQE 406
Cdd:cd03267 83 -----LVPWKRRKKflrriGVVFGqktqlwwdLPVIDSFYL--LAAIYDLPPARFKKRLDELSEL----LDLEEL-LDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 407 VRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEG 485
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
..
gi 504513498 486 RI 487
Cdd:cd03267 231 RL 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-220 |
1.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPVERQKRGIITIYQEF------ 90
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-------PIDYSRKGLMKLRESVgmvfqd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 91 --NLLPNMSVAENMFLGrePQSSGLFVDalAVNREAKAVLDylKLNIAPTTQ--VARLSVAQQQMVEIARALTLNAKLIV 166
Cdd:PRK13636 91 pdNQLFSASVYQDVSFG--AVNLKLPED--EVRKRVDNALK--RTGIEHLKDkpTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 167 MDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-203 |
1.33e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.41 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLL-------LE 73
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 74 SPVERQKRGIIT----IYQEFNLLPNMSVAENMfLGREPQSSGLfvdALAVNREaKAVLDYLKLNIAPTTQV---ARLSV 146
Cdd:PRK10619 81 VADKNQLRLLRTrltmVFQHFNLWSHMTVLENV-MEAPIQVLGL---SKQEARE-RAVKYLAKVGIDERAQGkypVHLSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 147 AQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRL 203
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-229 |
1.59e-18 |
|
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: 88.32 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGV-----WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWF--GGQQLLLLESP 75
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 VE---RQKRGIITIYQEFNLLPNMSVAENMflgrePQSSGL-FVDALAVNR-------------EAKAVLDYLklniaPT 138
Cdd:TIGR03269 357 PDgrgRAKRYIGILHQEYDLYPHRTVLDNL-----TEAIGLeLPDELARMKavitlkmvgfdeeKAEEILDKY-----PD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 139 TqvarLSVAQQQMVEIARALTLNAKLIVMDEPSAALSD-SEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQ 217
Cdd:TIGR03269 427 E----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|..
gi 504513498 218 DGRYTGSGDVAS 229
Cdd:TIGR03269 503 DGKIVKIGDPEE 514
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-212 |
1.74e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 86.32 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSF---SGVW--------ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 70 LLLESPVERQKR-GIITIYQE----FNllPNMSVAEnmFLGREPQSSGLfVDALAVNREAKAVLDYLKLNiapTTQVAR- 143
Cdd:COG4608 83 TGLSGRELRPLRrRMQMVFQDpyasLN--PRMTVGD--IIAEPLRIHGL-ASKAERRERVAELLELVGLR---PEHADRy 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 144 ---LSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEVDSlhRVV---RELKGR-GVSVVYVTHRLHEVFQLCDR 212
Cdd:COG4608 155 pheFSGGQRQRIGIARALALNPKLIVCDEPVSAL-DVSIQA--QVLnllEDLQDElGLTYLFISHDLSVVRHISDR 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
263-487 |
1.83e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 83.96 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLD--DAPYHPStplhALS 340
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPA----EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 QGIALVPEdrkKEGAVLGLSIRENIS-LSNLSSLMRWRWfvnTRKEDDLIDAYRQALHIkmvnsDQEVRKLSGGNQQKVI 419
Cdd:cd03266 78 RRLGFVSD---STGLYDRLTARENLEyFAGLYGLKGDEL---TARLEELADRLGMEELL-----DRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 420 LARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
281-490 |
2.69e-18 |
|
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: 87.55 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGF--SSGEFVlddapYHPStplHALSQGIALVPEDRKKEGAVLG 358
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRII-----YHVA---LCEKCGYVERPSKVGEPCPVCG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIR-ENISLSNLS-----------SLMRWRWFVnTRKEDDLIDAYRQALH----------------IKMVNSDQEV--- 407
Cdd:TIGR03269 87 GTLEpEEVDFWNLSdklrrrirkriAIMLQRTFA-LYGDDTVLDNVLEALEeigyegkeavgravdlIEMVQLSHRIthi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 408 -RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMA-ISDRIITLSEG 485
Cdd:TIGR03269 166 aRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENG 245
|
....*
gi 504513498 486 RISGE 490
Cdd:TIGR03269 246 EIKEE 250
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
281-493 |
5.11e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.79 E-value: 5.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQG-IALVpedRKKEGAVL-- 357
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG------QDLSRLKRReIPYL---RRRIGVVFqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 -----GLSIRENISLSnlsslMRwrwfVNTRKEDDLIDAYRQALhiKMVN-SDQE---VRKLSGGNQQKVILARCMALNP 428
Cdd:COG2884 88 frllpDRTVYENVALP-----LR----VTGKSRKEIRRRVREVL--DLVGlSDKAkalPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGEIHG 493
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
281-487 |
5.37e-18 |
|
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: 82.64 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY---HPSTplhaLSQGIALVPEDrkkegavL 357
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqlDPAD----LRRNIGYVPQD-------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 GL---SIRENISLSNLSSlmrwrwfvntrKEDDLIDAYRQALHIKMVNS-----DQEV----RKLSGGNQQKVILARCMA 425
Cdd:cd03245 88 TLfygTLRDNITLGAPLA-----------DDERILRAAELAGVTDFVNKhpnglDLQIgergRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLfdmaKRGVA--VIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERL----RQLLGdkTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-219 |
5.47e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKAL---AGAQPQ--TSGDIWFGGQQLLlleSP 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEvtITGSIVYNGHNIY---SP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 ----VERQKRgIITIYQEFNLLPnMSVAENMFLG---REPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTqvARLSVAQ 148
Cdd:PRK14239 78 rtdtVDLRKE-IGMVFQQPNPFP-MSIYENVVYGlrlKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSA--LGLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 149 QQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRgVSVVYVTHRLHEVFQLCDRFTVFQDG 219
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
5-220 |
5.89e-18 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 82.84 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLE--SPVER 78
Cdd:NF038007 1 MLNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSysQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRGIITIYQEFNLLPNMSVAENMFLgrePqssgLFVDALAVNREAKAVLDYLKL-NIAPTT--QVARLSVAQQQMVEIA 155
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVAL---P----LKYRGVAKKERIERVNQVLNLfGIDNRRnhKPMQLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 156 RALTLNAKLIVMDEPSAALsDSEvdSLHRVVRELK---GRGVSVVYVTHRlHEVFQLCDRFTVFQDGR 220
Cdd:NF038007 154 RAMVSNPALLLADEPTGNL-DSK--NARAVLQQLKyinQKGTTIIMVTHS-DEASTYGNRIINMKDGK 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
281-490 |
6.11e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGadgF---SSGEFVLDDAPYHpSTPLHALSQGIALVPEDrkkegAVL 357
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR---FydpTSGRILIDGVDIR-DLTLESLRRQIGVVPQD-----TFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 -GLSIRENISLSNLsslmrwrwfvnTRKEDDLIDAYRQA-LHiKMVNS-----DQEV----RKLSGGNQQKVILARCMAL 426
Cdd:COG1132 426 fSGTIRENIRYGRP-----------DATDEEVEEAAKAAqAH-EFIEAlpdgyDTVVgergVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 427 NPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAiSDRIITLSEGRISGE 490
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
251-487 |
8.53e-18 |
|
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: 86.36 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 251 PSETHHQDKPVRLAVKGLSREKPplDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY 330
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 331 HpSTPLHALSQGIALVPEDrkkeGAVLGLSIRENISLSNLSSlmrwrwfvntrKEDDLIDAYRQA-LHiKMVNS-----D 404
Cdd:COG4987 400 R-DLDEDDLRRRIAVVPQR----PHLFDTTLRENLRLARPDA-----------TDEELWAALERVgLG-DWLAAlpdglD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 405 QEV----RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEiMAISDRII 480
Cdd:COG4987 463 TWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG-LERMDRIL 540
|
....*..
gi 504513498 481 TLSEGRI 487
Cdd:COG4987 541 VLEDGRI 547
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
281-505 |
9.19e-18 |
|
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: 86.03 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGA--DGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKkegAVLG 358
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELT---LVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENISLSNLSSLMRWRWFVN--TRKEDDLIdayrQALHIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEP 436
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAYNamYLRAKNLL----RELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 437 TRGIdvgTKSEVhQVLFDMAK----RGVAVIVISSDLPEIMAISDRIITLSEGRISGEIHGDDATEEKLMTMM 505
Cdd:TIGR02633 169 SSSL---TEKET-EILLDIIRdlkaHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMM 237
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-237 |
1.04e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.19 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ----TSGDIWFGGQQLLLLeSP 75
Cdd:COG4170 2 PLLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKL-SP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 VERQK---RGIITIYQEFN--LLPNMSV----AENMFlgrEPQSSGLFVD-ALAVNREAKAVLDylKLNIAPTTQVAR-- 143
Cdd:COG4170 81 RERRKiigREIAMIFQEPSscLDPSAKIgdqlIEAIP---SWTFKGKWWQrFKWRKKRAIELLH--RVGIKDHKDIMNsy 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 144 ---LSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFqdg 219
Cdd:COG4170 156 pheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVL--- 232
|
250
....*....|....*...
gi 504513498 220 rYTGSgDVASTNVQEIIR 237
Cdd:COG4170 233 -YCGQ-TVESGPTEQILK 248
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
282-487 |
1.17e-17 |
|
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: 82.21 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALSQ-GIALVPEdrkkEGAVL-GL 359
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARlGIGYLPQ----EASIFrKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLS-NLSSLMRWRWfvnTRKEDDLIDAyrqaLHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:cd03218 91 TVEENILAVlEIRGLSKKER---EEKLEELLEE----FHITHL-RKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 439 GIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-220 |
1.23e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLnITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGdiwfggqQLLLLESPVERQKRGI 83
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLLPNMSVAENMFLGRepqsSGLFVDAlavnreAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAK 163
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGL----KGQWRDA------ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 164 LIVMDEPSAALsdsevDSLHR------VVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK11247 154 LLLLDEPLGAL-----DALTRiemqdlIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
282-491 |
1.26e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 82.13 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY-HPSTPLHALSQGIALVPedrkkegavlGLS 360
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDRMVVFQNYSLLP----------WLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSnLSSLMRWRwfvNTRKEDDLIDAyrqalHIKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEP 436
Cdd:TIGR01184 71 VRENIALA-VDRVLPDL---SKSERRAIVEE-----HIALVGlteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 437 TRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRIS--GEI 491
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNGPAAniGQI 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
262-487 |
1.33e-17 |
|
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: 85.57 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 262 RLAVKGLSREKPPLDAHgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHA--- 338
Cdd:COG4618 330 RLSVENLTVVPPGSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 339 ---LSQGIALVPedrkkegavlGlSIRENIS-LSNLSSlmrwrwfvntrkeDDLIDAYRQA-LHiKMVNS-----DQEV- 407
Cdd:COG4618 408 igyLPQDVELFD----------G-TIAENIArFGDADP-------------EKVVAAAKLAgVH-EMILRlpdgyDTRIg 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 408 ---RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDlPEIMAISDRIITLSE 484
Cdd:COG4618 463 eggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR-PSLLAAVDKLLVLRD 541
|
...
gi 504513498 485 GRI 487
Cdd:COG4618 542 GRV 544
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-220 |
1.37e-17 |
|
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: 85.48 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQKRGIITIY--QEFNLLPNmSV 98
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL----KQWDRETFGKHIGYlpQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 99 AENMFLGREPqssglfVDALAVNREAKAVLDY---LKLNIAPTTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:TIGR01842 409 AENIARFGEN------ADPEKIIEAAKLAGVHeliLRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 172 AALSDSEVDSLHRVVRELKGRGVSVVYVTHRLhEVFQLCDRFTVFQDGR 220
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGR 530
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-228 |
1.66e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQtSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLPNMSVAEnmFLg 105
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLS--QQQSPPFAMPVFQ--YL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 106 repqssGLFVDALAVNREAKAVLDYL--KLNIAP--TTQVARLSVAQQQMVEIARAL-----TLN--AKLIVMDEPSAAL 174
Cdd:COG4138 91 ------ALHQPAGASSEAVEQLLAQLaeALGLEDklSRPLTQLSGGEWQRVRLAAVLlqvwpTINpeGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 175 SDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-207 |
1.93e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPVE--RQKRG 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-------PVEgpGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IitIYQEFNLLPNMSVAENMFLGREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNA 162
Cdd:PRK11248 74 V--VFQNEGLLPWRNVQDNVAFGLQLAG----VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHE-VF 207
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEaVF 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-254 |
2.67e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESpveRQKRGIIT 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLP-NMSVAENMFLGREPQSSglFVDALAVNREAKAVLDYLKLNIAPTTQ--VARLSVAQQQMVEIARALTLNA 162
Cdd:PRK11231 80 LLPQHHLTPeGITVRELVAYGRSPWLS--LWGRLSAEDNARVNQAMEQTRINHLADrrLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVGR 242
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDV 237
|
250
....*....|..
gi 504513498 243 DVVFNRRPPSET 254
Cdd:PRK11231 238 EAEIHPEPVSGT 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
3.07e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKAL-----AGAQPQTSGDIWFGGQQLLLLESPVER 78
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRGIITIYQEFNLLPnMSVAENM-----FLGREPQssgLFVDALAVNREAKAVL-DYLKLNIAPTTqvARLSVAQQQMV 152
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVaygvkIVGWRPK---LEIDDIVESALKDADLwDEIKHKIHKSA--LDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRG-VSVVYVTHRLHEVFQLCDrFTVF 216
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSD-FTAF 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-225 |
3.50e-17 |
|
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: 79.28 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSF--SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGA-QPQtSGDIWFGGQQLLLLESPVERQkrg 82
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDlKPQ-QGEITLDGVPVSDLEKALSSL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 iitiyqefnllpnMSVAenmflgrePQSSGLFVDALavnREakavldylklNIApttqvARLSVAQQQMVEIARALTLNA 162
Cdd:cd03247 77 -------------ISVL--------NQRPYLFDTTL---RN----------NLG-----RRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 163 KLIVMDEPSAALS-DSEVDSLHRVVRELKGRgvSVVYVTHRLHEVFQLcDRFTVFQDGRYTGSG 225
Cdd:cd03247 118 PIVLLDEPTVGLDpITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-220 |
4.16e-17 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 82.06 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 10 NLAKSFSGVW-ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLllESPVERQKRGI---It 85
Cdd:COG1125 6 NVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR--DLDPVELRRRIgyvI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 iyQEFNLLPNMSVAENMflGREPQSSGlfVDALAVNREAKAVLDYLKLNiaPTTQVAR----LSVAQQQMVEIARALTLN 161
Cdd:COG1125 83 --QQIGLFPHMTVAENI--ATVPRLLG--WDKERIRARVDELLELVGLD--PEEYRDRypheLSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 162 AKLIVMDEPSAALsDSEV-DSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1125 155 PPILLMDEPFGAL-DPITrEQLQDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGR 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
281-490 |
5.37e-17 |
|
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: 80.11 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLD--DAPYHPSTplhaLSQGIALVPEDRKKEGAVLG 358
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPRE----VRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 lsiRENISLsnLSSLMRWRWFVNTRKEDDLIDAYrqALhikMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:cd03265 91 ---WENLYI--HARLYGVPGAERRERIDELLDFV--GL---LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 439 GIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
280-487 |
5.47e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG---ADgfsSGEFVLDDAPYHPSTPlhalsQGIALVPEDR---KKe 353
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilaPD---SGEVLWDGEPLDPEDR-----RRIGYLPEERglyPK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 gavlgLSIRENI----SLSNLSslmrwrwfvntRKE-DDLIDAYRQALHIKMvNSDQEVRKLSGGNQQKVILARCMALNP 428
Cdd:COG4152 86 -----MKVGEQLvylaRLKGLS-----------KAEaKRRADEWLERLGLGD-RANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 429 KVLIVDEPTRGID-VGTkSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG4152 149 ELLILDEPFSGLDpVNV-ELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
281-487 |
8.43e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDD------APYHPSTPLhaLSQGIALVPEdrkkeg 354
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglPPEKRNVGM--VFQDYALFPH------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 355 avlgLSIRENISLSnlssLMRWRWFVNTRKE--DDLIDayrqalhikMVN----SDQEVRKLSGGNQQKVILARCMALNP 428
Cdd:COG3842 92 ----LTVAENVAFG----LRMRGVPKAEIRArvAELLE---------LVGleglADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
8.80e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTePLLNITNLAKSF-SG---VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLES-- 74
Cdd:PRK10535 1 MT-ALLELKDIRRSYpSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAda 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 75 --PVERQKRGIItiYQEFNLLPNMSVAENMflgrepQSSGLFVDALAVNREAKAVLDYLKLNIAPTT--QVARLSVAQQQ 150
Cdd:PRK10535 80 laQLRREHFGFI--FQRYHLLSHLTAAQNV------EVPAVYAGLERKQRLLRAQELLQRLGLEDRVeyQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRlHEVFQLCDRFTVFQDGR 220
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
282-487 |
9.35e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.55 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALS-QGIALVPEDRkkegavlglS 360
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLHARArRGIGYLPQEA---------S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISL-SNLSSLMRWRWFVNTRKEDDLIDAYRQALHIKMVNsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRG 439
Cdd:PRK10895 89 IFRRLSVyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513498 440 IDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-220 |
1.10e-16 |
|
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: 79.51 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLpNMSVAE 100
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVS--QEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NMFLGREPQSSglfVDALAVNREAKAVLDYLKLNIAPTTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPSAAL-S 175
Cdd:cd03249 96 NIRYGKPDATD---EEVEEAAKKANIHDFIMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALdA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 176 DSEvdslhRVVRE-----LKGRgvSVVYVTHRLHEVfQLCDRFTVFQDGR 220
Cdd:cd03249 173 ESE-----KLVQEaldraMKGR--TTIVIAHRLSTI-RNADLIAVLQNGQ 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
282-487 |
1.29e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSqgialvPEDRKKEGAVL---- 357
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG------RPLAAWS------PWELARRRAVLpqhs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 ----GLSIRENISLSnlsslmRWRWFVNTRKEDDLIdayRQALHikMVN----SDQEVRKLSGGNQQKVILARCMA---- 425
Cdd:COG4559 85 slafPFTVEEVVALG------RAPHGSSAAQDRQIV---REALA--LVGlahlAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 426 ---LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
281-487 |
1.31e-16 |
|
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: 79.07 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQ-GIALvpedrkKEGAVLGL 359
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQvGVVL------QENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNLSSLMRwRWFVNTRKED------DLIDAYRQALHIKMVNsdqevrkLSGGNQQKVILARCMALNPKVLIV 433
Cdd:cd03252 91 SIRDNIALADPGMSME-RVIEAAKLAGahdfisELPEGYDTIVGEQGAG-------LSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 434 DEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
281-487 |
1.70e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 78.88 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYH-PSTPLHALSQGIALV-------PEdrkk 352
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdSKKDINKLRRKVGMVfqqfnlfPH---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 353 egavlgLSIRENISLSNLSSLMRwrwfvnTRKEddlidAYRQALHI-KMVN-SDQE---VRKLSGGNQQKVILARCMALN 427
Cdd:COG1126 92 ------LTVLENVTLAPIKVKKM------SKAE-----AEERAMELlERVGlADKAdayPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 428 PKVLIVDEPTRGID---VGtksEVHQVLFDMAKRGVAVIVISSDlpeiMA----ISDRIITLSEGRI 487
Cdd:COG1126 155 PKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHE----MGfareVADRVVFMDGGRI 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-220 |
1.87e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSF-SG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPVERQK 80
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL--PEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIITIYQefNLL----PNMSVAENMFLG-REPQSSGLfvdALAVNREAKAVL-DYLK-LNIA----PTTQVARLSVAQQ 149
Cdd:COG1101 80 KYIGRVFQ--DPMmgtaPSMTIEENLALAyRRGKRRGL---RRGLTKKRRELFrELLAtLGLGlenrLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 150 QmveiarALTL------NAKLIVMDEPSAAL---SDSEVDSL-HRVVRElkgRGVSVVYVTHRLHEVFQLCDRFTVFQDG 219
Cdd:COG1101 155 Q------ALSLlmatltKPKLLLLDEHTAALdpkTAALVLELtEKIVEE---NNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
.
gi 504513498 220 R 220
Cdd:COG1101 226 R 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-225 |
2.26e-16 |
|
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: 78.68 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIitIYQEfNLLPNMSVA 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV--VLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGREPQSSGLFVDALavnREAKAVLDYLKLNIAPTTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPSAALs 175
Cdd:cd03252 94 DNIALADPGMSMERVIEAA---KLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSAL- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 176 DSEvdSLHRVVRELKG--RGVSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSG 225
Cdd:cd03252 170 DYE--SEHAIMRNMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
281-487 |
2.60e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.88 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTplhalsqgialVPEDRKKEGAVL--- 357
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-----------LKEIRKKIGIIFqnp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 -----GLSIRENI--SLSNLSslmrwrwfVNTRKEDDLIDAYrqALHIKMVNS-DQEVRKLSGGNQQKVILARCMALNPK 429
Cdd:PRK13632 93 dnqfiGATVEDDIafGLENKK--------VPPKKMKDIIDDL--AKKVGMEDYlDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 430 VLIVDEPTRGIDVGTKSEVHQVLFDMAKRGV-AVIVISSDLPEIMaISDRIITLSEGRI 487
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
281-482 |
3.51e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.89 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVlddapyhpstplHALSQGIALVPEdRKKEGAVLGLS 360
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQ-RSEVPDSLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLSSLMRWRWFvnTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGI 440
Cdd:NF040873 74 VRDLVAMGRWARRGLWRRL--TRDDRAAVDDALERVGLADL-AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513498 441 DVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAIsDRIITL 482
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-226 |
3.69e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSF---SGVW--------ALSNAQLTVQRGEIHALLGENGAGKST----LLKALAgaqpqTSGDIWFGG 66
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 67 QQLLLLES----PVERQkrgIITIYQEFN--LLPNMSVAENMFLGREPQSSGLfvdaLAVNREAKAVLDYLKLNIAPTTQ 140
Cdd:PRK15134 347 QPLHNLNRrqllPVRHR---IQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTL----SAAQREQQVIAVMEEVGLDPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 141 ---VARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:PRK15134 420 hryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVL 499
|
250
....*....|
gi 504513498 217 QDGRYTGSGD 226
Cdd:PRK15134 500 RQGEVVEQGD 509
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
262-487 |
4.11e-16 |
|
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: 77.07 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 262 RLAVKGLS-REKPPLDAhgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALS 340
Cdd:cd03369 6 EIEVENLSvRYAPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-STIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 QGIALVPEDRkkegAVLGLSIRENISLSNlsslmrwrwfvntRKEDDLIdayRQALHIKMVNSDqevrkLSGGNQQKVIL 420
Cdd:cd03369 82 SSLTIIPQDP----TLFSGTIRSNLDPFD-------------EYSDEEI---YGALRVSEGGLN-----LSQGQRQLLCL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 421 ARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEImAISDRIITLSEGRI 487
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGEV 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
273-487 |
4.21e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 273 PPLDAHGIA--------LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIA 344
Cdd:PRK09536 2 PMIDVSDLSvefgdttvLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE-ALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 345 LVPEDrkkEGAVLGLSIRENISLSNLSSLMRWrwfvNTRKEDDLiDAYRQALHIKMVN--SDQEVRKLSGGNQQKVILAR 422
Cdd:PRK09536 81 SVPQD---TSLSFEFDVRQVVEMGRTPHRSRF----DTWTETDR-AAVERAMERTGVAqfADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 423 CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
281-487 |
4.52e-16 |
|
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: 77.06 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAP---YHPS-TPLhaLSQGIALVPEDRKkegAV 356
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRaIPY--LRRKIGVVFQDFR---LL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 LGLSIRENISLSnLSSLMRWRWFVNTRKED--DLIDAYRQALHIKMvnsdqevrKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:cd03292 91 PDRNVYENVAFA-LEVTGVPPREIRKRVPAalELVGLSHKHRALPA--------ELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-225 |
4.54e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.98 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSF--SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQlllLESPVERQKR 81
Cdd:TIGR01257 927 PGVCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD---IETNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMFL-----GREPQSSGLfvdalavnrEAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIAR 156
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFyaqlkGRSWEEAQL---------EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 157 ALTLNAKLIVMDEPSAALSDSEVDSLHRVVreLKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRsGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
281-487 |
5.28e-16 |
|
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: 78.94 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG---ADGFSSGEFVLDDapyhpsTPLHALSQ---------GIALVPE 348
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDG------EDLLKLSEkelrkirgrEIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 349 D-------RKKEGAVLGLSIRENISLSnlsslmrwrwfvntRKEddlidAYRQAL-HIKMVN-SDQEVRK------LSGG 413
Cdd:COG0444 94 DpmtslnpVMTVGDQIAEPLRIHGGLS--------------KAE-----ARERAIeLLERVGlPDPERRLdrypheLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 414 NQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-228 |
5.59e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.50 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSF---SGVW--------ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPqTSGDIWFGGQQLLL 71
Cdd:COG4172 273 PPLLEARDLKVWFpikRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 72 LESPVERQKRGIITI-----YQEFNllPNMSVAEnmfLGREpqssGLFVDALAVNREA--KAVLDYL-KLNIAPTTQvAR 143
Cdd:COG4172 352 LSRRALRPLRRRMQVvfqdpFGSLS--PRMTVGQ---IIAE----GLRVHGPGLSAAErrARVAEALeEVGLDPAAR-HR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 144 ----LSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEVDslHRVV---REL-KGRGVSVVYVTHRLHEVFQLCDRFTV 215
Cdd:COG4172 422 ypheFSGGQRQRIAIARALILEPKLLVLDEPTSAL-DVSVQ--AQILdllRDLqREHGLAYLFISHDLAVVRALAHRVMV 498
|
250
....*....|...
gi 504513498 216 FQDGRYTGSGDVA 228
Cdd:COG4172 499 MKDGKVVEQGPTE 511
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
263-486 |
6.21e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLdahgIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALS-- 340
Cdd:PRK11300 6 LSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIArm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 ------QGIALVPEdrkkegavlgLSIRENISLSN--------LSSLMRWRWFvnTRKEDDLIDayRQALHIKMVN---- 402
Cdd:PRK11300 81 gvvrtfQHVRLFRE----------MTVIENLLVAQhqqlktglFSGLLKTPAF--RRAESEALD--RAATWLERVGlleh 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 403 SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQvLFDMAKR--GVAVIVISSDLPEIMAISDRII 480
Cdd:PRK11300 147 ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDE-LIAELRNehNVTVLLIEHDMKLVMGISDRIY 225
|
....*.
gi 504513498 481 TLSEGR 486
Cdd:PRK11300 226 VVNQGT 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-215 |
6.42e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFS----GVW---------ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL 69
Cdd:PRK15079 6 KVLLEVADLKVHFDikdgKQWfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 70 LLLESPVERQKRG-IITIYQE--FNLLPNMSVAENMflgREP-QSSGLFVDALAVNREAKAVLdyLKLNIAPTtQVAR-- 143
Cdd:PRK15079 86 LGMKDDEWRAVRSdIQMIFQDplASLNPRMTIGEII---AEPlRTYHPKLSRQEVKDRVKAMM--LKVGLLPN-LINRyp 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 144 --LSVAQQQMVEIARALTLNAKLIVMDEPSAALSDS----EVDSLHRVVRELkgrGVSVVYVTHRLHEVFQLCDRFTV 215
Cdd:PRK15079 160 heFSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaqVVNLLQQLQREM---GLSLIFIAHDLAVVKHISDRVLV 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-201 |
6.56e-16 |
|
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: 76.24 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVERQkRGIIT 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP--LAEQRDEPH-ENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSVAENM-FLGREPQSSGLFVDALavnreakavLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:TIGR01189 78 LGHLPGLKPELSALENLhFWAAIHGGAQRTIEDA---------LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTH 201
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
7.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.92 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSG-VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVERQKRGI 83
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP--ITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEF-NLLPNMSVAENMFLGrePQSSGLfvDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNA 162
Cdd:PRK13652 81 GLVFQNPdDQIFSPTVEQDIAFG--PINLGL--DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQE 234
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-228 |
1.04e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 18 VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLespverqkrgiitiyqEFN--LLPN 95
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL----------------ELGagFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 MSVAENMFLgrepqsSGLFvdaLAVNR-EAKAVLD----------YLKLniaP-----TTQVARLSVAqqqmVeiarALT 159
Cdd:COG1134 103 LTGRENIYL------NGRL---LGLSRkEIDEKFDeivefaelgdFIDQ---PvktysSGMRARLAFA----V----ATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 160 LNAKLIVMDEpsaALS--DSE-VDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:COG1134 163 VDPDILLVDE---VLAvgDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-227 |
1.10e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQ-----RGeIHALLGENGAGKSTLLKALAG-AQPQtSGDIWFGGQQLLLLES----PVErqKRGIITIYQEF 90
Cdd:PRK11144 10 LGDLCLTVNltlpaQG-ITAIFGRSGAGKTSLINAISGlTRPQ-KGRIVLNGRVLFDAEKgiclPPE--KRRIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 91 NLLPNMSVAENMFLGREPQSSGLF---VDALAVnreaKAVLDYLklniaPTTqvarLSVAQQQMVEIARALTLNAKLIVM 167
Cdd:PRK11144 86 RLFPHYKVRGNLRYGMAKSMVAQFdkiVALLGI----EPLLDRY-----PGS----LSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 168 DEPSAALS---DSEV-DSLHRVVRELKgrgVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDV 227
Cdd:PRK11144 153 DEPLASLDlprKRELlPYLERLAREIN---IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-225 |
1.43e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 27 TVQRGEIHALLGENGAGKSTLLKALAGAQPQtSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLPNMSVAenmflgr 106
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLS--QQQTPPFAMPVF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 107 epQSSGLFVDALAVNREAKAVLDYL--KLNIAP--TTQVARLSVAQQQMVEIA-------RALTLNAKLIVMDEPSAALS 175
Cdd:PRK03695 88 --QYLTLHQPDKTRTEAVASALNEVaeALGLDDklGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 176 DSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
282-487 |
1.57e-15 |
|
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: 75.97 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALSQGIALVPEdrkkEGAVLGLSI 361
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKYLHSKVSLVGQ----EPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNLS-SLMRWRWFVNTRKEDDLIDAYRQALHikmVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGI 440
Cdd:cd03248 105 QDNIAYGLQScSFECVKEAAQKAHAHSFISELASGYD---TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513498 441 DVGTKSEVHQVLFDMAKRgVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03248 182 DAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-241 |
1.83e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESpvERQKRGIITIYQEFNLLPNMSVAENMFLG 105
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS--KAFARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 106 REPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDS-EVDSLHR 184
Cdd:PRK10575 110 RYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhQVDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 185 VVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVG 241
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
282-496 |
1.95e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 75.55 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSqgialvpED------RKKEGA 355
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG------QDLFALD-------EDararlrARHVGF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 356 VL-------GLSIRENISLSnlsslmrwrwfVNTRKEDDLIDAYRQALhikmvnsdQEV----------RKLSGGNQQKV 418
Cdd:COG4181 95 VFqsfqllpTLTALENVMLP-----------LELAGRRDARARARALL--------ERVglghrldhypAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 419 ILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDlPEIMAISDRIITLSEGRISGEIHGDDA 496
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVEDTAATAA 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
263-487 |
2.02e-15 |
|
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: 74.27 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhPSTPLHALSQG 342
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 IALVPEdrkkEGAVLGLSIRENISlsnlsslmrwrwfvntrkeddlidayrqalhikmvnsdqevRKLSGGNQQKVILAR 422
Cdd:cd03247 77 ISVLNQ----RPYLFDTTLRNNLG-----------------------------------------RRFSGGERQRLALAR 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 423 CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAIsDRIITLSEGRI 487
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-229 |
2.08e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQTsGDIWFGGQQLLLLESPVERQKrgIITIYQEfNLLPNMSVAENMFLG 105
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKH--LSWVGQN-PQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 106 RePQSSGLFVDALAVNREAKAVLDYLK--LNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAAL-SDSEvdsl 182
Cdd:PRK11174 447 N-PDASDEQLQQALENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLdAHSE---- 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 183 HRVVRELKG--RGVSVVYVTHRLHEVFQlCDRFTVFQDGRYTGSGDVAS 229
Cdd:PRK11174 522 QLVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
280-487 |
2.12e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 75.65 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEdrkkEGAVLGL 359
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR-DLNLRWLRSQIGLVSQ----EPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNlsslmrwrwfvNTRKEDDLIDAYRQALHIKMVNS-----DQEV----RKLSGGNQQKVILARCMALNPKV 430
Cdd:cd03249 92 TIAENIRYGK-----------PDATDEEVEEAAKKANIHDFIMSlpdgyDTLVgergSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 431 LIVDEPTRGIDVGTKSEVHQVLfDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-223 |
2.47e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.39 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 18 VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ---TSGDIWFGGQQLllleSPVERQKRgIITIYQEFNLLP 94
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR----KPDQFQKC-VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 95 NMSVAE-----NMFLGREPQSsglfvDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:cd03234 95 GLTVREtltytAILRLPRKSS-----DAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 170 PSAALSDSEVDSLHRVVRELKGRGvSVVYVThrLH----EVFQLCDRFTVFQDGR--YTG 223
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRN-RIVILT--IHqprsDLFRLFDRILLLSSGEivYSG 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
281-487 |
2.49e-15 |
|
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: 74.98 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDD------APYHPSTPLhaLSQGIALVPEdrkkeg 354
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlPPKDRDIAM--VFQNYALYPH------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 355 avlgLSIRENISLSnlsslmrwrwfVNTRKED-DLIDA-YRQA---LHIKMVnSDQEVRKLSGGNQQKVILARCMALNPK 429
Cdd:cd03301 87 ----MTVYDNIAFG-----------LKLRKVPkDEIDErVREVaelLQIEHL-LDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 430 VLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
248-501 |
2.58e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 248 RRPPSETHHQDKPVRLAVKGLSREKPP--LDAHGIA--------LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADG 317
Cdd:PRK13536 13 RLELSPIERKHQGISEAKASIPGSMSTvaIDLAGVSksygdkavVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 318 FSSGEFVLDDAPYhPSTPLHALSqGIALVPEDRKKEgavLGLSIRENIslsnlssLMRWRWF-VNTRKEDDLIDAYRQAL 396
Cdd:PRK13536 93 PDAGKITVLGVPV-PARARLARA-RIGVVPQFDNLD---LEFTVRENL-------LVFGRYFgMSTREIEAVIPSLLEFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 397 HIKMvNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAIS 476
Cdd:PRK13536 161 RLES-KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLC 239
|
250 260
....*....|....*....|....*
gi 504513498 477 DRIITLSEGRISGEIHGDDATEEKL 501
Cdd:PRK13536 240 DRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-220 |
2.82e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVW---------ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLES 74
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 75 PVERQ-KRGIITIYQE----FNllPNMSVAENMflgREPQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQV-ARLSVAQ 148
Cdd:PRK10419 82 AQRKAfRRDIQMVFQDsisaVN--PRKTVREII---REPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 149 QQMVEIARALTLNAKLIVMDEpsaALSDSEVDSLHRVVRELKG----RGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDE---AVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-225 |
4.69e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALA------GAQPQTSGDIWFGGQQLLLLESPV 76
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 77 ERQKRGIItiYQEFNLLPNMSVAENMflgrepqSSGLFVDALAVNREAKAVLD------------YLKLNiAPTTQvarL 144
Cdd:PRK14246 88 LRKEVGMV--FQQPNPFPHLSIYDNI-------AYPLKSHGIKEKREIKKIVEeclrkvglwkevYDRLN-SPASQ---L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 145 SVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKgRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGS 224
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
.
gi 504513498 225 G 225
Cdd:PRK14246 234 G 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
249-486 |
4.81e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.80 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 249 RPPSETHHQDKPVrLAVKGLSREkppLDAHgIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDD- 327
Cdd:PRK11607 7 RPQAKTRKALTPL-LEIRNLTKS---FDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 328 -----APYHpsTPLHALSQGIALVPEdrkkegavlgLSIRENISLSnLSSLMRWRWFVNTRKEDDLIDAYRQALhikmvn 402
Cdd:PRK11607 82 dlshvPPYQ--RPINMMFQSYALFPH----------MTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEF------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 403 SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIIT 481
Cdd:PRK11607 143 AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAI 222
|
....*
gi 504513498 482 LSEGR 486
Cdd:PRK11607 223 MNRGK 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
281-486 |
4.92e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLD--DAPYHPSTPLHALSQGIALVPED-------RK 351
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgqDLLKADPEAQKLLRQKIQIVFQNpygslnpRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 352 KEGAVLGLSIRENISLS------NLSSLMRwrwFVNTRKEDdlidaYRQALHIkmvnsdqevrkLSGGNQQKVILARCMA 425
Cdd:PRK11308 110 KVGQILEEPLLINTSLSaaerreKALAMMA---KVGLRPEH-----YDRYPHM-----------FSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-225 |
5.08e-15 |
|
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: 74.18 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 14 SFS---GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIitIYQEF 90
Cdd:cd03254 9 NFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV--VLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 91 NLLPNmSVAENMFLGREpqssglFVDALAVNREAKAV-LDYL--KLNIAPTTQV----ARLSVAQQQMVEIARALTLNAK 163
Cdd:cd03254 87 FLFSG-TIMENIRLGRP------NATDEEVIEAAKEAgAHDFimKLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 164 LIVMDEPSAALsDSEVDSL-HRVVREL-KGRgvSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSG 225
Cdd:cd03254 160 ILILDEATSNI-DTETEKLiQEALEKLmKGR--TSIIIAHRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-220 |
5.23e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLL--ESPVERQKRGIITIYQEFNLLPNMSV 98
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 99 AENMFL------GREPQSSGlfvdalavnrEAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:PRK10584 106 LENVELpallrgESSRQSRN----------GAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 173 ALS----DSEVDSLHRVVRELkgrGVSVVYVTHRLhEVFQLCDRFTVFQDGR 220
Cdd:PRK10584 176 NLDrqtgDKIADLLFSLNREH---GTTLILVTHDL-QLAARCDRRLRLVNGQ 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-228 |
5.81e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSF---------SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLE 73
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 74 SPVERQKrgIITIYQEfnllPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYLK----LNIAPTTQVARLSVAQQ 149
Cdd:PRK15112 82 YSYRSQR--IRMIFQD----PSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRqvglLPDHASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 150 QMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
281-487 |
7.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 7.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpstpLHALSQGIALvPEDRKKEGAVLGL- 359
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--------VDITDKKVKL-SDIRKKVGLVFQYp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 -------SIRENISL--SNLSslmrwrwfvntRKEDDLIDAYRQAlhIKMVNSDQEVRK------LSGGNQQKVILARCM 424
Cdd:PRK13637 93 eyqlfeeTIEKDIAFgpINLG-----------LSEEEIENRVKRA--MNIVGLDYEDYKdkspfeLSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 425 ALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
7.67e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.64 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSFSGV--WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQK 80
Cdd:PRK13632 5 SVMIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 81 RGIitIYQE-FNLLPNMSVAENMFLGRE-----PQSSGLFVDALAVNREAKAVLDYLKLNiapttqvarLSVAQQQMVEI 154
Cdd:PRK13632 85 IGI--IFQNpDNQFIGATVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVGMEDYLDKEPQN---------LSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 155 ARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFqLCDRFTVFQDGRYTGSGDVAST-NV 232
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIlNN 232
|
....*..
gi 504513498 233 QEIIRLM 239
Cdd:PRK13632 233 KEILEKA 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
282-487 |
8.35e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALSQGIALVPEDrkkegAVLG--L 359
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRAVLPQH-----SSLSfpF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLsnlsSLMRWRwfvNTRKEDD-LIDAYRQA---LHIkmvnSDQEVRKLSGGNQQKVILARCMA------LNPK 429
Cdd:PRK13548 92 TVEEVVAM----GRAPHG---LSRAEDDaLVAAALAQvdlAHL----AGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 430 VLIVDEPTRGIDVGTKSEVHQVLFDMA-KRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-220 |
8.45e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSG-VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLEsPVErqkRGII 84
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-PAD---RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TIYQEFNLLPNMSVAENMflgrepqSSGLFVDALA---VNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLN 161
Cdd:PRK11650 80 MVFQNYALYPHMSVRENM-------AYGLKIRGMPkaeIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 162 AKLIVMDEPsaaLSDseVDSLHRV-----VRELKGR-GVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK11650 153 PAVFLFDEP---LSN--LDAKLRVqmrleIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
261-469 |
8.48e-15 |
|
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: 77.02 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 261 VRLAVKGLSREKPPldaHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLHALS 340
Cdd:TIGR02868 333 PTLELRDLSAGYPG---APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 QGIALVPEDrkkeGAVLGLSIRENISLSNlsslmrwrwfvNTRKEDDLIDAYRQA------------LHIKMVnsdQEVR 408
Cdd:TIGR02868 409 RRVSVCAQD----AHLFDTTVRENLRLAR-----------PDATDEELWAALERVgladwlralpdgLDTVLG---EGGA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDmAKRGVAVIVISSDL 469
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-230 |
8.65e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqlLLLESPVERQKRGIITIY----QEFNLLPN 95
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-------SILGQPTRQALQKNLVAYvpqsEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 MSVAENMFLGREPQsSGLFVDALAVNRE----AKAVLDYLKLNiapTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:PRK15056 95 VLVEDVVMMGRYGH-MGWLRRAKKRDRQivtaALARVDMVEFR---HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 172 AALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDrFTVFQDGRYTGSGDVAST 230
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETT 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
281-487 |
8.67e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 73.91 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyHPSTPLHALSQGIALVPEDRkkeGAVLGLS 360
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQERNVGFVFQHY---ALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSnlsslMRWRwFVNTRKEDDLIDAYRQALhIKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEP 436
Cdd:cd03296 91 VFDNVAFG-----LRVK-PRSERPPEAEIRAKVHEL-LKLVQldwlADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 437 TRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-245 |
8.97e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.39 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIItiYQEfnllPN- 95
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV--FQD----PDd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 ----MSVAENMFLGrePQSSGLfvDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:PRK13647 91 qvfsSTVWDDVAFG--PVNMGL--DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 172 AALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVastnvqeiiRLMVGRDVV 245
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK---------SLLTDEDIV 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-201 |
1.07e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqlLLLESPVERQK----R 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-------LLNGGPLDFQRdsiaR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENM-FLGREPQSSGLFvdalavnrEAkavLDYLKLNIAPTTQVARLSVAQQQMVEIARALTL 160
Cdd:cd03231 74 GLLYLGHAPGIKTTLSVLENLrFWHADHSDEQVE--------EA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504513498 161 NAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTH 201
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
281-482 |
1.25e-14 |
|
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: 76.17 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPlHALSQGIALVPEdrkkEGAVLGLS 360
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQIAWVPQ----HPFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSnlsslmrwrwfvntRKE---------------DDLIDAYRQALHIKMvnsDQEVRKLSGGNQQKVILARCMA 425
Cdd:TIGR02857 412 IAENIRLA--------------RPDasdaeirealeraglDEFVAALPQGLDTPI---GEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAkRGVAVIVISSDlPEIMAISDRIITL 482
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
284-490 |
1.26e-14 |
|
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: 75.15 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 284 DISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQGIALVPEdRKKEGAVLG----- 358
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG------RTLFDSRKGIFLPPE-KRRIGYVFQearlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 --LSIRENislsnlssLMRWRWFVNTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEP 436
Cdd:TIGR02142 88 phLSVRGN--------LRYGMKRARPSERRISFERVIELLGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 437 TRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
1.32e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.05 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKA-------LAGAQPQtsGDIWFGGQQLLLLE- 73
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFRVE--GKVTFHGKNLYAPDv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 74 SPVERQKRgIITIYQEFNLLPNmSVAENMFLGREPQSSGLFVDALAVNREAKAVL-DYLKLNIAPTTQvaRLSVAQQQMV 152
Cdd:PRK14243 85 DPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALwDEVKDKLKQSGL--SLSGGQQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKgRGVSVVYVTHRLHEVFQLCDrFTVFQDGRYTGSG 225
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD-MTAFFNVELTEGG 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-220 |
1.33e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.53 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKAL-------AGAQpqTSGDIWFGGQQLLLLE-SPVE-RQKRGIItiYQEF 90
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEDIYDPDvDVVElRRRVGMV--FQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 91 NLLPnMSVAENMFLGrepqssglfvdaLAVNREA-KAVLDYL----------------KLNiaptTQVARLSVAQQQMVE 153
Cdd:COG1117 102 NPFP-KSIYDNVAYG------------LRLHGIKsKSELDEIveeslrkaalwdevkdRLK----KSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 154 IARALTLNAKLIVMDEPSAAL---SDSEVDSLhrvVRELKGRgVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALdpiSTAKIEEL---ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-220 |
1.42e-14 |
|
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: 72.91 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 19 WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPVERQKRGIITIYQEFNLLPNmSV 98
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI--GLHDLRSRISIIPQDPVLFSG-TI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 99 AENM-FLGRepQSSGLFVDALAVNREAKAVLDYLKLNIAPTTQV-ARLSVAQQQMVEIARALTLNAKLIVMDEPSAALsD 176
Cdd:cd03244 95 RSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGgENLSVGQRQLLCLARALLRKSKILVLDEATASV-D 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513498 177 SEVDSL-HRVVRElKGRGVSVVYVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:cd03244 172 PETDALiQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-225 |
1.43e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.90 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGV--WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllLLESPVER 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV--LSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRGIITIYQEfnllpnmsvAENMFLGREPQSSGLF-VDALAVNRE-----AKAVLDYLKLNIAPTTQVARLSVAQQQMV 152
Cdd:PRK13635 79 VRRQVGMVFQN---------PDNQFVGATVQDDVAFgLENIGVPREemverVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKG-RGVSVVYVTHRLHEVFQlCDRFTVFQDGRYTGSG 225
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
281-487 |
1.58e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALV---PEDR-----KK 352
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-FEKLRKHIGIVfqnPDNQfvgsiVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 353 EGAVLGLsirENISLSNlsslmrwrwfvntrkeDDLIDAYRQAL-HIKMVN-SDQEVRKLSGGNQQKVILARCMALNPKV 430
Cdd:PRK13648 103 YDVAFGL---ENHAVPY----------------DEMHRRVSEALkQVDMLErADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 431 LIVDEPTRGIDVGTKSEvhqvLFDMAKR-----GVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:PRK13648 164 IILDEATSMLDPDARQN----LLDLVRKvksehNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
281-487 |
1.78e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTP-LHALSQGIALVPEDrkKEGAVLGL 359
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRESVGMVFQD--PDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNLSSLMrwrwfvntrKEDDLIDAYRQAL------HIKmvnsDQEVRKLSGGNQQKVILARCMALNPKVLIV 433
Cdd:PRK13636 99 SVYQDVSFGAVNLKL---------PEDEVRKRVDNALkrtgieHLK----DKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 434 DEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-220 |
1.89e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.81 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAG--AQPQTSGDIWFGGQQLlllesPVERQKRGIITIYQEFNLLPNMSV 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL-----DKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 99 AENmflgrepqssglfvdalavnreakavLDYlklniapTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSE 178
Cdd:cd03213 100 RET--------------------------LMF-------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504513498 179 VDSLHRVVRELKGRGVSVVYVTHRL-HEVFQLCDRFTVFQDGR 220
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
281-487 |
2.19e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGadgfssgefVLddapyHPStplhalsQGIALV----PEDRKKE--- 353
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---------IL-----VPT-------SGEVRVlgyvPFKRRKEfar 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 --GAVLG--------LSIREniSLSNLSSLMRwrwfVNTRKEDDLIDAYRQALHI--KMvnsDQEVRKLSGGnqQKVila 421
Cdd:COG4586 96 riGVVFGqrsqlwwdLPAID--SFRLLKAIYR----IPDAEYKKRLDELVELLDLgeLL---DTPVRQLSLG--QRM--- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 422 RC---MAL--NPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG4586 162 RCelaAALlhRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
281-487 |
2.45e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.29 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALVPED-------RKKE 353
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-YSYRSQRIRMIFQDpstslnpRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 GAVLGLSIRENISLSnlsslmrwrwfvNTRKEDDLIDAYRQaLHIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIV 433
Cdd:PRK15112 107 SQILDFPLRLNTDLE------------PEQREKQIIETLRQ-VGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 434 DEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-225 |
2.53e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.68 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQ--KRGIITIYQEFNLLPNMS 97
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMFLGREpqssglFVDALAVNREAKAvLDYLK---LNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAAL 174
Cdd:PRK10070 123 VLDNTAFGME------LAGINAEERREKA-LDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 175 SDSEVDSLHRVVRELKGRGV-SVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
282-487 |
3.34e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhpSTPLH-ALSQGIALVPEDRkkegAVLGLS 360
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--SSLSHsVLRQGVAMVQQDP----VVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLS-NLSSLMRWRwFVNTRKEDDLIDAYRQALHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRG 439
Cdd:PRK10790 431 FLANVTLGrDISEEQVWQ-ALETVQLAELARSLPDGLYTPL---GEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513498 440 IDVGTKSEVHQVLfDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:PRK10790 507 IDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
278-487 |
4.03e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 278 HGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLfgadgfsSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKKEGAVL 357
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELLGRTVQREGRLARDIRKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 G-----------LSIRENISLSNLSSLMRWR----WFVNTRKEDdlidAYRQALHIKMVN-SDQEVRKLSGGNQQKVILA 421
Cdd:PRK09984 89 GyifqqfnlvnrLSVLENVLIGALGSTPFWRtcfsWFTREQKQR----ALQALTRVGMVHfAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 422 RCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
282-488 |
4.53e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.66 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpstpLHALSqGIALVPEDRKKEGAVLG--- 358
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--------LKVND-PKVDERLIRQEAGMVFQqfy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ----LSIRENISLSNLsslmRWRwfvNTRKEDdlidAYRQALHI-KMVNSDQEVR----KLSGGNQQKVILARCMALNPK 429
Cdd:PRK09493 88 lfphLTALENVMFGPL----RVR---GASKEE----AEKQARELlAKVGLAERAHhypsELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 430 VLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-225 |
4.89e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.42 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL-----LLLESpveRQKRGIitIYQEF- 90
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEV---RKTVGI--VFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 91 NLLPNMSVAENMFLGrePQSSGLFVDalAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEP 170
Cdd:PRK13639 89 DQLFAPTVEEDVAFG--PLNLGLSKE--EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 171 SAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
260-487 |
5.63e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 70.66 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 260 PVRLAVKGLSREKP--PLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG--ADGFSSGEFVLDDAPYHPstp 335
Cdd:cd03213 1 GVTLSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 336 lHALSQGIALVPEDRkkegAVLG-LSIRENISLSnlsslmrwrwfvntrkeddlidayrqalhikmvnsdQEVRKLSGGN 414
Cdd:cd03213 78 -RSFRKIIGYVPQDD----ILHPtLTVRETLMFA------------------------------------AKLRGLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 415 QQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVI----SSdlpEIMAISDRIITLSEGRI 487
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
282-495 |
9.69e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpstplhalsQGIALVpedRKKEGAvLGLSI 361
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG-------------QTINLV---RDKDGQ-LKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNLSSLMRWR----WFVNTRKEDdLIDAYRQAL-------------HIKMVNSDQEVR-----KLSGGNQQKVI 419
Cdd:PRK10619 84 KNQLRLLRTRLTMVFQhfnlWSHMTVLEN-VMEAPIQVLglskqeareravkYLAKVGIDERAQgkypvHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 420 LARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGEIHGDD 495
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-202 |
9.93e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQkrgII 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ---LC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 85 TIYQEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNREAKAVLDYlklniapttQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHR 202
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
256-487 |
1.03e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.76 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 256 HQDKPVRLAVKGLSREKPpLDAHGIAL--KDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDdapyhpS 333
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQI-LEKTGLSLgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID------G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 334 TPLHALSQgiALVPEDRKKEGAVLGLS---IRENISLSNLSSLMRWRWFVNTRKEDDLIDAYRQALHIKMVNSDQEvrKL 410
Cdd:PRK10070 90 VDIAKISD--AELREVRRKKIAMVFQSfalMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD--EL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 411 SGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10070 166 SGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
282-487 |
1.29e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG---ADgfsSGEFVLDDapyHPST--PLHALSQ-GIALVPED----RK 351
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkPD---SGRIFLDG---EDIThlPMHKRARlGIGYLPQEasifRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 352 kegavlgLSIRENI----SLSNLSSLMRwrwfvnTRKEDDLIDAyrqaLHIkmvnsdQEVRK-----LSGGNQQKVILAR 422
Cdd:COG1137 93 -------LTVEDNIlavlELRKLSKKER------EERLEELLEE----FGI------THLRKskaysLSGGERRRVEIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 423 CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
281-487 |
1.93e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSG--EFVLDDAPYHPSTPLHAL-----------SQGIALVP 347
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiEWIFKDEKNKKKTKEKEKvleklviqktrFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 348 EDRKKEGAVLGL--------SIRENISLSNLSslmrwrwfVNTRKEDdlidAYRQAL-HIKMVNSDQEVRK-----LSGG 413
Cdd:PRK13651 102 EIRRRVGVVFQFaeyqlfeqTIEKDIIFGPVS--------MGVSKEE----AKKRAAkYIELVGLDESYLQrspfeLSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 414 NQQKVILARCMALNPKVLIVDEPTRGID-VGTKsEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDpQGVK-EILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
282-484 |
2.24e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGefvlddapyhpsTPLHALSQGIALVPEDrkkegavlgLSI 361
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------------VIKRNGKLRIGYVPQK---------LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSnLSSLMRWRwfVNTRKEDDLIDAYR-QALHIkmvnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGI 440
Cdd:PRK09544 79 DTTLPLT-VNRFLRLR--PGTKKEDILPALKRvQAGHL----IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513498 441 DVGTKSEVHQvLFDMAKR--GVAVIVISSDLPEIMAISDRIITLSE 484
Cdd:PRK09544 152 DVNGQVALYD-LIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-224 |
2.64e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGqqllllESPVERQKRgiitiyqefnLLPNMSVa 99
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG------YVPFKRRKE----------FARRIGV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 enMFlGrepQSSGLF-----VDALAVNR--------EAKAVLDYLK--LNIAP--TTQVARLSVAQQQMVEIARALTLNA 162
Cdd:COG4586 100 --VF-G---QRSQLWwdlpaIDSFRLLKaiyripdaEYKKRLDELVelLDLGEllDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 163 KLIVMDEPSAALsdsEVDSLHRV---VREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR--YTGS 224
Cdd:COG4586 174 KILFLDEPTIGL---DVVSKEAIrefLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRiiYDGS 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
2.73e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.02 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSF-SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG-AQPQTSGDIWFGGQQLLLLESPVERQKRG 82
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGlLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLpNMSVAENMFLGREpqssGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNA 162
Cdd:PRK13644 81 IVFQNPETQFV-GRTVEEDLAFGPE----NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-203 |
3.44e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 71.62 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGqqlLLLESPVERQKRGIITIYQEFNLLPNMSVA 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG---VPVSSLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGREPQSSGLFVDALavnrEAKAVLDYLK-----LNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAAL 174
Cdd:TIGR02868 427 ENLRLARPDATDEELWAAL----ERVGLADWLRalpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180 190
....*....|....*....|....*....|.
gi 504513498 175 sDSEVDSlhRVVREL--KGRGVSVVYVTHRL 203
Cdd:TIGR02868 503 -DAETAD--ELLEDLlaALSGRTVVLITHHL 530
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-220 |
3.46e-13 |
|
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: 69.18 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQEfNLLPNMSVAE 100
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP--QD-TVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NMFLGREPQSSglfVDALAVNREAKAVLDYLKLNIAPTTQVA----RLSVAQQQMVEIARALTLNAKLIVMDEPSAAL-S 175
Cdd:cd03253 94 NIRYGRPDATD---EEVIEAAKAAQIHDKIMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSALdT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513498 176 DSEVDSLHRVVRELKGRgvSVVYVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:cd03253 171 HTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-226 |
3.65e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGA-QPQTSGDIWFGgqqlllleSPVERQKRGI 83
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlRPQKGAVLWQG--------KPLDYSKRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 I-------TIYQE---------------FNLlPNMSVAENMFLGRepqssglfVDalavnrEAKAVLDYLKLNIAPttqV 141
Cdd:PRK13638 73 LalrqqvaTVFQDpeqqifytdidsdiaFSL-RNLGVPEAEITRR--------VD------EALTLVDAQHFRHQP---I 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 142 ARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRY 221
Cdd:PRK13638 135 QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
....*
gi 504513498 222 TGSGD 226
Cdd:PRK13638 215 LTHGA 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-65 |
4.29e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 4.29e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFG 65
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG 375
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
282-487 |
4.61e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLhalSQGIALVPEDRKKEGAVLglsi 361
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSL---SQQKGLIRQLRQHVGFVF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 rENISL----SNLSSLMRWRWFVNTRKEDDLIDAYRQALhIKMVNSDQEV---RKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:PRK11264 92 -QNFNLfphrTVLENIIEGPVIVKGEPKEEATARARELL-AKVGLAGKETsypRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
263-487 |
4.92e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKppldAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDdapyhpSTPLHALSQG 342
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG------TAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 IALVPEDR-----KKEGAVLGLSIRENislsnlsslmrWRwfvntrkeddliDAYRQALH-IKMVNSDQE-VRKLSGGNQ 415
Cdd:PRK11247 83 TRLMFQDArllpwKKVIDNVGLGLKGQ-----------WR------------DAALQALAaVGLADRANEwPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 416 QKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
263-487 |
5.29e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 67.99 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPpldaHGIALKDISFQVHAGeVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpstplhalsqg 342
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 343 ialVPEDRKKEGAVLGL-----SIRENISLSNLSSLMRWRWFVNTRKEDDLIDAYRQALHIKMVNsDQEVRKLSGGNQQK 417
Cdd:cd03264 63 ---VLKQPQKLRRRIGYlpqefGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 418 VILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-220 |
5.77e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.31 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGG-----QQLLLLESpveRQKRGIITIYQEFNLLP 94
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDI---RKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 95 NmSVAENMFLGrePQSSGLFVDALA--VNREAKAV-LDYLKL-NIAPTtqvaRLSVAQQQMVEIARALTLNAKLIVMDEP 170
Cdd:PRK13637 99 E-TIEKDIAFG--PINLGLSEEEIEnrVKRAMNIVgLDYEDYkDKSPF----ELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 171 SAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-220 |
5.82e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.38 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqlLLLESPVERQKRGIITIYQE-FNLLPNMSVA 99
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD--LLTEENVWDIRHKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGREPQssGLFVDALaVNREAKAvLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEV 179
Cdd:PRK13650 101 DDVAFGLENK--GIPHEEM-KERVNEA-LELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504513498 180 DSLHRVVRELKGR-GVSVVYVTHRLHEVfQLCDRFTVFQDGR 220
Cdd:PRK13650 177 LELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
281-487 |
6.16e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 70.18 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHA-----LSQGIALVPEdrkkega 355
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRErrvgfVFQHYALFPH------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 356 vlgLSIRENIS--LSNLsslmrwRWFVNTRKE--DDLIDAYrQALHIKmvnsDQEVRKLSGGNQQKVILARCMALNPKVL 431
Cdd:COG1118 90 ---MTVAENIAfgLRVR------PPSKAEIRArvEELLELV-QLEGLA----DRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
257-486 |
7.39e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 257 QDKPVRLAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG---ADGFSSGE--FVLDDAPYH 331
Cdd:PRK09473 7 QQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSatFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 332 PSTPLHAL-SQGIALVPEDrkkegavlglsireniSLSNLSSLMRwrwfVNTRKEDDLI--------DAYRQAlhIKMVN 402
Cdd:PRK09473 87 PEKELNKLrAEQISMIFQD----------------PMTSLNPYMR----VGEQLMEVLMlhkgmskaEAFEES--VRMLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 403 SDQ--EVRK--------LSGGNQQKVILArcMAL--NPKVLIVDEPTRGIDVGTKSEVHQVLFDMaKR--GVAVIVISSD 468
Cdd:PRK09473 145 AVKmpEARKrmkmypheFSGGMRQRVMIA--MALlcRPKLLIADEPTTALDVTVQAQIMTLLNEL-KRefNTAIIMITHD 221
|
250
....*....|....*...
gi 504513498 469 LPEIMAISDRIITLSEGR 486
Cdd:PRK09473 222 LGVVAGICDKVLVMYAGR 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
281-487 |
1.12e-12 |
|
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: 67.56 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpsTPLHALsqGIALVPEdrkkegavlgLS 360
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV----SSLLGL--GGGFNPE----------LT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENIslsnlssLMRWRWFVNTRKE-DDLIDAyrqalhIKMVNS-----DQEVRKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:cd03220 101 GRENI-------YLNGRLLGLSRKEiDEKIDE------IIEFSElgdfiDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
270-487 |
1.13e-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: 70.74 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 270 REKPPLDahgIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALSQGIALVPED 349
Cdd:TIGR00957 1293 RYREDLD---LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-AKIGLHDLRFKITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 350 RkkegAVLGLSIRENIS-LSNLSSLMRWrWFVNTRKEDDLIDAYRQALHIKMVNSDQevrKLSGGNQQKVILARCMALNP 428
Cdd:TIGR00957 1369 P----VLFSGSLRMNLDpFSQYSDEEVW-WALELAHLKTFVSALPDKLDHECAEGGE---NLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVL---FDmakrGVAVIVISSDLPEIMAISdRIITLSEGRI 487
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIrtqFE----DCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
1.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 18 VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIW-----------FGGQQLLLLESPVERQKR----- 81
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknNHELITNPYSKKIKNFKElrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEFNLLPNMSVAENMF----LGREPQSSglfvDALAVNREAKAVLDYLKLNIAPTtqvaRLSVAQQQMVEIARA 157
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDIMFgpvaLGVKKSEA----KKLAKFYLNKMGLDDSYLERSPF----GLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 158 LTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
281-487 |
1.33e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.21 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLD--DAPYHPST--PLHALSQGIALVPEdrkkegav 356
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqDITHVPAEnrHVNTVFQSYALFPH-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 lgLSIRENISLSnLSSLMRWRWFVNTRKEDDLidayrqalhiKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVLI 432
Cdd:PRK09452 101 --MTVFENVAFG-LRMQKTPAAEITPRVMEAL----------RMVQleefAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 433 VDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
281-490 |
1.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.18 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY-HPSTPLHALSQGIALV---PEDRkkegaV 356
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYDKKSLLEVRKTVGIVfqnPDDQ-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 LGLSIRENISLSNLSSLMrwrwfvntrKEDDLIDAYRQALH-IKMVNSDQEV-RKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:PRK13639 92 FAPTVEEDVAFGPLNLGL---------SKEEVEKRVKEALKaVGMEGFENKPpHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
282-487 |
1.53e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.83 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDdapyhpstplhalsqGIALVPED----RKKEGAVL 357
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID---------------GDLLTEENvwdiRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 glsirENISlsnlsslmrwRWFVNTRKEDD--------------LIDAYRQALH-IKMVN-SDQEVRKLSGGNQQKVILA 421
Cdd:PRK13650 88 -----QNPD----------NQFVGATVEDDvafglenkgipheeMKERVNEALElVGMQDfKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 422 RCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEImAISDRIITLSEGRI 487
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-65 |
1.60e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.78 E-value: 1.60e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFG 65
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG 60
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-226 |
1.76e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 22 SNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL-LLLESPVERQKRGIITIYQEFNLLPNMSVAE 100
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NM-FLGRE----PQSsgLFVDALAVNREAkavldyLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALS 175
Cdd:PRK11831 104 NVaYPLREhtqlPAP--LLHSTVMMKLEA------VGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 176 DSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK11831 176 PITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-480 |
1.81e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 27 TVQRGEIHALLGENGAGKSTLLKALAGA------QPQTSGDiW------FGGQQLL-LLESPVERQKRGIITIyQEFNLL 93
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgDYEEEPS-WdevlkrFRGTELQnYFKKLYNGEIKVVHKP-QYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 PNmsvaenmflgrepQSSGLFVDALAVNREAKAVLDYLK-LNIAPTT--QVARLSVAQQQMVEIARALTLNAKLIVMDEP 170
Cdd:PRK13409 173 PK-------------VFKGKVRELLKKVDERGKLDEVVErLGLENILdrDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 171 SAALSDSEVDSLHRVVRELkGRGVSVVYVTHRLHEVFQLCDRFTVF--QDGRYTGSGDVASTNV-----------QEIIR 237
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNVHIAygEPGAYGVVSKPKGVRVgineylkgylpEENMR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 238 LmvgRD--VVFNRRPPSEThhQDKPVRLAVKGLSREKP--PLDAHGialkdisFQVHAGEVLGIAGLVGAGRTEIARCLF 313
Cdd:PRK13409 319 I---RPepIEFEERPPRDE--SERETLVEYPDLTKKLGdfSLEVEG-------GEIYEGEVIGIVGPNGIGKTTFAKLLA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 314 GADGFSSGEFVLD-DAPYHPstplhalsQGIAlvpedRKKEGAVLGL--SIRENISLSnlsslmrwrwFVNTrkedDLID 390
Cdd:PRK13409 387 GVLKPDEGEVDPElKISYKP--------QYIK-----PDYDGTVEDLlrSITDDLGSS----------YYKS----EIIK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 391 ayRQALHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMA-KRGVAVIVISSDL 469
Cdd:PRK13409 440 --PLQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDI 514
|
490
....*....|.
gi 504513498 470 PEIMAISDRII 480
Cdd:PRK13409 515 YMIDYISDRLM 525
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-226 |
1.83e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL--LLLESpverqKRGIITIYQEFNLLPNMS 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtkLQLDS-----WRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMFLGRePQSSGLFVDALAvnREAKAVLDYLKLNIAPTTQVAR----LSVAQQQMVEIARALTLNAKLIVMDEpsaA 173
Cdd:PRK10789 405 VANNIALGR-PDATQQEIEHVA--RLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDD---A 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 174 LSDSEVDSLHRVVRELK--GRGVSVVYVTHRLhEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRqwGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGN 532
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
410-487 |
1.95e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 1.95e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
281-487 |
1.97e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHAlSQGIALvpedRKKEGAVLG-- 358
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSE-KAIRLL----RQKVGMVFQqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 -----LSIRENI--------SLSNLSSLMRWRWFVNTRKEDDLIDAYrqALHikmvnsdqevrkLSGGNQQKVILARCMA 425
Cdd:COG4161 92 nlwphLTVMENLieapckvlGLSKEQAREKAMKLLARLRLTDKADRF--PLH------------LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
285-499 |
2.19e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 285 ISFQVHAGEVLGIAGLVGAGRTE----IArclfgadGF---SSGEFVLDD---APYHPST-PLHALSQGIALVPEdrkke 353
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTllnlIA-------GFlppDSGRILWNGqdlTALPPAErPVSMLFQENNLFPH----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 gavlgLSIRENISLSnLSSLMRwrwfvntrkeddLIDAYRQALH--IKMVN-SDQEVRK---LSGGNQQKVILARCMALN 427
Cdd:COG3840 86 -----LTVAQNIGLG-LRPGLK------------LTAEQRAQVEqaLERVGlAGLLDRLpgqLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRisgeIHGDDATEE 499
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGR----IAADGPTAA 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-220 |
2.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.42 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE-RQKRGII----------TIYQ 88
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDiRNKAGMVfqnpdnqivaTIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 89 EfnllpnmSVA---ENmfLGREPQSSGLFVD-ALavnreaKAVLDYLKLNIAPTTqvarLSVAQQQMVEIARALTLNAKL 164
Cdd:PRK13633 105 E-------DVAfgpEN--LGIPPEEIRERVDeSL------KKVGMYEYRRHAPHL----LSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGK 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
281-513 |
2.42e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.19 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEfvlddapyhpstplhalsqgIALVPEDRKKEGAVLGLS 360
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE--------------------VAWLGKDLLGMKDDEWRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISL---SNLSSLmrwrwfvNTRKE-DDLIDAYRQALHIKMvnSDQEVRK----------------------LSGGN 414
Cdd:PRK15079 96 VRSDIQMifqDPLASL-------NPRMTiGEIIAEPLRTYHPKL--SRQEVKDrvkammlkvgllpnlinrypheFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 415 QQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRisgeihg 493
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH------- 239
|
250 260
....*....|....*....|
gi 504513498 494 ddATEekLMTMMAICHDALH 513
Cdd:PRK15079 240 --AVE--LGTYDEVYHNPLH 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
282-487 |
2.74e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQG--------IALVPED---- 349
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG------EPLAKLNRAqrkafrrdIQMVFQDsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 350 ---RKKEGAVLGLSIRENISLSNLSSLMRwrwfvntrkeddlIDAYRQALHIKMVNSDQEVRKLSGGNQQKVILARCMAL 426
Cdd:PRK10419 102 vnpRKTVREIIREPLRHLLSLDKAERLAR-------------ASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 427 NPKVLIVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-237 |
2.79e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.65 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 8 ITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiy 87
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 88 QEFNLLPNMSVAENMFLGREPQSSG-LFVDALAVNREAkavLDYLKLniaptTQVAR-----LSVAQQQMVEIARALTLN 161
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSKGrLTAEDREIIDEA---IAYLDL-----EDLADryldeLSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 162 AKLIVMDEP--------SAALsdseVDSLHRVVRELkGRGVSVVyvthrLHEV-FQLC--DRFTVFQDGRYtgsgdVAST 230
Cdd:COG4604 154 TDYVLLDEPlnnldmkhSVQM----MKLLRRLADEL-GKTVVIV-----LHDInFASCyaDHIVAMKDGRV-----VAQG 218
|
....*..
gi 504513498 231 NVQEIIR 237
Cdd:COG4604 219 TPEEIIT 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-480 |
2.81e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.04 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 27 TVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqllllESPVERQK-----RGIItIYQEFNLLPN--MSVA 99
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY----------DEEPSWDEvlkrfRGTE-LQDYFKKLANgeIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 enmflgREPQssglFVDALA-----VNREA------KAVLDYL--KLNIAPTTQ--VARLSVAQQQMVEIARALTLNAKL 164
Cdd:COG1245 164 ------HKPQ----YVDLIPkvfkgTVRELlekvdeRGKLDELaeKLGLENILDrdISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVF--QDGRYtgsGDVA---STNV------- 232
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygEPGVY---GVVSkpkSVRVginqyld 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 233 ----QEIIRLmvgRD--VVFNRRPPSEThhQDKPVRLAVKGLSREKPpldahGIALKDISFQVHAGEVLGIAGLVGAGRT 306
Cdd:COG1245 311 gylpEENVRI---RDepIEFEVHAPRRE--KEEETLVEYPDLTKSYG-----GFSLEVEGGEIREGEVLGIVGPNGIGKT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 307 EIARCLFGADGFSSGEFVLD-DAPYHPstplhalsQGIAlvpedRKKEGAV---LGLSIRENISLSnlsslmrwrWFvnt 382
Cdd:COG1245 381 TFAKILAGVLKPDEGEVDEDlKISYKP--------QYIS-----PDYDGTVeefLRSANTDDFGSS---------YY--- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 383 rkEDDLIDayRQALHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMA-KRGVA 461
Cdd:COG1245 436 --KTEIIK--PLGLEKLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKT 508
|
490
....*....|....*....
gi 504513498 462 VIVISSDLPEIMAISDRII 480
Cdd:COG1245 509 AMVVDHDIYLIDYISDRLM 527
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
281-487 |
2.88e-12 |
|
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: 66.56 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARC---LFGADgfsSGEFVLDDAPYHPSTPLhalsqgialvpEDRKKEGAVL 357
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMinrLIEPT---SGEIFIDGEDIREQDPV-----------ELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 ---GL----SIRENISLsnLSSLMRWrwfvntrKEDDLIDAYRQALhiKMVNSDQEV------RKLSGGNQQKVILARCM 424
Cdd:cd03295 82 qqiGLfphmTVEENIAL--VPKLLKW-------PKEKIRERADELL--ALVGLDPAEfadrypHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 425 ALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-229 |
2.95e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 22 SNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQP----QTSGDIWFGGQQLllleSPVERQKRGIITIYQE----FNLL 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPV----APCALRGRKIATIMQNprsaFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 PNMSVAenmflGREpqsSGLFVDALAVNREAKAVLDYLKLNIAPTtqVARLSVAQ------QQMVeIARALTLNAKLIVM 167
Cdd:PRK10418 96 HTMHTH-----ARE---TCLALGKPADDATLTAALEAVGLENAAR--VLKLYPFEmsggmlQRMM-IALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 168 DEPSA---ALSDSEV-DSLHRVVRElkgRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVAS 229
Cdd:PRK10418 165 DEPTTdldVVAQARIlDLLESIVQK---RALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-202 |
3.43e-12 |
|
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: 64.48 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqllllESPVErqkrgiitiyqefnllpnmsvAE 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEG---------------------ED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NMFLGREPQ-SSGLFVDALAvnreakavldYlklniaPTTQVarLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDsev 179
Cdd:cd03223 66 LLFLPQRPYlPLGTLREQLI----------Y------PWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE--- 124
|
170 180
....*....|....*....|...
gi 504513498 180 DSLHRVVRELKGRGVSVVYVTHR 202
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGHR 147
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
281-487 |
3.49e-12 |
|
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: 66.10 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALVPEDrkkegAVL-GL 359
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQIGLVSQD-----VFLfND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNLSSlmrwrwfvntrKEDDLIDAYRQA-LHIKMVNSDQ------EVR--KLSGGNQQKVILARCMALNPKV 430
Cdd:cd03251 91 TVAENIAYGRPGA-----------TREEVEEAARAAnAHEFIMELPEgydtviGERgvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 431 LIVDEPTRGIDVGTKSEVHQVLfDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:cd03251 160 LILDEATSALDTESERLVQAAL-ERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-227 |
3.79e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVW--ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLllespverqkRG 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----------TN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGRE-----PQSSGlfVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARA 157
Cdd:TIGR01257 2007 ISDVHQNMGYCPQFDAIDDLLTGREhlylyARLRG--VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 158 LTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDV 227
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
263-487 |
4.39e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSRekppLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGE--FVLDDAPYHPstpLHALS 340
Cdd:PRK11701 7 LSVRGLTK----LYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQLRD---LYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 QgialvPEDRK-------------KEGAVLGLSIRENISlsnlSSLMR--WRWFVNTRKE--DDL----IDAYRqalhik 399
Cdd:PRK11701 80 E-----AERRRllrtewgfvhqhpRDGLRMQVSAGGNIG----ERLMAvgARHYGDIRATagDWLerveIDAAR------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 400 mvnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVgtksEVHQVLFDMAKR-----GVAVIVISSDLPEIMA 474
Cdd:PRK11701 145 ---IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGlvrelGLAVVIVTHDLAVARL 217
|
250
....*....|...
gi 504513498 475 ISDRIITLSEGRI 487
Cdd:PRK11701 218 LAHRLLVMKQGRV 230
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-226 |
4.40e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ--TSGDIWFGGQQLLLLEsPVERQKRG 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELS-PEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSvaeNMFL------------GREPQSSGLFVDALavnrEAKAVLDYLKLNIAPTTQVARLSVAQQQ 150
Cdd:PRK09580 80 IFMAFQYPVEIPGVS---NQFFlqtalnavrsyrGQEPLDRFDFQDLM----EEKIALLKMPEDLLTRSVNVGFSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALsdsEVDSLHRV---VRELKGRGVSVVYVTH--RLHEVFQlCDRFTVFQDGRYTGSG 225
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGL---DIDALKIVadgVNSLRDGKRSFIIVTHyqRILDYIK-PDYVHVLYQGRIVKSG 228
|
.
gi 504513498 226 D 226
Cdd:PRK09580 229 D 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-225 |
4.60e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.45 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLllleSPVERQ--KRGIITIYQEFNLLpNMS 97
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI----RTVTRAslRRNIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMFLGREPQSSGLFVDALavnrEAKAVLDYL-----KLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:PRK13657 425 IEDNIRVGRPDATDEEMRAAA----ERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 173 ALsDSEVDSlhRVVREL----KGRGVSVvyVTHRLHEVfQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13657 501 AL-DVETEA--KVKAALdelmKGRTTFI--IAHRLSTV-RNADRILVFDNGRVVESG 551
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
282-487 |
4.78e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY----HpstplHALSQGIALVpedrKKEGAVL 357
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqydH-----HYLHRQVALV----GQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 GLSIRENISlsnlsslmrwrwFVNTRKEDDLIDAYRQALHI-----KMVNS-DQEV----RKLSGGNQQKVILARCMALN 427
Cdd:TIGR00958 568 SGSVRENIA------------YGLTDTPDEEIMAAAKAANAhdfimEFPNGyDTEVgekgSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQvlfDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
274-487 |
4.85e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.78 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 274 PLDAHGiaLKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEfvLDDAPYH--PSTP---LHALSQGIALV-- 346
Cdd:PRK13641 17 PMEKKG--LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT--ITIAGYHitPETGnknLKKLRKKVSLVfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 347 -PEDRKKEGAVLglsirENISLSNLSslmrwrwFVNTRKEddlidAYRQALH-IKMVNSDQEVR-----KLSGGNQQKVI 419
Cdd:PRK13641 93 fPEAQLFENTVL-----KDVEFGPKN-------FGFSEDE-----AKEKALKwLKKVGLSEDLIskspfELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 420 LARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
281-486 |
5.20e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.53 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDApYHPSTPLHALSQGIALVpedRKKEgavLG-- 358
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD-GGWVDLAQASPREILAL---RRRT---IGyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ---LSIRENISLSNL--SSLMRWRWfvntrkedDLIDAYRQA------LHIKmvnsdqevRKL--------SGGNQQKVI 419
Cdd:COG4778 99 sqfLRVIPRVSALDVvaEPLLERGV--------DREEARARArellarLNLP--------ERLwdlppatfSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 420 LARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-225 |
5.46e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL---LLLESPVERQKRGIITIYQ--EFNLLP 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 95 NmSVAENMFLGrePQSSGlfvdalAVNREA-KAVLDYLKLNIAPTTQVAR----LSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:PRK13645 106 E-TIEKDIAFG--PVNLG------ENKQEAyKKVPELLKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 170 PSAALS-DSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13645 177 PTGGLDpKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
281-487 |
5.90e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.03 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSqGIALVPEdRKKEGAV---- 356
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG------VDLTALS-ERELRAA-RRKIGMIfqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 -LgLS---IRENISLSnlssLMRWRWFVNTRKE--DDLIDayrqalhikMVN-SDQE---VRKLSGGNQQKVILARCMAL 426
Cdd:COG1135 92 nL-LSsrtVAENVALP----LEIAGVPKAEIRKrvAELLE---------LVGlSDKAdayPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 427 NPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-477 |
5.97e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSG-------EFvLDDAPYHPSTPLHALSQGIALV-PEDRkke 353
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEvrvegrvEF-FNQNIYERRVNLNRLRRQVSMVhPKPN--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 gaVLGLSIRENISLSnlSSLMRWRWFV-------NTRKEDDLIDAYRQALHikmvnsdQEVRKLSGGNQQKVILARCMAL 426
Cdd:PRK14258 99 --LFPMSVYDNVAYG--VKIVGWRPKLeiddiveSALKDADLWDEIKHKIH-------KSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 427 NPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRG-VAVIVISSDLPEIMAISD 477
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-220 |
6.30e-12 |
|
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: 64.80 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllespverqkrgiITIYQEFNLLPNMSVA 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS----------------IAYVSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGREpqssglfVDalavNREAKAVLDY--LK--LNIAPT---TQV----ARLSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:cd03250 84 ENILFGKP-------FD----EERYEKVIKAcaLEpdLEILPDgdlTEIgekgINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 169 EPSAALsDSEVDS--LHRVVRELKGRGVSVVYVTHRLHeVFQLCDRFTVFQDGR 220
Cdd:cd03250 153 DPLSAV-DAHVGRhiFENCILGLLLNNKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
281-487 |
7.00e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.68 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLD--DAPYHPSTPLHALSQGIALVPED-------RK 351
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSGRELRPLRRRMQMVFQDpyaslnpRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 352 KEGAVLGLSIRenislsnlsslmrwrwfVNTRKEDDLIDAYRQALhIKMV--NSDQEVR---KLSGGNQQKVILARCMAL 426
Cdd:COG4608 113 TVGDIIAEPLR-----------------IHGLASKAERRERVAEL-LELVglRPEHADRyphEFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 427 NPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG4608 175 NPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-468 |
7.06e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 36 LLGENGAGKSTLLKALAGAQPQTSGDIWfggqqllllesPVERQKRGIITiyQEFNLLPNMSVAENMFLG---------R 106
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEAR-----------PQPGIKVGYLP--QEPQLDPTKTVRENVEEGvaeikdaldR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 107 EPQSSGLF------VDALAVNR-EAKAVLDYL-------KLNIA--------PTTQVARLSVAQQQMVEIARALTLNAKL 164
Cdd:TIGR03719 103 FNEISAKYaepdadFDKLAAEQaELQEIIDAAdawdldsQLEIAmdalrcppWDADVTKLSGGERRRVALCRLLLSKPDM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 165 IVMDEPSAALSDSEVDSLHRVVRELKGrgvSVVYVTHrlhevfqlcDRFtvFQDgrytgsgdvastNVQE-IIRLMVGRD 243
Cdd:TIGR03719 183 LLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH---------DRY--FLD------------NVAGwILELDRGRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 244 VVF-----------NRRPPSETHHQDKP----------VRLAVKG---------------LSREK-----------PP-- 274
Cdd:TIGR03719 237 IPWegnysswleqkQKRLEQEEKEESARqktlkrelewVRQSPKGrqakskarlaryeelLSQEFqkrnetaeiyiPPgp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 275 ------LDAHGIA--------LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpstplhalS 340
Cdd:TIGR03719 317 rlgdkvIEAENLTkafgdkllIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE------------T 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 QGIALVpeDRKKEGAVLGLSIRENISlSNLSSLMRWRWFVNTRkeddlidAYRQALHIKmvNSDQE--VRKLSGGNQQKV 418
Cdd:TIGR03719 385 VKLAYV--DQSRDALDPNKTVWEEIS-GGLDIIKLGKREIPSR-------AYVGRFNFK--GSDQQkkVGQLSGGERNRV 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 504513498 419 ILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAkrGVAViVISSD 468
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAV-VISHD 499
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
409-490 |
7.15e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRgVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
..
gi 504513498 489 GE 490
Cdd:PRK14271 242 EE 243
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-220 |
1.06e-11 |
|
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: 64.56 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 17 GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLpNM 96
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVS--QDVFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENMFLGREPQSSGLFVDALavnREAKAVLDYLKLNIAPTTQVA----RLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:cd03251 91 TVAENIAYGRPGATREEVEEAA---RAANAHEFIMELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 173 ALsDSEVDslhRVVRE-----LKGRGVSVvyVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:cd03251 168 AL-DTESE---RLVQAalerlMKNRTTFV--IAHRLSTIEN-ADRIVVLEDGK 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-204 |
1.07e-11 |
|
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: 64.27 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 16 SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDI-WFGGQQLLLLESPVERQKRGIITIYQEFNLLP 94
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 95 NMSVAENMFLGR--EPQSSGLFVDALAVNREakavLDYLKLniAPTTQVAR----LSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:cd03290 92 NATVEENITFGSpfNKQRYKAVTDACSLQPD----IDLLPF--GDQTEIGErginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 504513498 169 EPSAALSDSEVDSLHR--VVRELKGRGVSVVYVTHRLH 204
Cdd:cd03290 166 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-275 |
1.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.53 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE----RQKRGIITIYQEFNLLPN 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikpvRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 mSVAENMFLGrePQSSGlfvdalaVNREAKAVLDYLKLNIAPTTQ------VARLSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:PRK13643 101 -TVLKDVAFG--PQNFG-------IPKEKAEKIAAEKLEMVGLADefweksPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 170 PSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGdVASTNVQEIIRLMVGRDVVfnrr 249
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG-TPSDVFQEVDFLKAHELGV---- 245
|
250 260
....*....|....*....|....*.
gi 504513498 250 pPSETHHQDKPVRLAVkgLSREKPPL 275
Cdd:PRK13643 246 -PKATHFADQLQKTGA--VTFEKLPI 268
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-487 |
1.17e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCL-----FGADGFSSGEFVLD--DAPYHPSTPLHALSQGIALVPEdrkkeg 354
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDgqDIFKMDVIELRRRVQMVFQIPN------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 355 AVLGLSIRENISLSnlsslMRWRWFVNTRKEddLIDAYRQALHIKMVNSDQEVR------KLSGGNQQKVILARCMALNP 428
Cdd:PRK14247 93 PIPNLSIFENVALG-----LKLNRLVKSKKE--LQERVRWALEKAQLWDEVKDRldapagKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMaKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-219 |
1.31e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.11 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSF---SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLllESPVERQKR 81
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQE-FNLLPNMSVAENMFLGREPQssGLFVDALaVNREAKAVLDYLKLNIApTTQVARLSVAQQQMVEIARALTL 160
Cdd:PRK13642 82 KIGMVFQNpDNQFVGATVEDDVAFGMENQ--GIPREEM-IKRVDEALLAVNMLDFK-TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 161 NAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQlCDRFTVFQDG 219
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAG 216
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-241 |
1.48e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 23 NAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLPNMSVAENM 102
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA--QNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 103 FLGREPQSSgLFV-----DALAVNREAKAVldylKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDS 177
Cdd:PRK10253 103 ARGRYPHQP-LFTrwrkeDEEAVTKAMQAT----GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 178 EVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVASTNVQEIIRLMVG 241
Cdd:PRK10253 178 HQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-220 |
1.63e-11 |
|
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: 64.03 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKrgIITIYQEFNLLPNmSVAE 100
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK--VSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NMFLGRePQSSGLFVDALAVNREAKAVLDylKLNIAPTTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPSAALsd 176
Cdd:cd03248 107 NIAYGL-QSCSFECVKEAAQKAHAHSFIS--ELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSAL-- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504513498 177 sEVDSLHRVVRELKG--RGVSVVYVTHRLHEVfQLCDRFTVFQDGR 220
Cdd:cd03248 182 -DAESEQQVQQALYDwpERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
282-503 |
1.65e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPlHALSQGIALVPEDrkkegavlgLSI 361
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLARRLALLPQH---------HLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNLSSLMR--W--RWFVNTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPT 437
Cdd:PRK11231 88 PEGITVRELVAYGRspWlsLWGRLSAEDNARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 438 RGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGEihgddATEEKLMT 503
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ-----GTPEEVMT 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
273-486 |
2.06e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 273 PPLDAHGI--------ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHAlSQGIA 344
Cdd:PRK13537 6 APIDFRNVekrygdklVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHA-RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 345 LVPEDRKKEGavlGLSIRENIslsnlssLMRWRWFVNTRKEddlIDAYRQAL--HIKMVN-SDQEVRKLSGGNQQKVILA 421
Cdd:PRK13537 84 VVPQFDNLDP---DFTVRENL-------LVFGRYFGLSAAA---ARALVPPLleFAKLENkADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 422 RCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
282-487 |
2.99e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 63.57 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARcLFGADgfssgefvlddapYHPSTPLHALSQGIALVPED----RKKEGAV- 356
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLS-LITGD-------------LPPTYGNDVRLFGERRGGEDvwelRKRIGLVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 --LGLSIRENISLSNL------SSLMRWRWFvnTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNP 428
Cdd:COG1119 85 paLQLRFPRDETVLDVvlsgffDSIGLYREP--TDEQRERARELLELLGLAHL-ADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMAKRG-VAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-220 |
3.00e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKST---LLKALAgaQPqTSGDIWFGGQQLLLLESPVERQKRGIITiyQEfNLLPNMS 97
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLY--QP-TGGQVLLDGVPLVQYDHHYLHRQVALVG--QE-PVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMFLG--REPQSsglfvDALAVNREAKAVLDYLKLNIAPTTQVA----RLSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:TIGR00958 571 VRENIAYGltDTPDE-----EIMAAAKAANAHDFIMEFPNGYDTEVGekgsQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 172 AALsDSEVDSLHRVVRELKGRgvSVVYVTHRLHEVfQLCDRFTVFQDGR 220
Cdd:TIGR00958 646 SAL-DAECEQLLQESRSRASR--TVLLIAHRLSTV-ERADQILVLKKGS 690
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-225 |
3.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.00 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE----RQKRGIITIYQEFNLLPN 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikqiRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 mSVAENMFLGrePQSSGlfvdalaVNREAKAVLDYLKLNIAPTTQVAR------LSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:PRK13649 102 -TVLKDVAFG--PQNFG-------VSQEEAEALAREKLALVGISESLFeknpfeLSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 170 PSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-220 |
3.22e-11 |
|
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: 62.81 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLesPVERQKRGIITIyqefnllpnmsva 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI--PLEDLRSSLTII------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 enmflgrePQSSGLFVDALAVNreakavLD----YLKLNIAPTTQVAR----LSVAQQQMVEIARALTLNAKLIVMDEPS 171
Cdd:cd03369 88 --------PQDPTLFSGTIRSN------LDpfdeYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 172 AALsDSEVDSL-HRVVRELKgRGVSVVYVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:cd03369 154 ASI-DYATDALiQKTIREEF-TNSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-201 |
3.47e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGqqllllESPVERQKRGI 83
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNLL-PNMSVAENM-----FLGREPqssglfvdalavnREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARA 157
Cdd:PRK13539 75 CHYLGHRNAMkPALTVAENLefwaaFLGGEE-------------LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504513498 158 LTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTH 201
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
286-488 |
3.57e-11 |
|
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: 62.96 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 286 SFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDD------APYHpsTPLHALSQGIALVPEdrkkegavlgL 359
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglAPYQ--RPVSMLFQENNLFAH----------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNLSSLMrwrwfVNTRKEDDLIDAYRQalhikMVNSDQEVR---KLSGGNQQKVILARCMALNPKVLIVDEP 436
Cdd:TIGR01277 86 TVRQNIGLGLHPGLK-----LNAEQQEKVVDAAQQ-----VGIADYLDRlpeQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 437 TRGIDVGTKSEVHQVLFDMA-KRGVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:TIGR01277 156 FSALDPLLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-212 |
4.15e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEihALL--GENGAGKSTLLKALAGAQPQTSGDIWF-GGQQLLLLesPverQKrgiitIYqefnlLPNMS 97
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFL--P---QR-----PY-----LPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMFLgrePQSSGLFVDAlavnrEAKAVLDYLKL--------NIAPTTQVarLSVAQQQMVEIARALTLNAKLIVMDE 169
Cdd:COG4178 442 LREALLY---PATAEAFSDA-----ELREALEAVGLghlaerldEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504513498 170 PSAALSDSEVDSLHRVVRElKGRGVSVVYVTHRlHEVFQLCDR 212
Cdd:COG4178 512 ATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDR 552
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
402-487 |
4.25e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 402 NSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK--RGVAVIVISSDLPEIMAISDRI 479
Cdd:cd03233 111 KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKV 190
|
....*...
gi 504513498 480 ITLSEGRI 487
Cdd:cd03233 191 LVLYEGRQ 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
256-487 |
4.49e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 256 HQDKPVrlaVKGLSrekppldahgialkdISFQVHAgeVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTP 335
Cdd:PRK13638 11 YQDEPV---LKGLN---------------LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 336 -LHALSQGIALVPEDRKKEgaVLGLSIRENI--SLSNLSSLMRwrwfVNTRKEDD---LIDA--YRQalhikmvnsdQEV 407
Cdd:PRK13638 71 gLLALRQQVATVFQDPEQQ--IFYTDIDSDIafSLRNLGVPEA----EITRRVDEaltLVDAqhFRH----------QPI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 408 RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13638 135 QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-228 |
4.65e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 31 GEIHALLGENGAGKSTLLKALAGaQPQTSGdiwFGGQQLLLLESPVERQKRGIITIYQEFNLLPNMSVAENMF---LGRE 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG-RIQGNN---FTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVfcsLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 108 PQSSGLFVDALAvnreAKAVLDYLKLNIAPTTQVAR-----LSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSL 182
Cdd:PLN03211 170 PKSLTKQEKILV----AESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504513498 183 HRVVRELKGRGVSVVYVTHR-LHEVFQLCDRFTVFQDGR--YTGSGDVA 228
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRclFFGKGSDA 294
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
281-487 |
5.89e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.94 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPyhpSTPLHALSQGIALVPEDrkkegAVL--G 358
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTDLPPKDRNIAMVFQS-----YALypH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENISLSnlsslMRWRwfvNTRKEDdlIDA-YRQALhiKMVN-SDQEVRK---LSGGNQQKVILARCMALNPKVLIV 433
Cdd:COG3839 90 MTVYENIAFP-----LKLR---KVPKAE--IDRrVREAA--ELLGlEDLLDRKpkqLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 434 DEPTRGID----VGTKSEVHQVLfdmAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:COG3839 158 DEPLSNLDaklrVEMRAEIKRLH---RRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
281-499 |
6.14e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyHPSTPLhALSQGiaLVPEdrkkegavlgLS 360
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSALL-ELGAG--FHPE----------LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSnlSSLM-RWRWFVNtRKEDDLID-----AYRqalhikmvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:COG1134 105 GRENIYLN--GRLLgLSRKEID-EKFDEIVEfaelgDFI----------DQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 435 EptrGIDVG-----TKSevHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRisgeIHGDDATEE 499
Cdd:COG1134 172 E---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR----LVMDGDPEE 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-219 |
7.78e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLES-----PVeRQKRGIITIYQEFNLLP 94
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPV-RKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 95 NmSVAENMFLGrePQSSGLFVDalavnrEAKAVLDYLKLNIAPTTQVARLSVAQQ---QMVEIA--RALTLNAKLIVMDE 169
Cdd:PRK13646 101 D-TVEREIIFG--PKNFKMNLD------EVKNYAHRLLMDLGFSRDVMSQSPFQMsggQMRKIAivSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 170 PSAALSDSEVDSLHRVVRELK-GRGVSVVYVTHRLHEVFQLCDRFTVFQDG 219
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
284-487 |
8.05e-11 |
|
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: 61.74 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 284 DISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY---HPST-PLHALSQGIALVPEdrkkegavlgL 359
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaaPPADrPVSMLFQENNLFAH----------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLSNLSSLmrwrwfvNTRKEDdlidayRQALHI---KMVNSDQEVRK---LSGGNQQKVILARCMALNPKVLIV 433
Cdd:cd03298 86 TVEQNVGLGLSPGL-------KLTAED------RQAIEValaRVGLAGLEKRLpgeLSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 434 DEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-228 |
8.54e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQP--------QTSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNL 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLP--QAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 93 LPNMSVAENMFLGREPQSSGlfvdALAVNREAKAVLDYLKLNIAPTTQVAR----LSVAQQQMVEIARAL---------T 159
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARR----AGALTHRDGEIAWQALALAGATALVGRdvttLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 160 LNAKLIVMDEPSAALSDSE----VDSLHRVVRELKgrgVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHqhrlLDTVRRLARDWN---LGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-202 |
1.06e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLlllespverqkrgiiTIYQEFNLlpnmsvae 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN---------------QFGREASL-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 nmflgrepqssglfVDALAVNREAKAVLDYL---KLNIAPT--TQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALs 175
Cdd:COG2401 103 --------------IDAIGRKGDFKDAVELLnavGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL- 167
|
170 180 190
....*....|....*....|....*....|..
gi 504513498 176 DSEVD-----SLHRVVRElkgRGVSVVYVTHR 202
Cdd:COG2401 168 DRQTAkrvarNLQKLARR---AGITLVVATHH 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
409-494 |
1.10e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
....*.
gi 504513498 489 GEIHGD 494
Cdd:PRK10908 217 GGVGGE 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
228-487 |
1.25e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 228 ASTNVQEIIRLMVgrDVVFnrrpPSETHHQDKPVRLAVKGLSREKPplDAHGIALKDISFQVHAGEVLGIAGLVGAGRTE 307
Cdd:PRK11160 310 SARRINEITEQKP--EVTF----PTTSTAAADQVSLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 308 IARCLFGADGFSSGEFVLDDAP---YHPStplhALSQGIALVPEdRKKegaVLGLSIRENISLSNlsslmrwrwfvNTRK 384
Cdd:PRK11160 382 LLQLLTRAWDPQQGEILLNGQPiadYSEA----ALRQAISVVSQ-RVH---LFSATLRDNLLLAA-----------PNAS 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 385 EDDLIDAYRQALHIKMVNSDQEV--------RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMA 456
Cdd:PRK11160 443 DEALIEVLQQVGLEKLLEDDKGLnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA 522
|
250 260 270
....*....|....*....|....*....|.
gi 504513498 457 KrGVAVIVISSDLPEiMAISDRIITLSEGRI 487
Cdd:PRK11160 523 Q-NKTVLMITHRLTG-LEQFDRICVMDNGQI 551
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-206 |
1.25e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTE--PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLeSPvER 78
Cdd:PRK10247 1 MQEnsPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL-KP-EI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 79 QKRGIITIYQEFNLLPNmSVAENMFL-----GREPQSSGLFVDalavnreakavLDYLKLNIAPTTQ-VARLSVAQQQMV 152
Cdd:PRK10247 79 YRQQVSYCAQTPTLFGD-TVYDNLIFpwqirNQQPDPAIFLDD-----------LERFALPDTILTKnIAELSGGEKQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 153 EIARALTLNAKLIVMDEPSAALSDSEV----DSLHRVVRElkgRGVSVVYVTHRLHEV 206
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKhnvnEIIHRYVRE---QNIAVLWVTHDKDEI 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-226 |
1.30e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.91 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 31 GEIHALLGENGAGKSTLLKALAGAQP---QTSGDIWFGGQqllllesPVERQKRGIITIY-QEFNL-LPNMSVAEN-MF- 103
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGM-------PIDAKEMRAISAYvQQDDLfIPTLTVREHlMFq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 104 ----LGREPQSSGlfvdalavNREA-KAVLDYLKLNIAPTT------QVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:TIGR00955 124 ahlrMPRRVTKKE--------KRERvDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 173 ALsDSEvdSLHRVVRELKG---RGVSVVYVTHR-LHEVFQLCDRFTVFQDGR--YTGSGD 226
Cdd:TIGR00955 196 GL-DSF--MAYSVVQVLKGlaqKGKTIICTIHQpSSELFELFDKIILMAEGRvaYLGSPD 252
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
263-487 |
1.50e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 263 LAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVL---------DDA----- 328
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqdvatldADAlaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 329 ---------PYHPSTPLHAlSQGI------ALVPEDRKKEGAV-----LGLSIRENislsnlsslmrwrwfvntrkeddl 388
Cdd:PRK10535 85 rehfgfifqRYHLLSHLTA-AQNVevpavyAGLERKQRLLRAQellqrLGLEDRVE------------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 389 idaYRQAlhikmvnsdqevrKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSD 468
Cdd:PRK10535 140 ---YQPS-------------QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
250
....*....|....*....
gi 504513498 469 lPEIMAISDRIITLSEGRI 487
Cdd:PRK10535 204 -PQVAAQAERVIEIRDGEI 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-201 |
1.59e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFgGQQLLL--LESPVERQKRG 82
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLIVarLQQDPPRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 iiTIYqEFnllpnmsVAENM---------------FLGREPQSSGLfvdalavNREAK--AVLDYL-------------- 131
Cdd:PRK11147 82 --TVY-DF-------VAEGIeeqaeylkryhdishLVETDPSEKNL-------NELAKlqEQLDHHnlwqlenrinevla 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 132 KLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGrgvSVVYVTH 201
Cdd:PRK11147 145 QLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISH 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
262-487 |
1.77e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.42 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 262 RLAVKGLSREKPPLDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPY-HPSTPLHALS 340
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtGPGADRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 341 QGIALVPEDRKKEGAVLGLSI-------RENISLSNLSSLmrwrwfvntrkedDLIDAYRQALHikmvnsdqevrKLSGG 413
Cdd:COG4525 83 QKDALLPWLNVLDNVAFGLRLrgvpkaeRRARAEELLALV-------------GLADFARRRIW-----------QLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 414 NQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLS--EGRI 487
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVMSpgPGRI 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-174 |
2.11e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKS-------FSG---VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLL 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHypvkrglFKPerlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 71 LLESPVERQKRGIITI-----YQEFNllPNMSVAENMflgREPqssglfvdaLAVN-------REAKaVLDYLKLNIAPT 138
Cdd:PRK11308 81 KADPEAQKLLRQKIQIvfqnpYGSLN--PRKKVGQIL---EEP---------LLINtslsaaeRREK-ALAMMAKVGLRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513498 139 TQVAR----LSVAQQQMVEIARALTLNAKLIVMDEPSAAL 174
Cdd:PRK11308 146 EHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
3.82e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.54 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFggQQLLLLESPVERQKRGIITIYQEfnllpnmsvA 99
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY--NNQAITDDNFEKLRKHIGIVFQN---------P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGREPQSSGLF------VDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAA 173
Cdd:PRK13648 93 DNQFVGSIVKYDVAFglenhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 174 LSDSEVDSLHRVVRELKG-RGVSVVYVTHRLHEVFQ-----LCDRFTVFQDG 219
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSeHNITIISITHDLSEAMEadhviVMNKGTVYKEG 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
282-490 |
4.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGAdgFSSGEFVLD-DAPYHPSTPLHALSQGIALVPEDrkKEGAVLGLS 360
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGL--FEEFEGKVKiDGELLTAENVWNLRRKIGMVFQN--PDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLSSLMrwrwfvntrKEDDLIDAYRQAL-HIKMVN-SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:PRK13642 99 VEDDVAFGMENQGI---------PREEMIKRVDEALlAVNMLDfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 439 GIDVGTKSEVHQVLFDMA-KRGVAVIVISSDLPEiMAISDRIITLSEGRISGE 490
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDE-AASSDRILVMKAGEIIKE 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
4.35e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE----RQKRGIITIYQEFNLLPN 95
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkplRKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 96 mSVAENMFLGrePQSSGLFV-DALavnREAKAVLDYLKLniaPTTQVAR----LSVAQQQMVEIARALTLNAKLIVMDEP 170
Cdd:PRK13634 102 -TVEKDICFG--PMNFGVSEeDAK---QKAREMIELVGL---PEELLARspfeLSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 171 SAALSDS---EV-DSLHRVVRElkgRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13634 173 TAGLDPKgrkEMmEMFYKLHKE---KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
404-487 |
5.09e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 404 DQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITL 482
Cdd:PRK11432 131 DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVM 210
|
....*
gi 504513498 483 SEGRI 487
Cdd:PRK11432 211 NKGKI 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
281-494 |
6.08e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDRKkegAVLGLS 360
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNlsslmrwrWFVNTRKEDDLIDAYRQALHIKMVNSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGI 440
Cdd:PRK11614 97 VEENLAMGG--------FFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 441 DVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRISGEIHGD 494
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-487 |
6.35e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSqGIALvpedRKKEGAVLG--- 358
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQID-AIKL----RKEVGMVFQqpn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ----LSIRENISLSNLSSLMRWRWFVNTRKEDDLidayRQALHIKMVNS--DQEVRKLSGGNQQKVILARCMALNPKVLI 432
Cdd:PRK14246 101 pfphLSIYDNIAYPLKSHGIKEKREIKKIVEECL----RKVGLWKEVYDrlNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 433 VDEPTRGIDVGTKSEVHQVLFDMaKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-285 |
6.88e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSG----VWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG---AQPQTSGDIWFGGQQLL-LL 72
Cdd:PRK09473 8 QADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREILnLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 73 ESPVER-QKRGIITIYQE--FNLLPNMSVAENMF----LGREPQSSGLFvdalavnREAKAVLDYLKL-------NIAPt 138
Cdd:PRK09473 88 EKELNKlRAEQISMIFQDpmTSLNPYMRVGEQLMevlmLHKGMSKAEAF-------EESVRMLDAVKMpearkrmKMYP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 139 tqvARLSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEVDS-LHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:PRK09473 160 ---HEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL-DVTVQAqIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 217 QDGRYTGSGDVastnvqeiirlmvgRDVVFNrrpPSETHHQdkpvrlavkGLSREKPPLDAHGIALKDI 285
Cdd:PRK09473 236 YAGRTMEYGNA--------------RDVFYQ---PSHPYSI---------GLLNAVPRLDAEGESLLTI 278
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
284-492 |
7.69e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 60.50 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 284 DISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQGIALVPEDRKkegavLG----- 358
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG------EVLQDSARGIFLPPHRRR-----IGyvfqe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ------LSIRENISLSnlsslmRWRWFVNTRKE--DDLIDAyrqaLHIkmvnS---DQEVRKLSGGNQQKVILARCMALN 427
Cdd:COG4148 86 arlfphLSVRGNLLYG------RKRAPRAERRIsfDEVVEL----LGI----GhllDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI--SGEIH 492
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVvaSGPLA 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
409-487 |
8.16e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
282-487 |
8.94e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.48 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyHPSTPLHAlsqgialvpEDRKKeGAVLG--- 358
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHA---------RDRKV-GFVFQhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ----LSIRENISLSnLSSLMRWRwfvntRKEDDLIDAYRQALhIKMVN----SDQEVRKLSGGNQQKVILARCMALNPKV 430
Cdd:PRK10851 85 lfrhMTVFDNIAFG-LTVLPRRE-----RPNAAAIKAKVTQL-LEMVQlahlADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 431 LIVDEPTRGIDVGTKSEVHQVLFDMAK--RGVAVIViSSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFV-THDQEEAMEVADRVVVMSQGNI 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
281-487 |
9.00e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHAlSQGIALvpedRKKEGAVLG-- 358
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSD-KAIREL----RRNVGMVFQqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 -----LSIRENI--------SLSNLSSLMRWRWFVNTRKEDDLIDAYrqALHikmvnsdqevrkLSGGNQQKVILARCMA 425
Cdd:PRK11124 92 nlwphLTVQQNLieapcrvlGLSKDQALARAEKLLERLRLKPYADRF--PLH------------LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504513498 426 LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-201 |
9.59e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKAL-----AGAQPQTSGDIWFGGQQLLLLE-SPVERQKRgIITIYQEFNLLPNMSVA 99
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDvDPIEVRRE-VGMVFQYPNPFPHLTIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGrepqssgLFVDALAVNRE----------AKAVL-DYLK--LNIAPttqvARLSVAQQQMVEIARALTLNAKLIV 166
Cdd:PRK14267 104 DNVAIG-------VKLNGLVKSKKeldervewalKKAALwDEVKdrLNDYP----SNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 504513498 167 MDEPSAALSDSEVDSLHRVVRELKgRGVSVVYVTH 201
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELK-KEYTIVLVTH 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
9.90e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDI-WF-----GGQQLLLLESPVE---------------- 77
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkdekNKKKTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 --RQKRGIITIYQEFNLLPNmSVAENMFLGrePQSSGLfvdalaVNREAKA-VLDYLKLNIAPTTQVAR----LSVAQQQ 150
Cdd:PRK13651 102 eiRRRVGVVFQFAEYQLFEQ-TIEKDIIFG--PVSMGV------SKEEAKKrAAKYIELVGLDESYLQRspfeLSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 151 MVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGD 226
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-228 |
1.12e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWfggqqllllespverQKRGIITIYQEFNLLpNMSVAE 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------------AERSIAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 101 NMflgrepqssgLFVDALAVNREAKAV------LDYLKLNIAPTTQVAR----LSVAQQQMVEIARALTLNAKLIVMDEP 170
Cdd:PTZ00243 740 NI----------LFFDEEDAARLADAVrvsqleADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 171 SAALsDSEVDslHRVVREL---KGRGVSVVYVTHRLHeVFQLCDRFTVFQDGRYTGSGDVA 228
Cdd:PTZ00243 810 LSAL-DAHVG--ERVVEECflgALAGKTRVLATHQVH-VVPRADYVVALGDGRVEFSGSSA 866
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
282-483 |
1.48e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRT---EIARCLFGADgfsSGEFVLDDAPYhpstplhalsqgIALVPEDRKKE----- 353
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKStllKIVASLISPT---SGTLLFEGEDI------------STLKPEIYRQQvsyca 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 354 --GAVLGLSIRENIslsnlssLMRWRWFVNTRKEDDLI-DAYRQALHIKMVnsDQEVRKLSGGNQQKVILARCMALNPKV 430
Cdd:PRK10247 88 qtPTLFGDTVYDNL-------IFPWQIRNQQPDPAIFLdDLERFALPDTIL--TKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 431 LIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEImAISDRIITLS 483
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEI-NHADKVITLQ 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-203 |
1.54e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 14 SFS---GVWALSNAQLTV-QRGEIhALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQkrGIITIYQE 89
Cdd:PRK10790 347 SFAyrdDNLVLQNINLSVpSRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ--GVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 90 FNLLPNmSVAENMFLGREPQSSGLFvDALAVNREAKAVLDYLK-LNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:PRK10790 424 PVVLAD-TFLANVTLGRDISEEQVW-QALETVQLAELARSLPDgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190
....*....|....*....|....*....|....*
gi 504513498 169 EPSAALSDSEVDSLHRVVRELKGRGVSVVyVTHRL 203
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVV-IAHRL 535
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-220 |
1.65e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSF----SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ----TSGDIWFGGQQLLLLeSP 75
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRL-SP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 VERQK---RGIITIYQEFN--LLPNMSVAENM--------FLGREPQSSGLfvdalavnREAKAVLDYLKLNIAPTTQVA 142
Cdd:PRK15093 81 RERRKlvgHNVSMIFQEPQscLDPSERVGRQLmqnipgwtYKGRWWQRFGW--------RKRRAIELLHRVGIKDHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 143 R-----LSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:PRK15093 153 RsfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL 232
|
....
gi 504513498 217 QDGR 220
Cdd:PRK15093 233 YCGQ 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
281-477 |
1.79e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpstplHALSQG-IALVPEDRKKEGAVLGL 359
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNlVAYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SirENISLSNLSSLMRWRWFVNTRKEDDLIDAYRQalhIKMVN-SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:PRK15056 97 V--EDVVMMGRYGHMGWLRRAKKRDRQIVTAALAR---VDMVEfRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 504513498 439 GIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISD 477
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-201 |
2.39e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 22 SNAQLTVQRGEIHALLGENGAGKSTLLKALAG-AQPqTSGDIWFGGQqllllesPVERQKrgiitiyQEF--NLL----- 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARP-DAGEVLWQGE-------PIRRQR-------DEYhqDLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 ----PNMSVAENMflgrepqssgLFVDALAVNREAKAVLDYL-KLNIA-----PttqVARLSVAQQQMVEIARALTLNAK 163
Cdd:PRK13538 83 pgikTELTALENL----------RFYQRLHGPGDDEALWEALaQVGLAgfedvP---VRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 504513498 164 LIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTH 201
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-441 |
2.47e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLEspVERQKRGI 83
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS--FEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 ITIYQEFNllpnmsvaeNMFLGREPQSSGLFVdalavnreAKAVLDYLKLNiAPTTQVAR--------------LSVAQQ 149
Cdd:PRK10938 80 SDEWQRNN---------TDMLSPGEDDTGRTT--------AEIIQDEVKDP-ARCEQLAQqfgitalldrrfkyLSTGET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 150 QMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDvas 229
Cdd:PRK10938 142 RKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 230 tnVQEIIrlmvgRDVVFNRRPPSETHH------QDKPvrLAVKGLSREKPPLDAHGIA--------LKDISFQVHAGEVL 295
Cdd:PRK10938 219 --REEIL-----QQALVAQLAHSEQLEgvqlpePDEP--SARHALPANEPRIVLNNGVvsyndrpiLHNLSWQVNPGEHW 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 296 GIAGLVGAGRTEIARCLFG--ADGFS-----------SGEFVLDdapyhpstplhaLSQGIALVpedrkkeGAVLGLSIR 362
Cdd:PRK10938 290 QIVGPNGAGKSTLLSLITGdhPQGYSndltlfgrrrgSGETIWD------------IKKHIGYV-------SSSLHLDYR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 363 ENISLSN--LSSLMrwrwfvntrkedDLIDAYRQA--------------LHIKMVNSDQEVRKLSGGNQQKVILARCMAL 426
Cdd:PRK10938 351 VSTSVRNviLSGFF------------DSIGIYQAVsdrqqklaqqwldiLGIDKRTADAPFHSLSWGQQRLALIVRALVK 418
|
490
....*....|....*
gi 504513498 427 NPKVLIVDEPTRGID 441
Cdd:PRK10938 419 HPTLLILDEPLQGLD 433
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
376-482 |
2.57e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.76 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 376 WRWFvNTRKeddlidayRQA---LH---IKMvnsDQEVRK-----LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGT 444
Cdd:COG4170 126 WQRF-KWRK--------KRAielLHrvgIKD---HKDIMNsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTT 193
|
90 100 110
....*....|....*....|....*....|....*....
gi 504513498 445 KSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITL 482
Cdd:COG4170 194 QAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
281-487 |
2.86e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.07 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPLHALSQGIALVPEDrkKEGAVLGLS 360
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQN--PETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISL--SNLS-SLMRWRWFVNTRKEDDLIDAYRQalhikmvnsdQEVRKLSGGNQQKVILARCMALNPKVLIVDEPT 437
Cdd:PRK13644 95 VEEDLAFgpENLClPPIEIRKRVDRALAEIGLEKYRH----------RSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 438 RGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKI 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-226 |
2.89e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.45 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLakSFS----GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQllllespve 77
Cdd:PRK11160 335 DQVSLTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP--------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 rqkrgiITIYQEFNLLPNMSVAenmflgrePQSSGLFVDALAVN-REAKAVLDYLKLnIAPTTQVA-------------- 142
Cdd:PRK11160 404 ------IADYSEAALRQAISVV--------SQRVHLFSATLRDNlLLAAPNASDEAL-IEVLQQVGleklleddkglnaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 143 ------RLSVAQQQMVEIARALTLNAKLIVMDEPSAAL-SDSEVDSLHRVVRELKGRgvSVVYVTHRLHEVFQLcDRFTV 215
Cdd:PRK11160 469 lgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLdAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICV 545
|
250
....*....|.
gi 504513498 216 FQDGRYTGSGD 226
Cdd:PRK11160 546 MDNGQIIEQGT 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
407-487 |
3.39e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 407 VRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIV-ISSDLPEIMAISDRIITLSEG 485
Cdd:TIGR00955 164 VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEG 243
|
..
gi 504513498 486 RI 487
Cdd:TIGR00955 244 RV 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
281-487 |
3.71e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALVPEDrkkeGAVLGLS 360
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQD----AGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSnlsslmrwrwfvntrKED----DLIDAYR--QALHIKMVNSD-------QEVRKLSGGNQQKVILARCMALN 427
Cdd:PRK13657 425 IEDNIRVG---------------RPDatdeEMRAAAEraQAHDFIERKPDgydtvvgERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEVHQVLfDMAKRGVAVIVISSDLPEImAISDRIITLSEGRI 487
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAAL-DELMKGRTTFIIAHRLSTV-RNADRILVFDNGRV 547
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-206 |
4.18e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqllllespvERQKR-G 82
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNGKlR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 83 IITIYQEFNLLPNMSVAENMFLGREPQSSGlfVDALAVNREAKAVldylKLNIAPttqVARLSVAQQQMVEIARALTLNA 162
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLTVNRFLRLRPGTKK--EDILPALKRVQAG----HLIDAP---MQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513498 163 KLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEV 206
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
276-487 |
4.86e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 276 DAHGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLfgadgfsSGEFVLDDAPYHPSTPLhalsqGIAL----VPEDRK 351
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLI-------NGLLLPDDNPNSKITVD-----GITLtaktVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 352 KEGAVLglsirENISlsnlsslmrwRWFVNTRKEDD--------------LIDAYRQAL-HIKMVN-SDQEVRKLSGGNQ 415
Cdd:PRK13640 85 KVGIVF-----QNPD----------NQFVGATVGDDvafglenravprpeMIKIVRDVLaDVGMLDyIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 416 QKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFD-MAKRGVAVIVISSDLPEiMAISDRIITLSEGRI 487
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDE-ANMADQVLVLDDGKL 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
280-487 |
5.35e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.40 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAP------------------YHPSTPLHA--L 339
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirnkagmvfQNPDNQIVAtiV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 340 SQGIALVPEDRkkegAVLGLSIRENISlsnlsslmrwrwfvNTRKEDDLIDAYRQALHIkmvnsdqevrkLSGGNQQKVI 419
Cdd:PRK13633 104 EEDVAFGPENL----GIPPEEIRERVD--------------ESLKKVGMYEYRRHAPHL-----------LSGGQKQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 420 LARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEImAISDRIITLSEGRI 487
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
281-441 |
6.19e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG----ADGFS-SGEFVLDDAP-YHPSTPLHALsqgialvpedRKKEG 354
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndlIPGARvEGEILLDGEDiYDPDVDVVEL----------RRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 355 AV------LGLSIRENISLSnlsslMRWRWFVNTRKEDDLIdayRQALhiKMVNSDQEVR--------KLSGGNQQKVIL 420
Cdd:COG1117 96 MVfqkpnpFPKSIYDNVAYG-----LRLHGIKSKSELDEIV---EESL--RKAALWDEVKdrlkksalGLSGGQQQRLCI 165
|
170 180
....*....|....*....|.
gi 504513498 421 ARCMALNPKVLIVDEPTRGID 441
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALD 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
252-486 |
8.23e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 252 SETHHQDKPVRLAVKGLS----REKPPLDAhgiaLKDISFQVHAGEVLGIAGLVGAGRTEIA----RCLFGADGFSSGEF 323
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiafmQEQQKIAA----VRNLSFSLQRGETLAIVGESGSGKSVTAlalmRLLEQAGGLVQCDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 324 VLDDAPYHPSTPLHALSQGialvpEDRKKEGAVLGLSIRENISLSN---------LSSLmrwRWFVNTRKEDDLIDAYRQ 394
Cdd:PRK10261 78 MLLRRRSRQVIELSEQSAA-----QMRHVRGADMAMIFQEPMTSLNpvftvgeqiAESI---RLHQGASREEAMVEAKRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 395 ALHIKMVNSDQEVRK----LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDL 469
Cdd:PRK10261 150 LDQVRIPEAQTILSRyphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDM 229
|
250
....*....|....*..
gi 504513498 470 PEIMAISDRIITLSEGR 486
Cdd:PRK10261 230 GVVAEIADRVLVMYQGE 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-220 |
8.63e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.76 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVE----RQKRGIITIYQEFNLLPNm 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklRKKVSLVFQFPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENMFLGrePQSSGlfvdalAVNREAK-AVLDYLKlNIAPTTQVA-----RLSVAQQQMVEIARALTLNAKLIVMDEP 170
Cdd:PRK13641 102 TVLKDVEFG--PKNFG------FSEDEAKeKALKWLK-KVGLSEDLIskspfELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 171 SAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
282-491 |
1.01e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDdapyhpSTPLHALSQgiALVPEDRKKEgavLGLSI 361
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN------GQPMSKLSS--AAKAELRNQK---LGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNLSSL--MRWRWFVNTRKEDDLIDAYRQALhiKMVNSDQEVR----KLSGGNQQKVILARCMALNPKVLIVDE 435
Cdd:PRK11629 94 QFHHLLPDFTALenVAMPLLIGKKKPAEINSRALEML--AAVGLEHRANhrpsELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 436 PTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLpEIMAISDRIITLSEGRISGEI 491
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-467 |
1.65e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 348 EDRKKEGAVLG-------LSIRENISLS-NLSSLMRWRWFVNTR-----KEDDLIDAYRQALHIKMVNsdqevrkLSGGN 414
Cdd:PRK14267 82 EVRREVGMVFQypnpfphLTIYDNVAIGvKLNGLVKSKKELDERvewalKKAALWDEVKDRLNDYPSN-------LSGGQ 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504513498 415 QQKVILARCMALNPKVLIVDEPTRGID-VGTkSEVHQVLFDMAKRGVAVIVISS 467
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDpVGT-AKIEELLFELKKEYTIVLVTHS 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
409-487 |
1.72e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.94 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMA-KRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
280-487 |
1.80e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.35 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQGiALVpEDRKKEGAVLG- 358
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG------QDLTALSEK-ELR-KARRQIGMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ---LSIR---ENISLSnlsslMRwrwFVNTRKEDdlIDAYRQALhIKMVN-SDQEVR---KLSGGNQQKVILARCMALNP 428
Cdd:PRK11153 91 fnlLSSRtvfDNVALP-----LE---LAGTPKAE--IKARVTEL-LELVGlSDKADRypaQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-225 |
2.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG-----AQPQTSgdIWFGGQQLLLLESPVERQKRGIItiYQE-FNLL 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPNSK--ITVDGITLTAKTVWDIREKVGIV--FQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 PNMSVAENMFLGRE------PQSSGLFVDALAvnreAKAVLDYLKlniaptTQVARLSVAQQQMVEIARALTLNAKLIVM 167
Cdd:PRK13640 98 VGATVGDDVAFGLEnravprPEMIKIVRDVLA----DVGMLDYID------SEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 168 DEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVfQLCDRFTVFQDGRYTGSG 225
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
281-487 |
2.20e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpsTPLHALSQGIALVPEdRKKEGAVLGL- 359
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGD------IVVSSTSKQKEIKPV-RKKVGVVFQFp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 --SIRENISLSNLSslMRWRWFVNTRKEDDLIDAYRqalhIKMVNSDQEVRK-----LSGGNQQKVILARCMALNPKVLI 432
Cdd:PRK13643 94 esQLFEETVLKDVA--FGPQNFGIPKEKAEKIAAEK----LEMVGLADEFWEkspfeLSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504513498 433 VDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-63 |
2.65e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 2.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 6 LNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDI-W 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkW 378
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
410-478 |
2.68e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 2.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMaKRGVAVIVISSDLPEIMAISDR 478
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDR 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-202 |
3.14e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 31 GEIHALLGENGAGKSTLLKALAGAQP--QTSGDIWFGGqqlllleSPVERQKRGIITIYQEFNLL--PNMSVAENM---- 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG-------FPKKQETFARISGYCEQNDIhsPQVTVRESLiysa 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 103 FLgREPQSSG-----LFVDALAVNREakavLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDS 177
Cdd:PLN03140 979 FL-RLPKEVSkeekmMFVDEVMELVE----LDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180
....*....|....*....|....*
gi 504513498 178 EVDSLHRVVRELKGRGVSVVYVTHR 202
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-219 |
3.26e-08 |
|
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: 54.72 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 27 TVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqllllESPVErqkrgiiTI-YQEFNLLPNMSVAENMFLg 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI----------EIELD-------TVsYKPQYIKADYEGTVRDLL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 106 repqsSGLFVDALAVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEVDSL-HR 184
Cdd:cd03237 83 -----SSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL-DVEQRLMaSK 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 504513498 185 VVRELKGRGVSVVYVT-HRLHEVFQLCDRFTVFqDG 219
Cdd:cd03237 157 VIRRFAENNEKTAFVVeHDIIMIDYLADRLIVF-EG 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
282-488 |
3.43e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLD----------DAPYH-PSTPLHALSQGIALVPEDR 350
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPPRNvEGTVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 351 KKEGAVLGLsIRENISLSNLSSLMRWR--------WFVNTRKEDDLidayrQALHIkmvNSDQEVRKLSGGNQQKVILAR 422
Cdd:PRK11147 99 KRYHDISHL-VETDPSEKNLNELAKLQeqldhhnlWQLENRINEVL-----AQLGL---DPDAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 423 CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMakRGvAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
284-490 |
3.49e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 284 DISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGE--FVLDDAPYHPSTPLHALSQGIALVPEdrkkEGAVL-GLS 360
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEilFDGENIPAMSRSRLYTVRKRMSMLFQ----SGALFtDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISL-----SNL------SSLMRWRWFVNTRKEDDLIDAyrqalhikmvnsdqevrKLSGGNQQKVILARCMALNPK 429
Cdd:PRK11831 101 VFDNVAYplrehTQLpapllhSTVMMKLEAVGLRGAAKLMPS-----------------ELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 430 VLIVDEP-------TRGIDVGTKSEVHQVLfdmakrGVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:PRK11831 164 LIMFDEPfvgqdpiTMGVLVKLISELNSAL------GVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
281-485 |
3.56e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.71 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYH-PSTPLHALSQGIALVPEDRKKEGAVLGL 359
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRenislsnlsslmrwrwfvNTRKEDDLIDAYRQALHIKMVNSDQE-VRKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:PRK11248 96 QLA------------------GVEKMQRLEIAHQMLKKVGLEGAEKRyIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513498 439 GIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEG 485
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
243-487 |
4.17e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 243 DVVFNRRPPSEThhqdkPVRLAVKGLS---REKPPLDAhgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFS 319
Cdd:PLN03232 1218 AIIENNRPVSGW-----PSRGSIKFEDvhlRYRPGLPP---VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 320 SGEFVLDDAPYhPSTPLHALSQGIALVPEdrkkEGAVLGLSIRENISLsnlsslmrwrwfVNTRKEDDLIDAYRQAlHIK 399
Cdd:PLN03232 1290 KGRIMIDDCDV-AKFGLTDLRRVLSIIPQ----SPVLFSGTVRFNIDP------------FSEHNDADLWEALERA-HIK 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 400 MVNS------DQEV----RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDmAKRGVAVIVISSDL 469
Cdd:PLN03232 1352 DVIDrnpfglDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRL 1430
|
250
....*....|....*...
gi 504513498 470 PEIMAiSDRIITLSEGRI 487
Cdd:PLN03232 1431 NTIID-CDKILVLSSGQV 1447
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-216 |
4.52e-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: 55.56 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLAKSFSGVwalsnaQLTVQRGEIH-----ALLGENGAGKSTLLKALAGAQPQTSGDIWFGgqqllllesp 75
Cdd:COG1245 337 EEETLVEYPDLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 76 verqkrgiITI-Y--QEFNLLPNMSVAENMFLGREPQSSGLFVDALAVNReakavldyLKLNIAPTTQVARLSVAQQQMV 152
Cdd:COG1245 401 --------LKIsYkpQYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKP--------LGLEKLLDKNVKDLSGGELQRV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 153 EIARALTLNAKLIVMDEPSAALsDSE-----VDSLHRVVRElkgRGVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHL-DVEqrlavAKAIRRFAEN---RGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-220 |
5.33e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 1 MTEPLLNITNLA-KSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQP---QTSGDIWFGGQQLLLLESPV 76
Cdd:cd03233 2 STLSWRNISFTTgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 77 ERQkrgIITIYQEFNLLPNMSVAENM-FLGRepqssglfvdalavnreakavldyLKLNiapttQVAR-LSVAQQQMVEI 154
Cdd:cd03233 82 PGE---IIYVSEEDVHFPTLTVRETLdFALR------------------------CKGN-----EFVRgISGGERKRVSI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 155 ARALTLNAKLIVMDEPSAALsDSE-----VDSLHRVVRELKgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR 220
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGL-DSStaleiLKCIRTMADVLK--TTTFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
282-485 |
5.41e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGA--DGFSSGEFVLDDAPYHPSTPLhalsqgIALVPEDRKKEGAVlgl 359
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQFGREASL------IDAIGRKGDFKDAV--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 sirENISLSNLSSLMRWRwfvntRKeddlidayrqalhikmvnsdqeVRKLSGGNQQKVILARCMALNPKVLIVDEPTRG 439
Cdd:COG2401 117 ---ELLNAVGLSDAVLWL-----RR----------------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504513498 440 IDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMA--ISDRIITLSEG 485
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYG 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-219 |
5.73e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ---TSGDIwfggqqllllespverqkRGIITIYQEFNLLPNMS 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetSSVVI------------------RGSVAYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 VAENMFLGR--EPQSSGLFVDALAVNREakavldylkLNIAP---TTQVAR----LSVAQQQMVEIARALTLNAKLIVMD 168
Cdd:PLN03232 695 VRENILFGSdfESERYWRAIDVTALQHD---------LDLLPgrdLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 169 EPSAALsDSEVdsLHRVV-----RELKGRgvSVVYVTHRLHeVFQLCDRFTVFQDG 219
Cdd:PLN03232 766 DPLSAL-DAHV--AHQVFdscmkDELKGK--TRVLVTNQLH-FLPLMDRIILVSEG 815
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
271-487 |
6.71e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.64 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 271 EKPPLDAHGIALKDISFQVH-------------AGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHpSTPLH 337
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE-SWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 338 ALSQGIALVPEDRKkegAVLGLSIREnislsnLSSLMRWRWF--------VNTRKEDDLIDAY-RQALHIKMVNSdqevr 408
Cdd:PRK10575 82 AFARKVAYLPQQLP---AAEGMTVRE------LVAIGRYPWHgalgrfgaADREKVEEAISLVgLKPLAHRLVDS----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 409 kLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10575 148 -LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
281-487 |
8.89e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapyhpstplHALSQGIALVPEDRKkegavlgls 360
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD---------YAIPANLKKIKEVKR--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLsnLSSLMRWRWFVNTRKED----------DLIDAYRQALHI-KMVNSDQEVRK-----LSGGNQQKVILARCM 424
Cdd:PRK13645 88 LRKEIGL--VFQFPEYQLFQETIEKDiafgpvnlgeNKQEAYKKVPELlKLVQLPEDYVKrspfeLSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504513498 425 ALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
407-496 |
9.12e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 407 VRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGvAVIVISSDLP--EIMAISDRIITLSE 484
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPssRVYQMFDSVLVLSE 282
|
90
....*....|..
gi 504513498 485 GRISGEIHGDDA 496
Cdd:PLN03211 283 GRCLFFGKGSDA 294
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-222 |
1.10e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ---TSGDIWFGGQQlllLESPVERqkrgIITIYQEFNL-LPNM 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRP---LDSSFQR----SIGYVQQQDLhLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 97 SVAENM----FLgREPQSsglfVDALAVNREAKAVLDYLKLNIAPTTQVAR----LSVAQQQMVEIARALTLNAKLIV-M 167
Cdd:TIGR00956 852 TVRESLrfsaYL-RQPKS----VSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 168 DEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLHEV-FQLCDRFTVFQDGRYT 222
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAIlFEEFDRLLLLQKGGQT 982
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
409-490 |
1.72e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDlPEIMAISDRIITLSEGRI 487
Cdd:PRK10584 146 QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
...
gi 504513498 488 SGE 490
Cdd:PRK10584 225 QEE 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
410-487 |
1.94e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.43 E-value: 1.94e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
398-487 |
2.01e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.71 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 398 IKMVNSDQEVR-----KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPE 471
Cdd:PRK13634 129 IELVGLPEELLarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMED 208
|
90
....*....|....*.
gi 504513498 472 IMAISDRIITLSEGRI 487
Cdd:PRK13634 209 AARYADQIVVMHKGTV 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
228-490 |
2.21e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 228 ASTNVQEIIRLMVGRDVVFNRRPPSEThhqDKPVrLAVKG------LSREKPpldahgiALKDISFQVHAGEVLGIAGLV 301
Cdd:PLN03232 584 ANVSLQRIEELLLSEERILAQNPPLQP---GAPA-ISIKNgyfswdSKTSKP-------TLSDINLEIPVGSLVAIVGGT 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 302 GAGRTEIARCLFGadgfssgefvldDAPyHPSTPLHALSQGIALVPEdrkkEGAVLGLSIRENISL-SNLSSLMRWRWFV 380
Cdd:PLN03232 653 GEGKTSLISAMLG------------ELS-HAETSSVVIRGSVAYVPQ----VSWIFNATVRENILFgSDFESERYWRAID 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 381 NTRKEDDL-IDAYRQALHI--KMVNsdqevrkLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK 457
Cdd:PLN03232 716 VTALQHDLdLLPGRDLTEIgeRGVN-------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL 788
|
250 260 270
....*....|....*....|....*....|...
gi 504513498 458 RGVAVIVISSDLpEIMAISDRIITLSEGRISGE 490
Cdd:PLN03232 789 KGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEE 820
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
286-487 |
2.54e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.51 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 286 SFQVHAGEVLGIAGLVGAGRTE----IArclfgadGF---SSGEFVLDDAPYHPST----PLHALSQGIALVPEdrkkeg 354
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTllnlIA-------GFltpASGSLTLNGQDHTTTPpsrrPVSMLFQENNLFSH------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 355 avlgLSIRENISLSnLSSLMRwrwfVNTRKEDDLIDAYRQalhikMVNSDQEVR---KLSGGNQQKVILARCMALNPKVL 431
Cdd:PRK10771 86 ----LTVAQNIGLG-LNPGLK----LNAAQREKLHAIARQ-----MGIEDLLARlpgQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 432 IVDEPTRGIDVGTKSEVHQVLFDM-AKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
407-486 |
2.70e-07 |
|
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: 49.75 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 407 VRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDmaKRGvAVIVISSDLPEIMAISDRIITLSEGR 486
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE--YPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-201 |
2.96e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 38 GENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVerqkrgIITIYQEFNLLPNMSVAENMFLGREPQSSGLFVDa 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY------CTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLY- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 118 lavnreakAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVV 197
Cdd:PRK13541 106 --------AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVL 177
|
....
gi 504513498 198 YVTH 201
Cdd:PRK13541 178 LSSH 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
285-463 |
3.16e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 50.95 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 285 ISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTPlhALSQGIALVPEDRKKEGAvlgLSIREN 364
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYLGHAPGIKTT---LSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 365 islsnlssLMRWRWFVNTRK-EDDLIDAYRQALhikmvnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVG 443
Cdd:cd03231 94 --------LRFWHADHSDEQvEEALARVGLNGF------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|
gi 504513498 444 TKSEVHQVLFDMAKRGVAVI 463
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVV 179
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
377-490 |
4.16e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 377 RWfvntRKEDDliDAYRQALHIKMVN--SDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFD 454
Cdd:PRK10253 115 RW----RKEDE--EAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
|
90 100 110
....*....|....*....|....*....|....*..
gi 504513498 455 MAK-RGVAVIVISSDLPEIMAISDRIITLSEGRISGE 490
Cdd:PRK10253 189 LNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
404-487 |
4.34e-07 |
|
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: 53.09 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 404 DQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMaKRGVAVIVISSDLPEIMAISDRIITLS 483
Cdd:TIGR01257 1056 NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
....
gi 504513498 484 EGRI 487
Cdd:TIGR01257 1135 QGRL 1138
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-230 |
4.90e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 31 GEIHALLGENGAGKSTLLKALAGAQPQ----TSGDIWFGGqqllLLESPVERQKRG-IITIYQEFNLLPNMSVAENM-FL 104
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDG----ITPEEIKKHYRGdVVYNAETDVHFPHLTVGETLdFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 105 GR--EPQSSGLFVDALA-VNREAKAVLDYLKLNIAPTTQVAR-----LSVAQQQMVEIARALTLNAKLIVMDEPSAALSD 176
Cdd:TIGR00956 163 ARckTPQNRPDGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 177 SE----VDSLHRVVRELKgrGVSVVYVTHRLHEVFQLCDRFTVFQDGR--YTGSGDVAST 230
Cdd:TIGR00956 243 ATalefIRALKTSANILD--TTPLVAIYQCSQDAYELFDKVIVLYEGYqiYFGPADKAKQ 300
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
282-487 |
4.93e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGF--SSGEFVLDDapyhpstplhalsQGI-ALVPEDRKKEGAVLG 358
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKG-------------EDItDLPPEERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENISLSNLSSLMRwrwFVNTrkeddlidayrqalhikmvnsdqevrKLSGGNQQKVILARCMALNPKVLIVDEPTR 438
Cdd:cd03217 83 FQYPPEIPGVKNADFLR---YVNE--------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 439 GIDVGTKSEVHQVLFDMAKRGVAVIVISSdLPEIMA--ISDRIITLSEGRI 487
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITH-YQRLLDyiKPDRVHVLYDGRI 183
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
410-490 |
5.01e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.34 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
..
gi 504513498 489 GE 490
Cdd:PRK13652 218 AY 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-69 |
5.28e-07 |
|
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: 52.11 E-value: 5.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQL 69
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-224 |
5.31e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 RQKRGIITIYQEFNLLPNMSVAENMFLGREPQSSGLFVDA---LAVNREAKAVLDYLKLNIAPTTQvaRLSVAQQQMVEI 154
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRAckfAAIDEFIESLPNKYDTNVGPYGK--SLSGGQKQRIAI 1369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 155 ARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRG-VSVVYVTHRLHEVfQLCDRFTVFQDGRYTGS 224
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFNNPDRTGS 1439
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
281-486 |
5.67e-07 |
|
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: 50.16 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFvlddapYHPSTplhalsqgIALVPEdrkkEGAVLGLS 360
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV------SVPGS--------IAYVSQ----EPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISlsnlsslmrwrwFVNTRKEDDlidaYRQALH-------IK-MVNSDQ-EV----RKLSGGNQQKVILARCMALN 427
Cdd:cd03250 82 IRENIL------------FGKPFDEER----YEKVIKacalepdLEiLPDGDLtEIgekgINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 428 PKVLIVDEPTRGIDVGTKSEV-HQVLFDMAKRGVAVIVISSDLpEIMAISDRIITLSEGR 486
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
282-484 |
6.13e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.17 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTE----IARCLfgADGFS-SGEFVLDDapyHPSTPLHALSQGIALVPEDrkkegAV 356
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTL--SPAFSaSGEVLLNG---RRLTALPAEQRRIGILFQD-----DL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 L--GLSIRENISLSNLSSLMRwrwfvNTRKeddliDAYRQAL-HIKMVN-SDQEVRKLSGGNQQKVILARCMALNPKVLI 432
Cdd:COG4136 87 LfpHLSVGENLAFALPPTIGR-----AQRR-----ARVEQALeEAGLAGfADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504513498 433 VDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISdRIITLSE 484
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRqRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
283-488 |
6.17e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 283 KDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTP----LHALSQGIALVPEdrkkegavlg 358
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPaergVGMVFQSYALYPH---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENISLS-NLSslmrwrwfvNTRKEDdlIDayrqalhiKMVNSDQEV--------RK---LSGGNQQKVILARCMAL 426
Cdd:PRK11000 90 LSVAENMSFGlKLA---------GAKKEE--IN--------QRVNQVAEVlqlahlldRKpkaLSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 427 NPKVLIVDEPTRGIDVGTK-------SEVHQVLfdmakrGVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRvqmrieiSRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
289-485 |
7.51e-07 |
|
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: 52.32 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 289 VHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLddAPYHPSTPLHALSQGIALVPEDRKKEGAVLGlsiRENISLs 368
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--AGKSILTNISDVHQNMGYCPQFDAIDDLLTG---REHLYL- 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 369 nlssLMRWRWfVNTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEV 448
Cdd:TIGR01257 2036 ----YARLRG-VPAEEIEKVANWSIQSLGLSLY-ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190
....*....|....*....|....*....|....*..
gi 504513498 449 HQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEG 485
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
385-479 |
7.67e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 385 EDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIV 464
Cdd:cd03236 116 ERGKLDELVDQLELRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV 194
|
90
....*....|....*
gi 504513498 465 ISSDLPEIMAISDRI 479
Cdd:cd03236 195 VEHDLAVLDYLSDYI 209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
144-220 |
7.72e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 7.72e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 144 LSVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEVDSL-HRVVRElKGRGVSVVYVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASV-DVRTDSLiQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
407-486 |
9.14e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 407 VRKLSGGNQQKVILAR-CM----ALNP--KVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRI 479
Cdd:PRK03695 124 VNQLSGGEWQRVRLAAvVLqvwpDINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV 203
|
....*..
gi 504513498 480 ITLSEGR 486
Cdd:PRK03695 204 WLLKQGK 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-216 |
1.63e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 3 EPLLNITNLAKSfsgvwaLSNAQLTVQRGEIHA-----LLGENGAGKSTLLKALAGAQPQTSGDIWFGgqqllllespve 77
Cdd:PRK13409 338 ETLVEYPDLTKK------LGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 78 rqkrgiITI-Y--QEFNLLPNMSVAEnmFLGR-EPQSSGLFVDALAVNReakavldylkLNIAP--TTQVARLSVAQQQM 151
Cdd:PRK13409 400 ------LKIsYkpQYIKPDYDGTVED--LLRSiTDDLGSSYYKSEIIKP----------LQLERllDKNVKDLSGGELQR 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 152 VEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVREL-KGRGVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaEEREATALVVDHDIYMIDYISDRLMVF 527
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
404-491 |
1.69e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 404 DQEVRKLSGGNQQKVILARCMALNPK--VLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDlPEIMAISDRIIT 481
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWIID 160
|
90
....*....|..
gi 504513498 482 LS--EGRISGEI 491
Cdd:cd03238 161 FGpgSGKSGGKV 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
285-463 |
1.87e-06 |
|
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: 48.51 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 285 ISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTP-----LHALSQGIALVPEdrkkegavlgL 359
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephenILYLGHLPGLKPE----------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 SIRENISLsnlsslmrWRWFvnTRKEDDLIDayrQALhiKMVN----SDQEVRKLSGGNQQKVILARCMALNPKVLIVDE 435
Cdd:TIGR01189 89 SALENLHF--------WAAI--HGGAQRTIE---DAL--AAVGltgfEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180
....*....|....*....|....*...
gi 504513498 436 PTRGIDVGTKSEVHQVLFDMAKRGVAVI 463
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVL 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-206 |
1.88e-06 |
|
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: 50.71 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGII----TIYQ---EFNLL 93
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIpqdpVLFSgslRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 94 PNMSVA-ENMFLGREPQSSGLFVDALAVnreakavldylKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSA 172
Cdd:TIGR00957 1382 PFSQYSdEEVWWALELAHLKTFVSALPD-----------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190
....*....|....*....|....*....|....
gi 504513498 173 ALsDSEVDSLHRVVRELKGRGVSVVYVTHRLHEV 206
Cdd:TIGR00957 1451 AV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
409-487 |
1.90e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 1.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
408-466 |
2.59e-06 |
|
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: 47.53 E-value: 2.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 408 RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMakrGVAVIVIS 466
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVG 145
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
281-504 |
3.38e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADG----FSSGEFVLDDAPYhpstplhalsqgIALVPEDRKKegaV 356
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDL------------LRLSPRERRK---L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 357 LG-------------LSIRENISLSNLSSLMRW----RWF--VNTRKeddlidayRQA---LHIKMVNSDQEVRK----- 409
Cdd:PRK15093 87 VGhnvsmifqepqscLDPSERVGRQLMQNIPGWtykgRWWqrFGWRK--------RRAielLHRVGIKDHKDAMRsfpye 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK-RGVAVIVISSDLPEIMAISDRIITLSEGRIS 488
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|....*.
gi 504513498 489 geihgDDATEEKLMTM 504
Cdd:PRK15093 239 -----ETAPSKELVTT 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
282-485 |
3.44e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFgadgfssGEFVLDDAPYHPSTPLHALSQGIALVPEdrkkegavlglSI 361
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELEPSEGKIKHSGRISFSPQTSWIMPG-----------TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENISLSNLSSLMRWRWFVNT-RKEDDLidayrqalhIKMVNSDQEVR-----KLSGGNQQKVILARCMALNPKVLIVDE 435
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKAcQLEEDI---------ALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 436 PTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLpEIMAISDRIITLSEG 485
Cdd:TIGR01271 575 PFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
248-441 |
3.98e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 248 RRPPSETHHQDKPV-RLA--VKGLSR--EKPPLdahgiaLKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGE 322
Cdd:PRK15064 302 RQNPFIRFEQDKKLhRNAleVENLTKgfDNGPL------FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 323 FVLDDapyhpstplhalSQGIALVPEDRKKEgavlglsirenisLSNLSSLMRW--RWfvntRKEDDLIDAYRQALHiKM 400
Cdd:PRK15064 376 VKWSE------------NANIGYYAQDHAYD-------------FENDLTLFDWmsQW----RQEGDDEQAVRGTLG-RL 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504513498 401 VNSDQEVRK----LSGGNQQKVILARCMALNPKVLIVDEPTRGID 441
Cdd:PRK15064 426 LFSQDDIKKsvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-220 |
4.31e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 20 ALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQQLLLLESPVERQKRGIITiyQEFNLLpNMSVA 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVS--QNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 100 ENMFLGREPQSSGLFVDALAvnREAKAvLDYL-KLNIAPTTQV----ARLSVAQQQMVEIARALTLNAKLIVMDEPSAAL 174
Cdd:PRK11176 435 NNIAYARTEQYSREQIEEAA--RMAYA-MDFInKMDNGLDTVIgengVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504513498 175 sDSEVD-SLHRVVRELKGRGVSVVyVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:PRK11176 512 -DTESErAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGE 555
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-480 |
4.35e-06 |
|
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: 48.17 E-value: 4.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 404 DQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVL--FDMAKRGVAvIVISSDLPEIMAISDRII 480
Cdd:cd03237 110 DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrrFAENNEKTA-FVVEHDIIMIDYLADRLI 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-201 |
5.89e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 2 TEPLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqllllesPVERQKR 81
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-------TATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 82 GIITIYQEF--NLLPNMSVAENM-FL----GREPQ---SSGLFVDALAvnreakavlDYlklniaPTTQVARLSVAQQQM 151
Cdd:PRK13543 81 SRFMAYLGHlpGLKADLSTLENLhFLcglhGRRAKqmpGSALAIVGLA---------GY------EDTLVRQLSAGQKKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504513498 152 VEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVR-ELKGRGVSVVyVTH 201
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAALV-TTH 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
145-262 |
6.34e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 145 SVAQQQMVEIARALTLNAKLIVMDEPSAALsDSEVDSL-HRVVRElKGRGVSVVYVTHRLHEVFQlCDRFTVFQDGRYTG 223
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAV-DVRTDALiQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 224 ---------------SGDVAST---NVQEIIRLMVGRDVvfNRRPPSETHHQDKPVR 262
Cdd:PLN03130 1453 fdtpenllsnegsafSKMVQSTgaaNAQYLRSLVFGGDE--DRLAREESKALDGQRK 1507
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
271-487 |
6.61e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 271 EKPPLdAHGIalkdiSFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDapYHPST-PLHALSQGIALVPEd 349
Cdd:PLN03130 1250 ELPPV-LHGL-----SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKfGLMDLRKVLGIIPQ- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 350 rkkeGAVL-GLSIRENISLsnlsslmrwrwfVNTRKEDDLIDAYRQAlHIKMV---NS---DQEV----RKLSGGNQQKV 418
Cdd:PLN03130 1321 ----APVLfSGTVRFNLDP------------FNEHNDADLWESLERA-HLKDVirrNSlglDAEVseagENFSVGQRQLL 1383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 419 ILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK-SCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
408-504 |
6.95e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 408 RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMA-KRGVAVIVISSDLPEIMAiSDRIITLSEGR 486
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIVVFNNPD 1435
|
90
....*....|....*...
gi 504513498 487 ISGEIHGDDATEEKLMTM 504
Cdd:PTZ00265 1436 RTGSFVQAHGTHEELLSV 1453
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
281-487 |
8.04e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHALSQGIALVPEDRKkegaVLGLS 360
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASLRNQVALVSQNVH----LFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLSSLMRwrwfvntrkeDDLIDAYRQALHI----KMVNS-DQEVRK----LSGGNQQKVILARCMALNPKVL 431
Cdd:PRK11176 433 IANNIAYARTEQYSR----------EQIEEAARMAYAMdfinKMDNGlDTVIGEngvlLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 432 IVDEPTRGIDvgTKSE-VHQVLFDMAKRGVAVIVISSDLPEIMAiSDRIITLSEGRI 487
Cdd:PRK11176 503 ILDEATSALD--TESErAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
286-484 |
8.63e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 286 SFQVHAGEVLGIAGLVGAGRTEIARCLfgadgfsSGEFVLDDAPYHPS-TPLHALS--QGIALVPEDRKKEGAVL----- 357
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGELPLLSGERQSQfSHITRLSfeQLQKLVSDEWQRNNTDMlspge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 358 ---GLSIRENISlsnlsslmrwrwfvNTRKEDDLIDAYRQALHIKMVnSDQEVRKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:PRK10938 96 ddtGRTTAEIIQ--------------DEVKDPARCEQLAQQFGITAL-LDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSE 484
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-227 |
9.90e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 19 WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQ-QLLLLESPVERQKRGIITIyqEFNLLpnms 97
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGIENI--EFKML---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 98 vaenmFLGREPQSsglfvdalaVNREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEpsaALS-- 175
Cdd:PRK13546 112 -----CMGFKRKE---------IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSvg 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 176 -----DSEVDSLHrvvrELKGRGVSVVYVTHRLHEVFQLCDRFTVFQDGRYTGSGDV 227
Cdd:PRK13546 175 dqtfaQKCLDKIY----EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-220 |
1.10e-05 |
|
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: 47.16 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 6 LNITNLAKSFS--GVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQpQTSGDIWFGGQQLLLLESPVERQKRGI 83
Cdd:cd03289 3 MTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 84 IT----IYQ---EFNLLPNMSVAENMFLgREPQSSGLfvdalavnreaKAVLDYL--KLNIAPTTQVARLSVAQQQMVEI 154
Cdd:cd03289 82 IPqkvfIFSgtfRKNLDPYGKWSDEEIW-KVAEEVGL-----------KSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 155 ARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGrGVSVVYVTHRLHEVFQlCDRFTVFQDGR 220
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLE-CQRFLVIEENK 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
410-487 |
1.22e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.05 E-value: 1.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
248-488 |
1.27e-05 |
|
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: 48.02 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 248 RRPPSETHHQDKPVRLAVKGLSREKPPldahgiALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGAdgfssgefvLDD 327
Cdd:TIGR00957 626 RRTIKPGEGNSITVHNATFTWARDLPP------TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE---------MDK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 328 APYHPstplhALSQGIALVPEdrkkEGAVLGLSIRENISLSNLSSLMRWRwfvntrkedDLIDAYRQALHIKMVNSDQEV 407
Cdd:TIGR00957 691 VEGHV-----HMKGSVAYVPQ----QAWIQNDSLRENILFGKALNEKYYQ---------QVLEACALLPDLEILPSGDRT 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 408 R------KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDvgtkSEVHQVLFD-------MAKRGVAVIVIS--SDLPEI 472
Cdd:TIGR00957 753 EigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD----AHVGKHIFEhvigpegVLKNKTRILVTHgiSYLPQV 828
|
250
....*....|....*.
gi 504513498 473 maisDRIITLSEGRIS 488
Cdd:TIGR00957 829 ----DVIIVMSGGKIS 840
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
256-487 |
1.42e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 47.53 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 256 HQDKPVRLAVKGLSREKPplDAHgIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGadgfssgeFvlddAPYHPS-- 333
Cdd:PRK11174 343 ASNDPVTIEAEDLEILSP--DGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG--------F----LPYQGSlk 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 334 ---TPLHALSqgialvPEDRKKEGAVLGL-------SIRENISLSN-------LSSLMRwRWFVNtrkedDLIDAYRQAL 396
Cdd:PRK11174 408 ingIELRELD------PESWRKHLSWVGQnpqlphgTLRDNVLLGNpdasdeqLQQALE-NAWVS-----EFLPLLPQGL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 397 HIKMvnSDQEVRkLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDmAKRGVAVIVISSDLPEIMAIs 476
Cdd:PRK11174 476 DTPI--GDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW- 550
|
250
....*....|.
gi 504513498 477 DRIITLSEGRI 487
Cdd:PRK11174 551 DQIWVMQDGQI 561
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
280-464 |
1.62e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.70 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 280 IALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYHPSTpLHAlsQGIALVpEDRKKEGAVLGL 359
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKN-LYA--PDVDPV-EVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 360 ------SIRENISLSNLsslmrwrwfVNTRKE--DDLID-AYRQALHIKMVNSD--QEVRKLSGGNQQKVILARCMALNP 428
Cdd:PRK14243 100 pnpfpkSIYDNIAYGAR---------INGYKGdmDELVErSLRQAALWDEVKDKlkQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 504513498 429 KVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIV 464
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-170 |
1.72e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 10 NLAKSFSGvwalsnaqlTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFGGQqlllLESPVERQKRGIitiyqe 89
Cdd:PRK11147 333 QLVKDFSA---------QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAE------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 90 fnLLPNMSVAENMFLGREpqssglfvdALAVNREAKAVLDYLKLNIAP----TTQVARLSVAQQQMVEIARALTLNAKLI 165
Cdd:PRK11147 394 --LDPEKTVMDNLAEGKQ---------EVMVNGRPRHVLGYLQDFLFHpkraMTPVKALSGGERNRLLLARLFLKPSNLL 462
|
....*
gi 504513498 166 VMDEP 170
Cdd:PRK11147 463 ILDEP 467
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
282-464 |
1.93e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.64 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYH---PSTPLHALSQGIALVPEdrkkegavlg 358
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpdVAEACHYLGHRNAMKPA---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 LSIRENISLsnlsslmrWRWFVNTRKED--DLIDAY--RQALHIKMvnsdqevRKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:PRK13539 88 LTVAENLEF--------WAAFLGGEELDiaAALEAVglAPLAHLPF-------GYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIV 464
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
278-487 |
2.01e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 278 HGIALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFG-------ADGFS-SGEFVLDDAPYHPSTPLHaLSQGIALVPED 349
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaPRGARvTGDVTLNGEPLAAIDAPR-LARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 350 RKKEGAvlgLSIRENISLSNLSSLMRWRwfVNTRKEDDLID-AYRQALHIKMVNSDqeVRKLSGGNQQKVILARCMA--- 425
Cdd:PRK13547 92 AQPAFA---FSAREIVLLGRYPHARRAG--ALTHRDGEIAWqALALAGATALVGRD--VTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513498 426 ------LNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR---GVAVIVISSDLPEIMAisDRIITLSEGRI 487
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVLAIVHDPNLAARHA--DRIAMLADGAI 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-201 |
2.86e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.93 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 21 LSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQ--TSGDIWFGGQQLlllespVERQKRGIITIYQEFNLLPNMSV 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL------DKNFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 99 AENMFLGrepqssglfvdalAVNREakavldylklniapttqvarLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSE 178
Cdd:cd03232 97 REALRFS-------------ALLRG--------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|...
gi 504513498 179 VDSLHRVVRELKGRGVSVVYVTH 201
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIH 166
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
371-447 |
6.02e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 371 SSLMRWRWFVNTRKEDDLIDAYRQALHIKMVNS---------DQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGID 441
Cdd:PTZ00265 532 NELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSAlpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
....*.
gi 504513498 442 vgTKSE 447
Cdd:PTZ00265 612 --NKSE 615
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-212 |
6.23e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDI--------------WFGG------QQLLLLESPVERQKRGIIT 85
Cdd:PTZ00265 406 FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkWWRSkigvvsQDPLLFSNSIKNNIKYSLY 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 86 IYQEFNLLPNMSvAENMFLGRE---------PQSSGLFVDA---------LAVNREAKAVLDYLKLNIAPT--------- 138
Cdd:PTZ00265 486 SLKDLEALSNYY-NEDGNDSQEnknkrnscrAKCAGDLNDMsnttdsnelIEMRKNYQTIKDSEVVDVSKKvlihdfvsa 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 139 ----------TQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGRGVSV-VYVTHRL---- 203
Cdd:PTZ00265 565 lpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLstir 644
|
250
....*....|.
gi 504513498 204 --HEVFQLCDR 212
Cdd:PTZ00265 645 yaNTIFVLSNR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
407-510 |
6.39e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 407 VRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAK--RGVAVIVISSDLPEIMAISDRIITLSE 484
Cdd:TIGR00956 207 VRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQDAYELFDKVIVLYE 286
|
90 100
....*....|....*....|....*...
gi 504513498 485 GRIsgeIHGDDATEEK--LMTMMAICHD 510
Cdd:TIGR00956 287 GYQ---IYFGPADKAKqyFEKMGFKCPD 311
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-81 |
6.69e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 4 PLLNITNLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDI---------WFGGQQLLLL-- 72
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLra 390
|
90
....*....|
gi 504513498 73 -ESPVERQKR 81
Cdd:PRK10636 391 dESPLQHLAR 400
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
390-485 |
7.50e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 390 DAYRQALHikMVN-------SDQEV---RKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKrG 459
Cdd:COG4178 458 AELREALE--AVGlghlaerLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP-G 534
|
90 100
....*....|....*....|....*.
gi 504513498 460 VAVIVISSDlPEIMAISDRIITLSEG 485
Cdd:COG4178 535 TTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-65 |
9.15e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 9.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 10 NLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIW-FG 65
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFG 327
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
30-213 |
9.82e-05 |
|
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: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 30 RGEIHALLGENGAGKSTLLKALAGAqpqtsgdiwFGGQQLLLLESPVErqKRGIITIYQEFNLLpnmsvaenmflgrepq 109
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLA---------LGGAQSATRRRSGV--KAGCIVAAVSAELI---------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 110 ssgLFVDalavnreakavldylklniapttqvaRLSVAQQQMVEIARALTLNAK----LIVMDEPSAALSDSEVDSLHRV 185
Cdd:cd03227 73 ---FTRL--------------------------QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|....*...
gi 504513498 186 VRELKGRGVSVVYVTHRlHEVFQLCDRF 213
Cdd:cd03227 124 ILEHLVKGAQVIVITHL-PELAELADKL 150
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-222 |
1.77e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 28 VQRGEIHALLGENGAGKSTLLKALAGAqpqtsgdiwfggqqllllespverqkrgiitiyqefnLLPNmsvaenmflgre 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQ-------------------------------------LIPN------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 108 pqssglfvdalavnrEAKAVLDYLKLNIAPttQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVR 187
Cdd:cd03222 53 ---------------GDNDEWDGITPVYKP--QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|....*...
gi 504513498 188 ELKGRGV-SVVYVTHRLHEVFQLCDRFTVF--QDGRYT 222
Cdd:cd03222 116 RLSEEGKkTALVVEHDLAVLDYLSDRIHVFegEPGVYG 153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-65 |
2.57e-04 |
|
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: 43.77 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 10 NLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFG 65
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG 382
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
409-441 |
2.97e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 2.97e-04
10 20 30
....*....|....*....|....*....|....*
gi 504513498 409 KLSGGNQQKviLARCMAL--NPKVLIVDEPTRGID 441
Cdd:NF033858 136 KLSGGMKQK--LGLCCALihDPDLLILDEPTTGVD 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-67 |
3.49e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 3.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 504513498 26 LTVQRGEIHALLGENGAGKSTLLKALAGA-QPQtSGDIWFGGQ 67
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQ-SGEILLDGK 385
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-308 |
4.27e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 128 LDYLKLNIApttqVARLSVAQQQMVEIARALtlNAKLI----VMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRl 203
Cdd:PRK00635 465 LPYLTPERA----LATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 204 HEVFQLCDRftVFQDGryTGSGdvastnvqeiirlMVGRDVVFNRRPPSETHHQDKpvrLAVKGL----------SREKP 273
Cdd:PRK00635 538 EQMISLADR--IIDIG--PGAG-------------IFGGEVLFNGSPREFLAKSDS---LTAKYLrqeltipipeKRTNS 597
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504513498 274 P-----LDAHGIALKDISFQVHAGEVLGIAGLVGAGRTEI 308
Cdd:PRK00635 598 LgtltlSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSL 637
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
404-487 |
5.96e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 404 DQEVRKLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVIS--SDLPEIMAISDRIIT 481
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllQPAPETFDLFDDIIL 410
|
....*.
gi 504513498 482 LSEGRI 487
Cdd:PLN03140 411 LSEGQI 416
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
284-485 |
7.65e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 284 DISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEfvlddapyhpstpLHALSQGIALVPEDRKKEGAVLG----- 358
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-------------VLWQGEPIRRQRDEYHQDLLYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 359 ---LSIRENislsnLSSLMRWRWFVNtrkEDDLIDAYRQA-LHIKMvnsDQEVRKLSGGNQQKVILARCMALNPKVLIVD 434
Cdd:PRK13538 86 kteLTALEN-----LRFYQRLHGPGD---DEALWEALAQVgLAGFE---DVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504513498 435 EPTRGIDVGTKSEVHQVLFDMAKRGVAVIVIS-SDLPeimAISDRIITLSEG 485
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVILTThQDLP---VASDKVRKLRLG 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
410-487 |
7.89e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 7.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKR-GVAVIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-86 |
8.07e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 8.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513498 19 WALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWF-GGQQLLLLESPVERQKRGIITI 86
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNGQLTGIENI 106
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-225 |
1.04e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 5 LLNITNLAKSF----SGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAG----AQPQTSGDIWFGGQQLLLLEspv 76
Cdd:PRK11022 3 LLNVDKLSVHFgdesAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDLQRIS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 77 ERQKRGII-----TIYQEfnllPNMSVAENMFLGREpqssglFVDALAVN-------REAKAVlDYLKLNIAPTTQvARL 144
Cdd:PRK11022 80 EKERRNLVgaevaMIFQD----PMTSLNPCYTVGFQ------IMEAIKVHqggnkktRRQRAI-DLLNQVGIPDPA-SRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 145 SVAQQQM-------VEIARALTLNAKLIVMDEPSAALSDSEVDSLHRVVRELKGR-GVSVVYVTHRLHEVFQLCDRFTVF 216
Cdd:PRK11022 148 DVYPHQLsggmsqrVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVM 227
|
....*....
gi 504513498 217 QDGRYTGSG 225
Cdd:PRK11022 228 YAGQVVETG 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-65 |
1.33e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504513498 10 NLAKSFSGVWALSNAQLTVQRGEIHALLGENGAGKSTLLKALAGAQPQTSGDIWFG 65
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG 384
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
32-54 |
1.34e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 1.34e-03
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
409-480 |
2.55e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.09 E-value: 2.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513498 409 KLSGGNQQKVILARCMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGV-AVIVISSDLPEIMAISDRII 480
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
404-491 |
3.56e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.16 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 404 DQEVRKLSGGNQQKVILAR--CMALNPKVLIVDEPTRGIDVGTKSEVHQVLFDMAKRGVAVIVISSDlPEIMAISDRIIT 481
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVID 210
|
90
....*....|..
gi 504513498 482 L--SEGRISGEI 491
Cdd:cd03270 211 IgpGAGVHGGEI 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-64 |
3.60e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 3.60e-03
10 20
....*....|....*....|....*....
gi 504513498 36 LLGENGAGKSTLLKALAGAQPQTSGDIWF 64
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP 66
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
410-466 |
3.69e-03 |
|
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: 40.12 E-value: 3.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504513498 410 LSGGNQQKVILARCMALNPKVLIVDEPTRGIDVgtksEVHQVLFDMAKR-GVAVIVIS 466
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREfGITLFSVS 636
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
282-441 |
3.98e-03 |
|
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: 39.92 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 282 LKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDdapyhPSTPLHALSQGIALVPEdrkkegavlgLSI 361
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-----PGIKVGYLPQEPQLDPT----------KTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 362 RENI--SLSNLSSLMRWRWFVNTR--KEDDLIDAY--RQA-----------------LHIKM-----VNSDQEVRKLSGG 413
Cdd:TIGR03719 86 RENVeeGVAEIKDALDRFNEISAKyaEPDADFDKLaaEQAelqeiidaadawdldsqLEIAMdalrcPPWDADVTKLSGG 165
|
170 180
....*....|....*....|....*...
gi 504513498 414 NQQKVILARCMALNPKVLIVDEPTRGID 441
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
36-52 |
3.99e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.98 E-value: 3.99e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-204 |
4.05e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 128 LDYLKLNIAPTTqvarLSVAQQQMVEIARALTLNAK---LIVMDEPSAALSDSEVDSLHRVVRELKGRGVSVVYVTHRLH 204
Cdd:TIGR00630 818 LGYIRLGQPATT----LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD 893
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
35-62 |
4.73e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 4.73e-03
10 20
....*....|....*....|....*...
gi 504513498 35 ALLGENGAGKSTLLKALAGAQPQTSGDI 62
Cdd:PRK01889 199 ALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
281-487 |
4.82e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 39.70 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 281 ALKDISFQVHAGEVLGIAGLVGAGRTEIARCLFGADGFSSGEFVLDDAPYhPSTPLHALSQGIALVpedrKKEGAVLGLS 360
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL-TKLQLDSWRSRLAVV----SQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 361 IRENISLSNLSSlmrwrwfvntrKEDDLIDAYRQA-LHIKMVNSDQ----EVRK----LSGGNQQKVILARCMALNPKVL 431
Cdd:PRK10789 405 VANNIALGRPDA-----------TQQEIEHVARLAsVHDDILRLPQgydtEVGErgvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504513498 432 IVDEPTRGIDVGTKsevHQVLFDMAKRGVA-VIVISSDLPEIMAISDRIITLSEGRI 487
Cdd:PRK10789 474 ILDDALSAVDGRTE---HQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-215 |
9.59e-03 |
|
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: 36.97 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 30 RGEIHALLGENGAGKSTLLKALAGAQPQTSGDIwfggqqllllespverqkrgiitiyqefnllpnmsvaenmflgrepq 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513498 110 ssgLFVDAlavnREAKAVLDYLKLNIAPTTQVARLSVAQQQMVEIARALTLNAKLIVMDEPSAALSDS------EVDSLH 183
Cdd:smart00382 34 ---IYIDG----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqealllLLEELR 106
|
170 180 190
....*....|....*....|....*....|..
gi 504513498 184 RVVRELKGRGVSVVYVTHRLHEVFQLCDRFTV 215
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| |
