|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-508 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 973.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETE 80
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVIIHQELTLVPDLSVAENIFMGHELTlPGGRMNYPAMLHRAEALMRELKVpDMNVALPVSQYGGGYQQLVEIAKAL 160
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEIT-PGGIMDYDAMYLRAQKLLAQLKL-DINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 161 NKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQ 240
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 241 MVGREMSNLYPTEPHDVGEVIFEARNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNA 320
Cdd:PRK13549 239 MVGRELTALYPREPHTIGEVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 321 EVWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQISRMHLKTAS 400
Cdd:PRK13549 319 EIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 401 PSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVI 480
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
490 500
....*....|....*....|....*...
gi 1067238353 481 GDGQLRGDFINDGLTQEQVLAAALSHNN 508
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQVMEAALRSEH 506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-504 |
0e+00 |
|
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: 885.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGI 84
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGHELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQMVGR 244
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 245 EMSNLYPTEPHDVGEVIFEARNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNAEVWL 324
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 325 EGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLP 404
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 405 ITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
490 500
....*....|....*....|
gi 1067238353 485 LRGDFINDGLTQEQVLAAAL 504
Cdd:TIGR02633 481 LKGDFVNHALTQEQVLAAAL 500
|
|
| 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: 724.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 2 PDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEA 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD--SGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 AGIVIIHQELTLVPDLSVAENIFMGHELTlPGGRMNYPAMLHRAEALMRELKVpDMNVALPVSQYGGGYQQLVEIAKALN 161
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGREPR-RGGLIDWRAMRRRARELLARLGL-DIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 162 KQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQM 241
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 242 VGREMSNLYPTEPHDVGEVIFEARNVTCydvdnpkRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAE 321
Cdd:COG1129 237 VGRELEDLFPKRAAAPGEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-ADSGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 322 VWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQISRMHLKTASP 401
Cdd:COG1129 309 IRLDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 402 SLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMR 468
|
490 500
....*....|....*....|....*
gi 1067238353 482 DGQLRGDFINDGLTQEQVLAAALSH 506
Cdd:COG1129 469 EGRIVGELDREEATEEAIMAAATGG 493
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-497 |
0e+00 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 577.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGI 84
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGHElTLPGGRMNYPAMLHRAEALMRELKVPDmNVALPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNE-RAKRGVIDWNETNRRARELLAKVGLDE-SPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIP--RIITQMV 242
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADEVTedRIIRGMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 243 GREMSNLYPTEPHDVGEVIFEARNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRYNAE 321
Cdd:NF040905 239 GRDLEDRYPERTPKIGEVVFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNISGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 322 VWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQISRMHLKTASP 401
Cdd:NF040905 319 VFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 402 SLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
490
....*....|....*.
gi 1067238353 482 DGQLRGDFINDGLTQE 497
Cdd:NF040905 479 EGRITGELPREEASQE 494
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-509 |
8.48e-178 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 509.16 E-value: 8.48e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETEAAGI 84
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA--GSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGHELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALpVSQYGGGYQQLVEIAKALNKQA 164
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKL-VGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQMVGR 244
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 245 EMSNLYPTEPHDVGEVIFEARNVTcydvdnpkRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWL 324
Cdd:PRK10762 241 KLEDQYPRLDKAPGEVRLKVDNLS--------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-RTSGYVTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 325 EGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYAH-MTRIDAEAELGSIDQQISRMHLKTASPSL 403
Cdd:PRK10762 312 DGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRaGGSLKHADEQQAVSDFIRLFNIKTPSMEQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
490 500
....*....|....*....|....*.
gi 1067238353 484 QLRGDFINDGLTQEQVLAAALSHNNN 509
Cdd:PRK10762 472 RISGEFTREQATQEKLMAAAVGKLNR 497
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-504 |
1.20e-164 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 475.94 E-value: 1.20e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLlQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETE 80
Cdd:PRK11288 1 SSPYL-SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA--GSILIDGQEMRFASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVIIHQELTLVPDLSVAENIFMGHeltLP--GGRMNYPAMLHRAEALMRELKVpDMNVALPVSQYGGGYQQLVEIAK 158
Cdd:PRK11288 78 AAGVAIIYQELHLVPEMTVAENLYLGQ---LPhkGGIVNRRLLNYEAREQLEHLGV-DIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 159 ALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT-TAMADMDIPRI 237
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 238 ITQMVGREMSNLYPTEPHDVGEVIFEARNVTCYDVDNPkrkrvddISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgR 317
Cdd:PRK11288 234 VQAMVGREIGDIYGYRPRPLGEVRLRLDGLKGPGLREP-------ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATR-R 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 318 YNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAvldTYAHMTR----IDAEAELGSIDQQISR 393
Cdd:PRK11288 306 TAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINIS---ARRHHLRagclINNRWEAENADRFIRS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 394 MHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGV 473
Cdd:PRK11288 383 LNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGV 462
|
490 500 510
....*....|....*....|....*....|.
gi 1067238353 474 SNRVLVIGDGQLRGDFINDGLTQEQVLAAAL 504
Cdd:PRK11288 463 ADRIVVMREGRIAGELAREQATERQALSLAL 493
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-499 |
2.57e-160 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 464.89 E-value: 2.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQSIRET 79
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPD---SGEILIDGKPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAAGIVIIHQELTLVPDLSVAENIFMGHElTLPGGRMNYPAMLHRAEALMRE--LKV-PDMNVA-LPVsqyggGYQQLVE 155
Cdd:COG3845 78 IALGIGMVHQHFMLVPNLTVAENIVLGLE-PTKGGRLDRKAARARIRELSERygLDVdPDAKVEdLSV-----GEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIP 235
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 236 RIITQMVGREMSNLYPTEPHDVGEVIFEARNVTCydVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP 315
Cdd:COG3845 232 ELAELMVGREVLLRVEKAPAEPGEVVLEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 316 gRYNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYA-------HMTRIDAEAElgsid 388
Cdd:COG3845 310 -PASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAE----- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 389 QQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELA 468
Cdd:COG3845 384 ELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
|
490 500 510
....*....|....*....|....*....|.
gi 1067238353 469 EVLGVSNRVLVIGDGQLRGDFINDGLTQEQV 499
Cdd:COG3845 464 EILALSDRIAVMYEGRIVGEVPAAEATREEI 494
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
4.95e-141 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 416.11 E-value: 4.95e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETE 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK--GTITINNINYNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVIIHQELTLVPDLSVAENIFMGHELT---LPGGRMNYPAMLHRAEALMRE--LKV-PDMNVA-LPVSqygggYQQL 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIGRHLTkkvCGVNIIDWREMRVRAAMMLLRvgLKVdLDEKVAnLSIS-----HKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 154 VEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMD 233
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 234 IPRIITQMVGREMSNLYPTEPHDVG----EVIFEARNVTCYDvdnpkRKRVDDISFVLRRGEILGIAGLVGAGRTELVSA 309
Cdd:PRK09700 234 NDDIVRLMVGRELQNRFNAMKENVSnlahETVFEVRNVTSRD-----RKKVRDISFSVCRGEILGFAGLVGSGRTELMNC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 310 LFGAYPgRYNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLA---VLDTY-AHMTRIDAEAELG 385
Cdd:PRK09700 309 LFGVDK-RAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYkGAMGLFHEVDEQR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 386 SIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSS 465
Cdd:PRK09700 388 TAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSS 467
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1067238353 466 ELAEVLGVSNRVLVIGDGQLRGDFIN-DGLTQEQVLAAALSH 506
Cdd:PRK09700 468 ELPEIITVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWALPQ 509
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-506 |
8.87e-137 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 404.50 E-value: 8.87e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 8 MNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAAGIVII 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD--SGSILFQGKEIDFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 88 HQELTLVPDLSVAENIFMGhELTLPGGRMNYPAMLHRAEALMRELKV---PDMNVA-LPVSQygggyQQLVEIAKALNKQ 163
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLG-RYPTKGMFVDQDKMYRDTKAIFDELDIdidPRAKVAtLSVSQ-----MQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQMVG 243
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 244 REMSNLYPTEPHDVGEVIFEARNVTcyDVDNPKrkrVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVW 323
Cdd:PRK10982 233 RSLTQRFPDKENKPGEVILEVRNLT--SLRQPS---IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSAGTIT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 324 LEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYAHMTRIDAEAELGSiDQQ--ISRMHLKTASP 401
Cdd:PRK10982 307 LHGKKINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKS-DTQwvIDSMRVKTPGH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 402 SLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
490 500
....*....|....*....|....*
gi 1067238353 482 DGQLRGDFINDGLTQEQVLAAALSH 506
Cdd:PRK10982 466 NGLVAGIVDTKTTTQNEILRLASLH 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-503 |
1.14e-113 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 345.88 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETEAAGI 84
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGheltLPGGRMNYpamlHRAEALMRELKV---PDMNVA-LPVSQygggyQQLVEIAKAL 160
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFG----LPKRQASM----QKMKQLLAALGCqldLDSSAGsLEVAD-----RQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 161 NKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQ 240
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 241 MVgREMSNLYPTEPHDVGEVIFEARNVTCYD-----VDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP 315
Cdd:PRK15439 236 IT-PAAREKSLSASQKLWLELPGNRRQQAAGapvltVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 316 GRyNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITlavldTYAHMTR---IDAEAELGSIDQQIS 392
Cdd:PRK15439 315 AR-GGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC-----ALTHNRRgfwIKPARENAVLERYRR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 393 RMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLG 472
Cdd:PRK15439 389 ALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
490 500 510
....*....|....*....|....*....|.
gi 1067238353 473 VSNRVLVIGDGQLRGDFINDGLTQEQVLAAA 503
Cdd:PRK15439 469 MADRVLVMHQGEISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
258-485 |
1.19e-79 |
|
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: 246.57 E-value: 1.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 258 GEVIFEARNVTCydvdnpkRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPLKS 337
Cdd:cd03215 1 GEPVLEVRGLSV-------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-PASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLdtyahmtridaeaelgsidqqisrmhlktaspslpitsLSGGNQQKAV 417
Cdd:cd03215 73 IRAGIAYVPEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 418 LAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-226 |
9.91e-70 |
|
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: 220.38 E-value: 9.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAAGIV 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD--SGEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQeltlvpdLSVAEnifmgheltlpggrmnypamlhraealmrelkvpdmnvalpvsqygggyQQLVEIAKALNKQAR 165
Cdd:cd03216 79 MVYQ-------LSVGE-------------------------------------------------RQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 166 LLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-485 |
2.33e-67 |
|
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: 225.55 E-value: 2.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPH-GTWEGEILWDGQPLKAQSIRETeAAGIVIIHQE--LT 92
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHgGRISGEVLLDGRDLLELSEALR-GRRIGMVFQDpmTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPdLSVAENIfmghELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:COG1123 96 LNP-VTVGDQI----AEALENLGLSRAEARARVLELLEAVGLERRLDRYP-HQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 173 SSAL---TRGEIevlLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMAD-MDIPRIITQMVGREMS 247
Cdd:COG1123 170 TTALdvtTQAEI---LDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEiLAAPQALAAVPRLGAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 248 NLYPTEPHDVGEVIFEARNVTC-YDVDNPKRKR-VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEV 322
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKrYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsG----SI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 323 WLEGQVIDTRTP--LKSIRAGLCMVPEDRKRQgIIPDLGVGQNITLAvLDTYAHMTRIDAEAElgsIDQQISRMHLKTAS 400
Cdd:COG1123 323 LFDGKDLTKLSRrsLRELRRRVQMVFQDPYSS-LNPRMTVGDIIAEP-LRLHGLLSRAERRER---VAELLERVGLPPDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 401 PSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLV 479
Cdd:COG1123 398 ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAV 477
|
....*.
gi 1067238353 480 IGDGQL 485
Cdd:COG1123 478 MYDGRI 483
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-226 |
3.16e-46 |
|
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: 161.07 E-value: 3.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAAGIV 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT--SGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGHELTLPGG------RMNYPAMLHRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIAKA 159
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSGlllaraRREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 160 LNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-226 |
5.76e-45 |
|
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: 158.66 E-value: 5.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 2 PDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEA 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT--SGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 AGIVIIHQELTLVPDLSVAENI-----------FMGHELTLPGGRMNYPAMLHRAEALMRELK---VPDMNVA-LPvsqy 146
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGladRADEPAGnLS---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 147 gGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG0411 155 -YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
.
gi 1067238353 226 T 226
Cdd:COG0411 234 E 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-232 |
7.74e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.14 E-value: 7.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETEAAGIV 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR--PTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IihQELTLVPDLSVAENI-FMGhELTlpggRMNYPAMLHRAEALMRELKVPD-MNValPVSQYGGGYQQLVEIAKALNKQ 163
Cdd:COG1131 79 P--QEPALYPDLTVRENLrFFA-RLY----GLPRKEARERIDELLELFGLTDaADR--KVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADM 232
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-222 |
8.04e-38 |
|
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: 138.84 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSiRETEAAgI 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP--DSGSILIDGEDVRKEP-REARRQ-I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIfmgheltlpggrmNYPAMLH---------RAEALMRELKVPDMnVALPVSQYGGGYQQLVE 155
Cdd:COG4555 77 GVLPDERGLYDRLTVRENI-------------RYFAELYglfdeelkkRIEELIELLGLEEF-LDRRVGELSTGMKKKVA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-222 |
1.31e-37 |
|
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: 135.99 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQSIRETEAAGI 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPD---SGEIKVLGKDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIihQELTLVPDLSVAENIfmgheltlpggrmnypamlhraealmrelkvpdmnvalpvsQYGGGYQQLVEIAKALNKQA 164
Cdd:cd03230 78 LP--EEPSLYENLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-484 |
2.79e-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: 141.36 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGG----VNALNGIDIKVKPGECVGLCGENGAGKS----TLMKVLSavYPHGTWEGEILWDGQPLK 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLP--DPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 73 AQSIRETEA---AGIVIIHQE-LT-LVPDLSVAENIfmGHELTLPGGrMNYPAMLHRAEALMRELKVPDmnVALPVSQY- 146
Cdd:COG4172 80 GLSERELRRirgNRIAMIFQEpMTsLNPLHTIGKQI--AEVLRLHRG-LSGAAARARALELLERVGIPD--PERRLDAYp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 147 ---GGGYQQLVEIAKALNKQARLLILDEPSSAL---TRGEIevlLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIR 219
Cdd:COG4172 155 hqlSGGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQI---LDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 220 DGKHI--ATTAmadmdipRII-------TQM-VGREMSNLYPTEPHDvGEVIFEARNVTcydVDNPKRKR---------- 279
Cdd:COG4172 232 QGEIVeqGPTA-------ELFaapqhpyTRKlLAAEPRGDPRPVPPD-APPLLEARDLK---VWFPIKRGlfrrtvghvk 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 -VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRynAEVWLEGQVIDTRTP--LKSIRAGLCMVPED-------R 349
Cdd:COG4172 301 aVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE--GEIRFDGQDLDGLSRraLRPLRRRMQVVFQDpfgslspR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 350 krqgiipdLGVGQNIT--LAVldtyaHMTRIDAEAELGSIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPK 427
Cdd:COG4172 379 --------MTVGQIIAegLRV-----HGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPK 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-245 |
3.85e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.15 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 12 VKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSIRETEAAGIVII---H 88
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA--DSGEIRLDGKPVRIRSPRDAIRAGIAYVpedR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 89 QELTLVPDLSVAENIFMGH-ELTLPGGRMNYPAMLHRAEALMREL--KVPDMNvaLPVSQYGGGYQQLVEIAKALNKQAR 165
Cdd:COG1129 337 KGEGLVLDLSIRENITLASlDRLSRGGLLDRRRERALAEEYIKRLriKTPSPE--QPVGNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 166 LLILDEPssalTRG-------EIevlLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRII 238
Cdd:COG1129 415 VLILDEP----TRGidvgakaEI---YRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAIM 487
|
....*..
gi 1067238353 239 TQMVGRE 245
Cdd:COG1129 488 AAATGGA 494
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-174 |
7.16e-35 |
|
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: 127.76 E-value: 7.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYpHGTwEGEILWDGQPLKAQSIRETEaAGIVIIHQELTLVPDLSVA 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-SPT-EGTILLDGQDLTDDERKSLR-KEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 101 ENIFMGHELtlpgGRMNYPAMLHRAEALMRELKVPDMN---VALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSS 174
Cdd:pfam00005 78 ENLRLGLLL----KGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-225 |
1.20e-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: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSIRETeAAGI 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP--SSGEVLLDGRDLASLSRREL-ARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMgheltlpgGRMNYPAMLHR--------AEALMRELKVPDMnvAL-PVSQYGGGYQQLVE 155
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVAL--------GRYPHLGLFGRpsaedreaVEEALERTGLEHL--ADrPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 156 IAKALNKQARLLILDEPSSAL-TRGEIEVlLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLdLAHQLEV-LELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-222 |
7.31e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 124.85 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETEAAGIV 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMG-HELTLPGGRMNYPAMLHRAEALMRELKVpdmnvalPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGaYARRRAKRKARLERVYELFPRLKERRKQ-------LAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-222 |
2.59e-32 |
|
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: 121.91 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPhgtWEGEILWDGQPLKAQS-IRETEAAG 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEP---DSGSILIDGEDLTDLEdELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVPDLSVAENIfmgheltlpggrmnypamlhraealmrelkvpdmnvALPVSqygGGYQQLVEIAKALNKQ 163
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENI------------------------------------ALGLS---GGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 164 ARLLILDEPSSAL---TRGEIevlLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03229 119 PDVLLLDEPTSALdpiTRREV---RALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-222 |
7.35e-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: 128.48 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF-----GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRET 79
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT--SGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAAG--IVIIHQ--ELTLVPDLSVAENIFMGHELtlpGGRMNYPAMLHRAEALMRElkvpdmnVALPVSQYG-------G 148
Cdd:COG1123 338 RELRrrVQMVFQdpYSSLNPRMTVGDIIAEPLRL---HGLLSRAERRERVAELLER-------VGLPPDLADryphelsG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 149 GYQQLVEIAKALNKQARLLILDEPSSAL---TRGEIevlLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALdvsVQAQI---LNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-225 |
1.80e-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: 120.46 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIREteaagIV 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD--SGEVLFDGKPLDIAARNR-----IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAEN-IFMGhelTLPGgrMNYPAMLHRAEALMRELKVPDMNvALPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:cd03269 74 YLPEERGLYPKMKVIDQlVYLA---QLKG--LKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-222 |
1.92e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 118.89 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 7 QMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSIREteaagivi 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP--TSGEILIDGKDIAKLPLEE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 87 IHQELTLVPDLSvaenifmgheltlpggrmnypamlhraealmrelkvpdmnvalpvsqygGGYQQLVEIAKALNKQARL 166
Cdd:cd00267 71 LRRRIGYVPQLS-------------------------------------------------GGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 167 LILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-489 |
2.37e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.10 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 8 MNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSavyphgtweGEILWD-GQPLKAQSIReteaagIVI 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA---------GELEPDsGEVSIPKGLR------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 87 IHQELTLVPDLSVAENIFMGH---------------ELTLPGGRMNYPAMLH-------------RAEALMRELKVPDMN 138
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDaelraleaeleeleaKLAEPDEDLERLAELQeefealggweaeaRAEEILSGLGFPEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 139 VALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAkgvACVYISHK---LDevaAVCDTI 215
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHDryfLD---RVATRI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 216 AVIRDGK----------------------------------HI----------ATTA------------MADMDIPRIIT 239
Cdd:COG0488 220 LELDRGKltlypgnysayleqraerleqeaaayakqqkkiaKEeefirrfrakARKAkqaqsrikalekLEREEPPRRDK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 240 QMvgremsNLYPTEPHDVGEVIFEARNVTC-YDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgry 318
Cdd:COG0488 300 TV------EIRFPPPERLGKKVLELEGLSKsYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 319 naevwlegqvidtrtplksiraglcmvpedrkrqgiiPDLG---VGQNITLAVLDTyaHMTRIDAEA----ELGSIDQQI 391
Cdd:COG0488 367 -------------------------------------PDSGtvkLGETVKIGYFDQ--HQEELDPDKtvldELRDGAPGG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 392 SRMHLKTA------SPSL---PITSLSGGnqQKA--VLAKMLMAKPKVLILDEPTRGVDVGAKyEIykLMGALAA-EGvS 459
Cdd:COG0488 408 TEQEVRGYlgrflfSGDDafkPVGVLSGG--EKArlALAKLLLSPPNVLLLDEPTNHLDIETL-EA--LEEALDDfPG-T 481
|
570 580 590
....*....|....*....|....*....|....*
gi 1067238353 460 IIMVS--SELAEvlGVSNRVLVIGDGQLR---GDF 489
Cdd:COG0488 482 VLLVShdRYFLD--RVATRILEFEDGGVReypGGY 514
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-222 |
4.49e-31 |
|
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: 119.55 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETeaaGIV 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD--SGEILIDGRDVTGVPPERR---NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGheltLPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQAR 165
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 166 LLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
263-485 |
5.10e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.17 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEVWLEGQviDTRTPLKSI 338
Cdd:COG1131 2 EVRGLTkRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsG----EVRVLGE--DVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 RAGLCMVPEDrkrQGIIPDLGVGQNitlavLDTYAHMTRIDAEAELGSIDQQISRMHLkTASPSLPITSLSGGNQQKAVL 418
Cdd:COG1131 72 RRRIGYVPQE---PALYPDLTVREN-----LRFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 419 AKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-222 |
5.57e-31 |
|
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: 119.11 E-value: 5.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYphGTWEGEILWDGQPLKAQSIRE-TEAAGIVIIHQELTLV 94
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKElRRKVGLVFQNPDDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDlSVAENIFMGHE-LTLPGGRMNypamlHRAEALMRELKVPDMNvALPVSQYGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:cd03225 90 GP-TVEEEVAFGLEnLGLPEEEIE-----ERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067238353 174 SALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-222 |
8.40e-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: 119.36 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIREteaagiviIHQELTLV- 94
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT--SGEVLVDGKDITKKNLRE--------LRRKVGLVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 --PDL-----SVAENIFMGHEltlpggRMNYPA--MLHRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIAKALNKQAR 165
Cdd:COG1122 82 qnPDDqlfapTVEEDVAFGPE------NLGLPReeIRERVEEALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 166 LLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-222 |
1.62e-30 |
|
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: 117.15 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 12 VKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETEAAGIVII---- 87
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP--PASGEITLDGKPVTRRSPRDAIRAGIAYVpedr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 88 HQELtLVPDLSVAENIFMGHELTlpggrmnypamlhraealmrelkvpdmnvalpvsqygGGYQQLVEIAKALNKQARLL 167
Cdd:cd03215 85 KREG-LVLDLSVAENIALSSLLS-------------------------------------GGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 168 ILDEPssalTRG----EIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03215 127 ILDEP----TRGvdvgAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-222 |
1.85e-30 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 118.38 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF----GGVNALNGIDIKVKPGECVGLCGENGAGKSTL----MKVLSAVyphgtwEGEILWDGQPL----- 71
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLaraiLGLLKPT------SGSIIFDGKDLlklsr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 72 KAQSIRETEaagIVIIHQE--LTLVPDLSVAENIFmghELTLPGGRMNYPAMLHRAEALMRELKVPDMNVA--LPvSQYG 147
Cdd:cd03257 75 RLRKIRRKE---IQMVFQDpmSSLNPRMTIGEQIA---EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnrYP-HELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 148 GGYQQLVEIAKALNKQARLLILDEPSSAL---TRGEIevlLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALdvsVQAQI---LDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-232 |
2.60e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 118.16 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSIRETEAAGI 84
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP--RSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGheLTLPGGRMNYPAMLHRAEAL---MRELKvpdmnvalpvSQYG----GGYQQLVEIA 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLG--AYARRDRAEVRADLERVYELfprLKERR----------RQRAgtlsGGEQQMLAIG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 158 KALNKQARLLILDEPS---SALTRGEIevlLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADM 232
Cdd:COG0410 149 RALMSRPKLLLLDEPSlglAPLIVEEI---FEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-222 |
3.52e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.45 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFG----GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPhgtWEGEILWDGQPLKAQSirET 79
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRP---TSGEVLIDGQDISSLS--ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAA-------GIViiHQELTLVPDLSVAENIFMGHELtlpgGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQ 152
Cdd:COG1136 79 ELArlrrrhiGFV--FQFFNLLPELTALENVALPLLL----AGVSRKERRERARELLERVGLGDRLDHRP-SQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 153 LVEIAKALNKQARLLILDEPSSAL---TRGEIevlLDIIKGL-KAKGVACVYISHklD-EVAAVCDTIAVIRDGK 222
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLdskTGEEV---LELLRELnRELGTTIVMVTH--DpELAARADRVIRLRDGR 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-484 |
1.99e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 121.35 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 22 NGIDIKVKPGECVGLCGENGAGKS-TLMKVL------SAVYPHGtwegEILWDGQPL---KAQSIRETEAAGIVIIHQE- 90
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILrllpspPVVYPSG----DIRFHGESLlhaSEQTLRGVRGNKIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 91 -LTLVPDLSVAENIFmgHELTLPGGRMNYPAmlhRAEALMRELKVPDMNVALPVS----QYGGGYQQLVEIAKALNKQAR 165
Cdd:PRK15134 102 mVSLNPLHTLEKQLY--EVLSLHRGMRREAA---RGEILNCLDRVGIRQAAKRLTdyphQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 166 LLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK---HIATTAMADMDIPRIITQM 241
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRcveQNRAATLFSAPTHPYTQKL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 242 VGREMSNLYPTEPHDvGEVIFEARNVtcyDVDNPKRKR-----------VDDISFVLRRGEILGIAGLVGAGRTELVSAL 310
Cdd:PRK15134 257 LNSEPSGDPVPLPEP-ASPLLDVEQL---QVAFPIRKGilkrtvdhnvvVKNISFTLRPGETLGLVGESGSGKSTTGLAL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 311 FGAYPGRynAEVWLEGQVIDTRTPLKsiraglcMVPEDRKRQGIIPDLGVGQNITLAVLDTYA-----HMTRIDAEAELG 385
Cdd:PRK15134 333 LRLINSQ--GEIWFDGQPLHNLNRRQ-------LLPVRHRIQVVFQDPNSSLNPRLNVLQIIEeglrvHQPTLSAAQREQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 386 SIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVS 464
Cdd:PRK15134 404 QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFIS 483
|
490 500
....*....|....*....|
gi 1067238353 465 SELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK15134 484 HDLHVVRALCHQVIVLRQGE 503
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-222 |
4.10e-29 |
|
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: 114.12 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGG----VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEA 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 ---AGIVIIHQELTLVPDLSVAENIfmghELTLPGGRMNYPAMLHRAEALMRELKVPD-MNValPVSQYGGGYQQLVEIA 157
Cdd:cd03255 79 frrRHIGFVFQSFNLLPDLTALENV----ELPLLLAGVPKKERRERAEELLERVGLGDrLNH--YPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 158 KALNKQARLLILDEPSSAL---TRGEIevlLDIIKGL-KAKGVACVYISHKlDEVAAVCDTIAVIRDGK 222
Cdd:cd03255 153 RALANDPKIILADEPTGNLdseTGKEV---MELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
4.56e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.51 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLsA--VYPHgtwEGEILWDGQPLKAqsiRE 78
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI-AgfETPD---SGRILLDGRDVTG---LP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 79 TEAAGIVIIHQELTLVPDLSVAENIFMGheltLPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAK 158
Cdd:COG3842 74 PEKRNVGMVFQDYALFPHLTVAENVAFG----LRMRGVPKAEIRARVAELLELVGLEGLADRYP-HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 159 ALNKQARLLILDEPSSAL---TRGEIEVLLDIIkgLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALdakLREEMREELRRL--QRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-225 |
4.75e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMK-VLSAVYPHgtwEGEILWDGQPLKAQSIRET----E 80
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPD---SGEVLWDGEPLDPEDRRRIgylpE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGiviihqeltLVPDLSVAENI-FMGhelTLPGgrMNYPAMLHRAEALMRELKVPD-MNValPVSQYGGGYQQLVEIAK 158
Cdd:COG4152 79 ERG---------LYPKMKVGEQLvYLA---RLKG--LSKAEAKRRADEWLERLGLGDrANK--KVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 159 ALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-485 |
1.11e-28 |
|
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: 119.14 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILW----------------DGQ 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 70 PLK----------------AQSIRETEAAGIVIIHQE-LTLVPDLSVAENIFMG-HELTLPGGRMnypamLHRAEALMRE 131
Cdd:TIGR03269 81 PCPvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEAlEEIGYEGKEA-----VGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 132 LKVPD--MNVALPVSqygGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLD-IIKGLKAKGVACVYISHKLDEV 208
Cdd:TIGR03269 156 VQLSHriTHIARDLS---GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 209 AAVCDTIAVIRDGkhiattAMADMDIPRIITQMVGREMSNLYPTEPHDVGEVIFEARNVT--CYDVDNPKRKRVDDISFV 286
Cdd:TIGR03269 233 EDLSDKAIWLENG------EIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSkrYISVDRGVVKAVDNVSLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 287 LRRGEILGIAGLVGAGRTELVSALFGAYP---GRYNAEVWLEGQVIDTRTPLKSIRAglcmvpedRKRQGIIpdlgvGQN 363
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLEptsGEVNVRVGDEWVDMTKPGPDGRGRA--------KRYIGIL-----HQE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 364 ITLavldtYAHMTRIDAEAELGSID--QQISRMH----LKTAS----------PSLPiTSLSGGNQQKAVLAKMLMAKPK 427
Cdd:TIGR03269 374 YDL-----YPHRTVLDNLTEAIGLElpDELARMKavitLKMVGfdeekaeeilDKYP-DELSEGERHRVALAQVLIKEPR 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYK-LMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-218 |
1.32e-28 |
|
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: 112.95 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGG----VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSiretea 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP--TSGEVLVDGEPVTGPG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 AGIVIIHQELTLVPDLSVAENIFMGHELTlpggRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALN 161
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQ----GVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 162 KQARLLILDEPSSAL---TRGEI-EVLLDIikgLKAKGVACVYISHKLDEVAAVCDTIAVI 218
Cdd:cd03293 148 VDPDVLLLDEPFSALdalTREQLqEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-211 |
2.65e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.80 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQsiRETEAAGI 84
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS--AGEVLWNGEPIRDA--REDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGHELTlpggrmNYPAMLHRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALY------GLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAV 211
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-222 |
3.13e-28 |
|
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: 110.17 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKA---QSIRETeaagIVIIHQELT 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP--TSGEILIDGVDLRDldlESLRKN----IAYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDlSVAENIFmgheltlpggrmnypamlhraealmrelkvpdmnvalpvSqygGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:cd03228 87 LFSG-TIRENIL---------------------------------------S---GGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 173 SSAL-TRGEIEVlLDIIKGLkAKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:cd03228 124 TSALdPETEALI-LEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-222 |
4.92e-28 |
|
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: 111.89 E-value: 4.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFG-GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLS-AVYPHgtwEGEILWDGQPLKAQSIRETEAA- 82
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNgLVEPT---SGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 -GIVIIHQELTLVPDLSVAENIFMGHELTLPGGR----MNYPAMLHRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIA 157
Cdd:cd03256 78 rQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRslfgLFPKEEKQRALAALERVGLLDK-AYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 158 KALNKQARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
263-485 |
8.19e-28 |
|
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: 109.41 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPlksirag 341
Cdd:cd03230 2 EVRNLSkRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGEIKVLGKDIKKEPE------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 lcmvpEDRKRQGIIPdlgvgQNITLavldtYAHMTRIDaeaelgsidqqisrmHLKtaspslpitsLSGGNQQKAVLAKM 421
Cdd:cd03230 70 -----EVKRRIGYLP-----EEPSL-----YENLTVRE---------------NLK----------LSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 422 LMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-222 |
1.28e-27 |
|
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: 109.65 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQSIRETeaAGIVIIHQELTLV 94
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkES---SGSILLNGKPIKAKERRKS--IGYVMQDVDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDlSVAEnifmghELTLpgGRMNYPAMLHRAEALMRELKVPDMNVALPVSqYGGGYQQLVEIAKALNKQARLLILDEPSS 174
Cdd:cd03226 86 TD-SVRE------ELLL--GLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067238353 175 ALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-225 |
7.63e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.75 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 14 SFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIREteaagiviIHQELTL 93
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK--PSSGEILLDGKDLASLSPKE--------LARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 94 VPDLsvaenifmgheltlpggrMNYPAMLHRAEALMRELkvpdmnvalpvSqygGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:cd03214 78 VPQA------------------LELLGLAHLADRPFNEL-----------S---GGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 174 SAL-TRGEIEVlLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03214 126 SHLdIAHQIEL-LELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
280-484 |
1.02e-26 |
|
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: 107.52 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRkrqGIIPDLG 359
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLAvldtyAHMTRIDAEAElgSIDQQISRMhlktasPSL------PITSLSGGNQQKAVLAKMLMAKPKVLILDE 433
Cdd:cd03224 92 VEENLLLG-----AYARRRAKRKA--RLERVYELF------PRLkerrkqLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 434 PTRG-----VDvgakyEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:cd03224 159 PSEGlapkiVE-----EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
263-484 |
1.25e-26 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 107.17 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTcYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGaYPGRYNAEVWLEGQVIDTRTplksiragl 342
Cdd:cd03225 1 ELKNLS-FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG-LLGPTSGEVLVDGKDLTKLS--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 cmVPEDRKRQGII---PDLgvgQNITLAVLD-----------TYAHM-TRIDAEAELGSIDqqisrmHLKTASPSlpitS 407
Cdd:cd03225 70 --LKELRRKVGLVfqnPDD---QFFGPTVEEevafglenlglPEEEIeERVEEALELVGLE------GLRDRSPF----T 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.76e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.87 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSIRete 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP--TSGTVRLFGKPPRRARRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 aAGIVIihQELTLVPD--LSVAENIFMGHeltlpGGRMNYPAMLHRA------EAL----MRELKvpdmnvALPVSQYGG 148
Cdd:COG1121 77 -IGYVP--QRAEVDWDfpITVRDVVLMGR-----YGRRGLFRRPSRAdreavdEALervgLEDLA------DRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 149 GYQQLVEIAKALNKQARLLILDEPSSAL-TRGEiEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKH 223
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVdAATE-EALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-221 |
3.76e-26 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 106.36 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF-----GGV--NALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYphGTWEGEIL--WDGQPL---K 72
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNY--LPDSGSILvrHDGGWVdlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 73 AQ-----SIRETEaagIVIIHQELTLVPDLS----VAENIF-MGHELtlpggrmnyPAMLHRAEALMRELKVPDMNVALP 142
Cdd:COG4778 82 ASpreilALRRRT---IGYVSQFLRVIPRVSaldvVAEPLLeRGVDR---------EEARARARELLARLNLPERLWDLP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 143 VSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDG 221
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
280-484 |
4.38e-26 |
|
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: 106.22 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRkrqGIIPDLG 359
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-SGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLAvldTYAHMTRIDAEAELGSIDQQISRMHLKTASPSlpiTSLSGGNQQKAVLAKMLMAKPKVLILDEPTRG-- 437
Cdd:COG0410 95 VEENLLLG---AYARRDRAEVRADLERVYELFPRLKERRRQRA---GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGla 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 438 ---VDvgakyEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:COG0410 169 pliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-222 |
1.44e-25 |
|
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: 110.69 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKA---QSIRETeaagIVIIHQELT 92
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP--TSGRILIDGIDLRQidpASLRRQ----IGVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDlSVAENIFMGH-ELTLpggrmnypAMLHRA-------EALMR-----ELKVPDMNVALPvsqygGGYQQLVEIAKA 159
Cdd:COG2274 560 LFSG-TIRENITLGDpDATD--------EEIIEAarlaglhDFIEAlpmgyDTVVGEGGSNLS-----GGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 160 LNKQARLLILDEPSSAL-TRGEiEVLLDIIKGLkAKGVACVYISHKLdEVAAVCDTIAVIRDGK 222
Cdd:COG2274 626 LLRNPRILILDEATSALdAETE-AIILENLRRL-LKGRTVIIIAHRL-STIRLADRIIVLDKGR 686
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-225 |
3.58e-25 |
|
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: 103.78 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAAGIV 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD--SGKILLDGQDITKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGHELTlpggRMNYPAMLHRAEALMRELKVPDM--NVALPVSqygGGYQQLVEIAKALNKQ 163
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIR----GLSKKEREEKLEELLEEFHITHLrkSKASSLS---GGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 164 ARLLILDEPSSA---LTRGEIEvllDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03218 152 PKFLLLDEPFAGvdpIAVQDIQ---KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
280-503 |
4.06e-25 |
|
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: 108.45 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP--GRYNAEVWLEGQviDTRTPLKSIRAG-LCMVPEDRKRQgIIP 356
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhgGRISGEVLLDGR--DLLELSEALRGRrIGMVFQDPMTQ-LNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 dLGVGQNITLAVLDTyaHMTRIDAEAELGSIDQQISRMHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:COG1123 99 -VTVGDQIAEALENL--GLSRAEARARVLELLEAVGLERRLDRYPH----QLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 437 GVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRGDF-INDGLTQEQVLAAA 503
Cdd:COG1123 172 ALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGpPEEILAAPQALAAV 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-225 |
9.80e-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: 102.06 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETeaagIV 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR----IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGHELT-LPGGRMNypamlHRAEALMRELKVPDMNVALpVSQYGGGYQQLVEIAKALNKQA 164
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYgVPGAERR-----ERIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-226 |
1.12e-24 |
|
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: 101.52 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQplkaqSIRETEAAGIV 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD--SGEITFDGK-----SYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 I--IHQELTLVPDLSVAENIFMGheLTLPGGRMNypamlhRAEALMRELKVPDMNvALPVSQYGGGYQQLVEIAKALNKQ 163
Cdd:cd03268 74 IgaLIEAPGFYPNLTARENLRLL--ARLLGIRKK------RIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
274-485 |
1.50e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 101.18 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 274 NPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPLKSIRaglcMVPEDRKRQg 353
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-ESSGSILLNGKPIKAKERRKSIG----YVMQDVDYQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 354 iipdLG---VGQNITLavldtyahmTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:cd03226 84 ----LFtdsVREELLL---------GLKELDAGNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
276-501 |
1.52e-24 |
|
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: 102.24 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGqvIDTRTPLKSIRAGLCMVPEDRkrqGII 355
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP-DSGSILIDG--EDVRKEPREARRQIGVLPDER---GLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 PDLGVGQNITLavldtYAHMTRIDAEAELGSIDQQISRM----HLKTaspslPITSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:COG4555 87 DRLTVRENIRY-----FAELYGLFDEELKKRIEELIELLgleeFLDR-----RVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGDFINDGLTQEQVLA 501
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-225 |
1.77e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.50 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHgtwEGEILWDGQPLKAQSIRETeAAG 83
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPS---SGEVRLNGRPLAAWSPWEL-ARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVPDLSVAENIFMGHeltLPGGRmNYPAMLHRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIAKAL--- 160
Cdd:COG4559 77 RAVLPQHSSLAFPFTVEEVVALGR---APHGS-SAAQDRQIVREALALVGLAHL-AGRSYQTLSGGEQQRVQLARVLaql 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 161 ----NKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG4559 152 wepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-222 |
2.52e-24 |
|
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: 100.68 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPL---KAQSIRETEAA 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDGLKLtddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIihQELTLVPDLSVAENIFMGHELTLpggRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNK 162
Cdd:cd03262 79 GMVF--QQFNLFPHLTVLENITLAPIKVK---GMSKAEAEERALELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 163 QARLLILDEPSSAL---TRGEIevlLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03262 153 NPKVMLFDEPTSALdpeLVGEV---LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-245 |
2.72e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.61 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHGtweGEILWDGQPLKAQSIRET 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG---GTILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAAGIVIIHQELTLVPDLSVAENIFMGHELTLP----GGRMNYPAMLHR-AEALMRELKVPD-MNVALPVSQYGG----G 149
Cdd:PRK11300 78 ARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKtglfSGLLKTPAFRRAeSEALDRAATWLErVGLLEHANRQAGnlayG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 150 YQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIATTA 228
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
250
....*....|....*...
gi 1067238353 229 MADM-DIPRIITQMVGRE 245
Cdd:PRK11300 238 PEEIrNNPDVIKAYLGEA 255
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
280-435 |
6.55e-24 |
|
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: 97.72 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGQVIdTRTPLKSIRAGLCMVPEDRkrqGIIPDLG 359
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-TEGTILLDGQDL-TDDERKSLRKEIGYVFQDP---QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 360 VGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:pfam00005 76 VRENLRLGLLL--KGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
280-485 |
8.08e-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: 99.82 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIDTRTPLKSIRAGLCmvpedRKRQ--GI 354
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsGS----VLFDGEDITGLPPHEIARLGIG-----RTFQipRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVGQNITLAVLDTYAHMT----RIDAEAEL-GSIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:cd03219 87 FPELTVLENVMVAAQARTGSGLllarARREEREArERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
259-502 |
2.29e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.01 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVTC-YDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrynaevwlegqvidtrtPLK- 336
Cdd:COG1121 4 MPAIELENLTVsYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP------------------PTSg 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 SIRAGLCMVPEDRKRQGIIPdlgvgQNITLA------VLDT-----YAHM------TRIDAEAelgsIDQQISRM---HL 396
Cdd:COG1121 62 TVRLFGKPPRRARRRIGYVP-----QRAEVDwdfpitVRDVvlmgrYGRRglfrrpSRADREA----VDEALERVgleDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 397 KTAspslPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNR 476
Cdd:COG1121 133 ADR----PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR 208
|
250 260
....*....|....*....|....*.
gi 1067238353 477 VLVIGDGQLRGDFINDGLTQEQVLAA 502
Cdd:COG1121 209 VLLLNRGLVAHGPPEEVLTPENLSRA 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-225 |
2.53e-23 |
|
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: 98.21 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF----GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLS-AVYPHGtweGEILWDG-----QPLKAQ 74
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgLLEPDA---GFATVDGfdvvkEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 75 sireteaAGIVIIHQELTLVPDLSVAENI--------FMGHELTlpgGRMNYPAMLHRAEALMrELKVPDMnvalpvSQy 146
Cdd:cd03266 78 -------RRLGFVSDSTGLYDRLTARENLeyfaglygLKGDELT---ARLEELADRLGMEELL-DRRVGGF------ST- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 147 ggGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03266 140 --GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
263-485 |
2.84e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 96.74 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTcydVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGQVIDTRTPLksiragl 342
Cdd:cd03214 1 EVENLS---VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-SSGEILLDGKDLASLSPK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 cmvpEDRKRQGIIPdlgvgQNITLAVLDTYAHmtridaeaelgsidqqisRmhlktaspslPITSLSGGNQQKAVLAKML 422
Cdd:cd03214 70 ----ELARKIAYVP-----QALELLGLAHLAD------------------R----------PFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 423 MAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-222 |
3.10e-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: 97.75 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 30 PGECVGLCGENGAGKSTLMKVLSAV-YPHGtweGEILWDGQPLKAQSIR---ETEAAGIVIIHQELTLVPDLSVAENIFM 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLeKPDG---GTIVLNGTVLFDSRKKinlPPQQRKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 106 GheltLPGGRMNypAMLHRAEALMRELKVpDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL---TRGEIE 182
Cdd:cd03297 99 G----LKRKRNR--EDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALdraLRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1067238353 183 VLLDIIKglKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03297 172 PELKQIK--KNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-222 |
4.03e-23 |
|
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: 98.04 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGG----VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPHgtwEGEILWDGQPLKAQSIRET 79
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT---SGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAA--GIVIIHQELTLVPDLSVAENIfmGHELTLPGGRMNYpaMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIA 157
Cdd:cd03258 78 RKArrRIGMIFQHFNLLSSRTVFENV--ALPLEIAGVPKAE--IEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 158 KALNKQARLLILDEPSSAL----TRGEIEVLLDIIKGLkakGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03258 153 RALANNPKVLLCDEATSALdpetTQSILALLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-261 |
5.61e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRete 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 aAGIVIIHQELTLVPDLSVAENIfmgheltLPGGRmnYPAMLHR-AEALMR---ELKVPDMNVALPVSQYGGGYQQLVEI 156
Cdd:PRK13536 114 -ARIGVVPQFDNLDLEFTVRENL-------LVFGR--YFGMSTReIEAVIPsllEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 157 AKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMdipr 236
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL---- 259
|
250 260
....*....|....*....|....*
gi 1067238353 237 iITQMVGREMSNLYPTEPHDVGEVI 261
Cdd:PRK13536 260 -IDEHIGCQVIEIYGGDPHELSSLV 283
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
263-484 |
7.17e-23 |
|
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: 95.00 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTcydVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPlksiragl 342
Cdd:cd00267 1 EIENLS---FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-PTSGEILIDGKDIAKLPL-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 cmvPEDRKRQGIIPdlgvgqnitlavldtyahmtridaeaelgsidqqisrmhlktaspslpitSLSGGNQQKAVLAKML 422
Cdd:cd00267 69 ---EELRRRIGYVP--------------------------------------------------QLSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 423 MAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
280-486 |
7.27e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 96.58 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTrtplkSIRAGLCMVPEDRkrqGIIPDLG 359
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-PDSGEVLFDGKPLDI-----AARNRIGYLPEER---GLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VG-QNITLAVLdtyAHMTRIDAEAElgsIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGV 438
Cdd:cd03269 87 VIdQLVYLAQL---KGLKKEEARRR---IDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067238353 439 DVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-233 |
7.99e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.95 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF--GGVN-------ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVypHGTWEGEILWDGQPLkAQS 75
Cdd:TIGR02769 2 LLEVRDVTHTYrtGGLFgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL--EKPAQGTVSFRGQDL-YQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 76 IRETEAAgiviIHQELTLV---------PDLSVAENIF--MGHELtlpggRMNYPAMLHRAEALMRELKVPDMNVALPVS 144
Cdd:TIGR02769 79 DRKQRRA----FRRDVQLVfqdspsavnPRMTVRQIIGepLRHLT-----SLDESEQKARIAELLDMVGLRSEDADKLPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 145 QYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKH 223
Cdd:TIGR02769 150 QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
250
....*....|
gi 1067238353 224 IATTAMADMD 233
Cdd:TIGR02769 230 VEECDVAQLL 239
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-222 |
8.15e-23 |
|
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: 96.87 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKV---LSAVYPHGTWEGEILWDGQPLKAQSIRETE-- 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 -AAGIVIihQELTLVPdLSVAENIFMGheLTLPGGRMNyPAMLHRAEALMRELKVPDmNVALPVSQYG--GGYQQLVEIA 157
Cdd:cd03260 81 rRVGMVF--QKPNPFP-GSIYDNVAYG--LRLHGIKLK-EELDERVEEALRKAALWD-EVKDRLHALGlsGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 158 KALNKQARLLILDEPSSAL---TRGEIEvllDIIKGLKAKgVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03260 154 RALANEPEVLLLDEPTSALdpiSTAKIE---ELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
9.26e-23 |
|
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: 96.97 E-value: 9.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHgtwEGEILWDGQPLKAQSIRET 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD---SGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAA----GIVIihQELTLVPDLSVAENI-FMGHELTlpggRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLV 154
Cdd:COG1127 78 YELrrriGMLF--QGGALFDSLTVFENVaFPLREHT----DLSEAEIRELVLEKLELVGLPGAADKMP-SELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 155 EIAKALNKQARLLILDEPSSAL---TRGEIEVLldiIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMA 230
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|
gi 1067238353 231 DM---DIPRI 237
Cdd:COG1127 228 ELlasDDPWV 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
262-488 |
1.01e-22 |
|
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: 94.80 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTcydvdnpKR----KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPLKS 337
Cdd:cd03216 1 LELRGIT-------KRfggvKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PDSGEILVDGKEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPEdrkrqgiipdlgvgqnitlavldtyahmtridaeaelgsidqqisrmhlktaspslpitsLSGGNQQKAV 417
Cdd:cd03216 73 RRAGIAMVYQ------------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 418 LAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-485 |
1.52e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.09 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 18 VNALNGIDIKVKPGECVGLCGENGAGKS----TLMKVLSAVypHGTWEGEILW---------DGQPLKAQSIRETEAAGI 84
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQA--GGLVQCDKMLlrrrsrqviELSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQE--LTLVPDLSVAENIfmGHELTLPGGRMNYPAMLhRAEALMRELKVPDMNVALP--VSQYGGGYQQLVEIAKAL 160
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQI--AESIRLHQGASREEAMV-EAKRMLDQVRIPEAQTILSryPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 161 NKQARLLILDEPSSAL---TRGEIEVLLDIIKGLKAKGVacVYISHKLDEVAAVCDTIAVIRDGKHIAT----------- 226
Cdd:PRK10261 184 SCRPAVLIADEPTTALdvtIQAQILQLIKVLQKEMSMGV--IFITHDMGVVAEIADRVLVMYQGEAVETgsveqifhapq 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 227 --------------TAMADMDIPRIITQMVGREMSNLYPTEPHDV---GEVIFEARN-VTCYDVDNPKRKR-------VD 281
Cdd:PRK10261 262 hpytrallaavpqlGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTvvdGEPILQVRNlVTRFPLRSGLLNRvtrevhaVE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTPLKsiraglcMVPEDRKRQGIIPD---- 357
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIDTLSPGK-------LQALRRDIQFIFQDpyas 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 358 LGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRG 437
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1067238353 438 VDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-218 |
2.70e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 94.91 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 7 QMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMK-VLSAVYPHgtwEGEILWDGQPLKAQSIReteaagIV 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPT---SGSIRVFGKPLEKERKR------IG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPD--LSVAENIFMGheltlpggRMNYPAMLHRA-----EALMRELKVPDMnVAL---PVSQYGGGYQQLVE 155
Cdd:cd03235 72 YVPQRRSIDRDfpISVRDVVLMG--------LYGHKGLFRRLskadkAKVDEALERVGL-SELadrQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVI 218
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-222 |
2.75e-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: 95.38 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 10 GIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLsAVYPHGTwEGEILWDGQPLKAQSIRETeaaGIVIIHQ 89
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLI-AGFETPT-SGEILLDGKDITNLPPHKR---PVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 ELTLVPDLSVAENIFMGheLTLPggRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLIL 169
Cdd:cd03300 80 NYALFPHLTVFENIAFG--LRLK--KLPKAEIKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 170 DEPSSALT---RGEIEVLLDIIKglKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03300 155 DEPLGALDlklRKDMQLELKRLQ--KELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-237 |
3.91e-22 |
|
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: 95.26 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAA--- 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD--SGEVLIDGEDISGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 -GIVIihQELTLVPDLSVAENI-FMGHELTlpggRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKAL 160
Cdd:cd03261 79 mGMLF--QSGALFDSLTVFENVaFPLREHT----RLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 161 NKQARLLILDEPSSAL---TRGEIEvllDIIKGLK-AKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADM---D 233
Cdd:cd03261 152 ALDPELLLYDEPTAGLdpiASGVID---DLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELrasD 228
|
....
gi 1067238353 234 IPRI 237
Cdd:cd03261 229 DPLV 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
262-485 |
4.27e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 94.11 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVtCYDVDNpkRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGQVIDTRTPLKsIRAG 341
Cdd:COG4619 1 LELEGL-SFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP-TSGEIYLDGKPLSAMPPPE-WRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 LCMVPEDrkrqgiiPDLG---VGQNITLAVLDTYAHMTRIDAEAELgsidqqiSRMHLKTASPSLPITSLSGGNQQKAVL 418
Cdd:COG4619 76 VAYVPQE-------PALWggtVRDNLPFPFQLRERKFDRERALELL-------ERLGLPPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 419 AKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-235 |
5.50e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.44 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 24 IDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIretEAAGIVIIHQELTLVPDLSVAENI 103
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS--GRILWNGQDLTALPP---AERPVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 104 FMG-HeltlPGGRMNyPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL---TRG 179
Cdd:COG3840 93 GLGlR----PGLKLT-AEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALdpaLRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 180 EievLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGK---HIATTAMADMDIP 235
Cdd:COG3840 167 E---MLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRiaaDGPTAALLDGEPP 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-302 |
5.68e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETeAAGIV 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA--GTVLVAGDDVEALSARAA-SRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGHelTLPGGRMNYPAMLHRA--EALMRELKVpDMNVALPVSQYGGGYQQLVEIAKALNKQ 163
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGR--TPHRSRFDTWTETDRAavERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQMVG 243
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 244 REMsnLYPTEPhdvgevIFEARNVTCYDVDNPKRKRVDDISFVLRRGE--ILGIAGLVGAG 302
Cdd:PRK09536 238 ART--AVGTDP------ATGAPTVTPLPDPDRTEAAADTRVHVVGGGQpaARAVSRLVAAG 290
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-226 |
7.23e-22 |
|
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: 99.06 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSiRETEAAGIVIIHQELTLVP 95
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY--SGSILINGVDLSDLD-PASWRRQIAWVPQNPYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DlSVAENIFMGHElTLPGGRMNYPAMLHRAEALMRELkvPDMnVALPVSQYG----GGYQQLVEIAKALNKQARLLILDE 171
Cdd:COG4988 425 G-TIRENLRLGRP-DASDEELEAALEAAGLDEFVAAL--PDG-LDTPLGEGGrglsGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 172 PSSALTRGEIEVLLDIIKGLkAKGVACVYISHKLDEVAAvCDTIAVIRDGKHIAT 226
Cdd:COG4988 500 PTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-222 |
7.84e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.70 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKA---QSIRETeaagIVIIHQELT 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT--SGRILIDGVDIRDltlESLRRQ----IGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVpDLSVAENIFMgheltlpgGRMNYP-----AMLHRAEALmrelkvpDMNVALP------VSQYG----GGYQQLVEIA 157
Cdd:COG1132 425 LF-SGTIRENIRY--------GRPDATdeeveEAAKAAQAH-------EFIEALPdgydtvVGERGvnlsGGQRQRIAIA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 158 KALNKQARLLILDEPSSAL-TRGEIEvlldIIKGLKA--KGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:COG1132 489 RALLKDPPILILDEATSALdTETEAL----IQEALERlmKGRTTIVIAHRLSTIRN-ADRILVLDDGR 551
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
262-488 |
1.12e-21 |
|
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: 93.55 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVT-CYdvdnPKRKRV-DDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEVWLEGQVIdTRTPLK 336
Cdd:COG1122 1 IELENLSfSY----PGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsG----EVLVDGKDI-TKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 SIRAGLCMV---PEDrkrQGIIPDlgVGQNITLAV----LDTYAHMTRIDAEAELGSIDqqisrmHLKTASPSlpitSLS 409
Cdd:COG1122 72 ELRRKVGLVfqnPDD---QLFAPT--VEEDVAFGPenlgLPREEIRERVEEALELVGLE------HLADRPPH----ELS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 410 GGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-222 |
1.42e-21 |
|
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: 93.03 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGeCVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKA--QSIRETeaag 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP--PSSGTIRIDGQDVLKqpQKLRRR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVPDLSVAEniFMGHELTLpgGRMNYPAMLHRAEALMRELKVPDMNvALPVSQYGGGYQQLVEIAKALNKQ 163
Cdd:cd03264 74 IGYLPQEFGVYPNFTVRE--FLDYIAWL--KGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGLKAKgvACVYIS-HKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
280-486 |
1.43e-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: 92.95 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYpgRYNA-EVWLEGqvIDTRTPLKSIRAGLCMVPEDRkrqGIIPDL 358
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSgTAYING--YSIRTDRKAARQSLGYCPQFD---ALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNITLavldtYAHMTRIdaeaELGSIDQQISRMHLKTASPSL---PITSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:cd03263 91 TVREHLRF-----YARLKGL----PKSEIKEEVELLLRVLGLTDKankRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 436 RGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:cd03263 162 SGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-225 |
2.22e-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: 92.57 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGG--VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLS-AVYPHGtweGEILWDGQPLKAQsiRETEAA 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTS---GTAYINGYSIRTD--RKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIIHQELTLVPDLSVAENIFMGHELTlpgGRMNYPAMLHrAEALMRELK-VPDMNValPVSQYGGGYQQLVEIAKALN 161
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYARLK---GLPKSEIKEE-VELLLRVLGlTDKANK--RARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 162 KQARLLILDEPSSAL---TRGEIevlLDIIKGLKaKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03263 150 GGPSVLLLDEPTSGLdpaSRRAI---WDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
261-485 |
2.42e-21 |
|
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: 92.57 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVTC-YDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDT--RTPLKS 337
Cdd:cd03257 1 LLEVKNLSVsFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-PTSGSIIFDGKDLLKlsRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPED-------RKRqgiipdlgVGQNITLAVLdtyAHMTRIDAEAELGSIDQQISRMHLKTASPSLPITSLSG 410
Cdd:cd03257 80 RRKEIQMVFQDpmsslnpRMT--------IGEQIAEPLR---IHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 411 GNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-225 |
2.59e-21 |
|
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: 93.23 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 3 DYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPhgTWEGEILWDGQPLKAQSIRETEA 81
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPP--TYGNDVRLFGERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 A-GIV--IIHQELTlvPDLSVAE--------NIFMGHELTlpggrmnyPAMLHRAEALMRELKVPDM-NVALP-VSQygg 148
Cdd:COG1119 79 RiGLVspALQLRFP--RDETVLDvvlsgffdSIGLYREPT--------DEQRERARELLELLGLAHLaDRPFGtLSQ--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 149 GYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
261-485 |
3.45e-21 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 92.80 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVTC-YDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQvidtrtPLKSIR 339
Cdd:COG1120 1 MLEAENLSVgYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-PSSGEVLLDGR------DLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 aglcmvPEDR-KRQGIIP-DLGVGQNITlaVLDT-----YAHMTRI------DAEAelgsIDQQISRMHLKtaspSL--- 403
Cdd:COG1120 70 ------RRELaRRIAYVPqEPPAPFGLT--VRELvalgrYPHLGLFgrpsaeDREA----VEEALERTGLE----HLadr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGD 482
Cdd:COG1120 134 PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKD 213
|
...
gi 1067238353 483 GQL 485
Cdd:COG1120 214 GRI 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
263-485 |
4.49e-21 |
|
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: 92.56 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTC-YDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGQVIdTRTPLKSIRAG 341
Cdd:COG1124 3 EVRNLSVsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-WSGEVTFDGRPV-TRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 LCMVPED-------RKRqgiipdlgVGQnitlAVLDTYAHMTRIDAEAElgsIDQQISRMHLktaSPSL----PItSLSG 410
Cdd:COG1124 81 VQMVFQDpyaslhpRHT--------VDR----ILAEPLRIHGLPDREER---IAELLEQVGL---PPSFldryPH-QLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 411 GNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-225 |
4.78e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHgtwEGEILWDGQPLKAQSIRETeAAG 83
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPD---SGEVRLNGRPLADWSPAEL-ARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVPDLSVAENIFMgheltlpgGRMNYPAMLHRAEAL----MRELKVpdmnVALPVSQY---GGGYQQLVEI 156
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAM--------GRAPHGLSRAEDDALvaaaLAQVDL----AHLAGRDYpqlSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 157 AKAL------NKQARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK13548 146 ARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-222 |
5.85e-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: 89.97 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSavyphGTW---EGEILWDGQPLKaqSIRETEAAGIV-IIHQELTLVPD 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLIL-----GLLrptSGRVRLDGADIS--QWDPNELGDHVgYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 lSVAENIFmgheltlpggrmnypamlhraealmrelkvpdmnvalpvsqyGGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:cd03246 91 -SIAENIL------------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 177 TRGEIEVLLDIIKGLKAKGVACVYISHKLdEVAAVCDTIAVIRDGK 222
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-254 |
6.16e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMK-VLSAVYPHGtweGEILWDGQPLKAQSIRET 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRmLLGLTHPDA---GSISLCGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAAGIViiHQELTLVPDLSVAENIFM-GHELTLPGG--RMNYPAML------HRAEALMRELKvpdmnvalpvsqygGGY 150
Cdd:PRK13537 80 QRVGVV--PQFDNLDPDFTVRENLLVfGRYFGLSAAaaRALVPPLLefakleNKADAKVGELS--------------GGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 151 QQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAma 230
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA-- 221
|
250 260
....*....|....*....|....*
gi 1067238353 231 dmdiPR-IITQMVGREMSNLYPTEP 254
Cdd:PRK13537 222 ----PHaLIESEIGCDVIEIYGPDP 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-222 |
8.06e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKST----LMKVLSAvyphgtwEGEILWDGQPLKAQSIRETEA--AGIVIIHQE--L 91
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-------QGEIWFDGQPLHNLNRRQLLPvrHRIQVVFQDpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 92 TLVPDLSVAENIFMGHELTLPggRMNYPAMLHRAEALMRELKV-PDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILD 170
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHQP--TLSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 171 EPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-221 |
9.14e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.00 E-value: 9.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHGTWEGEILWDGQPLK-----AQSIRE 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlITGDKSAGSHIELLGRTVQregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 79 TEAAgIVIIHQELTLVPDLSVAENIFMGHELTLPGGR--MNYPAMLHRAEALMRELKVPDMNVALP-VSQYGGGYQQLVE 155
Cdd:PRK09984 84 SRAN-TGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcFSWFTREQKQRALQALTRVGMVHFAHQrVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDG 221
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-222 |
1.04e-20 |
|
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: 91.06 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYphGTWEGEILWDGQPLKAQSIRETEAAgIVIIHQELTLVpD 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY--DPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLF-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFMGheltlpggrmNYPAMLHRAEALMRELKVPDMNVALP------VSQYG----GGYQQLVEIAKALNKQARL 166
Cdd:cd03249 91 GTIAENIRYG----------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlVGERGsqlsGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 167 LILDEPSSAL-TRGEIEV--LLDIIkglkAKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:cd03249 161 LLLDEATSALdAESEKLVqeALDRA----MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
280-480 |
1.74e-20 |
|
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: 89.90 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDtrtplksiraglcmvpEDRKRQGIIPD-L 358
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-PTSGSIRVFGKPLE----------------KERKRIGYVPQrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNITLAVLDT-----YAHM------TRIDAEAelgsIDQQISRM---HLKTAspslPITSLSGGNQQKAVLAKMLMA 424
Cdd:cd03235 78 SIDRDFPISVRDVvlmglYGHKglfrrlSKADKAK----VDEALERVglsELADR----QIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 425 KPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVI 480
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
276-485 |
2.00e-20 |
|
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: 90.29 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIdTRTPL-KSIRAGLCMVPEDrkr 351
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpdsGK----ILLDGQDI-TKLPMhKRARLGIGYLPQE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 QGIIPDLGVGQNItLAVLDtyahMTRIDAEAELGSIDQQISRMHLKTASPSLPItSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:cd03218 84 ASIFRKLTVEENI-LAVLE----IRGLSKKEREEKLEELLEEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-222 |
2.11e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 89.77 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSF-GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETE--AA 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDVSDLRGRAIPylRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIIHQELTLVPDLSVAENIFMGHELTLPGGRMnypaMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNK 162
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPRE----IRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 163 QARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
282-488 |
7.91e-20 |
|
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: 88.12 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRrGEILGIAGLVGAGRTELVSALFGaypgrynaevwLE----GQVIDTRTPLKSIRAGLCMVPEDRkRQGII-- 355
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAG-----------LEkpdgGTIVLNGTVLFDSRKKINLPPQQR-KIGLVfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 -----PDLGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQisrmHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:cd03297 83 qyalfPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLD----HLLNRYPA----QLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-205 |
9.68e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.23 E-value: 9.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETE---A 81
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE--ITSGDLIVDGLKVNDPKVDERLirqE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 AGIVIihQELTLVPDLSVAENIFMGHELTLPGGRMNypamlhrAEALMREL--KVPDMNVA--LPvSQYGGGYQQLVEIA 157
Cdd:PRK09493 79 AGMVF--QQFYLFPHLTALENVMFGPLRVRGASKEE-------AEKQARELlaKVGLAERAhhYP-SELSGGQQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 158 KALNKQARLLILDEPSSALT---RGEIevlLDIIKGLKAKGVACVYISHKL 205
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDpelRHEV---LKVMQDLAEEGMTMVIVTHEI 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
280-484 |
9.87e-20 |
|
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: 86.47 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTPLksiraglcmVPEDRKRQGIipdlg 359
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-SGSILIDGEDLTDLEDE---------LPPLRRRIGM----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLavldtYAHMTRIDAEAELgsidqqisrmhlktaspslpitsLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD 439
Cdd:cd03229 81 VFQDFAL-----FPHLTVLENIALG-----------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 440 VGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:cd03229 133 PITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-222 |
1.01e-19 |
|
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: 88.17 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLsAVYPHGTwEGEILWDGQPLKAQSIRETeaaGIV 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLI-AGLERPD-SGTILFGGEDATDVPVQER---NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGHELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQAR 165
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 166 LLILDEPSSAL---TRGEIEVLL----DIIkglkakGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03296 157 VLLLDEPFGALdakVRKELRRWLrrlhDEL------HVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-225 |
1.35e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTL--MKV-LsaVYPHgtwEGEILWDGQPLKAQSIRETEAA 82
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTfyMIVgL--VKPD---SGRIFLDGEDITHLPMHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIIHQELTLVPDLSVAENIFMGHELTlpggRMNYPAMLHRAEALMRELKVPDM--NVALPVSqygGGYQQLVEIAKAL 160
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELR----KLSKKEREERLEELLEEFGITHLrkSKAYSLS---GGERRRVEIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 161 NKQARLLILDEPSSA---LTRGEIEvllDIIKGLKAKGVAcVYIS-HKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG1137 152 ATNPKFILLDEPFAGvdpIAVADIQ---KIIRHLKERGIG-VLITdHNVRETLGICDRAYIISEGKVLA 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-224 |
1.97e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLsAVYPHGTwEGEILWDGQPLkaqSIRETEAAGI 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRML-AGFEQPT-AGQIMLDGVDL---SHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMG-HELTLPGGRMNypamlHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQ 163
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGlKQDKLPKAEIA-----SRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 164 ARLLILDEPSSAL-----TRGEIEVlLDIikgLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:PRK11607 168 PKLLLLDEPMGALdkklrDRMQLEV-VDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-231 |
3.39e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.43 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVN---------ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPHGtweGEILWDGQPLKAQ 74
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQ---GNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 75 SIRETEA--AGIVIIHQE-LTLV-PDLSVAENIF--MGHELTLpggrmNYPAMLHRAEALMRELKVPDMNVALPVSQYGG 148
Cdd:PRK10419 80 NRAQRKAfrRDIQMVFQDsISAVnPRKTVREIIRepLRHLLSL-----DKAERLARASEMLRAVDLDDSVLDKRPPQLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 149 GYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIATT 227
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
....
gi 1067238353 228 AMAD 231
Cdd:PRK10419 235 PVGD 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-222 |
4.17e-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: 87.31 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 11 IVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQS---IRETEAAGIVII 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT--SGKVLIDGQDIAAMSrkeLRELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 88 HQELTLVPDLSVAENIFMGHELtlpggrmnypAMLHRAEALMRELKVPDMnVALP------VSQYGGGYQQLVEIAKALN 161
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEV----------QGVPRAEREERAAEALEL-VGLEgwehkyPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 162 KQARLLILDEPSSAL---TRGEI-EVLLDIIKGLKaKGVacVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03294 177 VDPDILLMDEAFSALdplIRREMqDELLRLQAELQ-KTI--VFITHDLDEALRLGDRIAIMKDGR 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-222 |
4.99e-19 |
|
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: 86.20 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVN-ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQS-IRETEAAG 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT--SGEIFIDGEDIREQDpVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIihQELTLVPDLSVAENIFMgheltlpggrmnYPAMLH--------RAEALMRELKVPDMNVA--LPvSQYGGGYQQL 153
Cdd:cd03295 79 YVI--QQIGLFPHMTVEENIAL------------VPKLLKwpkekireRADELLALVGLDPAEFAdrYP-HELSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 154 VEIAKALNKQARLLILDEPSSAL---TRGEIEVLLDIIKGLKAKGVacVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALdpiTRDQLQEEFKRLQQELGKTI--VFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-222 |
5.10e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.87 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSF-GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhGTwEGEILWDGQPLKaqSIRETEAA-- 82
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-PT-SGQVLVNGQDLS--RLKRREIPyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 ----GIViiHQELTLVPDLSVAENIFMGHELT-LPGGRMNY--PAML------HRAEALMRELkvpdmnvalpvSqygGG 149
Cdd:COG2884 78 rrriGVV--FQDFRLLPDRTVYENVALPLRVTgKSRKEIRRrvREVLdlvglsDKAKALPHEL-----------S---GG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 150 YQQLVEIAKALNKQARLLILDEPSSAL---TRGEIevlLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLdpeTSWEI---MELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
271-485 |
5.61e-19 |
|
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: 85.85 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 271 DVDNPKRK----RVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIdtrTPLKSIRAGLC 343
Cdd:cd03299 2 KVENLSKDwkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpdsGK----ILLNGKDI---TNLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 344 MVPEDrkrQGIIPDLGVGQNITlavldtYAHMTRIDAEAELGSIDQQISRM----HLKTASPslpiTSLSGGNQQKAVLA 419
Cdd:cd03299 75 YVPQN---YALFPHMTVYKNIA------YGLKKRKVDKKEIERKVLEIAEMlgidHLLNRKP----ETLSGGEQQRVAIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 420 KMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
262-482 |
7.73e-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: 84.84 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTC-YDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEVWLEGQVIDTRTPlkS 337
Cdd:COG4133 3 LEAENLSCrRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpsaG----EVLWNGEPIRDARE--D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPEdrkRQGIIPDLGVGQNITLavldtYAHMTRIDAEAElgSIDQQISRMHLKTASpSLPITSLSGGNQQKAV 417
Cdd:COG4133 73 YRRRLAYLGH---ADGLKPELTVRENLRF-----WAALYGLRADRE--AIDEALEAVGLAGLA-DLPVRQLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 418 LAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVsnRVLVIGD 482
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA--RVLDLGD 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-460 |
9.25e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 10 GIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVypHGTWEGEILWDGQPLKAQSIRETEAAGIVIIHQ 89
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGA--RKIQQGRVEVLGGDMADARHRRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 EL--TLVPDLSVAENI-FMGhelTLPGgrmnypamLHRAEalmRELKVPDMNVAL--------PVSQYGGGYQQLVEIAK 158
Cdd:NF033858 84 GLgkNLYPTLSVFENLdFFG---RLFG--------QDAAE---RRRRIDELLRATglapfadrPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 159 ALNKQARLLILDEPSSA---LTRGEievLLDIIKGLKAKG------VACVYIshklDEvAAVCDTIAVIRDGKHIAT--- 226
Cdd:NF033858 150 ALIHDPDLLILDEPTTGvdpLSRRQ---FWELIDRIRAERpgmsvlVATAYM----EE-AERFDWLVAMDAGRVLATgtp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 227 ------TAMADMD-------------------IPriitqmvgremsnlyPTEPHDVGEVIFEARNVTCydvdnpkrkR-- 279
Cdd:NF033858 222 aellarTGADTLEaafiallpeekrrghqpvvIP---------------PRPADDDDEPAIEARGLTM---------Rfg 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 ----VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEVWLEGQVIDtrtplksiraglcmvPED---R 349
Cdd:NF033858 278 dftaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPaseG----EAWLFGQPVD---------------AGDiatR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 350 KRQGIIP-------DLGVGQNitlavLDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKML 422
Cdd:NF033858 339 RRVGYMSqafslygELTVRQN-----LELHARLFHLPAAEIAARVAEMLERFDLADVADALP-DSLPLGIRQRLSLAVAV 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 1067238353 423 MAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSI 460
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTI 451
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
282-487 |
9.27e-19 |
|
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: 87.86 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPgrYNAEVWLEGQVidtrtpLKSIRAGLCMVPEdRKRQGII----- 355
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGlTRP--DEGEIVLNGRT------LFDSRKGIFLPPE-KRRIGYVfqear 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 --PDLGVGQNITLAVLDTYAHMTRIDAEA--ELGSIDQQISRmhlktaspslPITSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:TIGR02142 86 lfPHLSVRGNLRYGMKRARPSERRISFERviELLGIGHLLGR----------LPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRG 487
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-218 |
9.62e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 89.27 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 2 PDYLLQMNGIVKSFGGV-NALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPL---KAQSIR 77
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNGVPLadaDADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 78 ETeaagIVIIHQELTLVPDlSVAENIFMGheltLPGGRmnyPAMLHRA---EALMRELKVPDMNVALPVSQYG----GGY 150
Cdd:TIGR02857 396 DQ----IAWVPQHPFLFAG-TIAENIRLA----RPDAS---DAEIREAlerAGLDEFVAALPQGLDTPIGEGGaglsGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 151 QQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLkAKGVACVYISHKLdEVAAVCDTIAVI 218
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-222 |
1.09e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 84.61 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGqplKAQSIRETEAAGIV 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT--SGRIYIGG---RDVTDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENifMGHELTLPGGRMnyPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQAR 165
Cdd:cd03301 76 MVFQNYALYPHMTVYDN--IAFGLKLRKVPK--DEIDERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 166 LLILDEPSSAL-TRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03301 151 VFLMDEPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
1.29e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAvYPHGTwEGEILWDGQPLK----AQSI 76
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRAT-SGRIVFDGKDITdwqtAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 77 REteaaGIVIIHQELTLVPDLSVAENIFMGhelTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPVSqygGGYQQLVEI 156
Cdd:PRK11614 79 RE----AVAIVPEGRRVFSRMTVEENLAMG---GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMS---GGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 157 AKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
281-485 |
1.92e-18 |
|
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: 84.48 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTPLKSIRAglcmvpedRKRQGII----- 355
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGEDISGLSEAELYRL--------RRRMGMLfqsga 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 --PDLGVGQNITLAVldtyaHMTRIDAEAELgsidQQISRMH-----LKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKV 428
Cdd:cd03261 88 lfDSLTVFENVAFPL-----REHTRLSEEEI----REIVLEKleavgLRGAEDLYP-AELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 429 LILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-222 |
1.99e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHGtweGEILWDGQPLkaqsiRETEAagiVIIHQELTLV---PD 96
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTG---GQVLLDGVPL-----VQYDH---HYLHRQVALVgqePV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 L---SVAENIFMGHELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:TIGR00958 566 LfsgSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067238353 174 SALTrGEIEVLLDIIKglKAKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:TIGR00958 646 SALD-AECEQLLQESR--SRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
281-485 |
2.00e-18 |
|
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: 83.73 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALfgAYPGRYNA-EVWLEGQVID-TRTPLKSIRAGLCMVPEDRKrqgIIPDL 358
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--NLLEEPDSgTIIIDGLKLTdDKKNINELRQKVGMVFQQFN---LFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNITLAvLDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGV 438
Cdd:cd03262 92 TVLENITLA-PIKVKGMSKAEAEERALELLEKVGLADKADAYPA----QLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 439 D---VGakyEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03262 167 DpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-222 |
4.66e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVypHGTWEGEILWDGQPLkaQSIRETeaagIV 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--ETPSAGELLAGTAPL--AEARED----TR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTLVPDLSVAENIFMGheltLPGgrmNYPAMLHRA-EALMRELKVPDMNVALpvsqyGGGYQQLVEIAKALNKQA 164
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLG----LKG---QWRDAALQAlAAVGLADRANEWPAAL-----SGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 165 RLLILDEP---SSALTRGEIEvllDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK11247 153 GLLLLDEPlgaLDALTRIEMQ---DLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-237 |
5.70e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.40 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETEAAGI 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENIFMGHELTlpgGRMNYPAMLHRAEALMRELKVPDMNVALPVSqYGGGYQQLVEIAKALNKQA 164
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIR---DDLSAEQREDRANELMEEFHIEHLRDSMGQS-LSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA----TTAMADMDIPRI 237
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAhgtpTEILQDEHVKRV 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
280-486 |
6.99e-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: 82.42 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRYNAEVwlEGqvIDTRTPLKSIRAGLCMVPEDRkrqGIIPDL 358
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATV--DG--FDVVKEPAEARRRLGFVSDST---GLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNitlavLDTYAHMTRIDAEAELGSIDQQISRMHLKtASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGV 438
Cdd:cd03266 94 TAREN-----LEYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067238353 439 DVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
263-479 |
1.00e-17 |
|
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: 83.95 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNV-TCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNA--EVWLEGQVIDTRTP--LKS 337
Cdd:COG0444 3 EVRNLkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITsgEILFDGEDLLKLSEkeLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAG-LCMVPED-------RKRqgiipdlgVGQNITlAVLDTYAHMTRIDAEA------ELGSIDQQISRM----Hlkta 399
Cdd:COG0444 83 IRGReIQMIFQDpmtslnpVMT--------VGDQIA-EPLRIHGGLSKAEAREraiellERVGLPDPERRLdrypH---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 400 spslpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVL 478
Cdd:COG0444 150 -------ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
.
gi 1067238353 479 V 479
Cdd:COG0444 223 V 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-232 |
1.08e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 14 SFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLS---AVYPHGTWEGEILWDGQPLKAQSIRETEAAgIVIIHQE 90
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrliELYPEARVSGEVYLDGQDIFKMDVIELRRR-VQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 91 LTLVPDLSVAENIFMGHELT-LPGGRMNYPAMLHRA---EALMRELKvpdMNVALPVSQYGGGYQQLVEIAKALNKQARL 166
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNrLVKSKKELQERVRWAlekAQLWDEVK---DRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 167 LILDEPSSAL---TRGEIEVLLDIIKglkaKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADM 232
Cdd:PRK14247 168 LLADEPTANLdpeNTAKIESLFLELK----KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
280-488 |
1.14e-17 |
|
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: 82.38 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGA-YPGRYNAEVwlegqvidtrtplksirAGLcmVPEDRKRQgIIPDL 358
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTSGEVRV-----------------AGL--VPWKRRKK-FLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GV--GQNITLA----VLDTY---AHMTRIDAEAELGSIDQ-----QISRMhLKTaspslPITSLSGGNQQKAVLAKMLMA 424
Cdd:cd03267 97 GVvfGQKTQLWwdlpVIDSFyllAAIYDLPPARFKKRLDElsellDLEEL-LDT-----PVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 425 KPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
280-484 |
1.27e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.01 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG--AYPGRYNAEVWLEGQVIDT--RTPLKSIRA-GLCMVPEDrKRQGI 354
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRIGGSATFNGREILNlpEKELNKLRAeQISMIFQD-PMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVGQNITlAVLDTYAHMTRIDAEAE----LGSIDQQISRMHLKTaspsLPiTSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:PRK09473 111 NPYMRVGEQLM-EVLMLHKGMSKAEAFEEsvrmLDAVKMPEARKRMKM----YP-HEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-226 |
1.34e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.62 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEIL----WDGQPLKAQSIRETEAAGIVIIHQEL 91
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdeWVDMTKPGPDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 92 TLVPDLSVAENIFMGHELTLPG--GRMNYPAMLHRA---EALMREL--KVPDmnvalpvsQYGGGYQQLVEIAKALNKQA 164
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDelARMKAVITLKMVgfdEEKAEEIldKYPD--------ELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 165 RLLILDEPSSAL---TRgeIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:TIGR03269 447 RIVILDEPTGTMdpiTK--VDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-222 |
1.55e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKvLSAVYPHGTwEGEILWDGQPLKAQSIRETE 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKPT-EGQIFIDGEDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 aagIVIIHQELTLVPDLSVAENIfmGHELTlpggrmnypaMLHRAEALMRElKVPDmnvALP-----------VSQYGGG 149
Cdd:PRK11432 80 ---ICMVFQSYALFPHMSLGENV--GYGLK----------MLGVPKEERKQ-RVKE---ALElvdlagfedryVDQISGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 150 YQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
259-505 |
1.59e-17 |
|
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: 82.05 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVT-CYDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNAEVWLEGQvidtrtplks 337
Cdd:COG1119 1 DPLLELRNVTvRRG----GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGE---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 iRAGLCMVPEDRKRQGII-PDLG--VGQNITL---------AVLDTYAHMTRIDAEAelgsIDQQISRM---HLKTAsps 402
Cdd:COG1119 67 -RRGGEDVWELRKRIGLVsPALQlrFPRDETVldvvlsgffDSIGLYREPTDEQRER----ARELLELLglaHLADR--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 403 lPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEG-VSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:COG1119 139 -PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLK 217
|
250 260
....*....|....*....|....
gi 1067238353 482 DGQLrgdfINDGLTQEQVLAAALS 505
Cdd:COG1119 218 DGRV----VAAGPKEEVLTSENLS 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.62e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFG-GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLkaqsirET 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS--GRILFDGKPI------DY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EAAGIVIIHQELTLV---PD-----LSVAENIFMGH-ELTLPGGRMNypamlHRAEALMRELKVPDMNVAlPVSQYGGGY 150
Cdd:PRK13636 73 SRKGLMKLRESVGMVfqdPDnqlfsASVYQDVSFGAvNLKLPEDEVR-----KRVDNALKRTGIEHLKDK-PTHCLSFGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 151 QQLVEIAKALNKQARLLILDEPSSAL-TRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLdPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-224 |
1.85e-17 |
|
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: 81.50 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKA---QSIREteaaGIVIIHQELT 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ--KGQILIDGIDIRDisrKSLRS----MIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDlSVAENIFMGHELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:cd03254 88 LFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 173 SSALTRGEIEVLLDIIKGLKaKGVACVYISHKLDEVAAVcDTIAVIRDGKHI 224
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNA-DKILVLDDGKII 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-222 |
1.94e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.36 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MP-DYLLQMNGIVKSFGG----VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKA-- 73
Cdd:PRK10584 1 MPaENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLHQmd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 74 -QSIRETEAAGIVIIHQELTLVPDLSVAENIfmgheltlpggrmNYPAMLH---------RAEALMRELKVPDMNVALPv 143
Cdd:PRK10584 79 eEARAKLRAKHVGFVFQSFMLIPTLNALENV-------------ELPALLRgessrqsrnGAKALLEQLGLGKRLDHLP- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 144 SQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKlDEVAAVCDTIAVIRDGK 222
Cdd:PRK10584 145 AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
280-485 |
1.97e-17 |
|
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: 81.03 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRYnaEVWLEGQVIDTRTPlksIRAGLCMVPEDRkrqGIIPDL 358
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSG--EILIDGRDVTGVPP---ERRNIGMVFQDY---ALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNI----TLAVLDTYAHMTRIDAEAELGSIDQQISRMhlktaspslpITSLSGGNQQKAVLAKMLMAKPKVLILDEP 434
Cdd:cd03259 88 TVAENIafglKLRGVPKAEIRARVRELLELVGLEGLLNRY----------PHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 435 TRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03259 158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-206 |
2.49e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWD----GQPLKAQSIRE-TE 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfSKTPSDKAIRElRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVIihQELTLVPDLSVAENIFmghELTLPGGRMNYPAMLHRAEALMRELKVPDMNVALPVsQYGGGYQQLVEIAKAL 160
Cdd:PRK11124 83 NVGMVF--QQYNLWPHLTVQQNLI---EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067238353 161 NKQARLLILDEPSSALTRgEIEV-LLDIIKGLKAKGVACVYISHKLD 206
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDP-EITAqIVSIIRELAETGITQVIVTHEVE 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
280-488 |
3.55e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.48 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQvidtrtPLKSIRAGlcMVPEDRKRQGII- 355
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERptsGQ----VLVNGQ------DLSRLKRR--EIPYLRRRIGVVf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 ------PDLGVGQNITLAVLDTYAHMTRIDAEaelgsIDQQISRMHLKTASPSLPITsLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:COG2884 86 qdfrllPDRTVYENVALPLRVTGKSRKEIRRR-----VREVLDLVGLSDKAKALPHE-LSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-225 |
3.68e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtwEGEILWDGQPLKAQSIRE-----------TEAAGIVIIHQ 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG---QGEILLNGRPLSDWSAAElarhraylsqqQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 ELTL-VPDLSVAEnifmgheltlpggrMNYPAMLHRAEALMRELKVPDmnvalPVSQYGGGYQQLVEIAKAL-------N 161
Cdd:COG4138 89 YLALhQPAGASSE--------------AVEQLLAQLAEALGLEDKLSR-----PLTQLSGGEWQRVRLAAVLlqvwptiN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 162 KQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:COG4138 150 PEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-225 |
7.27e-17 |
|
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: 79.56 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 18 VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDG---QPLKAQSIReteaAGIVIIHQELTLV 94
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT--SGSVLLDGtdiRQLDPADLR----RNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDlSVAENIFMGheltlpggrmnypAMLHRAEALMRELKVPDMNV---------ALPVSQYG----GGYQQLVEIAKALN 161
Cdd:cd03245 91 YG-TLRDNITLG-------------APLADDERILRAAELAGVTDfvnkhpnglDLQIGERGrglsGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 162 KQARLLILDEPSSALTRGEIEVLLDIIKGLKAkGVACVYISHKLdEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
262-485 |
1.47e-16 |
|
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: 78.76 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTCYDVDnpkRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPG-RYNAEVWLEGQVI-DTRTPLK 336
Cdd:cd03260 1 IELRDLNVYYGD---KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGaPDEGEVLLDGKDIyDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 SIRAGLCMVpedrkRQGIIP-DLGVGQNITLAV-LDTYAHMTRIDAEAElgsidQQISRMHLKT-ASPSLPITSLSGGNQ 413
Cdd:cd03260 78 ELRRRVGMV-----FQKPNPfPGSIYDNVAYGLrLHGIKLKEELDERVE-----EALRKAALWDeVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 414 QKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEgVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-484 |
1.53e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGryNAEVWLEGQVIDTRTPLKSIRAGLcmVPEdrkRQGIIPDL 358
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPD--AGSISLCGEPVPSRARHARQRVGV--VPQ---FDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNitLAVLDTYAHMTRIDAEAELGSIdQQISRMHLKTASPslpITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGV 438
Cdd:PRK13537 96 TVREN--LLVFGRYFGLSAAAARALVPPL-LEFAKLENKADAK---VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 439 DVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK13537 170 DPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
276-489 |
1.61e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 78.03 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynAEVWlegQVIDTRTPLKSIRAGlCMVpedrKRQ 352
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpdsGE--ITFD---GKSYQKNIEALRRIG-ALI----EAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 353 GIIPDLGVGQNitlavLDTYAHMTRIDAEAelgsIDQQISRMHLKtASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILD 432
Cdd:cd03268 82 GFYPNLTAREN-----LRLLARLLGIRKKR----IDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 433 EPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGDF 489
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-231 |
2.08e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.62 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 7 QMNGIVKSFGG----VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPHGtweGEILWDGQPLKAQSIRETEA 81
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTS---GRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 A--GIVIIHQELTLVPDLSVAENIFMGHELtlpggrmnypAMLHRAEALMRELKVPDMnVAL-------PvSQYGGGYQQ 152
Cdd:PRK11153 80 ArrQIGMIFQHFNLLSSRTVFDNVALPLEL----------AGTPKAEIKARVTELLEL-VGLsdkadryP-AQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 153 LVEIAKALNKQARLLILDEPSSAL----TRGEIEVLLDIIKGLkakGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTA 228
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALdpatTRSILELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
...
gi 1067238353 229 MAD 231
Cdd:PRK11153 225 VSE 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-274 |
2.56e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.76 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAvYPHGTwEGEILWDGQPLKAQSireTE 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETPD-SGRIMLDGQDITHVP---AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVIIHQELTLVPDLSVAENIFMGHELT-LPGGRMNYPAMlhraEALmRELKVPDMNVALPvSQYGGGYQQLVEIAKA 159
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFGLRMQkTPAAEITPRVM----EAL-RMVQLEEFAQRKP-HQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 160 LNKQARLLILDEPSSALT---RGEIEVLLdiiKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKhiattaMADMDIP 235
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDyklRKQMQNEL---KALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR------IEQDGTP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1067238353 236 RIITQmvgrEMSNLYPTEphDVGEV-IFEARNVTCYDVDN 274
Cdd:PRK09452 230 REIYE----EPKNLFVAR--FIGEInIFDATVIERLDEQR 263
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-226 |
3.41e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILW---DGQPLKAQSIRETE- 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA--GEVHYrmrDGQLRDLYALSEAEr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 ------AAGIVIIHQELTLVPDLSVAENIfmGHELTLPGGRmNYPAMlhRAEAL--MRELKVPDMNVALPVSQYGGGYQQ 152
Cdd:PRK11701 84 rrllrtEWGFVHQHPRDGLRMQVSAGGNI--GERLMAVGAR-HYGDI--RATAGdwLERVEIDAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 153 LVEIAKALNKQARLLILDEPSSALtrgEIEV---LLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGL---DVSVqarLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
280-483 |
5.06e-16 |
|
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: 77.51 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGryNAEVWLEGQVIDTRTPlksiraglcmvpeDR----KRQGI 354
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPT--SGGVILEGKQITEPGP-------------DRmvvfQNYSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVGQNITLAVLDTYAHMTRIDAEAelgSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDEP 434
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKSERRA---IVEEHIALVGLTEAADKRP-GQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 435 TRGVDVGAKYEIY-KLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:TIGR01184 142 FGALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
262-488 |
5.44e-16 |
|
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: 76.86 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTcYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRynAEVWLEGqvIDTRT-PLKSIR 339
Cdd:cd03245 3 IEFRNVS-FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTS--GSVLLDG--TDIRQlDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 AGLCMVPEDrkrqgiiPDLGVG---QNITLAvlDTYAHMTRIDAEAELGSIDQQISRmHLKtaSPSLPI----TSLSGGN 412
Cdd:cd03245 78 RNIGYVPQD-------VTLFYGtlrDNITLG--APLADDERILRAAELAGVTDFVNK-HPN--GLDLQIgergRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 413 QQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAeVLGVSNRVLVIGDGQLRGD 488
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-222 |
6.47e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.48 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 10 GIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPH-GTWE-GEILWDG-QPLKAQS--IRE-TEAA 82
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeQPEaGTIRvGDITIDTaRSLSQQKglIRQlRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIihQELTLVPDLSVAENIFMGHELTLPGGRmnyPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNK 162
Cdd:PRK11264 88 GFVF--QNFNLFPHRTVLENIIEGPVIVKGEPK---EEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 163 QARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
275-486 |
7.50e-16 |
|
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: 76.46 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 275 PKRKRVDDISFVLRRGeILGIAGLVGAGRTELVSALFGAYPGRYNAeVWLEGQviDTRTPLKSIRAGLCMVPEDrkrQGI 354
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGT-IRIDGQ--DVLKQPQKLRRRIGYLPQE---FGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVgqnitLAVLDTYAHMTRIDAEAELGSIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEP 434
Cdd:cd03264 84 YPNFTV-----REFLDYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 435 TRGVDVGAKYEIYKLMGALAAEgvSIIMVSSELAE-VLGVSNRVLVIGDGQLR 486
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-238 |
1.10e-15 |
|
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: 75.64 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGIVIIHQELTLVP 95
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAEnifmgheltlpggrmnypamlhraeaLMRelkvpDMNVALpvsqyGGGYQQLVEIAKALNKQARLLILDEPSSA 175
Cdd:cd03217 91 GVKNAD--------------------------FLR-----YVNEGF-----SGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 176 LTRGEIEVLLDIIKGLKAKGVACVYISHK---LDEVAAvcDTIAVIRDGKHIATtamADMDIPRII 238
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIKP--DRVHVLYDGRIVKS---GDKELALEI 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-223 |
1.23e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 76.37 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLkAQSIRETEAAGIVIIHQELTLVpDLSV 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV--PENGRVLVDGHDL-ALADPAWLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 100 AENIFMGHElTLPGGRMNYPAMLHRAEALMRELK------VPDMNVALpvsqyGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:cd03252 93 RDNIALADP-GMSMERVIEAAKLAGAHDFISELPegydtiVGEQGAGL-----SGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 174 SALtrgEIEVLLDIIKGLKA--KGVACVYISHKLDEVAA-----VCDTIAVIRDGKH 223
Cdd:cd03252 167 SAL---DYESEHAIMRNMHDicAGRTVIIIAHRLSTVKNadriiVMEKGRIVEQGSH 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-222 |
1.57e-15 |
|
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: 76.11 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYphGTWEGEILWDGQPLKA---QSIRETeaagIVIIHQELTLVPDl 97
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY--DVSSGSILIDGQDIREvtlDSLRRA----IGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SVAENIFMGheltlpggrmNYPAMLHRAEALMRELKVPDMNVALP------VSQYG----GGYQQLVEIAKALNKQARLL 167
Cdd:cd03253 90 TIGYNIRYG----------RPDATDEEVIEAAKAAQIHDKIMRFPdgydtiVGERGlklsGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 168 ILDEPSSAL-TRGEIEVLLDIIKGLKAKGVacVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:cd03253 160 LLDEATSALdTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-222 |
1.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDG----QPLKAQSIRETeaAGIVIIHQEL 91
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ---KGKVLVSGidtgDFSKLQGIRKL--VGIVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 92 TLVpDLSVAENIFMGHE-LTLPGGRMNypamlHRAEALMRELKVPDMNVALPVSqYGGGYQQLVEIAKALNKQARLLILD 170
Cdd:PRK13644 89 QFV-GRTVEEDLAFGPEnLCLPPIEIR-----KRVDRALAEIGLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 171 EPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVcDTIAVIRDGK 222
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGK 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-225 |
1.86e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF----GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVL-------SAVYPHGTWEGEILwDGQPLkA 73
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVATL-DADAL-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 74 QSIRETEAagivIIHQELTLVPDLSVAEN-----IFMGHELTlpggrmnypAMLHRAEALMRELKVPDmNVALPVSQYGG 148
Cdd:PRK10535 82 QLRREHFG----FIFQRYHLLSHLTAAQNvevpaVYAGLERK---------QRLLRAQELLQRLGLED-RVEYQPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 149 GYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKlDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
261-486 |
1.94e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.07 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVTcydvdnpkrKR------VDDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGrynaEVWLEGQVIDt 331
Cdd:COG4152 1 MLELKGLT---------KRfgdktaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilaPDSG----EVLWDGEPLD- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 332 rtplKSIRAGLCMVPEDRkrqGIIPDLGVGQNIT-LAVLdtyAHMTRIDAEAElgsIDQQISRMHLKTASPSlPITSLSG 410
Cdd:COG4152 67 ----PEDRRRIGYLPEER---GLYPKMKVGEQLVyLARL---KGLSKAEAKRR---ADEWLERLGLGDRANK-KVEELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 411 GNQQKAVLAKMLMAKPKVLILDEPTRGVD-VGAKyEIYKLMGALAAEGVSIIMvSS---ELAEVLgvSNRVLVIGDGQLR 486
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDpVNVE-LLKDVIRELAAKGTTVIF-SShqmELVEEL--CDRIVIINKGRKV 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-222 |
2.35e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 13 KSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQ---PLkaqsireteaagiviih 88
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILePT---SGRVEVNGRvsaLL----------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 89 qELT--LVPDLSVAENIFMgheltlpGGRMnypaM-LHRAEalMRElKVPDMnVA---------LPVSQYGGGYQQLVEI 156
Cdd:COG1134 94 -ELGagFHPELTGRENIYL-------NGRL----LgLSRKE--IDE-KFDEI-VEfaelgdfidQPVKTYSSGMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 157 AKALNKQARLLILDepssaltrgeiEVL-----------LDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG1134 158 AVATAVDPDILLVD-----------EVLavgdaafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-222 |
3.30e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.00 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 25 DIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHGtweGEILWDGQPLKAQSIRETEaagIVIIHQELTLVPDLSVAENI 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPAS---GSLTLNGQDHTTTPPSRRP---VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 104 FMG-HeltlPGGRMNyPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSALT---RG 179
Cdd:PRK10771 93 GLGlN----PGLKLN-AAQREKLHAIARQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1067238353 180 EIEVLLDIIkgLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK10771 167 EMLTLVSQV--CQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-225 |
3.93e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.82 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAAgIVIIHQEltlvPD--- 96
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGMVLSEETVWDVRRQ-VGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 --LSVAENIFMGheltLPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSS 174
Cdd:PRK13635 95 vgATVQDDVAFG----LENIGVPREEMVERVDQALRQVGMEDFLNREP-HRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 175 ALT-RGEIEVlLDIIKGLKAKGVACVY-ISHKLDEvAAVCDTIAVIRDGKHIA 225
Cdd:PRK13635 170 MLDpRGRREV-LETVRQLKEQKGITVLsITHDLDE-AAQADRVIVMNKGEILE 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
259-488 |
4.08e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 74.69 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVT-CYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRT---ELVSALFGAYPGrynaEVWLEGQVIDTRTP 334
Cdd:COG1136 2 SPLLELRNLTkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLDRPTSG----EVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 335 --LKSIRaglcmvpedRKRQGII-------PDLGVGQNITLAVLdtYAHMTRIDAEAElgsIDQQISRMHLKTASPSLPi 405
Cdd:COG1136 78 reLARLR---------RRHIGFVfqffnllPELTALENVALPLL--LAGVSRKERRER---ARELLERVGLGDRLDHRP- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELaEVLGVSNRVLVIGDGQ 484
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
....
gi 1067238353 485 LRGD 488
Cdd:COG1136 222 IVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
263-485 |
4.18e-15 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 74.45 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGrynaEVWLEGQVID--TRTPLK 336
Cdd:cd03255 2 ELKNLSkTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldrPTSG----EVRVDGTDISklSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 SIRaglcmvpedRKRQGII-------PDLGVGQNITLAVLdtYAHMTRIDAEAELGSIdqqISRMHLKTASPSLPiTSLS 409
Cdd:cd03255 78 AFR---------RRHIGFVfqsfnllPDLTALENVELPLL--LAGVPKKERRERAEEL---LERVGLGDRLNHYP-SELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 410 GGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVS--SELAEvlgVSNRVLVIGDGQL 485
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVThdPELAE---YADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
263-481 |
4.23e-15 |
|
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: 74.43 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRynaevwlEGQVIDTRTPLKSIRAG 341
Cdd:cd03293 2 EVRNVSkTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-------SGEVLVDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 LCMVPEDrkrQGIIPDLGVGQNITLAVLdtyahMTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKM 421
Cdd:cd03293 75 RGYVFQQ---DALLPWLTVLDNVALGLE-----LQGVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 422 LMAKPKVLILDEPTRGVDVGAKYEIYK-LMGALAAEGVSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-225 |
4.25e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLkaqsirETEAAGIVIIHQELTLV---PD 96
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ---KGAVLWQGKPL------DYSKRGLLALRQQVATVfqdPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 lsvaENIFmgheltlpggrmnYPAMLHRAEALMRELKVPDMNVA-----------------LPVSQYGGGYQQLVEIAKA 159
Cdd:PRK13638 88 ----QQIF-------------YTDIDSDIAFSLRNLGVPEAEITrrvdealtlvdaqhfrhQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 160 LNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-483 |
6.04e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRYNAEVWleGQVIDTRTplKSIRAGLCMVPE-DRkrqgIIPD 357
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGmTSPDAGKITVL--GVPVPARA--RLARARIGVVPQfDN----LDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 358 LGVGQNitLAVLDTYAHMTRIDAEAELGSIdQQISRMHLKTaspSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRG 437
Cdd:PRK13536 129 FTVREN--LLVFGRYFGMSTREIEAVIPSL-LEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 438 VDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
283-484 |
6.08e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 283 ISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGRynaeVWLEGQVIdTRTPlksiraglcmvPEDRK------RQG 353
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGflpPDSGR----ILWNGQDL-TALP-----------PAERPvsmlfqENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 354 IIPDLGVGQNITLAvLDTYAHMTRIDAEAelgsIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDE 433
Cdd:COG3840 82 LFPHLTVAQNIGLG-LRPGLKLTAEQRAQ----VEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 434 PTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-222 |
7.95e-15 |
|
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: 73.68 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKA---QSIRETeaagIVIIHQELT 92
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE--LSSGSILIDGVDISKiglHDLRSR----ISIIPQDPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDlSVAENIFMGHELTlpggrmnyPAMLHRA--EALMREL--KVP---DMNVALPVSQYGGGYQQLVEIAKALNKQAR 165
Cdd:cd03244 89 LFSG-TIRSNLDPFGEYS--------DEELWQAleRVGLKEFveSLPgglDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 166 LLILDEPSSALTRGEIEVLLDIIKGlKAKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
263-484 |
8.48e-15 |
|
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: 72.42 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYDvdNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGQVIDTrTPLKSIRag 341
Cdd:cd03228 2 EFKNVSfSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-TSGEILIDGVDLRD-LDLESLR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 lcmvpedrKRQGIIPdlgvgQNITLavLDtyahmtridaeaelGSIDQQIsrmhlktaspslpitsLSGGNQQKAVLAKM 421
Cdd:cd03228 76 --------KNIAYVP-----QDPFL--FS--------------GTIRENI----------------LSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 422 LMAKPKVLILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGVsNRVLVIGDGQ 484
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-243 |
8.56e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLS-----AVYPHG-TWEGEILWDGQPLKAQSIRETEAAGIVIIHQELTLV 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgGGAPRGaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PdLSVAENIFMGHeltLPGGRMNYPAMLHRAEALMRELKVPDMN--VALPVSQYGGGYQQLVEIAKALNK---------Q 163
Cdd:PRK13547 97 A-FSAREIVLLGR---YPHARRAGALTHRDGEIAWQALALAGATalVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQMV 242
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
.
gi 1067238353 243 G 243
Cdd:PRK13547 253 G 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
278-480 |
9.06e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 278 KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNAEVWLEGQVID-TRTPLKSIRAGLCMVPEDrKRQGIIP 356
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQD-PLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITLAVLDTYAHMTRidaeaelGSIDQQISRMHLKTA-SPSL----PiTSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:PRK15079 114 RMTIGEIIAEPLRTYHPKLSR-------QEVKDRVKAMMLKVGlLPNLinryP-HEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVI 480
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-222 |
9.24e-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: 73.66 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLlqmNGIVK----SFG-----GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPL 71
Cdd:cd03248 4 APDHL---KGIVKfqnvTFAyptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ--PQGGQVLLDGKPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 72 KAQSIRETEAAgIVIIHQELTLVPDlSVAENIFMGHElTLPGGRMNYPAMLHRAEALMREL-KVPDMNVALPVSQYGGGY 150
Cdd:cd03248 79 SQYEHKYLHSK-VSLVGQEPVLFAR-SLQDNIAYGLQ-SCSFECVKEAAQKAHAHSFISELaSGYDTEVGEKGSQLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 151 QQLVEIAKALNKQARLLILDEPSSAL-TRGEIEVLLDIIKGLKAKGVacVYISHKLDEVAAVcDTIAVIRDGK 222
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALdAESEQQVQQALYDWPERRTV--LVIAHRLSTVERA-DQILVLDGGR 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-258 |
9.98e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 2 PDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSiRETEA 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLESWS-SKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 AGIVIIHQELTLVPDLSVAENIFMgheltlpgGRMNYPAMLHRAEALMRElKVPDMnVAL----P-----VSQYGGGYQQ 152
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRELVAI--------GRYPWHGALGRFGAADRE-KVEEA-ISLvglkPlahrlVDSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 153 LVEIAKALNKQARLLILDEPSSALTRG-EIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMAD 231
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAhQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
250 260
....*....|....*....|....*..
gi 1067238353 232 MDIPRIITQMVGREMSNLyptePHDVG 258
Cdd:PRK10575 235 LMRGETLEQIYGIPMGIL----PHPAG 257
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
1.09e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.26 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 19 NALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQSIRETEAAgIVIIHQEltlvPD- 96
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQ---SGEIKIDGITISKENLKEIRKK-IGIIFQN----PDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 ----LSVAENIFMGHE-LTLPGGRM-----NYPAMLHRAEALMRElkvpdmnvalpvSQY-GGGYQQLVEIAKALNKQAR 165
Cdd:PRK13632 95 qfigATVEDDIAFGLEnKKVPPKKMkdiidDLAKKVGMEDYLDKE------------PQNlSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 166 LLILDEPSSALT-RGEIEVlLDIIKGLKAKGVACVY-ISHKLDEvAAVCDTIAVIRDGKHIAT 226
Cdd:PRK13632 163 IIIFDESTSMLDpKGKREI-KKIMVDLRKTRKKTLIsITHDMDE-AILADKVIVFSEGKLIAQ 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-225 |
1.35e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 14 SFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETeAAGIVIIHQELTL 93
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQSGTVFLGDKPISMLSSRQL-ARRLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 94 VPDLSVAENIFMGHE--LTLpGGRMNyPAMLHRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIAKALNKQARLLILDE 171
Cdd:PRK11231 88 PEGITVRELVAYGRSpwLSL-WGRLS-AEDNARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 172 PSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-222 |
1.42e-14 |
|
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: 70.94 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAvyphgtwegeilwdgqplkaqsiRETEAAGIV 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-----------------------ELEPDEGIV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IIHQELTlvpdlsvaenifMGHeltlpggrmnypamlhraealmrelkvpdmnvalpVSQYGGGYQQLVEIAKALNKQAR 165
Cdd:cd03221 58 TWGSTVK------------IGY-----------------------------------FEQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 166 LLILDEPSSALTRGEIEVLldiIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03221 91 LLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-225 |
1.44e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.14 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 18 VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YP-HGTWE--GEILWDGQPLKAQSIReteaagiVIIHQELTL 93
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPtSGEVRvaGLVPWKRRKKFLRRIG-------VVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 94 VPDLSVAENIFMGHEL-TLPGGRmnYPAMLHRAEALM---RELKVPDMNVALpvsqyggGYQQLVEIAKALNKQARLLIL 169
Cdd:cd03267 107 WWDLPVIDSFYLLAAIyDLPPAR--FKKRLDELSELLdleELLDTPVRQLSL-------GQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 170 DEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
254-502 |
1.50e-14 |
|
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: 76.41 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 254 PHDVGEVIFEarNVTC-YDVDNPKRkrVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGqvI 329
Cdd:COG2274 468 PRLKGDIELE--NVSFrYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEptsGR----ILIDG--I 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 330 DTRT-PLKSIRAGLCMVPEDrkrqgiiPDLGVG---QNITLAvlDTYAHMTRIDAEAELGSIDQQISRMH--LKTaspsl 403
Cdd:COG2274 538 DLRQiDPASLRRQIGVVLQD-------VFLFSGtirENITLG--DPDATDEEIIEAARLAGLHDFIEALPmgYDT----- 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PI----TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAeVLGVSNRVLV 479
Cdd:COG2274 604 VVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS-TIRLADRIIV 681
|
250 260
....*....|....*....|...
gi 1067238353 480 IGDGQLrgdfINDGlTQEQVLAA 502
Cdd:COG2274 682 LDKGRI----VEDG-THEELLAR 699
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
260-485 |
1.52e-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: 72.20 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 260 VIFEARNVTCY---DVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRYNAEVWLEGqvidTRTPL 335
Cdd:cd03213 2 VTLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVLING----RPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 336 KSIRAGLCMVPEDrkrQGIIPDLGVGQNITLAVldtyahmtridaeaelgsidqqisrmHLKtaspslpitSLSGGNQQK 415
Cdd:cd03213 78 RSFRKIIGYVPQD---DILHPTLTVRETLMFAA--------------------------KLR---------GLSGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 416 AVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSEL-AEVLGVSNRVLVIGDGQL 485
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-222 |
1.57e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEaAGIV 85
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT--SGHIRFHGTDVSRLHARDRK-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 86 IihQELTLVPDLSVAENIFMGheLT-LP-GGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQ 163
Cdd:PRK10851 80 F--QHYALFRHMTVFDNIAFG--LTvLPrRERPNAAAIKAKVTQLLEMVQLAHLADRYP-AQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 164 ARLLILDEPSSAL---TRGEIEVLL-DIIKGLKAKGvacVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK10851 155 PQILLLDEPFGALdaqVRKELRRWLrQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-222 |
1.72e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.38 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKS----TLMKVLSAvypHGTWEGEILWDGQP---LKAQSIRETEAAGIVIIH 88
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA---NGRIGGSATFNGREilnLPEKELNKLRAEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 89 QE--LTLVPDLSVAENIFmghELTlpggrmnypaMLHR----AEALMRELKVPDMnVALPVS---------QYGGGYQQL 153
Cdd:PRK09473 104 QDpmTSLNPYMRVGEQLM---EVL----------MLHKgmskAEAFEESVRMLDA-VKMPEArkrmkmyphEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 154 VEIAKALNKQARLLILDEPSSAL---TRGEIEVLLDIIKglKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALdvtVQAQIMTLLNELK--REFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
277-485 |
2.85e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.62 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDrkrQGIIP 356
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNItLAVLDTYAHMTridAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:PRK10895 92 RLSVYDNL-MAVLQIRDDLS---AEQREDRANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067238353 437 GVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-222 |
3.44e-14 |
|
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: 71.88 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPL---KAQSIRETeaagIVIIHQELTL 93
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD--SGRILIDGHDVrdyTLASLRRQ----IGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 94 VPDlSVAENIFMG-----HELTLPGGRMnypAMLHraEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLI 168
Cdd:cd03251 88 FND-TVAENIAYGrpgatREEVEEAARA---ANAH--EFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 169 LDEPSSAL-TRGEiEVLLDIIKGLKAKGVACVyISHKLDEVAAVcDTIAVIRDGK 222
Cdd:cd03251 162 LDEATSALdTESE-RLVQAALERLMKNRTTFV-IAHRLSTIENA-DRIVVLEDGK 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
277-499 |
3.95e-14 |
|
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: 71.83 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTP--LKSIRAGLCMVPEDrkrQGI 354
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGSVLIDGTDINKLKGkaLRQLRRQIGMIFQQ---FNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVGQNI---TLAVLDTYAHM----TRIDAEAELGSIDQ-QISRMHLKTASpslpitSLSGGNQQKAVLAKMLMAKP 426
Cdd:cd03256 90 IERLSVLENVlsgRLGRRSTWRSLfglfPKEEKQRALAALERvGLLDKAYQRAD------QLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRGDFINDGLTQEQV 499
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
281-485 |
5.79e-14 |
|
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: 71.55 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIDT--RTPLKSIRaglcmvpedrKRQGI- 354
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsGE----ILVDGQDITGlsEKELYELR----------RRIGMl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 ------IPDLGVGQNITLAvLDTYAHMTR--IDAEAELgsidqQISRMHLKTASPSLPiTSLSGGnQQKAV-LAKMLMAK 425
Cdd:COG1127 88 fqggalFDSLTVFENVAFP-LREHTDLSEaeIRELVLE-----KLELVGLPGAADKMP-SELSGG-MRKRVaLARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 426 PKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
280-482 |
5.89e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.97 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNA--EVWLEGQVIDTrtplksiraglcmVPEDRKRQGII-- 355
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAsgEVLLNGRRLTA-------------LPAEQRRIGILfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 -----PDLGVGQNITLAVLDTYAHMTRID-AEAELgsidQQISRMHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:COG4136 84 ddllfPHLSVGENLAFALPPTIGRAQRRArVEQAL----EEAGLAGFADRDPA----TLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLM-GALAAEGVSIIMVSSELAEVLGVSnRVLVIGD 482
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
281-485 |
6.00e-14 |
|
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: 70.90 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRynAEVWLEGQVI----DTRTPLksIRAGLCMVPEDRKrqgII 355
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTS--GTIRVNGQDVsdlrGRAIPY--LRRKIGVVFQDFR---LL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 PDLGVGQNITLAVLDTYAhmTRIDAEAELGSIDQQISRMHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:cd03292 91 PDRNVYENVAFALEVTGV--PPREIRKRVPAALELVGLSHKHRALPA----ELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 436 RGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-222 |
6.26e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.80 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 10 GIVKSF----GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVyphgtwE----GEILWDGQPLKAQSIRETEA 81
Cdd:COG1135 6 NLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL------ErptsGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 A--GIVIIHQELTLVPDLSVAENIfmghELTLPGGRMNYPAMLHRAEALMrELkvpdmnVAL-------PvSQYGGGYQQ 152
Cdd:COG1135 80 ArrKIGMIFQHFNLLSSRTVAENV----ALPLEIAGVPKAEIRKRVAELL-EL------VGLsdkadayP-SQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 153 LVEIAKALNKQARLLILDEPSSAL---TRGEI-EVLLDIIKGLkakGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALdpeTTRSIlDLLKDINREL---GLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-226 |
9.57e-14 |
|
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: 70.21 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 25 DIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQsirETEAAGIVIIHQELTLVPDLSVAENIF 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLINGVDVTAA---PPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 105 MGHEltlPGGRMNyPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVL 184
Cdd:cd03298 93 LGLS---PGLKLT-AEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1067238353 185 LDIIKGLKA-KGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:cd03298 168 LDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
276-478 |
1.04e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRYNAEVWLE-GQV-----IDTRTPLKSIRagLCMVP 346
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApdeGVIKRNGKLRiGYVpqklyLDTTLPLTVNR--FLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 347 EDRKRQGIIPDLgvgqnitlavldtyahmTRIDAEaelgsidqqisrmHLKTAspslPITSLSGGNQQKAVLAKMLMAKP 426
Cdd:PRK09544 94 PGTKKEDILPAL-----------------KRVQAG-------------HLIDA----PMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVL 478
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-207 |
1.12e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.88 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIREteaaGI 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGPGAER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIihQELTLVPDLSVAENIFMGheLTLPGgrMNYPAMLHRAEALMRELKVPDMNvALPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:PRK11248 75 VF--QNEGLLPWRNVQDNVAFG--LQLAG--VEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 165 RLLILDEPSSAL---TRGEIEVLLDIIKGLKAKGVacVYISHKLDE 207
Cdd:PRK11248 148 QLLLLDEPFGALdafTREQMQTLLLKLWQETGKQV--LLITHDIEE 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-225 |
1.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.98 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHGTWEGEILWDGQPLKAQSIRET-EAAGIVIIHQELTLVpDL 97
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPNSKITVDGITLTAKTVWDIrEKVGIVFQNPDNQFV-GA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SVAENIFMGheltLPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSALT 177
Cdd:PRK13640 101 TVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067238353 178 RGEIEVLLDIIKGL-KAKGVACVYISHKLDEvAAVCDTIAVIRDGKHIA 225
Cdd:PRK13640 176 PAGKEQILKLIRKLkKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLA 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
263-485 |
1.75e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 72.87 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTcydVDNPKRKRV-DDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrYNAEVWLEGQVIDTRTPlKSIRAG 341
Cdd:COG4988 338 ELEDVS---FSYPGGRPAlDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSILINGVDLSDLDP-ASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 LCMVPEdrkrQGIIPDLGVGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMH--LKTaspslPITS----LSGGNQQK 415
Cdd:COG4988 413 IAWVPQ----NPYLFAGTIRENLRLGRPD--ASDEELEAALEAAGLDEFVAALPdgLDT-----PLGEggrgLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 416 AVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAeVLGVSNRVLVIGDGQL 485
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
251-484 |
1.76e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 251 PTEPHDVGEV-IFEARNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPG--RYNAEVWLEGQ 327
Cdd:TIGR00955 11 FGRVAQDGSWkQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 328 VIDtrtpLKSIRAGLCMVPEDrkrqgiipDLGVGqniTLAVLDTY---AHM---TRIDAEAELGSIDQQISRMHLKTASP 401
Cdd:TIGR00955 91 PID----AKEMRAISAYVQQD--------DLFIP---TLTVREHLmfqAHLrmpRRVTKKEKRERVDEVLQALGLRKCAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 402 SL-----PITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMV----SSELAEVLg 472
Cdd:TIGR00955 156 TRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF- 234
|
250
....*....|..
gi 1067238353 473 vsNRVLVIGDGQ 484
Cdd:TIGR00955 235 --DKIILMAEGR 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
283-485 |
1.85e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 283 ISFVLRRGEILGIAGLVGAGRTELVSALFGAyPGRYNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDRKrqgIIPDLGVGQ 362
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 363 NITLA--VLDTYAHMTRIDAEAELgsidqqISRMHLKTASPSlpiTSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDV 440
Cdd:PRK11614 100 NLAMGgfFAERDQFQERIKWVYEL------FPRLHERRIQRA---GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067238353 441 GAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
277-500 |
1.88e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.34 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG---------AYPGRynaevwlEGQVIDTRTPLKSIRAGLC---- 343
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArlapdagevHYRMR-------DGQLRDLYALSEAERRRLLrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 344 -MVPEDrKRQGIIPDLGVGQNITLAVLDTYA-HMTRIDAEAE--LGSIDQQISRMHlktaspSLPiTSLSGGNQQKAVLA 419
Cdd:PRK11701 92 gFVHQH-PRDGLRMQVSAGGNIGERLMAVGArHYGDIRATAGdwLERVEIDAARID------DLP-TTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 420 KMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLrgdfINDGLTqEQ 498
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV----VESGLT-DQ 238
|
..
gi 1067238353 499 VL 500
Cdd:PRK11701 239 VL 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-221 |
2.23e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.12 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVN--ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLsavyphgTWEGEILWDGQPLKAQSIreteAA 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGDATVAGKSI----LT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIIHQELTLVPDLSVAENIFMGHE-LTLPGGRMNYPamlhrAEALMRELKVPDMNVALPV------SQYGGGYQQLVE 155
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGREhLYLYARLRGVP-----AEEIEKVANWSIQSLGLSLyadrlaGTYSGGNKRKLS 2080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDG 221
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-215 |
2.31e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.36 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMK-VLSAVYPHgtwEGEILWDGQPLKAQSiRETEAAG 83
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKiVASLISPT---SGTLLFEGEDISTLK-PEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVPDlSVAENIFMGHELtlpggRMNYPAMLHRAEALMReLKVPDMNVALPVSQYGGGYQQLVEIAKALNKQ 163
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPWQI-----RNQQPDPAIFLDDLER-FALPDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 164 ARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTI 215
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVI 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-232 |
2.44e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 71.29 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 24 IDIKVKPGECVGLCGENGAGKSTLMKVLSavyphGTW---EGEILWDGQPL--KAQSI-RETEAAGIVIIHQELTLVPDL 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIA-----GLErpdSGRIRLGGEVLqdSARGIfLPPHRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SVAENIFMGHeltlpggrmnypamlHRAEALMRELKVPDMnVAL---------PVSQYGGGYQQLVEIAKALNKQARLLI 168
Cdd:COG4148 93 SVRGNLLYGR---------------KRAPRAERRISFDEV-VELlgighlldrRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 169 LDEPSSAL---TRGEIevlLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADM 232
Cdd:COG4148 157 MDEPLAALdlaRKAEI---LPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
263-497 |
2.70e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYDVDNPKR-KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRYNAEVWLEGQVIDTRTPL---- 335
Cdd:PRK13651 4 KVKNIVkIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlLLPDTGTIEWIFKDEKNKKKTKEkekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 336 -------KSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLDTYA----HMTRIDAEAElgsidqQISRMHLKTASpsLP 404
Cdd:PRK13651 84 leklviqKTRFKKIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIfgpvSMGVSKEEAK------KRAAKYIELVG--LD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 405 IT-------SLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD-VGAKyEIYKLMGALAAEGVSIIMVSSELAEVLGVSNR 476
Cdd:PRK13651 156 ESylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVK-EILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
250 260
....*....|....*....|.
gi 1067238353 477 VLVIGDGQLrgdfINDGLTQE 497
Cdd:PRK13651 235 TIFFKDGKI----IKDGDTYD 251
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-222 |
2.90e-13 |
|
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: 69.10 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQ---PLKAqsireteA 81
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP--PDSGTVTVRGRvssLLGL-------G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 AGiviihqeltLVPDLSVAENI-FMGHELTLPGGRMnyPAMLHRAEALmRELKvPDMNvaLPVSQYGGGYQQLVEIAKAL 160
Cdd:cd03220 93 GG---------FNPELTGRENIyLNGRLLGLSRKEI--DEKIDEIIEF-SELG-DFID--LPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 161 NKQARLLILDEpssALTRGEI---EVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:cd03220 158 ALEPDILLIDE---VLAVGDAafqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-203 |
4.33e-13 |
|
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: 68.29 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQsiRETEAAGIVIIHQELTLVP 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL--AGRVLLNGGPLDFQ--RDSIARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIFMGHELtlpggrmnypamlHRAEALMRELKvpDMNVA----LPVSQYGGGYQQLVEIAKALNKQARLLILDE 171
Cdd:cd03231 87 TLSVLENLRFWHAD-------------HSDEQVEEALA--RVGLNgfedRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 1067238353 172 PSSALTRGEIEVLLDIIKGLKAKGVACVYISH 203
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
257-485 |
4.41e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 257 VGEVIFEARNVTC-YDVDNPKR-KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRY----------NAEVWL 324
Cdd:PRK13631 17 SDDIILRVKNLYCvFDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYgtiqvgdiyiGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 325 EGQVIDTRTP----LKSIRAGLCMV---PEDRK-RQGIIPDLGVGQnITLAVldtyahmTRIDAeAELGSIdqQISRMHL 396
Cdd:PRK13631 97 HELITNPYSKkiknFKELRRRVSMVfqfPEYQLfKDTIEKDIMFGP-VALGV-------KKSEA-KKLAKF--YLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 397 KTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNR 476
Cdd:PRK13631 166 DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADE 245
|
....*....
gi 1067238353 477 VLVIGDGQL 485
Cdd:PRK13631 246 VIVMDKGKI 254
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
279-485 |
4.64e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 279 RVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGryNAEVWLEGQVIDTRTP--LKSIRAGLCmvpedrKRQGIIP 356
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEAWSAaeLARHRAYLS------QQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITL---AVLDTYAHMTRIDAEAELGSIDQQISRmhlktaspslPITSLSGGNQQKAVLAKMLM-----AKP-- 426
Cdd:PRK03695 83 AMPVFQYLTLhqpDKTRTEAVASALNEVAEALGLDDKLGR----------SVNQLSGGEWQRVRLAAVVLqvwpdINPag 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-176 |
4.76e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.28 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLS-AVYPHGTWEGEILWDGQPLKAqsiRETEAAGIVIIHQELTLVPDLSV 99
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAFSASGEVLLNGRRLTA---LPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 100 AENIFMGheltLPGGrMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:COG4136 94 GENLAFA----LPPT-IGRAQRRARVEQALEEAGLAGFADRDP-ATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
280-485 |
4.85e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 69.06 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRynAEVWLEGQVIDT--RTPLKSIRAGLCMVPEDRKrQGIIP 356
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKPAQ--GTVSFRGQDLYQldRKQRRAFRRDVQLVFQDSP-SAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITlavlDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:TIGR02769 104 RMTVRQIIG----EPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 437 GVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
277-484 |
7.88e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVI-DTRTPLKSIRAGLCMV---PEDRK-R 351
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-SGKIIIDGVDItDKKVKLSDIRKKVGLVfqyPEYQLfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 QGIIPDLGVG-QNITLAVLDTYahmTRIDAEAELGSIDQQIsrmhLKTASPslpiTSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:PRK13637 99 ETIEKDIAFGpINLGLSEEEIE---NRVKRAMNIVGLDYED----YKDKSP----FELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-232 |
8.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 18 VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEILWDGQPLKAQSIRE-TEAAGIVIIHQELTLVpD 96
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--FEGKVKIDGELLTAENVWNlRRKIGMVFQNPDNQFV-G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFMGHEltlpGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:PRK13642 97 ATVEDDVAFGME----NQGIPREEMIKRVDEALLAVNMLDFKTREP-ARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 177 TRGEIEVLLDIIKGLKAK-GVACVYISHKLDEvAAVCDTIAVIRDGKHIATTAMADM 232
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyQLTVLSITHDLDE-AASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-218 |
8.78e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETEAA--GIVIIHQE--LTLVP 95
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIfmGHELtlpggRMNYPAMlhRAEALMRELKVPDMNVAL-P--VSQY----GGGYQQLVEIAKALNKQARLLI 168
Cdd:PRK15079 114 RMTIGEII--AEPL-----RTYHPKL--SRQEVKDRVKAMMLKVGLlPnlINRYphefSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 169 LDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVI 218
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-237 |
1.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.57 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQS---IRETEAAGIVIIHQELT 92
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPT---SGEVLIKGEPIKYDKkslLEVRKTVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDlSVAENIFMGH-ELTLPggrmnypaMLHRAEALMRELKVPDMN--VALPVSQYGGGYQQLVEIAKALNKQARLLIL 169
Cdd:PRK13639 91 LFAP-TVEEDVAFGPlNLGLS--------KEEVEKRVKEALKAVGMEgfENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 170 DEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA------------TTAMADMDIPRI 237
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKegtpkevfsdieTIRKANLRLPRV 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-222 |
1.07e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWdGQPLK----AQs 75
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePD---SGTVKL-GETVKigyfDQ- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 76 ireteaagiviiHQElTLVPDLSVAENIF----MGHELTLPG--GRMNYPamlhraealmrelkvPDMnVALPVSQYGGG 149
Cdd:COG0488 386 ------------HQE-ELDPDKTVLDELRdgapGGTEQEVRGylGRFLFS---------------GDD-AFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 150 yqqlvE-----IAKALNKQARLLILDEPSSAL---TRGEIEVLLDIIKGlkakgvACVYISHklDE--VAAVCDTIAVIR 219
Cdd:COG0488 437 -----EkarlaLAKLLLSPPNVLLLDEPTNHLdieTLEALEEALDDFPG------TVLLVSH--DRyfLDRVATRILEFE 503
|
...
gi 1067238353 220 DGK 222
Cdd:COG0488 504 DGG 506
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-184 |
1.11e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 23 GIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQsiRETeaagiviIHQELTLV-------P 95
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR--PDAGEVLWQGEPIRRQ--RDE-------YHQDLLYLghqpgikT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIFMGHELTLPGGRmnypAMLHRAEALMRELKVPDmnvaLPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSA 175
Cdd:PRK13538 88 ELTALENLRFYQRLHGPGDD----EALWEALAQVGLAGFED----VPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
....*....
gi 1067238353 176 LTRGEIEVL 184
Cdd:PRK13538 160 IDKQGVARL 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-225 |
1.38e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 28 VKPGECVGLCGENGAGKSTLMKVLSAVYPHgtwEGEILWDGQPLKAQSIREteaagivIIHQELTLVPDLSVAENIFMGH 107
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQPLEAWSAAE-------LARHRAYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 108 ELTL--PGGRMNY--PAMLHR-AEALMRELKVPDmnvalPVSQYGGGYQQLVEIA-------KALNKQARLLILDEPSSA 175
Cdd:PRK03695 89 YLTLhqPDKTRTEavASALNEvAEALGLDDKLGR-----SVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 176 LTRGEiEVLLD-IIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK03695 164 LDVAQ-QAALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
280-486 |
1.60e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGryNAEVWLEGQVIDTRTPlKSIRAGLCMVPEDrkrQGIIPDL 358
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPT--AGTVLVAGDDVEALSA-RAASRRVASVPQD---TSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNITLAvldTYAHMTRIDA--EAELGSIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:PRK09536 93 DVRQVVEMG---RTPHRSRFDTwtETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 437 GVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-222 |
1.65e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 15 FGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETE--AAGIVIIHQELT 92
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA--GKIWFSGHDITRLKNREVPflRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDLSVAENIFMghELTLPGGRMNypAMLHRAEALMRELKVPDMNVALPVsQYGGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:PRK10908 90 LLMDRTVYDNVAI--PLIIAGASGD--DIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 173 SSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
284-504 |
1.85e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 284 SFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRynAEVWLEGQViDTRTPlksiraglcmvPEDR------KRQGIIP 356
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPAS--GSLTLNGQD-HTTTP-----------PSRRpvsmlfQENNLFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITLAV-----LDTYAHMTRidaeaelgsidQQI-SRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:PRK10771 85 HLTVAQNIGLGLnpglkLNAAQREKL-----------HAIaRQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRGDFINDGLTQEQVLAAAL 504
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
261-485 |
2.02e-12 |
|
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: 66.84 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVT-CYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAypGRYNA-EVWLEGQVIdTRTPLKSI 338
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL--ERPTSgSVLVDGTDL-TLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 RaglcmvpEDRKRQGIIpdlgvGQNITL----AVLDTYAHMTRIdAEAELGSIDQQISRM-------HLKTASPSlpitS 407
Cdd:cd03258 78 R-------KARRRIGMI-----FQHFNLlssrTVFENVALPLEI-AGVPKAEIEERVLELlelvgleDKADAYPA----Q 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-224 |
2.38e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.22 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHGtweGEILWDGQ---PLKAQSIRETeaagIVIIHQELTLVp 95
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQS---GRILIDGTdirTVTRASLRRN----IAVVFQDAGLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIFMGHELTLPGGRMnypAMLHRAEAL---MRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:PRK13657 422 NRSIEDNIRVGRPDATDEEMR---AAAERAQAHdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 173 SSAL---TRGEIEVLLDIIKglkaKGVACVYISHKLDEVAAVcDTIAVIRDGKHI 224
Cdd:PRK13657 499 TSALdveTEAKVKAALDELM----KGRTTFIIAHRLSTVRNA-DRILVFDNGRVV 548
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-224 |
2.55e-12 |
|
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: 65.65 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETeaagIVIIHQELTLVPDLSVA 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 101 ENIFMGheltlpggrmnypamlhraeALMRELKvpdmnvalpvsqygGGYQQLVEIAKALNKQARLLILDEPSSALTRGE 180
Cdd:cd03213 101 ETLMFA--------------------AKLRGLS--------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067238353 181 IEVLLDIIKGLKAKGVACVYISHKL-DEVAAVCDTIAVIRDGKHI 224
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
280-485 |
2.80e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGA-YPGRYNAEVwlegqvidtrtplksirAGlcMVP-EDRK------- 350
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVPTSGEVRV-----------------LG--YVPfKRRKefarrig 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 351 -----RQGIIPDLgvgqnitlAVLDTY---AHMTRIDAE---------AELGSIDQQISRmhlktaspslPITSLSGGNQ 413
Cdd:COG4586 99 vvfgqRSQLWWDL--------PAIDSFrllKAIYRIPDAeykkrldelVELLDLGELLDT----------PVRQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 414 QKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-222 |
2.84e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.52 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 26 IKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQS---IRETEAAGIVIIHQELTLVPDLSVAEN 102
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE--PTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 103 IFMGHELTlpggrmNYPAMLHRAEAL--MRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL---T 177
Cdd:PRK10070 127 TAFGMELA------GINAEERREKALdaLRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALdplI 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 178 RGEIEvllDIIKGLKAKGV-ACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK10070 200 RTEMQ---DELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGE 242
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
263-486 |
2.94e-12 |
|
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: 69.02 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTC-YDvdNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrYNA-EVWLEGQviDTRT-PLKSIR 339
Cdd:COG4987 335 ELEDVSFrYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--PQSgSITLGGV--DLRDlDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 AGLCMVPEDrkrqgiiPDL---GVGQNITLAvldtyahmtRIDA-EAELGsidQQISRMHLKTASPSLPI---------- 405
Cdd:COG4987 409 RRIAVVPQR-------PHLfdtTLRENLRLA---------RPDAtDEELW---AALERVGLGDWLAALPDgldtwlgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGAlAAEGVSIIMVSSELAEvLGVSNRVLVIGDGQL 485
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG-LERMDRILVLEDGRI 547
|
.
gi 1067238353 486 R 486
Cdd:COG4987 548 V 548
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
408-488 |
3.05e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.27 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRG 487
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
.
gi 1067238353 488 D 488
Cdd:PRK09493 217 D 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-222 |
3.22e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 68.69 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYphGTWEGEILWDGQPLKA---QSIRetEAAGIViiHQELTLVPDl 97
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY--DVTSGRILIDGQDIRDvtqASLR--AAIGIV--PQDTVLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SVAENIFMGheltlpggrmnypamlhRAEALMREL-------KVPDMNVALP------VSQYG----GGYQQLVEIAKAL 160
Cdd:COG5265 447 TIAYNIAYG-----------------RPDASEEEVeaaaraaQIHDFIESLPdgydtrVGERGlklsGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 161 NKQARLLILDEPSSAL---TRGEIEVLLDIIkglkAKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:COG5265 510 LKNPPILIFDEATSALdsrTERAIQAALREV----ARGRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-222 |
3.40e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLS---AVYPHG-TWEGEILWDGQPL-KAQSIRETEAAGIVIihQELTLVP 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrliEIYDSKiKVDGKVLYFGKDIfQIDAIKLRKEVGMVF--QQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIfmGHELTLPGGRMNYPAMLHRAEALMRELKVPDMNVAL--PVSQYGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:PRK14246 104 HLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnsPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067238353 174 SALTRGEIEVLLDIIKGLKaKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGE 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-222 |
4.14e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVypHGTWEGEILWDGQPLKAQS-------IRETeaAGIVIIHQELT 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVPTQGSVRVDDTLITSTSknkdikqIRKK--VGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVpDLSVAENIFMGHEltlpggrmNYPAMLHRAEALMRE-LKVPDMNVAL----PVsQYGGGYQQLVEIAKALNKQARLL 167
Cdd:PRK13649 98 LF-EETVLKDVAFGPQ--------NFGVSQEEAEALAREkLALVGISESLfeknPF-ELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 168 ILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-222 |
4.15e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 64.64 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVN--ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSavyphGTWE---GEILWDGQPLkaQSIRETE 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-----GDLKpqqGEITLDGVPV--SDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVIIHQELTLVpDLSVAENIfmgheltlpgGRmnypamlhraealmrelkvpdmnvalpvsQYGGGYQQLVEIAKAL 160
Cdd:cd03247 74 SSLISVLNQRPYLF-DTTLRNNL----------GR-----------------------------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 161 NKQARLLILDEPSSAL-TRGEIEVLLDIIKGLKAKGVacVYISHKLDEVAAVcDTIAVIRDGK 222
Cdd:cd03247 114 LQDAPIVLLDEPTVGLdPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGK 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
281-484 |
4.89e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.79 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALfgaypgryNA-------EVWLEGQVI-DTRTPLKSIRAGLCMVPedrkrQ 352
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCI--------NLleepdsgTITVDGEDLtDSKKDINKLRRKVGMVF-----Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 353 G--IIPDLGVGQNITLA---VLdtyaHMTRIDAEAElgsIDQQISRMHL---KTASPSlpitSLSGGNQQKAVLAKMLMA 424
Cdd:COG1126 85 QfnLFPHLTVLENVTLApikVK----KMSKAEAEER---AMELLERVGLadkADAYPA----QLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 425 KPKVLILDEPTRGVD---VGakyEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:COG1126 154 EPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
280-486 |
6.60e-12 |
|
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: 65.08 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGqvIDTRTPLKSIRAGLCMVPEDRKrqgIIPDLG 359
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATVAG--HDVVREPREVRRRIGIVFQDLS---VDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLavldtYAHMTRIDAEAELGSIDQQISRMHLKTASPSLpITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD 439
Cdd:cd03265 90 GWENLYI-----HARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067238353 440 VGAKYEIYKLMGAL-AAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
280-485 |
7.52e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 64.82 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIdTRTPLKSIRAGLCMVPEDrkrqgiiPDLG 359
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-SGSILIDGVDI-SKIGLHDLRSRISIIPQD-------PVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VG---QNitLAVLDTYAhmtriDAEaelgsIDQQISRMHLKTASPSLPI----------TSLSGGNQQKAVLAKMLMAKP 426
Cdd:cd03244 91 SGtirSN--LDPFGEYS-----DEE-----LWQALERVGLKEFVESLPGgldtvveeggENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYK-LMGALAaeGVSIIMVSSELAEVLGvSNRVLVIGDGQL 485
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKtIREAFK--DCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
273-462 |
7.69e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 64.98 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 273 DNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNA--EVWLEGQVIDTRTPLKSIraglCMVPEDRK 350
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsgQILFNGQPRKPDQFQKCV----AYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 351 rqgIIPDLGVGQNITLAVLdtyAHMTRIDAEAELGSIDQQ--ISRMHLKTASPSLpITSLSGGNQQKAVLAKMLMAKPKV 428
Cdd:cd03234 92 ---LLPGLTVRETLTYTAI---LRLPRKSSDAIRKKRVEDvlLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190
....*....|....*....|....*....|....
gi 1067238353 429 LILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIM 462
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVIL 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
156-439 |
8.77e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIP 235
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 236 RIITQMVGRE-MSNLYPTEPHDV--------GEVIFEARNVTcydVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTEL 306
Cdd:PRK10938 226 ALVAQLAHSEqLEGVQLPEPDEPsarhalpaNEPRIVLNNGV---VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 307 VSALFGAYPGRYNAEVWLEGQvidtrtplksiRAGLCMVPEDRKRQ-GIIP-----DLGVGQNITLAVLDTYAHMTRI-- 378
Cdd:PRK10938 303 LSLITGDHPQGYSNDLTLFGR-----------RRGSGETIWDIKKHiGYVSsslhlDYRVSTSVRNVILSGFFDSIGIyq 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 379 ---DAEAELGsiDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD 439
Cdd:PRK10938 372 avsDRQQKLA--QQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
254-485 |
9.98e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.11 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 254 PHDVGEVIFEarNVT-CYDVDNPKrkrVDDISFVLRRGEILGIAGLVGAGRTELVSALfgayPGRYNAEvwlEGQV---- 328
Cdd:COG1132 334 PPVRGEIEFE--NVSfSYPGDRPV---LKDISLTIPPGETVALVGPSGSGKSTLVNLL----LRFYDPT---SGRIlidg 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 329 IDTRT-PLKSIRAGLCMVPEDrkrqgiiPDL--G-VGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMH--LKTasps 402
Cdd:COG1132 402 VDIRDlTLESLRRQIGVVPQD-------TFLfsGtIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPdgYDT---- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 403 lPI----TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAEVLGVsNRVL 478
Cdd:COG1132 469 -VVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNA-DRIL 545
|
....*..
gi 1067238353 479 VIGDGQL 485
Cdd:COG1132 546 VLDDGRI 552
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
280-478 |
1.05e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.79 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRynaevwlEGQVidTRTPlksiRAGLCMVPEdrkrQGIIPD-- 357
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPT-------SGTV--RRAG----GARVAYVPQ----RSEVPDsl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 358 -LGVGQNITLAVLDTYAHMTRIDAEAELgSIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:NF040873 71 pLTVRDLVAMGRWARRGLWRRLTRDDRA-AVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1067238353 437 GVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVL 478
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
280-485 |
1.16e-11 |
|
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: 65.36 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRynAEVWLEGQVIDT--RTPLKSIRaglcmvpedRKRQGIip 356
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTS--GKVLIDGQDIAAmsRKELRELR---------RKKISM-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 dlgVGQNITL----AVLDTYAH---MTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:cd03294 107 ---VFQSFALlphrTVLENVAFgleVQGVPRAEREERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
280-485 |
1.22e-11 |
|
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: 64.43 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTPlKSIRAGLCMVPEDrkrqGIIPDLG 359
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLALADP-AWLRRQVGVVLQE----NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLAvlDTYAHMTRIDAEAELGSIDQQISRMHLKTASpslpI-----TSLSGGNQQKAVLAKMLMAKPKVLILDEP 434
Cdd:cd03252 92 IRDNIALA--DPGMSMERVIEAAKLAGAHDFISELPEGYDT----IvgeqgAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 435 TRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAEVLGvSNRVLVIGDGQL 485
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
263-492 |
1.23e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 65.11 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTC-YDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTEL---VSALFGAYPGrynaEVWLEGQVIDTRTPlksi 338
Cdd:COG1116 9 ELRGVSKrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLlrlIAGLEKPTSG----EVLVDGKPVTGPGP---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 RAGlcMVP-EDRkrqgIIPDLGVGQNITLAVLDtyAHMTRIDAEAElgsIDQQISRMHLKTASPSLPiTSLSGGNQQKAV 417
Cdd:COG1116 81 DRG--VVFqEPA----LLPWLTVLDNVALGLEL--RGVPKAERRER---ARELLELVGLAGFEDAYP-HQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 418 LAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGAL-AAEGVSIIMVSSELAEVLGVSNRVLVIGD--GQLRGDFIND 492
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVD 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-241 |
1.24e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTL-MKVLSAVYPHGTwEGEILWDGQPLKAQSIRETEAAGIVII---HQELTLVPD 96
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNI-SGTVFKDGKEVDVSTVSDAIDAGLAYVtedRKGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFMGHeltLPG----GRMNYPAMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:NF040905 355 DDIKRNITLAN---LGKvsrrGVIDENEEIKVAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 173 ssalTRGeIEV-----LLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQM 241
Cdd:NF040905 432 ----TRG-IDVgakyeIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
262-485 |
1.43e-11 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 63.00 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTcYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIDTRTPLksi 338
Cdd:cd03246 1 LEVENVS-FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRptsGR----VRLDGADISQWDPN--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 raglcmvpEDRKRQGIIPdlgvgQNITLavLDtyahmtridaeaelGSIDQQIsrmhlktaspslpitsLSGGNQQKAVL 418
Cdd:cd03246 73 --------ELGDHVGYLP-----QDDEL--FS--------------GSIAENI----------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 419 AKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELaEVLGVSNRVLVIGDGQL 485
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
280-485 |
1.45e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGRynaeVWLEGQVIDTRTPlksiraglcmvPEDRKrqgiip 356
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGletPDSGR----IVLNGRDLFTNLP-----------PRERR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 dlgVG---QNitlavldtYA---HMT------------RIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVL 418
Cdd:COG1118 77 ---VGfvfQH--------YAlfpHMTvaeniafglrvrPPSKAEIRARVEELLELVQLEGLADRYP-SQLSGGQRQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 419 AKMLMAKPKVLILDEPTRGVDVGAKYEIYK-LMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
280-484 |
1.57e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.87 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVID-TRTPLKSIRAGLCMVPEDRKRQgiIPDL 358
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS-SGRILFDGKPIDySRKGLMKLRESVGMVFQDPDNQ--LFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 GVGQNITLAVLDTyaHMTRIDAEAELGSIDQQISRMHLKTAspslPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGV 438
Cdd:PRK13636 99 SVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGIEHLKDK----PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067238353 439 DVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
277-487 |
1.69e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYpgRYNA-EVWLEGQVIdtrTPLKS-----IRAGLCMVPEDRK 350
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAgKIWFSGHDI---TRLKNrevpfLRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 351 rqgIIPDLGVGQNITLAVldtyahmtrIDAEAELGSIDQQIS----RMHLKTASPSLPItSLSGGNQQKAVLAKMLMAKP 426
Cdd:PRK10908 90 ---LLMDRTVYDNVAIPL---------IIAGASGDDIRRRVSaaldKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRG 487
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
280-485 |
1.73e-11 |
|
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: 64.28 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGRynaeVWLEGQVIDTRTPlksiraglcmvpedRKRQgiip 356
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlerPDSGT----ILFGGEDATDVPV--------------QERN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 dLG-VGQNITLavldtYAHMT---------RIDAEAELGS---IDQQISR----MHLKTASPSLPiTSLSGGNQQKAVLA 419
Cdd:cd03296 76 -VGfVFQHYAL-----FRHMTvfdnvafglRVKPRSERPPeaeIRAKVHEllklVQLDWLADRYP-AQLSGGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 420 KMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
276-485 |
2.19e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTE-------LVSALFGaypgrynaEVWLEGQVIdTRTPL-KSIRAGLCMVPE 347
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSG--------RIFLDGEDI-THLPMhKRARLGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 348 D----RKrqgiipdLGVGQNItLAVLDTyAHMTRIDAEAELGSIDQQISRMHLKTaSPSLpitSLSGGNQQKAVLAKMLM 423
Cdd:COG1137 86 EasifRK-------LTVEDNI-LAVLEL-RKLSKKEREERLEELLEEFGITHLRK-SKAY---SLSGGERRRVEIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 424 AKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIM----VSselaEVLGVSNRVLVIGDGQL 485
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLItdhnVR----ETLGICDRAYIISEGKV 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
282-506 |
2.32e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALfGAYPGRYNAEVWLEGQVID--TRTPLKSIRaglcmvpEDRKRQGII---- 355
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNHFDfsKTPSDKAIR-------ELRRNVGMVfqqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 ---PDLGVGQNITLA---VLDtyahMTRIDAEAElgsIDQQISRMHLKTASPSLPItSLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:PRK11124 92 nlwPHLTVQQNLIEApcrVLG----LSKDQALAR---AEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL--RGDfiNDGLTQEQVLAAA--LS 505
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIveQGD--ASCFTQPQTEAFKnyLS 241
|
.
gi 1067238353 506 H 506
Cdd:PRK11124 242 H 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
282-486 |
2.47e-11 |
|
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: 65.12 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGR--YNAEVWLEGqvidtrtplksiRAGLCMVPEDRkRQGII- 355
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGlerPDSGRirLGGEVLQDS------------ARGIFLPPHRR-RIGYVf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 ------PDLGVGQNITlavldtYAhMTRIDAEAELGSIDQQISRMHLktaSPSL--PITSLSGGNQQKAVLAKMLMAKPK 427
Cdd:COG4148 84 qearlfPHLSVRGNLL------YG-RKRAPRAERRISFDEVVELLGI---GHLLdrRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-222 |
2.90e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDG-----QPLKAQSIRETeaAGIVIIHQELTL 93
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT---SGKIIIDGvditdKKVKLSDIRKK--VGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 94 VPDlSVAENIFMGheltlpggrmnyPAMLHRAEALMRELKVPDMN-VALPVSQY--------GGGYQQLVEIAKALNKQA 164
Cdd:PRK13637 97 FEE-TIEKDIAFG------------PINLGLSEEEIENRVKRAMNiVGLDYEDYkdkspfelSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 165 RLLILDEPSSALT-RGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK13637 164 KILILDEPTAGLDpKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-485 |
2.97e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQviDTRTPLKSIRAGLCMVPEdrkRQGIIP 356
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGK--DIETNLDAVRQSLGMCPQ---HNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITLavldtYAHM---TRIDAEAELGSIDQQISRMHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDE 433
Cdd:TIGR01257 1017 HLTVAEHILF-----YAQLkgrSWEEAQLEMEAMLEDTGLHHKRNEEAQ----DLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 434 PTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
258-485 |
3.12e-11 |
|
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: 63.40 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 258 GEVIFEarNVT-CYdvdNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrynaevWLEGQV----IDTR 332
Cdd:cd03254 1 GEIEFE--NVNfSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-------PQKGQIlidgIDIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 333 T-PLKSIRAGLCMVPEDrkrQGIIPDlGVGQNITLAvlDTYAHMTRIDAEAELGSIDQQIsrMHLKT---ASPSLPITSL 408
Cdd:cd03254 69 DiSRKSLRSMIGVVLQD---TFLFSG-TIMENIRLG--RPNATDEEVIEAAKEAGAHDFI--MKLPNgydTVLGENGGNL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 409 SGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGvSNRVLVIGDGQL 485
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-205 |
3.13e-11 |
|
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: 65.46 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPlkAQSIRETEAAGIVIIHQELTLVP 95
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVP--VSSLDQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIFMGHElTLPGGRMNypAMLHRA--EALMRELkvPDmNVALPVSQYG----GGYQQLVEIAKALNKQARLLIL 169
Cdd:TIGR02868 422 DTTVRENLRLARP-DATDEELW--AALERVglADWLRAL--PD-GLDTVLGEGGarlsGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 1067238353 170 DEPSSALTRG-EIEVLLDIIKGLKAKGVacVYISHKL 205
Cdd:TIGR02868 496 DEPTEHLDAEtADELLEDLLAALSGRTV--VLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-222 |
3.23e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 11 IVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYP----------------HGTWEGEILWDGQ-P-LK 72
Cdd:PRK11174 356 EILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslkingielreldPESWRKHLSWVGQnPqLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 73 AQSIRETEAAGIVIIHQE-LTLVPDLS-VAENIFMgheltLPGGrMNYPamlhraealmrelkVPDMNVALPVSQygggy 150
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEqLQQALENAwVSEFLPL-----LPQG-LDTP--------------IGDQAAGLSVGQ----- 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 151 QQLVEIAKALNKQARLLILDEPSSAL-TRGEIEVLldiiKGLK--AKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLdAHSEQLVM----QALNaaSRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQ 560
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
280-483 |
3.33e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.47 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGryNAEVWLEGQVIDTRTPLKSIRAGLCmvpedRKRQGI---- 354
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPT--GGTILLRGQHIEGLPGHQIARMGVV-----RTFQHVrlfr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 ----IPDLGVGQ------NITLAVLDTYAHmTRIDAEAeLGSIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMA 424
Cdd:PRK11300 94 emtvIENLLVAQhqqlktGLFSGLLKTPAF-RRAESEA-LDRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 425 KPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
3.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETEAAGIVIIHQELTLVP 95
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS--GSVLIRGEPITKENIREVRKFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 DLSVAENIFMGH-ELTLpggrmNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDEPSS 174
Cdd:PRK13652 93 SPTVEQDIAFGPiNLGL-----DEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 175 ALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-243 |
3.70e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 15 FGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETeAAGIVIIHQELTLV 94
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA--HGHVWLDGEHIQHYASKEV-ARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDLSVAENIFMG---HELTLPGGRMNYPAMLHRAealMRELKVPDMnVALPVSQYGGGYQQLVEIAKALNKQARLLILDE 171
Cdd:PRK10253 94 GDITVQELVARGrypHQPLFTRWRKEDEEAVTKA---MQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 172 PSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADMDIPRIITQMVG 243
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-222 |
4.27e-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: 62.43 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVL-SAVYPHgtwEGEILWDGQPLKAQSIRETEAAgIVIIHQELTLvpdls 98
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLEAE---EGKIEIDGIDISTIPLEDLRSS-LTIIPQDPTL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 99 vaeniFMGhelTLpggRMNY-PAMLHRAEALMRELKVPDMNVALpvSQyggGYQQLVEIAKALNKQARLLILDEPSSALT 177
Cdd:cd03369 94 -----FSG---TI---RSNLdPFDEYSDEEIYGALRVSEGGLNL--SQ---GQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067238353 178 RGEIEVLLDIIKGLkAKGVACVYISHKLDEVAAvCDTIAVIRDGK 222
Cdd:cd03369 158 YATDALIQKTIREE-FTNSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
5.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRET-EAAGIVIIHQELTLVPDLs 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK--SGEIFYNNQAITDDNFEKLrKHIGIVFQNPDNQFVGSI- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 99 VAENIFMGHELTLpggrMNYPAMLHRAEALMRELKVPDMNVALPVSqYGGGYQQLVEIAKALNKQARLLILDEPSSALTR 178
Cdd:PRK13648 101 VKYDVAFGLENHA----VPYDEMHRRVSEALKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067238353 179 GEIEVLLDIIKGLKA-KGVACVYISHKLDEvAAVCDTIAVIRDGK 222
Cdd:PRK13648 176 DARQNLLDLVRKVKSeHNITIISITHDLSE-AMEADHVIVMNKGT 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
260-485 |
6.26e-11 |
|
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: 62.63 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 260 VIFEarNVT-CYDvdnPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY---PGRynaeVWLEGQVIDTRTpL 335
Cdd:cd03253 1 IEFE--NVTfAYD---PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdvsSGS----ILIDGQDIREVT-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 336 KSIRAGLCMVPEDRkrqgIIPDLGVGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMHLKTASpslpI-----TSLSG 410
Cdd:cd03253 71 DSLRRAIGVVPQDT----VLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDT----IvgergLKLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 411 GNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAEVLGvSNRVLVIGDGQL 485
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
282-506 |
6.31e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSAL-FGAYPGryNAEVWLEGQVIDTRTPL--KSIRaglcmvpEDRKRQGII--- 355
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD--SGQLNIAGHQFDFSQKPseKAIR-------LLRQKVGMVfqq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 ----PDLGVGQNITLA---VLDtyahMTRIDAEAElgsIDQQISRMHLKTASPSLPItSLSGGNQQKAVLAKMLMAKPKV 428
Cdd:COG4161 91 ynlwPHLTVMENLIEApckVLG----LSKEQAREK---AMKLLARLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 429 LILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL--RGD---FINdglTQEQVLAAA 503
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIieQGDashFTQ---PQTEAFAHY 239
|
...
gi 1067238353 504 LSH 506
Cdd:COG4161 240 LSH 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-222 |
6.53e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSavYPHGTWEGEILWDGQPLKAqsIRETE 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN--FLEKPSEGSIVVNGQTINL--VRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 A--------------AGIVIIHQELTLVPDLSVAENIfmgheltlpggrMNYPAM---LHRAEALMRELKVPDmNVALPV 143
Cdd:PRK10619 77 GqlkvadknqlrllrTRLTMVFQHFNLWSHMTVLENV------------MEAPIQvlgLSKQEARERAVKYLA-KVGIDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 144 SQYG-------GGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIA 216
Cdd:PRK10619 144 RAQGkypvhlsGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
....*.
gi 1067238353 217 VIRDGK 222
Cdd:PRK10619 224 FLHQGK 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-198 |
6.63e-11 |
|
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: 61.49 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETeaaGIViiHQELTLVPDLSVA 100
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNFQRST---GYV--EQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 101 ENIfmgheltlpggrmnypamlhRAEALMRELKVPDmnvalpvsqygggyQQLVEIAKALNKQARLLILDEPSSALTRGE 180
Cdd:cd03232 98 EAL--------------------RFSALLRGLSVEQ--------------RKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|
gi 1067238353 181 IEVLLDIIKGLKAKG--VAC 198
Cdd:cd03232 144 AYNIVRFLKKLADSGqaILC 163
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
280-485 |
6.92e-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: 61.66 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrynaevWLEGQV----IDTRT-PLKSIRAGLCMVPEDrkrqgi 354
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-------AEEGKIeidgIDISTiPLEDLRSSLTIIPQD------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 iPDLGVGqniTL-AVLDTYAHMTridaeaelgsiDQQIsRMHLKTASPSLpitSLSGGNQQKAVLAKMLMAKPKVLILDE 433
Cdd:cd03369 91 -PTLFSG---TIrSNLDPFDEYS-----------DEEI-YGALRVSEGGL---NLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 434 PTRGVDVGAKYEIYKLMGALAAeGVSIIMVSSELAEVLGVsNRVLVIGDGQL 485
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
261-497 |
7.57e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVT-CYDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGaYPGRYNAEVWLEGQVIDTRTPLKSir 339
Cdd:PRK11607 19 LLEIRNLTkSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIMLDGVDLSHVPPYQR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 aglcmvPEDRKRQ--GIIPDLGVGQNITLAVldtyaHMTRIdAEAELGS-IDQQISRMHLKTASPSLPiTSLSGGNQQKA 416
Cdd:PRK11607 92 ------PINMMFQsyALFPHMTVEQNIAFGL-----KQDKL-PKAEIASrVNEMLGLVHMQEFAKRKP-HQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 417 VLAKMLMAKPKVLILDEPTRGVDVGAKYEI-YKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGdgqlRGDFINDGLT 495
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN----RGKFVQIGEP 234
|
..
gi 1067238353 496 QE 497
Cdd:PRK11607 235 EE 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
276-504 |
8.94e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALfgaypGRYNA----EVWLEGQVIDTRTPlKSIRAGLCMVPEdrkr 351
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF-----ARLLTpqsgTVFLGDKPISMLSS-RQLARRLALLPQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 QGIIPdlgvgQNITLAVLDTY------AHMTRIDAEAElGSIDQQISRMHLKTASPSlPITSLSGGNQQKAVLAKMLMAK 425
Cdd:PRK11231 84 HHLTP-----EGITVRELVAYgrspwlSLWGRLSAEDN-ARVNQAMEQTRINHLADR-RLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 426 PKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLrgdfINDGlTQEQVLAAAL 504
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV----MAQG-TPEEVMTPGL 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-232 |
9.99e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVN----ALNGIDIKVKPGECVGLCGENGAGKS----TLMKVLSavYPHGTWEGEILWDGQPLKAQSI 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLID--YPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 77 RETE---AAGIVIIHQE--LTLVPDLSVAENIfMGHELTLPGGrmNYPAMLHRAEALMRELKVPDMNVALPV--SQYGGG 149
Cdd:PRK11022 81 KERRnlvGAEVAMIFQDpmTSLNPCYTVGFQI-MEAIKVHQGG--NKKTRRQRAIDLLNQVGIPDPASRLDVypHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 150 YQQLVEIAKALNKQARLLILDEPSSAL----TRGEIEVLLDIikgLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALdvtiQAQIIELLLEL---QQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
....*..
gi 1067238353 226 TTAMADM 232
Cdd:PRK11022 235 TGKAHDI 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-485 |
1.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALfGAYPGRYNAEVWLEGQVIDTRTPLKSIRAglcmvPEDRKRQGII------ 355
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIYDSKIKVDGKVLYFGKDIFQIDA-----IKLRKEVGMVfqqpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 -PDLGVGQNITLAvLDTYAhmtrIDAEAELGSIDQQISR-------MHLKTASPSlpiTSLSGGNQQKAVLAKMLMAKPK 427
Cdd:PRK14246 102 fPHLSIYDNIAYP-LKSHG----IKEKREIKKIVEECLRkvglwkeVYDRLNSPA---SQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYKLMGALAAEgVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
289-485 |
1.07e-10 |
|
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: 61.35 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 289 RGEILGIAGLVGAGRTELVSaLFGAYPGRYNAEVWLEGQVIDTRTPlksIRAGLCMVPEDrkrQGIIPDLGVGQNITLAv 368
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLN-LIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQE---NNLFAHLTVEQNVGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 369 LDTYAHMTRIDAEAelgsIDQQISRMHLKTASPSLPITsLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYK 448
Cdd:cd03298 95 LSPGLKLTAEDRQA----IEVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1067238353 449 LMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03298 170 LVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
278-485 |
1.13e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 278 KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGA--YPGRYNAE-VWLEG---QVIDTRTPLKSIRAGLCMVPEDrKR 351
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEkLEFNGqdlQRISEKERRNLVGAEVAMIFQD-PM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 QGIIPDLGVGQNI--TLAVLDTYAHMTRIDAEAELGS---IDQQISRMHLKTASpslpitsLSGGNQQKAVLAKMLMAKP 426
Cdd:PRK11022 100 TSLNPCYTVGFQImeAIKVHQGGNKKTRRQRAIDLLNqvgIPDPASRLDVYPHQ-------LSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALA-AEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
262-485 |
1.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTcYDVDNPKRKR-VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRYNAEVwleGQVIDTRTP----L 335
Cdd:PRK13643 4 FEKVNYT-YQPNSPFASRaLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTV---GDIVVSSTSkqkeI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 336 KSIRAGLCMV---PEDRK-RQGIIPDLGVG-QNITLavldTYAHMTRIDAEA-ELGSIDQQISRmhlktASPslpiTSLS 409
Cdd:PRK13643 80 KPVRKKVGVVfqfPESQLfEETVLKDVAFGpQNFGI----PKEKAEKIAAEKlEMVGLADEFWE-----KSP----FELS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 410 GGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-222 |
1.32e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETeaaGIVIihQELTLVPDLSVA 100
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRT---GFVT--QDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 101 ENIFMGHELTLPGGrMNYPAMLHRAEALMRELKVPDMNVALPVSQY----GGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:PLN03211 159 ETLVFCSLLRLPKS-LTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067238353 177 TRGEIEVLLDIIKGLKAKGVACVYISHK-LDEVAAVCDTIAVIRDGK 222
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-222 |
1.39e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIREteaagiviIHQELTLV---PDl 97
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES--GQIIIDGDLLTEENVWD--------IRHKIGMVfqnPD- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 svaeNIFMGHELT------LPGGRMNYPAMLHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLLILDE 171
Cdd:PRK13650 92 ----NQFVGATVEddvafgLENKGIPHEEMKERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 172 PSSALT-RGEIEvLLDIIKGLKAK-GVACVYISHKLDEVaAVCDTIAVIRDGK 222
Cdd:PRK13650 167 ATSMLDpEGRLE-LIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-176 |
1.46e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 61.13 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHGTWEGEILWDGQPLKAQSIRETeaagIVIIHQELTLVPDLSV 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTSGQILFNGQPRKPDQFQKC----VAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 100 AENI-FMgheLTLPGGRMNYPAMLHRAEALMRELKVPDMNVALP-VSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:cd03234 99 RETLtYT---AILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-225 |
1.48e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETEAA-- 82
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIIHQELTLVPDLSVAENI-FMGHELTlpggrmNYPAMLHRAEALMRELKVPDMNVA-LPVSQYGGGYQQLVEIAKAL 160
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVaYPLREHT------QLPAPLLHSTVMMKLEAVGLRGAAkLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 161 NKQARLLILDEP---SSALTRGeieVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK11831 159 ALEPDLIMFDEPfvgQDPITMG---VLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-224 |
1.55e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVL---SAVYPHGTWEGEILWDGQPL---KAQ 74
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVTITGSIVYNGHNIyspRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 75 SIRETEAAGIVIihQELTLVPdLSVAENIFMGheLTLPGgrMNYPAMLHraEALMRELK-------VPDM--NVALPVSq 145
Cdd:PRK14239 81 TVDLRKEIGMVF--QQPNPFP-MSIYENVVYG--LRLKG--IKDKQVLD--EAVEKSLKgasiwdeVKDRlhDSALGLS- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 146 ygGGYQQLVEIAKALNKQARLLILDEPSSAL---TRGEIEvllDIIKGLKAKgVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK14239 151 --GGQQQRVCIARVLATSPKIILLDEPTSALdpiSAGKIE---ETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGD 224
|
..
gi 1067238353 223 HI 224
Cdd:PRK14239 225 LI 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
280-485 |
1.62e-10 |
|
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: 61.10 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGaYPGRYNAEVWLEGQVIdtrTPLKSIRAGLCMVPEDrkrQGIIPDLG 359
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-FETPTSGEILLDGKDI---TNLPPHKRPVNTVFQN---YALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNI----TLAVLDTYAHMTRIDAEAELGSIDQQISRMhlktaspslpITSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:cd03300 89 VFENIafglRLKKLPKAEIKERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 436 RGVDV----GAKYEIYKLMGALaaeGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03300 159 GALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
262-485 |
1.71e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 60.02 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTcYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRynaevwlEGQVIDTRTPLKSIrag 341
Cdd:cd03247 1 LSINNVS-FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-------QGEITLDGVPVSDL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 342 lcmvpEDRKRQGIipdlgvgqnitlAVLDTYAHMTRidaeaelGSIDQQISRmhlktaspslpitSLSGGNQQKAVLAKM 421
Cdd:cd03247 70 -----EKALSSLI------------SVLNQRPYLFD-------TTLRNNLGR-------------RFSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 422 LMAKPKVLILDEPTRGVDVGAKYEIYKLMgALAAEGVSIIMVSSELAEVLGVsNRVLVIGDGQL 485
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLI-FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
280-488 |
1.73e-10 |
|
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: 61.01 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVidtrTPLksIRAGLcmvpedrkrqGIIP 356
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsGT----VTVRGRV----SSL--LGLGG----------GFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITL--AVL-----DTYAHMTRIDAEAELG-SIDqqisrmhlktaspsLPITSLSGGnqQKAVL--AKMLMAKP 426
Cdd:cd03220 98 ELTGRENIYLngRLLglsrkEIDEKIDEIIEFSELGdFID--------------LPVKTYSSG--MKARLafAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-217 |
1.87e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 10 GIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSiRETEAAgiviIHQ 89
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT--GGELYYQGQDLLKAD-PEAQKL----LRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 ELTLV---PDLSVAENIFMGHELTLPggrMNYPAMLHRAEalmRELKVPDM--NVALPVSQYG-------GGYQQLVEIA 157
Cdd:PRK11308 93 KIQIVfqnPYGSLNPRKKVGQILEEP---LLINTSLSAAE---RREKALAMmaKVGLRPEHYDryphmfsGGQRQRIAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 158 KALNKQARLLILDEPSSAL---TRGEI-EVLLDIIKGLkakGVACVYISHKLDEVAAVCDTIAV 217
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALdvsVQAQVlNLMMDLQQEL---GLSYVFISHDLSVVEHIADEVMV 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
277-511 |
2.03e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVID--TRTPLKSIRAGLCMVPEDrkrQGI 354
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGENIPamSRSRLYTVRKRMSMLFQS---GAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVGQNITLAVLDtyaHmTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDEP 434
Cdd:PRK11831 96 FTDMNVFDNVAYPLRE---H-TQLPAPLLHSTVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 435 TRGVDVGAKYEIYKLMGAL-AAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLrgdfINDGLTQEqvlaaaLSHNNNDR 511
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKI----VAHGSAQA------LQANPDPR 238
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-76 |
2.33e-10 |
|
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: 62.89 E-value: 2.33e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 24 IDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQSI 76
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYrPE---SGEILLDGQPVTADNR 401
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
276-485 |
2.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSAlFGAYPGRYNAEVWLEGQVIDTRTPLKSIRaglcmvpEDRKRQGII 355
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQH-FNALLKPSSGTITIAGYHITPETGNKNLK-------KLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 PDLGVGQNITLAVLDTYAHMTR----IDAEAELGSIdQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:PRK13641 91 FQFPEAQLFENTVLKDVEFGPKnfgfSEDEAKEKAL-KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
408-509 |
2.80e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLrg 487
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTL-- 213
|
90 100
....*....|....*....|....*
gi 1067238353 488 dfINDGLTQE---QVLAAALSHNNN 509
Cdd:PRK10938 214 --AETGEREEilqQALVAQLAHSEQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-222 |
3.02e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.73 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYphGTWEGEILWDGQPL---KAQSIRETeaagIVIIHQELTLVPD 96
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY--DIDEGEILLDGHDLrdyTLASLRNQ----VALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 lSVAENI------FMGHELTLPGGRMNYP-----AMLHRAEALMRElkvpdmNVALpvsqYGGGYQQLVEIAKALNKQAR 165
Cdd:PRK11176 432 -TIANNIayarteQYSREQIEEAARMAYAmdfinKMDNGLDTVIGE------NGVL----LSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 166 LLILDEPSSAL-TRGE--IEVLLDIIKglKAKGVacVYISHKLDEVAAVcDTIAVIRDGK 222
Cdd:PRK11176 501 ILILDEATSALdTESEraIQAALDELQ--KNRTS--LVIAHRLSTIEKA-DEILVVEDGE 555
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-205 |
3.10e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF--GGV--NALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPHGtweGEILWDGQPLKAQS---- 75
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTS---GDVIFNGQPMSKLSsaak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 76 --IRETEAAGIVIIHQeltLVPDLSVAENIFMGhelTLPGGRmnypamlHRAEALMRELkvpDMNVALPV--------SQ 145
Cdd:PRK11629 82 aeLRNQKLGFIYQFHH---LLPDFTALENVAMP---LLIGKK-------KPAEINSRAL---EMLAAVGLehranhrpSE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 146 YGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGL-KAKGVACVYISHKL 205
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
261-485 |
3.29e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.90 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRT---ELVSALFGAYPGrynaEVWLEGQVIdTRTPLKS 337
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSttvRLIDGLLEAESG----QIIIDGDLL-TEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPEDRKRQ----GIIPDLGVG-QNITLAvldtYAHM-TRIDAEAELgsidqqISRMHLKTASPSlpitSLSGG 411
Cdd:PRK13650 79 IRHKIGMVFQNPDNQfvgaTVEDDVAFGlENKGIP----HEEMkERVNEALEL------VGMQDFKEREPA----RLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 412 NQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVlGVSNRVLVIGDGQL 485
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
273-484 |
3.62e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 273 DNPKRKRVDDISFVLRRGEILGIAGLVGAGRTelVSAL-----FGAYPGRYNAE-VWLEG---QVID----TRTPLKSIR 339
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKS--VTALalmrlLEQAGGLVQCDkMLLRRrsrQVIElseqSAAQMRHVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 -AGLCMVPEDrKRQGIIPDLGVGQNITLAVlDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVL 418
Cdd:PRK10261 103 gADMAMIFQE-PMTSLNPVFTVGEQIAESI-RLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP-HQLSGGMRQRVMI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 419 AKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-203 |
4.28e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSavyphgtweGEILWD-GQPLKAQSI------- 76
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN---------GEVLLDdGRIIYEQDLivarlqq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 77 ---RETE-------AAGIviihQEltlvpdlsVAENIFMGHELTLPGGRMNYPAMLHRAEALMREL----------KVPD 136
Cdd:PRK11147 74 dppRNVEgtvydfvAEGI----EE--------QAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLdhhnlwqlenRINE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 137 MNVAL------PVSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAkgvACVYISH 203
Cdd:PRK11147 142 VLAQLgldpdaALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISH 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-176 |
4.33e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSF--GGVN---ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSirETE 80
Cdd:COG1101 2 LELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP--PDSGSILIDGKDVTKLP--EYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 AAGIVI-IHQELTL--VPDLSVAENIFMGhelTLPGGRMNY-PAMLHRAEALMRELkVPDMNVAL------PVSQYGGGY 150
Cdd:COG1101 78 RAKYIGrVFQDPMMgtAPSMTIEENLALA---YRRGKRRGLrRGLTKKRRELFREL-LATLGLGLenrldtKVGLLSGGQ 153
|
170 180
....*....|....*....|....*.
gi 1067238353 151 QQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAAL 179
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-218 |
4.93e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.07 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgTWE---GEILWDGQPLKAQSIRETEA---AGIVIIHQ 89
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHvtaDRFRWNGIDLLKLSPRERRKiigREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 ELT--LVPDLSV----AENI----FMGHELTLPGGRMNYP-AMLHRA-----EALMRelkvpdmnvALPvSQYGGGYQQL 153
Cdd:COG4170 97 EPSscLDPSAKIgdqlIEAIpswtFKGKWWQRFKWRKKRAiELLHRVgikdhKDIMN---------SYP-HELTEGECQK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 154 VEIAKALNKQARLLILDEPSSAL---TRGEIEVLLDiiKGLKAKGVACVYISHKLDEVAAVCDTIAVI 218
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMestTQAQIFRLLA--RLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
280-486 |
5.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGqvIDTRTP--LKSIRAGLCMVPEDRKRQ----G 353
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSG--IDTGDFskLQGIRKLVGIVFQNPETQfvgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 354 IIPDLGVG-QNITLAVLDTYAHMTRIDAEAELGSIdqqisRMHlktaSPSlpitSLSGGNQQKAVLAKMLMAKPKVLILD 432
Cdd:PRK13644 95 VEEDLAFGpENLCLPPIEIRKRVDRALAEIGLEKY-----RHR----SPK----TLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 433 EPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEvLGVSNRVLVIGDGQLR 486
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIV 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-215 |
5.19e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMK-VLSAVYPhgtwegeilwdgqplKAQSIRETEAAG 83
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAP---------------DEGVIKRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVPDLSVAENIFMgheLTLPGGRMN--YPAmLHRAEA--LMRElkvpdmnvalPVSQYGGGYQQLVEIAKA 159
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLTVNRFL---RLRPGTKKEdiLPA-LKRVQAghLIDA----------PMQKLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 160 LNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTI 215
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
275-486 |
5.48e-10 |
|
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: 59.19 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 275 PKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIdTRTPlksiraglcmvPEDRkr 351
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEptsGR----IYIGGRDV-TDLP-----------PKDR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 qgiipDLG-VGQNITLavldtYAHMT---------------------RIDAEAELGSIDQQISRmhlktaspsLPiTSLS 409
Cdd:cd03301 73 -----DIAmVFQNYAL-----YPHMTvydniafglklrkvpkdeideRVREVAELLQIEHLLDR---------KP-KQLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 410 GGNQQKAVLAKMLMAKPKVLILDEPTRGVD----VGAKYEIYKLMGALaaeGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03301 133 GGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
.
gi 1067238353 486 R 486
Cdd:cd03301 210 Q 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
276-468 |
5.52e-10 |
|
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: 61.53 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG-AYPGRynAEVWLEGQVIDTRTPlKSIRAGLCMVPEdrkrQGI 354
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTE--GSIAVNGVPLADADA-DSWRDQIAWVPQ----HPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 IPDLGVGQNITLAVLDTYAHMTRIDAE-AELGSIDQQISRMHlktaspSLPI----TSLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:TIGR02857 407 LFAGTIAENIRLARPDASDAEIREALErAGLDEFVAALPQGL------DTPIgeggAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELA 468
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLA 518
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-226 |
6.01e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGqplkaQSIRETE 80
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKG-----ESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 81 A-----AGIVIIHQELTLVPDLSVAEniFMghELTLPGGR--MNYPAM--LHRAEALMRELKVPDM-------NVALPVS 144
Cdd:CHL00131 78 PeerahLGIFLAFQYPIEIPGVSNAD--FL--RLAYNSKRkfQGLPELdpLEFLEIINEKLKLVGMdpsflsrNVNEGFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 145 qygGGYQQLVEIAKALNKQARLLILDEPSSALtrgEIEVLLDIIKG---LKAKGVACVYISHK---LDEVaaVCDTIAVI 218
Cdd:CHL00131 154 ---GGEKKRNEILQMALLDSELAILDETDSGL---DIDALKIIAEGinkLMTSENSIILITHYqrlLDYI--KPDYVHVM 225
|
....*...
gi 1067238353 219 RDGKHIAT 226
Cdd:CHL00131 226 QNGKIIKT 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
283-511 |
6.16e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.78 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 283 ISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrYnaevwlEGQVIDTRTPLKSIraglcmVPEDRKRQgiipdLG-VG 361
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--Y------QGSLKINGIELREL------DPESWRKH-----LSwVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 362 QNITL---AVLDTYAhMTRIDAEAElgSIDQQISRMHLKTASPSLPI----------TSLSGGNQQKAVLAKMLMAKPKV 428
Cdd:PRK11174 430 QNPQLphgTLRDNVL-LGNPDASDE--QLQQALENAWVSEFLPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 429 LILDEPTRGVDvgAKYEiYKLMGAL--AAEGVSIIMVSSELAEVLGVsNRVLVIGDGQL--RGDFinDGLTQEQVL-AAA 503
Cdd:PRK11174 507 LLLDEPTASLD--AHSE-QLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIvqQGDY--AELSQAGGLfATL 580
|
....*...
gi 1067238353 504 LSHNNNDR 511
Cdd:PRK11174 581 LAHRQEEI 588
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
263-481 |
6.25e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.04 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTCydvDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQVIDTRTPlkSIRAGL 342
Cdd:cd03231 2 EADELTC---ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-PLAGRVLLNGGPLDFQRD--SIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 CMVpedrkrqGIIPdlgvGQNITLAVLDTYAHMTRIDAEAelgSIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKML 422
Cdd:cd03231 76 LYL-------GHAP----GIKTTLSVLENLRFWHADHSDE---QVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 423 MAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-497 |
6.98e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 292 ILGIAGLVGAGRTELV---SALFGAYP-GRYNAEVWLEGQVIdTRTPLKSIRAGLCMV---PEDrkrqgiIPDLGVGQNI 364
Cdd:PRK14247 31 ITALMGPSGSGKSTLLrvfNRLIELYPeARVSGEVYLDGQDI-FKMDVIELRRRVQMVfqiPNP------IPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 365 TLAVldtyaHMTRI-DAEAELgsidQQISRMHLKTASP--------SLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:PRK14247 104 ALGL-----KLNRLvKSKKEL----QERVRWALEKAQLwdevkdrlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 436 RGVDVGAKYEIYKLMGALAAEgVSIIMVSSELAEVLGVSNRVLVIGDGQLrgdfINDGLTQE 497
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI----VEWGPTRE 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
295-485 |
7.24e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 295 IAGLVGA---GRTELVSALFGAYPGRYNAEVWlEGQVID-TRTPLKSIRAGLCMVPEDRKRQGIIPDLGVGQNITLAVLD 370
Cdd:PRK13638 29 VTGLVGAngcGKSTLFMNLSGLLRPQKGAVLW-QGKPLDySKRGLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 371 TY-AHMTRIDAEAeLGSIDQQISRMHlktaspslPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKL 449
Cdd:PRK13638 108 VPeAEITRRVDEA-LTLVDAQHFRHQ--------PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1067238353 450 MGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13638 179 IRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
408-498 |
7.53e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLvigdgqlrg 487
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI--------- 223
|
90
....*....|.
gi 1067238353 488 dFINDGLTQEQ 498
Cdd:PRK10619 224 -FLHQGKIEEE 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-204 |
8.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQsiRETEAAGIVIIHQELTLVPDLSV 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPE---KGEILFERQSIKKD--LCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 100 AENIFmgHELTLPGGRMNYpamlhraEALMRELKVPDMnVALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRG 179
Cdd:PRK13540 92 RENCL--YDIHFSPGAVGI-------TELCRLFSLEHL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 1067238353 180 EIEVLLDIIKGLKAKGVACVYISHK 204
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
276-485 |
8.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGaypgrynaeVWLEGQVIDTRTPLKSIRAGLCMVPEDRKRQGII 355
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLING---------LLLPDDNPNSKITVDGITLTAKTVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 ---PDlgvGQNITLAVLDTYA-----------HMTRI--DAEAELGSIDQQisrmhlkTASPSlpitSLSGGNQQKAVLA 419
Cdd:PRK13640 90 fqnPD---NQFVGATVGDDVAfglenravprpEMIKIvrDVLADVGMLDYI-------DSEPA----NLSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 420 KMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGvSNRVLVIGDGQL 485
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKL 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
283-485 |
9.27e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.71 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 283 ISFVLRRGEILGIAGLVGAGRtelvSALFGAYPGRYNAEvwlEGQVIDTRTPLKSIRAGLCMVpedRKRQGIipdlgVGQ 362
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGK----STLFLHFNGILKPT---SGEVLIKGEPIKYDKKSLLEV---RKTVGI-----VFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 363 NItlavlDTYAHMTRIDAEAELGSIDQQISRMHLKT------------ASPSLPITSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:PRK13639 86 NP-----DDQLFAPTVEEDVAFGPLNLGLSKEEVEKrvkealkavgmeGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
259-485 |
9.92e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.23 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVtCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGR---TELVSALFGAYPGrynaEVWLEGQVIDTRTpl 335
Cdd:PRK13632 5 SVMIKVENV-SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKstiSKILTGLLKPQSG----EIKIDGITISKEN-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 336 ksiraglcmVPEDRKRQGII---PDlgvGQNITLAVLDTYA-----------HMTRI--DAEAELGsIDQQISRmhlkta 399
Cdd:PRK13632 78 ---------LKEIRKKIGIIfqnPD---NQFIGATVEDDIAfglenkkvppkKMKDIidDLAKKVG-MEDYLDK------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 400 SPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGV-SIIMVSSELAEVLgVSNRVL 478
Cdd:PRK13632 139 EPQ----NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVI 213
|
....*..
gi 1067238353 479 VIGDGQL 485
Cdd:PRK13632 214 VFSEGKL 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
259-504 |
1.03e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVTC---YDVDNPKRKRVD---DISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVI--- 329
Cdd:PRK15112 2 ETLLEVRNLSKtfrYRTGWFRRQTVEavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 330 DTRTPLKSIRaglcMVPED-------RKRQGIIPDLGVGQNitlavldtyahmTRIDAEAELGSIDQQISRMHLKTASPS 402
Cdd:PRK15112 81 DYSYRSQRIR----MIFQDpstslnpRQRISQILDFPLRLN------------TDLEPEQREKQIIETLRQVGLLPDHAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 403 LPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGAL-AAEGVSIIMVSSELAEVLGVSNRVLVIG 481
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMH 224
|
250 260
....*....|....*....|...
gi 1067238353 482 DGQLrgdfINDGLTQEqVLAAAL 504
Cdd:PRK15112 225 QGEV----VERGSTAD-VLASPL 242
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-184 |
1.10e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.88 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETEAAgIVIIHQELTLVPDlSV 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS--EGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 100 AENIFMGHeltlPGgrmnypAMLHRAEALMRELKVPDMNVALP------VSQYG----GGYQQLVEIAKALNKQARLLIL 169
Cdd:PRK10789 406 ANNIALGR----PD------ATQQEIEHVARLASVHDDILRLPqgydteVGERGvmlsGGQKQRISIARALLLNAEILIL 475
|
170
....*....|....*.
gi 1067238353 170 DEPSSALT-RGEIEVL 184
Cdd:PRK10789 476 DDALSAVDgRTEHQIL 491
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
280-467 |
1.14e-09 |
|
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: 60.84 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGqVIDTRTPLKSIRAGLCMVPEDRKrqgiIPDLG 359
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-QGEVTLDG-VPVSSLDQDEVRRRVSVCAQDAH----LFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLAVLD-TYAHMTRIDAEAELGS-IDQQISRMHLKTASPSlpiTSLSGGNQQKAVLAKMLMAKPKVLILDEPTRG 437
Cdd:TIGR02868 425 VRENLRLARPDaTDEELWAALERVGLADwLRALPDGLDTVLGEGG---ARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 1067238353 438 VDVGAKYEIYKLMGAlAAEGVSIIMVSSEL 467
Cdd:TIGR02868 502 LDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-224 |
1.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 19 NALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYPHgtwEGEILW---DGQPLKAQSIRETEAAGIVI---IHQEL 91
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlLLPD---TGTIEWifkDEKNKKKTKEKEKVLEKLVIqktRFKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 92 TLVPDL--------SVAE-NIFmghELTLPGGRMNYPAML--HRAEALMRELKVPDMnVALPVS-------QYGGGYQQL 153
Cdd:PRK13651 98 KKIKEIrrrvgvvfQFAEyQLF---EQTIEKDIIFGPVSMgvSKEEAKKRAAKYIEL-VGLDESylqrspfELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 154 VEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-195 |
1.52e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHG-TWEGEILWDGQPLKAQSIRETEAagivIIHQELTLVPDLSV 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVLLNGMPIDAKEMRAISA----YVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 100 AEN-IFMGHeLTLPgGRMNYPAMLHRAEALMREL---KVPDMNVALPVSQYG--GGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:TIGR00955 117 REHlMFQAH-LRMP-RRVTKKEKRERVDEVLQALglrKCANTRIGVPGRVKGlsGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180
....*....|....*....|..
gi 1067238353 174 SALTRGEIEVLLDIIKGLKAKG 195
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKG 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
244-461 |
1.58e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 244 REMSNLYPTEPHDVGEVIFEARNVtCYDVDNPKRKRV--DDISFVLRRGEILGIAGLVGAGRTELVSALfgayPGRYNAE 321
Cdd:TIGR00956 742 SDDVNDEKDMEKESGEDIFHWRNL-TYEVKIKKEKRVilNNVDGWVKPGTLTALMGASGAGKTTLLNVL----AERVTTG 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 322 VWLEGQVIDTRTPLKSI---RAGLCmvpedrKRQGI-IPDLGVGQNITL-AVLDTYAHMTRIDAEAELGSIDQQISRMHL 396
Cdd:TIGR00956 817 VITGGDRLVNGRPLDSSfqrSIGYV------QQQDLhLPTSTVRESLRFsAYLRQPKSVSKSEKMEYVEEVIKLLEMESY 890
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 397 KTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLI-LDEPTRGVDVGAKYEIYKLMGALAAEGVSII 461
Cdd:TIGR00956 891 ADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
278-497 |
1.58e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 278 KRVDDISFVLRRGEILGIAGLVGAG--RTELVSALFGAYPGR--YNAEVWLEGQVIDTRT--PLKSIRAGlcmvpedrKR 351
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRrpWRF*TWCANRRALRRTig*HRPVR*G--------RR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 QGIipdlgVGQNiTLAVLDTYAHMTRIDAEAElgsIDQQISRMHLkTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:NF000106 99 ESF-----SGRE-NLYMIGR*LDLSRKDARAR---ADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGdgqlRGDFINDGLTQE 497
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVID----RGRVIADGKVDE 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-222 |
1.75e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.95 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA--------VYPHG--TWEGEILWDgqplkaqsIRETeaAGIVIIHQ 89
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAllipsegkVYVDGldTSDEENLWD--------IRNK--AGMVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 ELTLVPDLsVAENIFMGHEltlpggRMNYPAMLHRA---EAL----MRELK--VPDMnvalpvsqYGGGYQQLVEIAKAL 160
Cdd:PRK13633 95 DNQIVATI-VEEDVAFGPE------NLGIPPEEIRErvdESLkkvgMYEYRrhAPHL--------LSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 161 NKQARLLILDEPSSAL-TRGEIEVLLDIIKGLKAKGVACVYISHKLDEvAAVCDTIAVIRDGK 222
Cdd:PRK13633 160 AMRPECIIFDEPTAMLdPSGRREVVNTIKELNKKYGITIILITHYMEE-AVEADRIIVMDSGK 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-225 |
2.19e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.84 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 4 YLLQMNGIvkSFG----GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKA---QS 75
Cdd:PRK11160 337 VSLTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQ---QGEILLNGQPIADyseAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 76 IReteaAGIVIIHQELTLVPDlSVAENIFMG------HELTlpggrmnypAMLHRA--EALMRELKVPDMNVALPVSQYG 147
Cdd:PRK11160 412 LR----QAISVVSQRVHLFSA-TLRDNLLLAapnasdEALI---------EVLQQVglEKLLEDDKGLNAWLGEGGRQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 148 GGYQQLVEIAKALNKQARLLILDEPSSAL---TRGEI-EVLLDIIKGlkaKGVacVYISHKLDEVAAVcDTIAVIRDGKH 223
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLdaeTERQIlELLAEHAQN---KTV--LMITHRLTGLEQF-DRICVMDNGQI 551
|
..
gi 1067238353 224 IA 225
Cdd:PRK11160 552 IE 553
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-203 |
2.60e-09 |
|
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: 56.39 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 24 IDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEIlwdGQPlkaqsiretEAAGIVIIHQElTLVPDLSVAENI 103
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGS--GRI---GMP---------EGEDLLFLPQR-PYLPLGTLREQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 104 FmgheltlpggrmnYPamlhraeaLMRELkvpdmnvalpvsqyGGGYQQLVEIAKALNKQARLLILDEPSSALTrgeIEV 183
Cdd:cd03223 85 I-------------YP--------WDDVL--------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD---EES 126
|
170 180
....*....|....*....|
gi 1067238353 184 LLDIIKGLKAKGVACVYISH 203
Cdd:cd03223 127 EDRLYQLLKELGITVISVGH 146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-222 |
2.74e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.56 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 18 VNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPhgTwEGEILWDG-QPLKaqsiRETE-AAGI-VIIHQELTL 93
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVP--T-SGEVRVLGyVPFK----RRKEfARRIgVVFGQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 94 VPDLSVAENiFmgheltlpggrmnypamlhraeALMREL-KVPDmnvalpvSQYGGGYQQLVE---IAKALNKQAR---- 165
Cdd:COG4586 108 WWDLPAIDS-F----------------------RLLKAIyRIPD-------AEYKKRLDELVElldLGELLDTPVRqlsl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 166 -----------------LLILDEPssalTRGeievlLDI---------IKGLKAK-GVACVYISHKLDEVAAVCDTIAVI 218
Cdd:COG4586 158 gqrmrcelaaallhrpkILFLDEP----TIG-----LDVvskeairefLKEYNRErGTTILLTSHDMDDIEALCDRVIVI 228
|
....
gi 1067238353 219 RDGK 222
Cdd:COG4586 229 DHGR 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
266-466 |
2.84e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 266 NVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTrtPLKSIRAGLCMV 345
Cdd:PRK13540 3 DVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILFERQSIKK--DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 346 PEdrkRQGIIPDLGVGQNiTLAVLDTYAHMTRIDAEAELGSIDQQISrmhlktaspsLPITSLSGGNQQKAVLAKMLMAK 425
Cdd:PRK13540 80 GH---RSGINPYLTLREN-CLYDIHFSPGAVGITELCRLFSLEHLID----------YPCGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067238353 426 PKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSE 466
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
280-484 |
3.40e-09 |
|
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: 57.06 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRynAEVWL--EGQVIDtrtplksiragLCMVPED-----RKR 351
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYlPDS--GSILVrhDGGWVD-----------LAQASPReilalRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 qgiipDLG-VGQniTLAV------LDTYAH------MTRIDAEAELGSIdqqISRMHLKTASPSLPITSLSGGNQQKAVL 418
Cdd:COG4778 94 -----TIGyVSQ--FLRViprvsaLDVVAEpllergVDREEARARAREL---LARLNLPERLWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 419 AKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-497 |
3.56e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALfgaypGRYN---AEVWLEGQV-------IDTRTPLKSIRAGLCMV- 345
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-----NRMNeleSEVRVEGRVeffnqniYERRVNLNRLRRQVSMVh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 346 PEdrkrqgiiPDLgvgqnITLAVLDTYAHMTRI---DAEAELGSI-----------DQQISRMHlKTAspslpiTSLSGG 411
Cdd:PRK14258 95 PK--------PNL-----FPMSVYDNVAYGVKIvgwRPKLEIDDIvesalkdadlwDEIKHKIH-KSA------LDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 412 NQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEG-VSIIMVSSELAEVLGVSNRVLVIGDGQLR-GDF 489
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNENRiGQL 234
|
....*...
gi 1067238353 490 INDGLTQE 497
Cdd:PRK14258 235 VEFGLTKK 242
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
282-485 |
3.74e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSaLFGAYPGRYNAEVWLEGQVIDTRTplKSIRAGLcmvpedRKRQ-GII----- 355
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTSGDVIFNGQPMSKLS--SAAKAEL------RNQKlGFIyqfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 --PDLGVGQNITLAVLdtYAHMTRIDAEAELGSIDQQISRMHLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDE 433
Cdd:PRK11629 98 llPDFTALENVAMPLL--IGKKKPAEINSRALEMLAAVGLEHRANHRPS----ELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 434 PTRGVDVGAKYEIYKLMGAL-AAEGVSIIMVSSELaEVLGVSNRVLVIGDGQL 485
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRL 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-215 |
3.99e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 28 VKPGECVGLCGENGAGKSTLMKVL---------SAVYPhGTWegEILWDGQPLKAQSIRETEaagIVI--IHQELTLVPD 96
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLkneisadggSYTFP-GNW--QLAWVNQETPALPQPALE---YVIdgDREYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFMGHELTLPGGRMNYP---AMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:PRK10636 98 LHDANERNDGHAIATIHGKLDAIdawTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1067238353 174 SALtrgEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTI 215
Cdd:PRK10636 178 NHL---DLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-225 |
4.49e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 10 GIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVypHGTWEGEILWDGqplkaQSIRETEAA--GIVII 87
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGDLFIGE-----KRMNDVPPAerGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 88 HQELTLVPDLSVAENIFMGheLTLPGG-------RMNYPA-MLHRAEALMRELKvpdmnvALpvsqyGGGYQQLVEIAKA 159
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFG--LKLAGAkkeeinqRVNQVAeVLQLAHLLDRKPK------AL-----SGGQRQRVAIGRT 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 160 LNKQARLLILDEPSSALTRG-EIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIrDGKHIA 225
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL-DAGRVA 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-256 |
4.52e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVyphGTWEGEILWDGQ-PLKAQSIRETEA--- 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM---NELESEVRVEGRvEFFNQNIYERRVnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 ---AGIVIIHQELTLVPdLSVAENIFMGHELTLPGGRMNYPAMLH---RAEALMRELKVPDMNVALPVSqygGGYQQLVE 155
Cdd:PRK14258 85 rlrRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVEsalKDADLWDEIKHKIHKSALDLS---GGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKG-VACVYISHKLDEVAAVCDTIAVIRDGKHiattamadmdi 234
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNEN----------- 229
|
250 260
....*....|....*....|..
gi 1067238353 235 prIITQMVGREMSNLYPTEPHD 256
Cdd:PRK14258 230 --RIGQLVEFGLTKKIFNSPHD 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-232 |
4.77e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSF---------GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPL---- 71
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS--GELLIDDHPLhfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 72 ---KAQSIReteaagivIIHQEltlvPDLSVAENIFMGHELTLP---GGRMNYPAMLHRAEALMRELKV-PDMNVALPvS 144
Cdd:PRK15112 82 ysyRSQRIR--------MIFQD----PSTSLNPRQRISQILDFPlrlNTDLEPEQREKQIIETLRQVGLlPDHASYYP-H 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 145 QYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGKH 223
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
....*....
gi 1067238353 224 IATTAMADM 232
Cdd:PRK15112 229 VERGSTADV 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
253-464 |
5.11e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.67 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 253 EPHDVGEVIFEarNVTcydVDNP-KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrynaevWLEGQVI-- 329
Cdd:COG4178 356 ETSEDGALALE--DLT---LRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP-------YGSGRIArp 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 330 -DTRT---------PLKSIRAGLCMvPEDRKRqgiIPDLGVGQNITLAVLDTYAHmtRIDAEAELGSIdqqisrmhlkta 399
Cdd:COG4178 424 aGARVlflpqrpylPLGTLREALLY-PATAEA---FSDAELREALEAVGLGHLAE--RLDEEADWDQV------------ 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 400 spslpitsLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLmgaLAAEGVSIIMVS 464
Cdd:COG4178 486 --------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELPGTTVIS 539
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
259-485 |
5.12e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVTcYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTplksi 338
Cdd:PRK13635 3 EEIIRVEHIS-FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMVLSEET----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 raglcmVPEDRKRQGII---PDlgvGQNITLAVLDTYA---HMTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGN 412
Cdd:PRK13635 76 ------VWDVRRQVGMVfqnPD---NQFVGATVQDDVAfglENIGVPREEMVERVDQALRQVGMEDFLNREP-HRLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 413 QQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGvSNRVLVIGDGQL 485
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
290-484 |
7.56e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 290 GEILGIAGLVGAGRTELVSALfgayPGRYNAEVWLEGQVIDTRTPLKSIRAGLCMVPEDrkrQGIIPDLGVGQNITL-AV 368
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL----AGRIQGNNFTGTILANNRKPTKQILKRTGFVTQD---DILYPHLTVRETLVFcSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 369 LDTYAHMTRidaEAELGSIDQQISRMHLKTASPSLP----ITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKY 444
Cdd:PLN03211 167 LRLPKSLTK---QEKILVAESVISELGLTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067238353 445 EIYKLMGALAAEGVSIIM-VSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-225 |
7.82e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.67 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIREteaagiviIHQELTLV-- 94
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL--PQRGRVKVMGREVNAENEKW--------VRSKVGLVfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 -PD-----LSVAENIFMG-HELTLPGGRMNypamlHRAEALMRELKVPDMNVALPvSQYGGGYQQLVEIAKALNKQARLL 167
Cdd:PRK13647 87 dPDdqvfsSTVWDDVAFGpVNMGLDKDEVE-----RRVEEALKAVRMWDFRDKPP-YHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 168 ILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIA 225
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
263-485 |
1.03e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.03 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTC-YDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIdTRTPlksi 338
Cdd:COG3842 7 ELENVSKrYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdsGR----ILLDGRDV-TGLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 raglcmvPEDRkrqgiipdlGVG---QNitlavldtYA---HMT-----------RIDAEAElgsIDQQISRM------- 394
Cdd:COG3842 74 -------PEKR---------NVGmvfQD--------YAlfpHLTvaenvafglrmRGVPKAE---IRARVAELlelvgle 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 395 HLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAK----YEIYKLmgaLAAEGVSIIMVSSELAEV 470
Cdd:COG3842 127 GLADRYPH----QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLReemrEELRRL---QRELGITFIYVTHDQEEA 199
|
250
....*....|....*
gi 1067238353 471 LGVSNRVLVIGDGQL 485
Cdd:COG3842 200 LALADRIAVMNDGRI 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-514 |
1.09e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLrg 487
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRL-- 240
|
90 100
....*....|....*....|....*..
gi 1067238353 488 dfINDGLTQEqvLAAALSHNNNDRKTA 514
Cdd:PRK14271 241 --VEEGPTEQ--LFSSPKHAETARYVA 263
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
265-502 |
1.13e-08 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 55.70 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 265 RNVTcYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALfgayPGRYNAEvwlEGQV----IDTRT-PLKSIR 339
Cdd:cd03251 4 KNVT-FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYDVD---SGRIlidgHDVRDyTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 AGLCMVPEDRkrqgIIPDLGVGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMHLKTASPslpI----TSLSGGNQQK 415
Cdd:cd03251 76 RQIGLVSQDV----FLFNDTVAENIAYGRPG--ATREEVEEAARAANAHEFIMELPEGYDTV---IgergVKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 416 AVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIImVSSELAEVLGvSNRVLVIGDGQLrgdfINDGlT 495
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKI----VERG-T 219
|
....*..
gi 1067238353 496 QEQVLAA 502
Cdd:cd03251 220 HEELLAQ 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
408-485 |
1.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 1.28e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-209 |
1.30e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 3 DYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSavyphgtweGEilwdGQPlKAQSIRETEAA 82
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT---------GQ----EQP-DSGTIEIGETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 GIVIIHQEL-TLVPDLSVAENIFMGHELTLPGGR-MNYPAMLHRAealmrELKVPDMNValPVSQYGGGYQQLVEIAKAL 160
Cdd:TIGR03719 386 KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKReIPSRAYVGRF-----NFKGSDQQK--KVGQLSGGERNRVHLAKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 161 NKQARLLILDEPSSALtrgEIEVLLDIIKGLKAKGVACVYISHK---LDEVA 209
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHDrwfLDRIA 507
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
260-504 |
1.49e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.55 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 260 VIFEARNVTcydVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGRynaeVWLEGQvidtrtPLK 336
Cdd:PRK13548 1 AMLEARNLS---VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGelsPDSGE----VRLNGR------PLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 SIRaglcmvPEDR-KRQGIIPdlgvgQNITLA----VLD-----TYAHMTRIDAEAELgsIDQQISRM---HLKtaspSL 403
Cdd:PRK13548 68 DWS------PAELaRRRAVLP-----QHSSLSfpftVEEvvamgRAPHGLSRAEDDAL--VAAALAQVdlaHLA----GR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLM------AKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNR 476
Cdd:PRK13548 131 DYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADR 210
|
250 260
....*....|....*....|....*...
gi 1067238353 477 VLVIGDGQLRGdfinDGlTQEQVLAAAL 504
Cdd:PRK13548 211 IVLLHQGRLVA----DG-TPAEVLTPET 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
261-503 |
1.77e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.58 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVtCYDVDNpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIdTRTPLKSIRA 340
Cdd:PRK13652 3 LIETRDL-CYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGEPI-TKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 341 GLCMVPEDRKRQGIIPDlgVGQNITLAV----LDTYAHMTRIDAEAELGSIDqqisrmHLKTASPSlpitSLSGGNQQKA 416
Cdd:PRK13652 79 FVGLVFQNPDDQIFSPT--VEQDIAFGPinlgLDEETVAHRVSSALHMLGLE------ELRDRVPH----HLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 417 VLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD-FINDGL 494
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYgTVEEIF 226
|
....*....
gi 1067238353 495 TQEQVLAAA 503
Cdd:PRK13652 227 LQPDLLARV 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
407-485 |
2.08e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.07 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 407 SLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-221 |
2.25e-08 |
|
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: 54.64 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 9 NGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMkvLSAVYPHGTWEGEILWDGQPLKAQSIRETEAA--GIVI 86
Cdd:cd03290 5 NGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 87 IHQELTLVPDLSVAENIFMGHeltlPGGRMNYPAMLHrAEALMrelkvPDMNVaLPV---SQYG-------GGYQQLVEI 156
Cdd:cd03290 83 YAAQKPWLLNATVEENITFGS----PFNKQRYKAVTD-ACSLQ-----PDIDL-LPFgdqTEIGerginlsGGQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 157 AKALNKQARLLILDEPSSALTRGEIEVLLD--IIKGLKAKGVACVYISHKLDEVAAVcDTIAVIRDG 221
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHA-DWIIAMKDG 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
263-484 |
2.39e-08 |
|
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: 54.85 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVT-CYdvdnPKRKRV---DDISFVLRRGEILGIAGLVGAGRTELVSALFgaypgRY----NAEVWLEGQviDTRT- 333
Cdd:cd03249 2 EFKNVSfRY----PSRPDVpilKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-----RFydptSGEILLDGV--DIRDl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 334 PLKSIRAGLCMVPEDrkrqgiiPDL---GVGQNITLAvlDTYAHMTRIDAEAELGSIDQQISrmhlktaspSLPI----- 405
Cdd:cd03249 71 NLRWLRSQIGLVSQE-------PVLfdgTIAENIRYG--KPDATDEEVEEAAKKANIHDFIM---------SLPDgydtl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 -----TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKlmgAL--AAEGVSIIMVSSELAEVLGvSNRVL 478
Cdd:cd03249 133 vgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQE---ALdrAMKGRTTIVIAHRLSTIRN-ADLIA 208
|
....*.
gi 1067238353 479 VIGDGQ 484
Cdd:cd03249 209 VLQNGQ 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
280-485 |
2.62e-08 |
|
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: 56.23 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTelVSA-----LFGAYPGRYNAEVWLEGQVIDTRTP--LKSIRAGlcmvpedrkRQ 352
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKS--VTAlsilrLLPDPAAHPSGSILFDGQDLLGLSEreLRRIRGN---------RI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 353 GII---------PDLGVGQNITlAVLDTYAHMTRIDAEAElgsIDQQISRMHLKtaSPSLPITS----LSGGNQQKAVLA 419
Cdd:COG4172 95 AMIfqepmtslnPLHTIGKQIA-EVLRLHRGLSGAAARAR---ALELLERVGIP--DPERRLDAyphqLSGGQRQRVMIA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 420 KMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
280-486 |
2.69e-08 |
|
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: 56.30 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEVWLEGQVIDTRTPlksiraglcmvpedrkrqgiiP 356
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptaG----SVRLDGADLSQWDR---------------------E 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLG--VG---QNITLavLDtyahmtridaeaelGSIDQQISRMhlKTASP-----------------SLP------I--- 405
Cdd:COG4618 403 ELGrhIGylpQDVEL--FD--------------GTIAENIARF--GDADPekvvaaaklagvhemilRLPdgydtrIgeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 -TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAeVLGVSNRVLVIGDGQ 484
Cdd:COG4618 465 gARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGR 543
|
..
gi 1067238353 485 LR 486
Cdd:COG4618 544 VQ 545
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
280-483 |
2.72e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.14 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVIDTRTpLKSIRAGLCMV---PEDRKRQGIIP 356
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNQAITDDN-FEKLRKHIGIVfqnPDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 -DLGVG-QNITLAvldtYAHMTRIDAEA--ELGSIDQQISRMHlktaspslpitSLSGGNQQKAVLAKMLMAKPKVLILD 432
Cdd:PRK13648 103 yDVAFGlENHAVP----YDEMHRRVSEAlkQVDMLERADYEPN-----------ALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 433 EPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGvSNRVLVIGDG 483
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-232 |
2.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY--PHGTWE-GEILWDGQPLKAQSIRETEAAGIVIIHQELTLVPD 96
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqpTEGKVTvGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFmgheltlpgGRMNYPAMLHRAEALMRE-LKVPDMNVAL----PVsQYGGGYQQLVEIAKALNKQARLLILDE 171
Cdd:PRK13643 101 TVLKDVAF---------GPQNFGIPKEKAEKIAAEkLEMVGLADEFweksPF-ELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 172 PSSALT-RGEIEvLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMADM 232
Cdd:PRK13643 171 PTAGLDpKARIE-MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
263-464 |
3.20e-08 |
|
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: 53.90 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTCydvDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGrynaevwLEGQVIDTRTPLKSIRagl 342
Cdd:TIGR01189 2 AARNLAC---SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-------DSGEVRWNGTPLAEQR--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 cmvpEDRKRQ--------GIIPDLGVGQNitlavLDTYAHmtriDAEAELGSIDQQISRMHLkTASPSLPITSLSGGNQQ 414
Cdd:TIGR01189 69 ----DEPHENilylghlpGLKPELSALEN-----LHFWAA----IHGGAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 415 KAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVS 464
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTT 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-440 |
3.63e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.10 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 4 YLLQMNGIVKSF-GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVyphgtwEGEIlwDGQPLKAQSIReteaa 82
Cdd:TIGR03719 3 YIYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDF--NGEARPQPGIK----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 83 gIVIIHQELTLVPDLSVAENIFMG---------------HELTLPGGRMNYPA-----------------MLHRAEALMR 130
Cdd:TIGR03719 70 -VGYLPQEPQLDPTKTVRENVEEGvaeikdaldrfneisAKYAEPDADFDKLAaeqaelqeiidaadawdLDSQLEIAMD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 131 ELKVPDMNvaLPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAa 210
Cdd:TIGR03719 149 ALRCPPWD--ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVA- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 211 vcDTIAVIRDGKHI-----------------ATTAMADMDIPRIITQMV--------GR------------EMSN----- 248
Cdd:TIGR03719 226 --GWILELDRGRGIpwegnysswleqkqkrlEQEEKEESARQKTLKRELewvrqspkGRqakskarlaryeELLSqefqk 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 249 ------LY-PTEPHdVGEVIFEARNVT-CYDvdnpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAypgryna 320
Cdd:TIGR03719 304 rnetaeIYiPPGPR-LGDKVIEAENLTkAFG----DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 321 evwlegqvidtRTPLK-SIRAG----LCMVpeDRKRQGIIPDLGVGQNITlavlDTYAHMtridaeaELGSID----QQI 391
Cdd:TIGR03719 372 -----------EQPDSgTIEIGetvkLAYV--DQSRDALDPNKTVWEEIS----GGLDII-------KLGKREipsrAYV 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1067238353 392 SRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDV 440
Cdd:TIGR03719 428 GRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-195 |
3.81e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgTWEGEILWDGQPLKAQSIRETEA-AGiviiHQElTLV 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGDIDDPDVAEACHyLG----HRN-AMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDLSVAENI-----FMGHELTLPggrmnypamlhrAEALMRelkvpdMNVA----LPVSQYGGGYQQLVEIAKALNKQAR 165
Cdd:PRK13539 86 PALTVAENLefwaaFLGGEELDI------------AAALEA------VGLAplahLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|
gi 1067238353 166 LLILDEPSSALTRGEIEVLLDIIKGLKAKG 195
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQG 177
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-507 |
3.99e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 55.90 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYnaevwleGQVIDTRTPLKSI-----RAGLCMVPEDRKR 351
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS-------GEILLNGFSLKDIdrhtlRQFINYLPQEPYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 -QGIIPD---LGVGQNITlavldtyahMTRIDAEAELGSIDQQISRMHLK-TASPSLPITSLSGGNQQKAVLAKMLMAKP 426
Cdd:TIGR01193 560 fSGSILEnllLGAKENVS---------QDEIWAACEIAEIKDDIENMPLGyQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 427 KVLILDEPTRGVDVGAKYEIYKLMGALAAEgvSIIMVSSELaEVLGVSNRVLVIGDGQLRGDFINDGLTQEQVLAAALSH 506
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
.
gi 1067238353 507 N 507
Cdd:TIGR01193 708 N 708
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-224 |
4.37e-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: 53.42 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPH-GTWEGEILWDGQPLKaqSIRETEAAGIVIIHQELTLVPDLSV 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGIPYK--EFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 100 AENI-FmghELTLPGGRMnypamlhraealmrelkvpdmnvalpVSQYGGGYQQLVEIAKALNKQARLLILDEPssalTR 178
Cdd:cd03233 101 RETLdF---ALRCKGNEF--------------------------VRGISGGERKRVSIAEALVSRASVLCWDNS----TR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 179 G-EIEVLLDIIKGLK-----AKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:cd03233 148 GlDSSTALEILKCIRtmadvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-222 |
4.46e-08 |
|
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: 56.18 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 11 IVKSF--GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQSIRETEAAGIVIIH 88
Cdd:TIGR01257 934 LVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 89 QelTLVPDLSVAENIFMGHELTlpgGRMNYPAMLhRAEALMRELKVPDMNVAlPVSQYGGGYQQLVEIAKALNKQARLLI 168
Cdd:TIGR01257 1012 N--ILFHHLTVAEHILFYAQLK---GRSWEEAQL-EMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 169 LDEPSSALTRGEIEVLLDIIKGLKAkGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-222 |
5.08e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 53.24 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLmkvLSAVYphgtweGEIlwdgQPLKaqsireteaaGIVIIHQELTLVP---- 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSL---LSALL------GEL----EKLS----------GSVSVPGSIAYVSqepw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 --DLSVAENIFMGHELtlpggrmnYPAMLH---RAEALMRELKVpdmnvaLP------VSQYG----GGYQQLVEIAKAL 160
Cdd:cd03250 77 iqNGTIRENILFGKPF--------DEERYEkviKACALEPDLEI------LPdgdlteIGEKGinlsGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 161 NKQARLLILDEPSSALtrgEIEVLLDI----IKGLKAKGVACVYISHKLdEVAAVCDTIAVIRDGK 222
Cdd:cd03250 143 YSDADIYLLDDPLSAV---DAHVGRHIfencILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
281-488 |
5.40e-08 |
|
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: 53.59 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALFG---AYPGrynaEVWLEGQVIdtrTPL-KSIRAGLcmvpedRKRQ-GIi 355
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGldrPTSG----TVRLAGQDL---FALdEDARARL------RARHvGF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 pdlgVGQNITLavldtYAHMTRID-----------------AEAELGsidqqisRM---HLKTASPSlpitSLSGGNQQK 415
Cdd:COG4181 95 ----VFQSFQL-----LPTLTALEnvmlplelagrrdararARALLE-------RVglgHRLDHYPA----QLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 416 AVLAKMLMAKPKVLILDEPTRGVD--VGAKyeIYKLMGALAAE-GVSIIMVSS--ELAEvlgVSNRVLVIGDGQLRGD 488
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFELNRErGTTLVLVTHdpALAA---RCDRVLRLRAGRLVED 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-222 |
5.46e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.09 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLmkvLSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGIVIIHQELtlvp 95
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 dlsvaenIFMGhelTLpggRMNY-PAMLHRAEALMR---ELKVPDMNVALP-----VSQYGG-----GYQQLVEIAKALN 161
Cdd:cd03289 88 -------IFSG---TF---RKNLdPYGKWSDEEIWKvaeEVGLKSVIEQFPgqldfVLVDGGcvlshGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 162 KQARLLILDEPSSALTRGEIEVlldIIKGLKAKGVACVYI--SHKLdEVAAVCDTIAVIRDGK 222
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQV---IRKTLKQAFADCTVIlsEHRI-EAMLECQRFLVIEENK 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
280-488 |
5.56e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.93 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVidtrTPLKSIRAGLcmvpedrkrqgiIP 356
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsGR----VEVNGRV----SALLELGAGF------------HP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DLGVGQNITL--AVL-----DTYAHMTRIDAEAELGS-IDQQIsrmhlKTASpslpitslSGgnqQKAVL--AKMLMAKP 426
Cdd:COG1134 102 ELTGRENIYLngRLLglsrkEIDEKFDEIVEFAELGDfIDQPV-----KTYS--------SG---MRARLafAVATAVDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 427 KVLILDEptrGVDVG-----AKyeIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGD 488
Cdd:COG1134 166 DILLVDE---VLAVGdaafqKK--CLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
275-485 |
7.09e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.92 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 275 PKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGaypgrynaevwLE----GQVIDTRTPL--------KSIRAGL 342
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-----------LEspsqGNVSWRGEPLaklnraqrKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 CMVPED-------RKRQGIIpdlgvgqnitlaVLDTYAHMTRIDAEAELGSIDQQISRMHLKTASPS-LPiTSLSGGNQQ 414
Cdd:PRK10419 92 QMVFQDsisavnpRKTVREI------------IREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRP-PQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 415 KAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
261-488 |
7.21e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.57 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVT-CYDvDNPKrkrVDDISFVLRRGEILGIAGLVGAGRT---ELVSALFGAYPGrynaEVWLEGQVIdTRTPlk 336
Cdd:PRK09452 14 LVELRGISkSFD-GKEV---ISNLDLTINNGEFLTLLGPSGCGKTtvlRLIAGFETPDSG----RIMLDGQDI-THVP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 siraglcmvPEDRkrqgiiPDLGVGQNITLavldtYAHMTRID-----------AEAELGSIDQQISRM-HLKTASPSLP 404
Cdd:PRK09452 83 ---------AENR------HVNTVFQSYAL-----FPHMTVFEnvafglrmqktPAAEITPRVMEALRMvQLEEFAQRKP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 405 iTSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDvgakyeiYKLMGALAAE--------GVSIIMVSSELAEVLGVSNR 476
Cdd:PRK09452 143 -HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD-------YKLRKQMQNElkalqrklGITFVFVTHDQEEALTMSDR 214
|
250
....*....|..
gi 1067238353 477 VLVIGDGQLRGD 488
Cdd:PRK09452 215 IVVMRDGRIEQD 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
280-486 |
7.28e-08 |
|
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: 55.40 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAyPGRYNAEVWLEGQVIDTRTPLKSIRAGLCmvpedrKRQGIIPDLG 359
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGKSILTNISDVHQNMGYC------PQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNitlaVLDTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLPITsLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD 439
Cdd:TIGR01257 2028 TGRE----HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067238353 440 VGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
277-485 |
7.63e-08 |
|
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: 53.46 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRT---ELVSALFGAYPGrynaEVWLEGQVIDTRTPLKsIRAGLCMVPEdrkRQG 353
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTttmKMINRLIEPTSG----EIFIDGEDIREQDPVE-LRRKIGYVIQ---QIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 354 IIPDLGVGQNITLA-VLDTYAHMTRIDAEAELgsidqqISRMHLKTAS-----PSlpitSLSGGNQQKAVLAKMLMAKPK 427
Cdd:cd03295 86 LFPHMTVEENIALVpKLLKWPKEKIRERADEL------LALVGLDPAEfadryPH----ELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-224 |
8.34e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQsireTEAAGIVIIHQELTLV---PDL 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS--GTITIAGYHITPE----TGNKNLKKLRKKVSLVfqfPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SVAENIFMGhelTLPGGRMNYPAMLHRAE--AL--MRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:PRK13641 97 QLFENTVLK---DVEFGPKNFGFSEDEAKekALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 174 SALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
263-485 |
9.15e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTCYdvdnPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPG---RYNAEVWLEGQVIDTRTpLKSIR 339
Cdd:PRK10418 6 ELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVAPCA-LRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 AGLCMvpeDRKRQGIIP-----DLGVGQNITLAVLDTYAHMTRIDAEAELGSiDQQISRMHlktaspslPItSLSGGNQQ 414
Cdd:PRK10418 81 IATIM---QNPRSAFNPlhtmhTHARETCLALGKPADDATLTAALEAVGLEN-AARVLKLY--------PF-EMSGGMLQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 415 KAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
259-439 |
9.63e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVTcyDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAyPGRYNAEVWlegqvidtrtPLKSI 338
Cdd:TIGR03719 2 QYIYTMNRVS--KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGEAR----------PQPGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 RAGlcMVPEDRKrqgIIPDLGVGQNITLAVLDTYAHMTRIDA------------------EAELGSI---------DQQI 391
Cdd:TIGR03719 69 KVG--YLPQEPQ---LDPTKTVRENVEEGVAEIKDALDRFNEisakyaepdadfdklaaeQAELQEIidaadawdlDSQL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 392 SR-MH-LKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD 439
Cdd:TIGR03719 144 EIaMDaLRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
277-464 |
1.25e-07 |
|
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: 51.39 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgrynaevWLEGQVIDTRtplksiRAGLCMVPedrkRQGIIP 356
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP-------WGSGRIGMPE------GEDLLFLP----QRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 357 DlgvgqnitlavldtyahmtridaeaelGSIDQQISRMHLKTaspslpitsLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:cd03223 77 L---------------------------GTLREQLIYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*...
gi 1067238353 437 GVDVGAKYEIYKLmgaLAAEGVSIIMVS 464
Cdd:cd03223 121 ALDEESEDRLYQL---LKELGITVISVG 145
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
282-470 |
1.27e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALFGaYPGRYNAEVWLEGQVIDtrtplKSIRAGL-CMVPEDRKRQGIIPDLGV 360
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMG-FVRLASGKISILGQPTR-----QALQKNLvAYVPQSEEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 361 gqniTLAVLDTYAHM--TRIDAEAELGSIDQQISRMHLKTASPSlPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGV 438
Cdd:PRK15056 99 ----DVVMMGRYGHMgwLRRAKKRDRQIVTAALARVDMVEFRHR-QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|..
gi 1067238353 439 DVGAKYEIYKLMGALAAEGVSIIMVSSELAEV 470
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSV 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-246 |
1.31e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTlmkvlSAVYPH--GTWEGEILWDGQPLKA--QSIRETea 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAHv*GPDAGRRPWRF*TWCAnrRALRRT-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 agiVIIHQELTL--VPDLSVAENIFM-GHELTLpgGRMNYPAmlhRAEALMRELKVPDMnVALPVSQYGGGYQQLVEIAK 158
Cdd:NF000106 87 ---IG*HRPVR*grRESFSGRENLYMiGR*LDL--SRKDARA---RADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 159 ALNKQARLLILDEPSSAL---TRGEIevlLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIRDGKhiattAMADMDIP 235
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLdprTRNEV---WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR-----VIADGKVD 229
|
250
....*....|.
gi 1067238353 236 RIITQMVGREM 246
Cdd:NF000106 230 ELKTKVGGRTL 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
400-464 |
1.33e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 1.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 400 SPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAkyeIYKLMGALAAEGVSIIMVS 464
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIFIS 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
408-513 |
1.36e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.83 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLvigdgqlrg 487
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI--------- 215
|
90 100
....*....|....*....|....*.
gi 1067238353 488 dFINDGLTQEQVLAAALSHNNNDRKT 513
Cdd:PRK11264 216 -FMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-224 |
1.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEgEILWDGQ-PLKAQSIRETE----AAGIVIIHQELTLV 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAiPANLKKIKEVKrlrkEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDlSVAENIFMGhELTLPGgrmNYPAMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSS 174
Cdd:PRK13645 105 QE-TIEKDIAFG-PVNLGE---NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 175 ALT-RGEiEVLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:PRK13645 180 GLDpKGE-EDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
408-485 |
2.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 2.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
254-504 |
2.53e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.57 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 254 PHDVGEVIFeaRNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGrynaevwlEGQVIDTR 332
Cdd:TIGR00958 473 LNLEGLIEF--QDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPT--------GGQVLLDG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 333 TPL-----KSIRAGLCMVPEDrkrqgiiPDL---GVGQNITLAVldTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLP 404
Cdd:TIGR00958 543 VPLvqydhHYLHRQVALVGQE-------PVLfsgSVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 405 ITS-LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMgalAAEGVSIIMVSSELAEVLGvSNRVLVIGDG 483
Cdd:TIGR00958 614 KGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKG 689
|
250 260
....*....|....*....|.
gi 1067238353 484 QLRGDFINDGLTQEQVLAAAL 504
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-222 |
2.67e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 15 FGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGT---WEGEILWDGQPL-KAQSIRETEAAgIVIIHQE 90
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyrYSGDVLLGGRSIfNYRDVLEFRRR-VGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 91 LTLVPdLSVAENIFMG---HELtLPggRMNYPAMlhrAEALMRELKVPDM---NVALPVSQYGGGYQQLVEIAKALNKQA 164
Cdd:PRK14271 110 PNPFP-MSIMDNVLAGvraHKL-VP--RKEFRGV---AQARLTEVGLWDAvkdRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 165 RLLILDEPSSALTRGEIEVLLDIIKGLkAKGVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGR 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
409-479 |
2.91e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.27 E-value: 2.91e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 409 SGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLV 479
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMV 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
277-484 |
3.00e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTelVSALF---------GAYPG---RYNAEVWLEGqviDTRTpLKSIRAG-LC 343
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKS--VTALSilrllpsppVVYPSgdiRFHGESLLHA---SEQT-LRGVRGNkIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 344 MVpedrkRQGIIPDLGVGQNI--TLA-VLDTYAHMTRidaEAELGSIDQQISRMHLKTASPSL---PiTSLSGGNQQKAV 417
Cdd:PRK15134 96 MI-----FQEPMVSLNPLHTLekQLYeVLSLHRGMRR---EAARGEILNCLDRVGIRQAAKRLtdyP-HQLSGGERQRVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 418 LAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-216 |
3.03e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 3 DYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKV---LSAVYPHGTWEGEILWDGQPLKAQSIRET 79
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 80 EA-AGIVIIHQELTLVPDlSVAENIFMGHELTlpGGRMNYPAMLHRA---EALMRELKVPDMNVALPVSqygGGYQQLVE 155
Cdd:PRK14243 88 EVrRRIGMVFQKPNPFPK-SIYDNIAYGARIN--GYKGDMDELVERSlrqAALWDEVKDKLKQSGLSLS---GGQQQRLC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 156 IAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKgVACVYISHKLDEVAAVCDTIA 216
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTA 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
278-479 |
3.13e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.43 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 278 KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GrynaEVWLEGQVIDT--RTPLKSIRAGLCMVPED---- 348
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEptsG----EILFDGQDITGlsGRELRPLRRRMQMVFQDpyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 349 ---RKR-----------QGIIPDLGVGQNItLAVLDT----------YAHMtridaeaelgsidqqisrmhlktaspslp 404
Cdd:COG4608 108 lnpRMTvgdiiaeplriHGLASKAERRERV-AELLELvglrpehadrYPHE----------------------------- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067238353 405 itsLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLV 479
Cdd:COG4608 158 ---FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAV 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
408-485 |
3.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 3.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-224 |
3.25e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 15 FGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKV---LSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGIV-IIHQE 90
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRREVgMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 91 LTLVPDLSVAENIFMGHELT-LPGGRMNYPAMLHRA---EALMRELKvpDMNVALPVSQYGGGYQQLVeIAKALNKQARL 166
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNgLVKSKKELDERVEWAlkkAALWDEVK--DRLNDYPSNLSGGQRQRLV-IARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 167 LILDEPSSAL---TRGEIEVLLDIIKglkaKGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:PRK14267 171 LLMDEPTANIdpvGTAKIEELLFELK----KEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
408-484 |
3.33e-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: 3.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAkyeIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
248-450 |
4.23e-07 |
|
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: 50.93 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 248 NLYPTepHDVGEVIFeaRNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQ 327
Cdd:cd03248 2 SLAPD--HLKGIVKF--QNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVLLDGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 328 VIdTRTPLKSIRAGLCMVPEDrkrqgiiPDL---GVGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMhlktasPSLP 404
Cdd:cd03248 77 PI-SQYEHKYLHSKVSLVGQE-------PVLfarSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISEL------ASGY 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 405 ITS-------LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLM 450
Cdd:cd03248 141 DTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
5.27e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA-VYP-HGT---WEGEILWDGQPLKAQSIRETeaAGIVIIHQELTLV 94
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGlLQPtSGTvtiGERVITAGKKNKKLKPLRKK--VGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 95 PDlSVAENIFMGheltlPggrMNYPAMLHRAEALMRE-LKVpdmnVALPVS-------QYGGGYQQLVEIAKALNKQARL 166
Cdd:PRK13634 100 EE-TVEKDICFG-----P---MNFGVSEEDAKQKAREmIEL----VGLPEEllarspfELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 167 LILDEPSSALT-RGEIEvLLDIIKGL-KAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIAT 226
Cdd:PRK13634 167 LVLDEPTAGLDpKGRKE-MMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
263-502 |
5.56e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 52.03 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTcydVDNPKRKR--VDDISFVLRRGEILGIAGLVGAGRTELVSALfgayPGRYN---AEVWLEGQVIDTRTpLKS 337
Cdd:TIGR02203 332 EFRNVT---FRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLI----PRFYEpdsGQILLDGHDLADYT-LAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPEDRkrqgIIPDLGVGQNITLAVLDTYAhMTRIDAEAELGSIDQQISRMHLKTASPslpITS----LSGGNQ 413
Cdd:TIGR02203 404 LRRQVALVSQDV----VLFNDTIANNIAYGRTEQAD-RAEIERALAAAYAQDFVDKLPLGLDTP---IGEngvlLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 414 QKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGvSNRVLVIGDGQLrgdfINDG 493
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI----VERG 549
|
....*....
gi 1067238353 494 lTQEQVLAA 502
Cdd:TIGR02203 550 -THNELLAR 557
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
283-486 |
6.31e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 283 ISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQVI-----DTRTPLKSIRAGLCMvpedrKRQGIIPD 357
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-SGEVSLVGQPLhqmdeEARAKLRAKHVGFVF-----QSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 358 LGVGQNITLAVLdtyahmtrIDAEAELGSIDQQIS---RMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDEP 434
Cdd:PRK10584 103 LNALENVELPAL--------LRGESSRQSRNGAKAlleQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 435 TRGVDVGAKYEIYKLMGALAAE-GVSIIMVS--SELAevlGVSNRVLVIGDGQLR 486
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVThdLQLA---ARCDRRLRLVNGQLQ 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
258-485 |
6.60e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 258 GEVIFEARNVTCYDVDNPKRKR---VDDISFVLRRGEILGIAGLVGAGRTEL---VSALFGAYPGRynaeVWLEGqvIDT 331
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGK----VYVDG--LDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 332 RTP--LKSIRAGLCMV---PEDRKRQGIIP-DLGVG-QNITLAVLDTyahMTRIDaEAeLGSIDQQISRMHlktaSPSLp 404
Cdd:PRK13633 75 SDEenLWDIRNKAGMVfqnPDNQIVATIVEeDVAFGpENLGIPPEEI---RERVD-ES-LKKVGMYEYRRH----APHL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 405 itsLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGvSNRVLVIGDG 483
Cdd:PRK13633 145 ---LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSG 220
|
..
gi 1067238353 484 QL 485
Cdd:PRK13633 221 KV 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-255 |
6.86e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVyPHGTWE---GEILWDGQPLKAQSIRETE---AAGIVIIHQ 89
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRvtaDRMRFDDIDLLRLSPRERRklvGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 90 EltlvPD--LSVAENIfmGHEL--TLPG----GR--MNYPAMLHRAEALMRELKVPDMNVALPVSQY--GGGYQQLVEIA 157
Cdd:PRK15093 97 E----PQscLDPSERV--GRQLmqNIPGwtykGRwwQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYelTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 158 KALNKQARLLILDEPSSAL---TRGEIEVLLDIIKglKAKGVACVYISHKLDEVAAVCDTIAVIRDGKHIATTAMAD-MD 233
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMeptTQAQIFRLLTRLN--QNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKElVT 248
|
250 260
....*....|....*....|...
gi 1067238353 234 IP-RIITQMVGREMSNLYPTEPH 255
Cdd:PRK15093 249 TPhHPYTQALIRAIPDFGSAMPH 271
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
261-485 |
8.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVTCYDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRT---ELVSALFGAYPGRynaeVWLEGQVIdTRTPLKS 337
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSttaRLIDGLFEEFEGK----VKIDGELL-TAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAGLCMVPEDrkrqgiiPDlgvGQNITLAVLDTYAHMTR---IDAEAELGSIDQQ---ISRMHLKTASPSlpitSLSGG 411
Cdd:PRK13642 79 LRRKIGMVFQN-------PD---NQFVGATVEDDVAFGMEnqgIPREEMIKRVDEAllaVNMLDFKTREPA----RLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067238353 412 NQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVlGVSNRVLVIGDGQL 485
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
406-485 |
8.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEgVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
292-486 |
9.25e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 292 ILGIAGLVGAGRTELVSALFG-AYP--GRynaeVWLEGQVidtrtpLKSIRAGLCMVPEDRK--------RqgIIPDLGV 360
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGlTRPqkGR----IVLNGRV------LFDAEKGICLPPEKRRigyvfqdaR--LFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 361 GQNITlavldtYAhMTRIDAE-----AELGSIDQQISRmhlktaspsLPITsLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:PRK11144 94 RGNLR------YG-MAKSMVAqfdkiVALLGIEPLLDR---------YPGS-LSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 436 RGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLR 486
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-221 |
9.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.55 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKAQS-------IRETeaAGIVIIHQELT 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT--GTVTVDDITITHKTkdkyirpVRKR--IGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 93 LVPDlSVAENIFMGHEltlpGGRMNYPAMLHRAEALMRELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQARLLILDEP 172
Cdd:PRK13646 98 LFED-TVEREIIFGPK----NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067238353 173 SSALTRGEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDG 221
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
258-440 |
1.08e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.12 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 258 GEVIFEarNVTcYDVDNpKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGrynaevwlEGQV----IDTR 332
Cdd:PRK13657 333 GAVEFD--DVS-FSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQ--------SGRIlidgTDIR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 333 T-PLKSIRAGLCMVPEDrkrqGIIPDLGVGQNITLAVLD-TYAHMTR-IDAEAELGSIDQQISRMHLKTASPSLpitSLS 409
Cdd:PRK13657 401 TvTRASLRRNIAVVFQD----AGLFNRSIEDNIRVGRPDaTDEEMRAaAERAQAHDFIERKPDGYDTVVGERGR---QLS 473
|
170 180 190
....*....|....*....|....*....|.
gi 1067238353 410 GGNQQKAVLAKMLMAKPKVLILDEPTRGVDV 440
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-203 |
1.30e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGI 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLS------VAENIFMGHELTLPGGRMNYPAMLhraEALMRELKVPDMNVALPVSQ-YGGGYQQLVEIA 157
Cdd:PRK09580 81 FMAFQYPVEIPGVSnqfflqTALNAVRSYRGQEPLDRFDFQDLM---EEKIALLKMPEDLLTRSVNVgFSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067238353 158 KALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISH 203
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
280-502 |
1.31e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.87 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEIL-----------GIAGLVG---AGRTELVSALFGAYPgrynaevWLEGQV-IDTRtPLKS-----IR 339
Cdd:PRK10790 343 IDNVSFAYRDDNLVlqninlsvpsrGFVALVGhtgSGKSTLASLLMGYYP-------LTEGEIrLDGR-PLSSlshsvLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 340 AGLCMVPEDrkrqgiiPdlgvgqnITLAvlDT-YAHMT---RIDAEAelgsIDQQISRMHLKTASPSLPI---------- 405
Cdd:PRK10790 415 QGVAMVQQD-------P-------VVLA--DTfLANVTlgrDISEEQ----VWQALETVQLAELARSLPDglytplgeqg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKlmgALAA--EGVSIIMVSSELAEVLGVSNrVLVIGDG 483
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ---ALAAvrEHTTLVVIAHRLSTIVEADT-ILVLHRG 550
|
250 260
....*....|....*....|.
gi 1067238353 484 QL--RGdfindglTQEQVLAA 502
Cdd:PRK10790 551 QAveQG-------THQQLLAA 564
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-219 |
1.33e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.88 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKaQSIRETEAAgIVIIHQELTLVPD 96
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTR-QALQKNLVA-YVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFMgheltlpgGRMNYPAMLHRAEALMRE-----LKVPDMnVALPVSQYG---GGYQQLVEIAKALNKQARLLI 168
Cdd:PRK15056 95 VLVEDVVMM--------GRYGHMGWLRRAKKRDRQivtaaLARVDM-VEFRHRQIGelsGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 169 LDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVCDTIAVIR 219
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-222 |
1.46e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.87 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPhgtW-EGEILWDGQPLKA---QSIREteaaGIVIIHQELTLVPD 96
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP---LtEGEIRLDGRPLSSlshSVLRQ----GVAMVQQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 lSVAENIFMGHELT-------LpggrmnypAMLHRAEaLMRELkvPDmNVALPVSQYGG----GYQQLVEIAKALNKQAR 165
Cdd:PRK10790 430 -TFLANVTLGRDISeeqvwqaL--------ETVQLAE-LARSL--PD-GLYTPLGEQGNnlsvGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 166 LLILDEPSSALTRG---EIEVLLDIIKglkaKGVACVYISHKLDEVAAVcDTIAVIRDGK 222
Cdd:PRK10790 497 ILILDEATANIDSGteqAIQQALAAVR----EHTTLVVIAHRLSTIVEA-DTILVLHRGQ 551
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-222 |
1.53e-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: 51.10 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSA----VYPHGTWEGEILWDGQPLKAQsireteaagiviihqeltlvpD 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemdkVEGHVHMKGSVAYVPQQAWIQ---------------------N 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 97 LSVAENIFMGHELTLPggrmNYPAMLhRAEALMRELKVPDMNVALPVSQYG----GGYQQLVEIAKALNKQARLLILDEP 172
Cdd:TIGR00957 713 DSLRENILFGKALNEK----YYQQVL-EACALLPDLEILPSGDRTEIGEKGvnlsGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 173 SSALTRGEIEVLLDIIKGLKA--KGVACVYISHKLDEVAAVcDTIAVIRDGK 222
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGK 838
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
261-503 |
1.73e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.73 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 261 IFEARNVT-CYDVDNpkrKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRynAEVWLEGQVIDTRTpLKSI 338
Cdd:PRK13647 4 IIEVEDLHfRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQR--GRVKVMGREVNAEN-EKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 RAGLCMVPEDRKRQ----GIIPDLGVG-QNITLAvldtyAHMTRIDAEAELGSIDQQisrmHLKTASPSlpitSLSGGNQ 413
Cdd:PRK13647 78 RSKVGLVFQDPDDQvfssTVWDDVAFGpVNMGLD-----KDEVERRVEEALKAVRMW----DFRDKPPY----HLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 414 QKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLRGDFINDG 493
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSL 224
|
250
....*....|
gi 1067238353 494 LTQEQVLAAA 503
Cdd:PRK13647 225 LTDEDIVEQA 234
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-215 |
1.83e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 1.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 142 PVSQYGGGYQQLVEIAKALNKQAR---LLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKLDeVAAVCDTI 215
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VIKCADWI 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-78 |
1.94e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 1.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDGQPLKAQSIRE 78
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGKPVTAEQPED 394
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
275-484 |
1.94e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.41 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 275 PKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNaevwLEGQV----IDTRTPLKSIRAGLCMVPE-DR 349
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS----VEGDIhyngIPYKEFAEKYPGEIIYVSEeDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 350 KrqgiIPDLGVGQNITLAvLDTYAHmtridaeaelgsidqQISRmhlktaspslpitSLSGGNQQKAVLAKMLMAKPKVL 429
Cdd:cd03233 94 H----FPTLTVRETLDFA-LRCKGN---------------EFVR-------------GISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 430 ILDEPTRGVDVGAKYEIYKLMGALA--AEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
265-485 |
2.23e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.52 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 265 RNVTCyDVDNP--KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRynaevWlegQVIDTRTPLKSIRAgL 342
Cdd:COG4170 7 RNLTI-EIDTPqgRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-----W---HVTADRFRWNGIDL-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 343 CMVPEDRKRQgiipdlgVGQNITLAVLDTYAHMtriDAEAELGsidQQIS------------------------------ 392
Cdd:COG4170 77 KLSPRERRKI-------IGREIAMIFQEPSSCL---DPSAKIG---DQLIeaipswtfkgkwwqrfkwrkkraiellhrv 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 393 --RMHLKTASpSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAA-EGVSIIMVSSELAE 469
Cdd:COG4170 144 giKDHKDIMN-SYP-HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLES 221
|
250
....*....|....*.
gi 1067238353 470 VLGVSNRVLVIGDGQL 485
Cdd:COG4170 222 ISQWADTITVLYCGQT 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-222 |
2.27e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 23 GIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWE--GEILWDGQPLKAQSIRETEAAgIVIIHQELTLVPDLSVA 100
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQtaGRVLLDGKPVAPCALRGRKIA-TIMQNPRSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 101 ENifmGHELTLPGGRmnyPAMLHRAEALMRELKVPDMNVALPVS--QYGGGYQQLVEIAKALNKQARLLILDEPSSALTR 178
Cdd:PRK10418 100 TH---ARETCLALGK---PADDATLTAALEAVGLENAARVLKLYpfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067238353 179 GEIEVLLDIIKGLKAK-GVACVYISHKLDEVAAVCDTIAVIRDGK 222
Cdd:PRK10418 174 VAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-502 |
2.27e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 407 SLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEG-VSIIMVSSELAEVlGVSNRVLVIGDGQL 485
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFNNPDR 1436
|
90
....*....|....*..
gi 1067238353 486 RGDFINDGLTQEQVLAA 502
Cdd:PTZ00265 1437 TGSFVQAHGTHEELLSV 1453
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
408-485 |
2.44e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.72 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDV----GAKYEIYKLMGALaaeGVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrSMREKIRELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
..
gi 1067238353 484 QL 485
Cdd:PRK11432 214 KI 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-222 |
2.54e-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: 50.29 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 16 GGVNALNGIDIKVKPGECVGLCGENGAGKSTLmkvLSAVYPHGTWEGEILWDGQPLKAQSIRETEAAGIVIIHQELtlvp 95
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVF---- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 dlsvaenIFMGhelTLpggRMNY-PAMLHRAEALMR---ELKVPDMNVALP-----VSQYGG-----GYQQLVEIAKALN 161
Cdd:TIGR01271 1303 -------IFSG---TF---RKNLdPYEQWSDEEIWKvaeEVGLKSVIEQFPdkldfVLVDGGyvlsnGHKQLMCLARSIL 1369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 162 KQARLLILDEPSSALTrgeiEVLLDII-KGLKAKGVACVYI--SHKLdEVAAVCDTIAVIRDGK 222
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLD----PVTLQIIrKTLKQSFSNCTVIlsEHRV-EALLECQQFLVIEGSS 1428
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-236 |
2.62e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTL----MKVLSavyphgTWEGEILWDGQPLKAQSIREteaagiviIHQELTLVP- 95
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLlltfMRMVE------VCGGEIRVNGREIGAYGLRE--------LRRQFSMIPq 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 96 -----DLSVAENIFMGHELTlpggrmnyPAMLHRAEAL--MRElKVP------DMNVALPVSQYGGGYQQLVEIAKALNK 162
Cdd:PTZ00243 1392 dpvlfDGTVRQNVDPFLEAS--------SAEVWAALELvgLRE-RVAsesegiDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 163 QARLLIL-DEPSS----ALTRgeiEVLLDIIKGLKAKGVacVYISHKLDEVAAvCDTIAVIRDGkhiattAMADMDIPR 236
Cdd:PTZ00243 1463 KGSGFILmDEATAnidpALDR---QIQATVMSAFSAYTV--ITIAHRLHTVAQ-YDKIIVMDHG------AVAEMGSPR 1529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-101 |
2.87e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 7 QMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILWDGQPLKAQSIRETeAAGIVI 86
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD--SGEVLVDGLDVATTPSREL-AKRLAI 79
|
90
....*....|....*
gi 1067238353 87 IHQELTLVPDLSVAE 101
Cdd:COG4604 80 LRQENHINSRLTVRE 94
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
408-483 |
3.26e-06 |
|
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: 47.91 E-value: 3.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVS--SELAEVLgVSNRVLVIGDG 483
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYI-KPDRVHVLYDG 181
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
406-512 |
4.84e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRER 657
|
90 100
....*....|....*....|....*..
gi 1067238353 486 RGDFINDGLTQEQVLAAALSHNNNDRK 512
Cdd:PTZ00265 658 GSTVDVDIIGEDPTKDNKENNNKNNKD 684
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-203 |
6.51e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 48.65 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILwdgQPlkaqsiretEAAGIVIIHQELTLvPDLSVA 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS--GRIA---RP---------AGARVLFLPQRPYL-PLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 101 ENifmgheLTLPGGRMNYPamLHRAEALMRELK----VPDMNVALPVSQ-YGGGYQQLVEIAKALNKQARLLILDEPSSA 175
Cdd:COG4178 444 EA------LLYPATAEAFS--DAELREALEAVGlghlAERLDEEADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*...
gi 1067238353 176 LTRGEIEVLLDIIKGlKAKGVACVYISH 203
Cdd:COG4178 516 LDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-52 |
6.59e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 6.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLS 52
Cdd:PRK10636 308 LPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA 359
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
387-483 |
7.79e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.16 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 387 IDQQISRM-------HLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GV 458
Cdd:PRK10851 113 IKAKVTQLlemvqlaHLADRYPA----QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKF 188
|
90 100
....*....|....*....|....*
gi 1067238353 459 SIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK10851 189 TSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
408-485 |
8.89e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.71 E-value: 8.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-172 |
9.06e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 9 NGIVkSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHG-----------TWEGEILWDgqpLKaQSIr 77
Cdd:PRK10938 265 NGVV-SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrRGSGETIWD---IK-KHI- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 78 eteaaGIVI--IHQELTLvpDLSVAENIFMGH--ELTLpggrmnYPAMLHRAEALMRE-LKVPDMNVAL---PVSQYGGG 149
Cdd:PRK10938 339 -----GYVSssLHLDYRV--STSVRNVILSGFfdSIGI------YQAVSDRQQKLAQQwLDILGIDKRTadaPFHSLSWG 405
|
170 180
....*....|....*....|...
gi 1067238353 150 YQQLVEIAKALNKQARLLILDEP 172
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEP 428
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
259-463 |
1.04e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.09 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 259 EVIFEARNVTcYDVdnPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALfgaypGRYNAEVwlEGQVIDTRTPLKSI 338
Cdd:PRK10575 9 DTTFALRNVS-FRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-----GRHQPPS--EGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 RAGLCMvpedRKRQGIIPDLGVGQNITLAVLDTYAHMTRIDAEAELGSIDQQ-----ISRMHLKTASPSLpITSLSGGNQ 413
Cdd:PRK10575 79 SSKAFA----RKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREkveeaISLVGLKPLAHRL-VDSLSGGER 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 414 QKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMV 463
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAV 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
267-488 |
1.39e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 267 VTCYDVDNPKRKRV--DDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPG-------RYNAEVWLEGQvidtrtPLKS 337
Cdd:PRK13547 2 LTADHLHVARRHRAilRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgaRVTGDVTLNGE------PLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 338 IRAglcmvPEDRKRQGIIPDLG------VGQNITLavLDTYAHMTRidaEAELGSIDQQISRMHLKTASPSL----PITS 407
Cdd:PRK13547 76 IDA-----PRLARLRAVLPQAAqpafafSAREIVL--LGRYPHARR---AGALTHRDGEIAWQALALAGATAlvgrDVTT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKML---------MAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE---GVSIIMVSSELAEVLgvSN 475
Cdd:PRK13547 146 LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVLAIVHDPNLAARH--AD 223
|
250
....*....|...
gi 1067238353 476 RVLVIGDGQLRGD 488
Cdd:PRK13547 224 RIAMLADGAIVAH 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
406-485 |
1.43e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.57 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 406 TSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEgVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
407-500 |
1.54e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 407 SLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGVSNRVLVIgdgqLR 486
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFF----LD 222
|
90
....*....|....
gi 1067238353 487 GDFINDGLTQEQVL 500
Cdd:PRK14239 223 GDLIEYNDTKQMFM 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
117-215 |
1.71e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 117 NYPAMLHRAEALMrELKVPDMNVALPVSQYGGGYQQLVEIAKALNKQAR---LLILDEPSSALTRGEIEVLLDIIKGLKA 193
Cdd:TIGR00630 802 AVPSISRKLQTLC-DVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
|
90 100
....*....|....*....|..
gi 1067238353 194 KGVACVYISHKLDeVAAVCDTI 215
Cdd:TIGR00630 881 KGNTVVVIEHNLD-VIKTADYI 901
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
281-464 |
1.73e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.21 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 281 DDISFVLRRGEILGIAGLVGAGRTELVSALFGaYPGrYNA---EVWLEGQVIdtrtplksiragLCMVPEDRKRQGI--- 354
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPK-YEVtsgSILLDGEDI------------LELSPDERARAGIfla 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 ------IPDLGVGQNITLAVldTYAHMTRIDAEAELGSIDQQISRMHLKTASPSLPI-TSLSGGNQQKAVLAKMLMAKPK 427
Cdd:COG0396 83 fqypveIPGVSVSNFLRTAL--NARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVS 464
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIIT 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-176 |
2.32e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 21 LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWE-GEILWDGQPLKAQSIRETeaaGIViiHQELTLVPDLSV 99
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITgGDRLVNGRPLDSSFQRSI---GYV--QQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 100 AENIFMGHELTLPGG-----RMNYpamlhrAEALMRELKVPDMNVALpVSQYGGGYQqlVEIAKALN-------KQARLL 167
Cdd:TIGR00956 854 RESLRFSAYLRQPKSvskseKMEY------VEEVIKLLEMESYADAV-VGVPGEGLN--VEQRKRLTigvelvaKPKLLL 924
|
....*....
gi 1067238353 168 ILDEPSSAL 176
Cdd:TIGR00956 925 FLDEPTSGL 933
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
262-462 |
2.69e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 262 FEARNVTCYDVDnpkRKRVDDISFVLRRGEILGIAGLVGAGRTEL---VSALFGAYPGRynaeVWLEGQVIDTRTPLKSI 338
Cdd:PRK13539 3 LEGEDLACVRGG---RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLPPAAGT----IKLDGGDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 R-AGlcmvpedrKRQGIIPDLGVGQNITL--AVLDTyahmtridaeaELGSIDQQISRMHLKTASPsLPITSLSGGNQQK 415
Cdd:PRK13539 76 HyLG--------HRNAMKPALTVAENLEFwaAFLGG-----------EELDIAAALEAVGLAPLAH-LPFGYLSAGQKRR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067238353 416 AVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIM 462
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-199 |
2.80e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTweGEILWDGQPLKaqsiRETEAAGI 84
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVES--GQIQIDGKTAT----RGDRSRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 85 VIIHQELTLVPDLSVAENI-FMG-----HELTLPGGRMNYPAMLHRAEALMRELKvpdmnvalpvsqygGGYQQLVEIAK 158
Cdd:PRK13543 85 AYLGHLPGLKADLSTLENLhFLCglhgrRAKQMPGSALAIVGLAGYEDTLVRQLS--------------AGQKKRLALAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1067238353 159 ALNKQARLLILDEPSSALTRGEIEVLLDIIKG-LKAKGVACV 199
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLDLEGITLVNRMISAhLRGGGAALV 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-66 |
3.79e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 3.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 6 LQMNGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGtwEGEILW 66
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD--SGTVKW 378
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-176 |
3.79e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 5 LLQMNGIVKSFGG--VNALNGidiKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDgqpL----KAQSIR 77
Cdd:PRK13409 340 LVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLkPD---EGEVDPE---LkisyKPQYIK 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 78 eteaagiviIHQELTlVPDL--SVAENI---FMGHELTLPGGrmnypamLHRaeaLMrELKVPDMNvalpvsqygGGYQQ 152
Cdd:PRK13409 411 ---------PDYDGT-VEDLlrSITDDLgssYYKSEIIKPLQ-------LER---LL-DKNVKDLS---------GGELQ 460
|
170 180
....*....|....*....|....
gi 1067238353 153 LVEIAKALNKQARLLILDEPSSAL 176
Cdd:PRK13409 461 RVAIAACLSRDADLYLLDEPSAHL 484
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
404-484 |
4.29e-05 |
|
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: 44.24 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLMAKPK--VLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELaEVLGVSNRVLVIG 481
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIIDFG 162
|
...
gi 1067238353 482 DGQ 484
Cdd:cd03238 163 PGS 165
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-205 |
4.58e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.05 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVNA--LNGIDIkVKPGECVGLCGENGAGKSTLMKVLSA-VYPH-GTWEGEILWD-------GQPLKA--QSIRETEAAg 83
Cdd:cd03236 11 GPNSfkLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGkLKPNlGKFDDPPDWDeildefrGSELQNyfTKLLEGDVK- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 84 IVIIHQELTLVP---DLSVAENIFMGHEltlpggrmnypamLHRAEALMREL---KVPDMNvalpVSQYGGGYQQLVEIA 157
Cdd:cd03236 89 VIVKPQYVDLIPkavKGKVGELLKKKDE-------------RGKLDELVDQLelrHVLDRN----IDQLSGGELQRVAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067238353 158 KALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKGVACVYISHKL 205
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
277-470 |
4.91e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 277 RKRVDDISFVLRRGEILGIAGLVGAGRTEL---VSALFGAYPGrynaEVWLEGQVIDTRTPlksiraglcmvpeDRKRQG 353
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLlkiVASLISPTSG----TLLFEGEDISTLKP-------------EIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 354 I-----IPDLgVGQnitlAVLDTYAHMTRIDAEA-ELGSIDQQISRMHLKTASPSLPITSLSGGNQQKAVLAKMLMAKPK 427
Cdd:PRK10247 83 VsycaqTPTL-FGD----TVYDNLIFPWQIRNQQpDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1067238353 428 VLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEV 470
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEI 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
265-484 |
5.09e-05 |
|
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: 44.38 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 265 RNVTCY--DVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPgRYNAEVWLEGQV--------IDTRTP 334
Cdd:cd03250 4 EDASFTwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-KLSGSVSVPGSIayvsqepwIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 335 LKSIRAGLcmvPEDRKR-QGII------PDLGVgqnitLAVLDtyahMTRIdaeAELGsidqqisrmhlktaspslpiTS 407
Cdd:cd03250 83 RENILFGK---PFDEERyEKVIkacalePDLEI-----LPDGD----LTEI---GEKG--------------------IN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVD--VGAKyeIYK--LMGALaAEGVSIIMVSSELaEVLGVSNRVLVIGDG 483
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDahVGRH--IFEncILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
.
gi 1067238353 484 Q 484
Cdd:cd03250 204 R 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
408-488 |
5.94e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSElAEVLGVSNRVLVIGDGQLRG 487
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
.
gi 1067238353 488 D 488
Cdd:PRK10535 224 N 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-206 |
6.73e-05 |
|
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: 43.47 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 18 VNALNGIDIKVKPGECVGLCGENGAGKSTLMKvlsavyphgtwegEILWDGQPLKAQSIRETEAAGIVIIHQELTLVPDL 97
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SvaenifMGHeltLPGGRmnypamlhraealmrelkvpdmnvalPVSQYGGGYQQLVEIAKALNKQAR--LLILDEPSSA 175
Cdd:cd03238 75 G------LGY---LTLGQ--------------------------KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190
....*....|....*....|....*....|.
gi 1067238353 176 LTRGEIEVLLDIIKGLKAKGVACVYISHKLD 206
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-178 |
6.89e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 19 NALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEI-LWDGQplkaqsireteaagiviIHQELTLVPDL 97
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVdVPDNQ-----------------FGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 98 SVAENIFMGHELtlpggrmnypamLHRA----EALMRElkvpdmnvalPVSQYGGGYQQLVEIAKALNKQARLLILDEPS 173
Cdd:COG2401 107 GRKGDFKDAVEL------------LNAVglsdAVLWLR----------RFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
....*
gi 1067238353 174 SALTR 178
Cdd:COG2401 165 SHLDR 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
378-435 |
7.58e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 7.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 378 IDAeAELGSIDQQISR-MH-LKTASPSLPITSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:PRK11819 133 IDA-ADAWDLDSQLEIaMDaLRCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
283-511 |
7.99e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 283 ISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYNAEVWLE--GQVIDTRTPL-KSIRAGLCMVPEDRKRQGIIPDLG 359
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIEllGRTVQREGRLaRDIRKSRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNITLAVLDT-------YAHMTRIDAEAELGSIdQQISRMHLKTASpslpITSLSGGNQQKAVLAKMLMAKPKVLILD 432
Cdd:PRK09984 103 VLENVLIGALGStpfwrtcFSWFTREQKQRALQAL-TRVGMVHFAHQR----VSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 433 EPTRGVDV-GAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQLrgdfINDGLTQeqvlaaalsHNNNDR 511
Cdd:PRK09984 178 EPIASLDPeSARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV----FYDGSSQ---------QFDNER 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
404-489 |
8.78e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAkyeIYKLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK15064 435 SVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
....*.
gi 1067238353 484 QLRgDF 489
Cdd:PRK15064 512 GVV-DF 516
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-221 |
9.09e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 38 GENGAGKSTLMKVLSAVYphgTWEGEILWDGQPLKAQSIRETEAAGIVIIH------QELTLVPDLSVAENIFMGHEltl 111
Cdd:cd03240 29 GQNGAGKTTIIEALKYAL---TGELPPNSKGGAHDPKLIREGEVRAQVKLAfenangKKYTITRSLAILENVIFCHQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 112 pgGRMNYPAMLHRAealmrelkvpdmnvalpvsQYGGGYQQLVEI------AKALNKQARLLILDEPSSALTRGEIE-VL 184
Cdd:cd03240 103 --GESNWPLLDMRG-------------------RCSGGEKVLASLiirlalAETFGSNCGILALDEPTTNLDEENIEeSL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1067238353 185 LDIIKGLKAKGV-ACVYISHKLDEVAAVCDTIAVIRDG 221
Cdd:cd03240 162 AEIIEERKSQKNfQLIVITHDEELVDAADHIYRVEKDG 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
280-485 |
9.43e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 44.68 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRT---------ELVSAlfgaypGrynaEVWLEGQVIdTRTPlksiraglcmvPEDRk 350
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKStllrmiaglEDPTS------G----EILIGGRDV-TDLP-----------PKDR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 351 rqgiipDLG-VGQNITLavldtYAHMT------------RIDAEAelgsIDQQISRM-------HLKTASPSlpitSLSG 410
Cdd:COG3839 76 ------NIAmVFQSYAL-----YPHMTvyeniafplklrKVPKAE----IDRRVREAaellgleDLLDRKPK----QLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 411 GNQQKAVLAKMLMAKPKVLILDEPTRGVDvgAK------YEIYKLMGALaaeGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLD--AKlrvemrAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
.
gi 1067238353 485 L 485
Cdd:COG3839 212 I 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
280-485 |
9.99e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAY-PGRynAEVWLEGQVID--TRTPLKSIR-AGLCMVPEDRkrqGII 355
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTR--GQVLIDGVDIAkiSDAELREVRrKKIAMVFQSF---ALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 PDLGVGQNITLAVldtyaHMTRIDAEAELGSIDQQISRMHLKTASPSLPiTSLSGGNQQKAVLAKMLMAKPKVLILDEPT 435
Cdd:PRK10070 119 PHMTVLDNTAFGM-----ELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 436 RGVDVGAKYEIY-KLMGALAAEGVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK10070 193 SALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
278-484 |
1.06e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 278 KRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAypgryNAEVWlegQVIDTRTPLKSIRAgLCMVPEDRKRQgiipd 357
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-----TKDNW---RVTADRMRFDDIDL-LRLSPRERRKL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 358 lgVGQNITL------AVLDTYAHMTRIDAEAELGSI-------------DQQISRMHL------KTASPSLPItSLSGGN 412
Cdd:PRK15093 87 --VGHNVSMifqepqSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrkRRAIELLHRvgikdhKDAMRSFPY-ELTEGE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 413 QQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGAL-AAEGVSIIMVSSELAEVLGVSNRVLVIGDGQ 484
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
276-502 |
1.23e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.82 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 276 KRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALfGAYPGRYNAEVWLEGQVIDtRTPLKSIRAGLCMVPEDRKRQGii 355
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL-SRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 356 pDLGVGQnitLAVLDTYAHMT-----RIDAEAELGSIDQQISRMHLKTASpslpITSLSGGNQQKAVLAKMLMAKPKVLI 430
Cdd:PRK10253 95 -DITVQE---LVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQS----VDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 431 LDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQLrgdfINDGLTQEQVLAA 502
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKI----VAQGAPKEIVTAE 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-212 |
1.24e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 20 ALNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAV-YPHgtwEGEILWDGqplkaqsireteAAGIVIIHQELTlvPDLS 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPN---KGTVDIKG------------SAALIAISSGLN--GQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 99 VAENIfmghELTlpgGRMNYPAMLHRAEALMRELKVPDMN--VALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:PRK13545 102 GIENI----ELK---GLMMGLTKEKIKEIIPEIIEFADIGkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1067238353 177 TRGEIEVLLDIIKGLKAKGVACVYISHKLDEVAAVC 212
Cdd:PRK13545 175 DQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFC 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-103 |
1.34e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.06 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 6 LQMNGIVKSF-GGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKV---LSAVYphgtwEGEILWDGQPlkaqsIRETEA 81
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERIT-----SGEIWIGGRV-----VNELEP 73
|
90 100
....*....|....*....|....
gi 1067238353 82 A--GIVIIHQELTLVPDLSVAENI 103
Cdd:PRK11650 74 AdrDIAMVFQNYALYPHMSVRENM 97
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
280-506 |
1.59e-04 |
|
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: 43.69 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 280 VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYpgRYNAEVWLEGQVIDTrTPLKSIRAGLCMVPEdrkrQGIIPDLG 359
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL--NTEGDIQIDGVSWNS-VPLQKWRKAFGVIPQ----KVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 360 VGQNitlavLDTYA-----HMTRIDAEAELGS-IDQQISRMHLKTASPSLpitSLSGGNQQKAVLAKMLMAKPKVLILDE 433
Cdd:cd03289 93 FRKN-----LDPYGkwsdeEIWKVAEEVGLKSvIEQFPGQLDFVLVDGGC---VLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067238353 434 PTRGVDvGAKYEIYKLMGALAAEGVSIIMVSSELAEVLGVsNRVLVIGDGQLRG-DFINDGLTQEQVLAAALSH 506
Cdd:cd03289 165 PSAHLD-PITYQVIRKTLKQAFADCTVILSEHRIEAMLEC-QRFLVIEENKVRQyDSIQKLLNEKSHFKQAISP 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
265-485 |
1.60e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.91 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 265 RNVTC-YDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALfgaypgryNA-------EVWLEGQVIDTRTPlK 336
Cdd:COG1135 5 ENLSKtFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI--------NLlerptsgSVLVDGVDLTALSE-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 337 SIRAglcmvpedrKRQGIipdlG-------------VGQNITLAVldTYAHMTRidaeAElgsIDQQISRM-------HL 396
Cdd:COG1135 76 ELRA---------ARRKI----GmifqhfnllssrtVAENVALPL--EIAGVPK----AE---IRKRVAELlelvglsDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 397 KTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSN 475
Cdd:COG1135 134 ADAYPS----QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICD 209
|
250
....*....|
gi 1067238353 476 RVLVIGDGQL 485
Cdd:COG1135 210 RVAVLENGRI 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
258-487 |
1.60e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.24 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 258 GEVIFeaRNVT-CYD-VDNPKrkrVDDISFVLRRGEILGIAGLVGAGRTELVSaLFGAYPGRYNAEVWLEGQVIDTRTpL 335
Cdd:PRK11176 340 GDIEF--RNVTfTYPgKEVPA---LRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYDIDEGEILLDGHDLRDYT-L 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 336 KSIRAGLCMVPEDRKrqgIIPDLgVGQNITLAVLDTYAHmTRIDAEAELGSIDQQISRMH--LKTAspslpI----TSLS 409
Cdd:PRK11176 413 ASLRNQVALVSQNVH---LFNDT-IANNIAYARTEQYSR-EQIEEAARMAYAMDFINKMDngLDTV-----IgengVLLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 410 GGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIImVSSELAEVLGvSNRVLVIGDGQL--RG 487
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIveRG 560
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
407-475 |
1.66e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.62 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 407 SLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALaAEGVSIIMVSSELAEVLGVSN 475
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
282-514 |
1.71e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 44.32 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 282 DISFVLRRGEILGIAGLVGAGRTELVSALFGAYpgrynaEVwLEGQVIDTRTPLKSIRaglcmVPEDRKRQGII---PDL 358
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF------DV-SEGDIRFHDIPLTKLQ-----LDSWRSRLAVVsqtPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 359 ---GVGQNITLAVLDtyAHMTRIDAEAELGSIDQQISRMhlktasPSLPITS-------LSGGNQQKAVLAKMLMAKPKV 428
Cdd:PRK10789 401 fsdTVANNIALGRPD--ATQQEIEHVARLASVHDDILRL------PQGYDTEvgergvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 429 LILDEPTRGVDVGAKYEIYKLMgALAAEGVSIIMVSSELAEVLGVSNrVLVIGDGQL--RGDfiNDGLTQE--------- 497
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNL-RQWGEGRTVIISAHRLSALTEASE-ILVMQHGHIaqRGN--HDQLAQQsgwyrdmyr 548
|
250
....*....|....*...
gi 1067238353 498 -QVLAAALSHNNNDRKTA 514
Cdd:PRK10789 549 yQQLEAALDDAPEIREEA 566
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
270-442 |
2.04e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 270 YDVDNPKRKR-----------VDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRYnaevwLEGQVIDTRTPLKSI 338
Cdd:PLN03140 875 YFVDMPAEMKeqgvtedrlqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY-----IEGDIRISGFPKKQE 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 R----AGLCmvpedrkRQGII--PDLGVGQNITLAV-------LDTYAHMTRIDAEAELGSIDqqisrmHLKTASPSLP- 404
Cdd:PLN03140 950 TfariSGYC-------EQNDIhsPQVTVRESLIYSAflrlpkeVSKEEKMMFVDEVMELVELD------NLKDAIVGLPg 1016
|
170 180 190
....*....|....*....|....*....|....*...
gi 1067238353 405 ITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGA 442
Cdd:PLN03140 1017 VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
385-485 |
2.59e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 385 GSIDQQIsRMHLK----TASPSL-PITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAkyeIYKLMGALAAEGVS 459
Cdd:PLN03073 601 GVPEQKL-RAHLGsfgvTGNLALqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGG 676
|
90 100
....*....|....*....|....*.
gi 1067238353 460 IIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
422-461 |
3.21e-04 |
|
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: 41.85 E-value: 3.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1067238353 422 LMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSII 461
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAIL 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
272-434 |
3.86e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.38 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 272 VDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYPGRyNAEVWLEGQvidtrtPLKSIRAGLCMVPEDrkr 351
Cdd:PRK11248 9 ADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGK------PVEGPGAERGVVFQN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 352 QGIIPDLGVGQNITLAVldtyaHMTRIDAEAELGSIDQQISRMHLKTASpSLPITSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
...
gi 1067238353 432 DEP 434
Cdd:PRK11248 153 DEP 155
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
286-468 |
5.39e-04 |
|
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: 42.46 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 286 VLRRGEILGIAGLVGAGRTELVSALFGAY-P--GRYNAEV-WLEgqVIDT------RTPLKSIRAGLCMVPedRKRQGI- 354
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELkPnlGDYDEEPsWDE--VLKRfrgtelQDYFKKLANGEIKVA--HKPQYVd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 355 -IPDLGVGQNITLavldtyahMTRIDaeaELGSIDQQISRMHLKtasPSL--PITSLSGGNQQKAVLAKMLMAKPKVLIL 431
Cdd:COG1245 171 lIPKVFKGTVREL--------LEKVD---ERGKLDELAEKLGLE---NILdrDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 1067238353 432 DEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELA 468
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLA 273
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-176 |
5.99e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 29 KPGECVGLCGENGAGKSTLMKVLSAVYPHGTWEGEILWDGQPLKaqsiRETEAAGIVIIHQELTLVPDLSVAENIFMGHE 108
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKK----QETFARISGYCEQNDIHSPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067238353 109 LTLPGGRMNYPAMLHRAEAL----MRELKvpDMNVALP-VSQYGGGYQQLVEIAKALNKQARLLILDEPSSAL 176
Cdd:PLN03140 980 LRLPKEVSKEEKMMFVDEVMelveLDNLK--DAIVGLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
408-485 |
7.11e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 41.71 E-value: 7.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAAE-GVSIIMVSSELAEVLGVSNRVLVIGDGQL 485
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
400-483 |
7.88e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 400 SPSLPITSLSGGNQQKAVLAKMLMAKPK--VLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSElAEVLGVSNRV 477
Cdd:PRK00635 469 TPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRI 547
|
....*.
gi 1067238353 478 LVIGDG 483
Cdd:PRK00635 548 IDIGPG 553
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
404-499 |
8.77e-04 |
|
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: 41.92 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLMAK---PKVLILDEPTRGVDVGakyEIYKLM---GALAAEGVSIIMVSSELaEVLGVSNRV 477
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFD---DIKKLLevlQRLVDKGNTVVVIEHNL-DVIKTADYI 901
|
90 100
....*....|....*....|...
gi 1067238353 478 LVIG-DGQLRGDFINDGLTQEQV 499
Cdd:TIGR00630 902 IDLGpEGGDGGGTVVASGTPEEV 924
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
378-468 |
9.16e-04 |
|
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: 41.20 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 378 IDAEAELGSIDQQISRMHLKtasPSLP--ITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLMGALAA 455
Cdd:cd03236 111 LKKKDERGKLDELVDQLELR---HVLDrnIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAE 187
|
90
....*....|...
gi 1067238353 456 EGVSIIMVSSELA 468
Cdd:cd03236 188 DDNYVLVVEHDLA 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
263-455 |
1.01e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 41.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 263 EARNVTC-YDVDNPKRKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGAYP---GRynaeVWLEGQVIDTRTPlksi 338
Cdd:COG4525 5 TVRHVSVrYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApssGE----ITLDGVPVTGPGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 339 raglcmvpeDR----KRQGIIPDLGVGQNITLAVldtyaHMTRIDAEAELGSIDQQISRMHLKTASPSlPITSLSGGNQQ 414
Cdd:COG4525 77 ---------DRgvvfQKDALLPWLNVLDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARR-RIWQLSGGMRQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067238353 415 KAVLAKMLMAKPKVLILDEPtrgvdvgakyeiyklMGALAA 455
Cdd:COG4525 142 RVGIARALAADPRFLLMDEP---------------FGALDA 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
62-208 |
1.31e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 62 GEILWDGQPLKAQSIRETEAAgIVIIHQELTLVpDLSVAENIFMGHE-LTLPGGRM--NYPAMLHRAEALMRELkvpDMN 138
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKEdATREDVKRacKFAAIDEFIESLPNKY---DTN 1351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 139 VALPVSQYGGGYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLKAKG-VACVYISHKLDEV 208
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI 1422
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
404-481 |
1.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 404 PITSLSGGNQQKAVLAKMLMA---KPKVLILDEPTRGVDVGAKYEIYKLMGALAAEGVSIIMVSSELaEVLGVSNRVLVI 480
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLEL 884
|
.
gi 1067238353 481 G 481
Cdd:PRK00635 885 G 885
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
372-483 |
1.51e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.78 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 372 YAHMTRID--------AEAELGSIDQ---QISRM----HLKTASPSlpitSLSGGNQQKAVLAKMLMAKPKVLILDEPTR 436
Cdd:PRK11000 87 YPHLSVAEnmsfglklAGAKKEEINQrvnQVAEVlqlaHLLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1067238353 437 GVD----VGAKYEIYKLMGALaaeGVSIIMVSSELAEVLGVSNRVLVIGDG 483
Cdd:PRK11000 163 NLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-176 |
1.59e-03 |
|
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: 40.92 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 11 IVKSFGG----VNAlnGidiKVKPGECVGLCGENGAGKSTLMKVLSAVY-PHgtwEGEILWDgqpL----KAQSIrETEA 81
Cdd:COG1245 347 LTKSYGGfsleVEG--G---EIREGEVLGIVGPNGIGKTTFAKILAGVLkPD---EGEVDED---LkisyKPQYI-SPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 82 agiviihqeltlvpDLSVAENIFMGHELTLPGGrmnypamLHRAEaLMRELKVPDMnVALPVSQYGGGYQQLVEIAKALN 161
Cdd:COG1245 415 --------------DGTVEEFLRSANTDDFGSS-------YYKTE-IIKPLGLEKL-LDKNVKDLSGGELQRVAIAACLS 471
|
170
....*....|....*
gi 1067238353 162 KQARLLILDEPSSAL 176
Cdd:COG1245 472 RDADLYLLDEPSAHL 486
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-225 |
2.07e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 17 GVN--ALNGIDIkVKPGECVGLCGENGAGKSTLMKVLS-AVYPH-GTWEGEILWDG--------------QPLKAQSIRe 78
Cdd:PRK13409 84 GVNgfKLYGLPI-PKEGKVTGILGPNGIGKTTAVKILSgELIPNlGDYEEEPSWDEvlkrfrgtelqnyfKKLYNGEIK- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 79 teaagivIIH--QELTLVPDL---SVAEnifmgheltlpggrmnypaMLHRAE--ALMREL-KVPDMNVAL--PVSQYGG 148
Cdd:PRK13409 162 -------VVHkpQYVDLIPKVfkgKVRE-------------------LLKKVDerGKLDEVvERLGLENILdrDISELSG 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 149 GYQQLVEIAKALNKQARLLILDEPSSALTRGEIEVLLDIIKGLkAKGVACVYISHKLdevaAVCDTIAvirDGKHIA 225
Cdd:PRK13409 216 GELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL----AVLDYLA---DNVHIA 284
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-224 |
2.36e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 28 VKPGECVGLCGENGAGKSTLMKVLSA--VYPHGTWEGEILWDGQPLkaQSIRETEAAGIVIIHQELTLVPDLSVAENIFM 105
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASntDGFHIGVEGVITYDGITP--EEIKKHYRGDVVYNAETDVHFPHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 106 GHELTLPGGRMN------YPAmlHRAEALM--------RELKV-PDMnvalpVSQYGGGYQQLVEIAKALNKQARLLILD 170
Cdd:TIGR00956 162 AARCKTPQNRPDgvsreeYAK--HIADVYMatyglshtRNTKVgNDF-----VRGVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 171 EpssaLTRG-EIEVLLDIIKGLKA-----KGVACVYISHKLDEVAAVCDTIAVIRDGKHI 224
Cdd:TIGR00956 235 N----ATRGlDSATALEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEGYQI 290
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-52 |
2.37e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1067238353 9 NGIVKSFGGVNALNGIDIKVKPGECVGLCGENGAGKSTLMKVLS 52
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMIT 371
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
258-440 |
2.54e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 258 GEVIFEARNVTcydvdnpK----RKRVDDISFVLRRGEILGIAGLVGAGRTELVSALFGaypgrynaevwLEgqvidtrT 333
Cdd:PRK11819 321 GDKVIEAENLS-------KsfgdRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG-----------QE-------Q 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 334 PLK-SIRAG----LCMVpeDRKRQGIIPDLGVGQNITlavlDTYAHMT----RIDAEAELGSI-----DQQisrmhlKta 399
Cdd:PRK11819 376 PDSgTIKIGetvkLAYV--DQSRDALDPNKTVWEEIS----GGLDIIKvgnrEIPSRAYVGRFnfkggDQQ------K-- 441
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067238353 400 spslPITSLSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDV 440
Cdd:PRK11819 442 ----KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
408-464 |
2.80e-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: 40.50 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067238353 408 LSGGNQQKAVLAKMLMAKPKVLILDEPTRGVDVGAKYEIYKLmgaLAAEGVSIIMVS 464
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVS 636
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-106 |
4.46e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067238353 1 MPDYLLQMNGIVKSFGGVNA-LNGIDIKVKPGECVGLCGENGAGKSTLMKVLSAVYPHgtWEGEilwdgqplkaqsIRET 79
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE--FEGE------------ARPA 67
|
90 100
....*....|....*....|....*..
gi 1067238353 80 EAAGIVIIHQELTLVPDLSVAENIFMG 106
Cdd:PRK11819 68 PGIKVGYLPQEPQLDPEKTVRENVEEG 94
|
|
| |
